ID THIG_BACSU Reviewed; 256 AA. AC O31618; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 22-FEB-2012, entry version 85. DE RecName: Full=Thiazole synthase; DE EC=2.8.1.10; GN Name=thiG; Synonyms=yjbT; OrderedLocusNames=BSU11690; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; 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 [2] RP FUNCTION, AND CATALYTIC ACTIVITY. RC STRAIN=168 / CU1065; RX PubMed=14567704; DOI=10.1021/bi034902z; RA Park J.-H., Dorrestein P.C., Zhai H., Kinsland C., McLafferty F.W., RA Begley T.P.; RT "Biosynthesis of the thiazole moiety of thiamin pyrophosphate (vitamin RT B1)."; RL Biochemistry 42:12430-12438(2003). RN [3] RP REACTION MECHANISM. RX PubMed=15489164; DOI=10.1016/j.chembiol.2004.08.009; RA Dorrestein P.C., Zhai H., McLafferty F.W., Begley T.P.; RT "The biosynthesis of the thiazole phosphate moiety of thiamin: the RT sulfur transfer mediated by the sulfur carrier protein ThiS."; RL Chem. Biol. 11:1373-1381(2004). RN [4] RP REACTION MECHANISM, MUTAGENESIS OF LYS-98, AND ROLE OF LYS-98 IN RP SCHIFF BASE FORMATION WITH DXP. RC STRAIN=168 / CU1065; RX PubMed=15012138; DOI=10.1021/ja039616p; RA Dorrestein P.C., Zhai H., Taylor S.V., McLafferty F.W., Begley T.P.; RT "The biosynthesis of the thiazole phosphate moiety of thiamin (vitamin RT B1): the early steps catalyzed by thiazole synthase."; RL J. Am. Chem. Soc. 126:3091-3096(2004). RN [5] RP REACTION PRODUCTS, AND REACTION MECHANISM. RX PubMed=19216519; DOI=10.1021/ja806752h; RA Hazra A., Chatterjee A., Begley T.P.; RT "Biosynthesis of the thiamin thiazole in Bacillus subtilis: RT identification of the product of the thiazole synthase-catalyzed RT reaction."; RL J. Am. Chem. Soc. 131:3225-3229(2009). RN [6] RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 3-255 IN COMPLEX WITH SULFUR RP CARRIER PROTEIN THIS AND PHOSPHATE, MUTAGENESIS OF GLU-100 AND RP ASP-184, SUBUNIT, AND REACTION MECHANISM. RX PubMed=15362849; DOI=10.1021/bi0488911; RA Settembre E.C., Dorrestein P.C., Zhai H., Chatterjee A., RA McLafferty F.W., Begley T.P., Ealick S.E.; RT "Thiamin biosynthesis in Bacillus subtilis: structure of the thiazole RT synthase/sulfur carrier protein complex."; RL Biochemistry 43:11647-11657(2004). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-255. RG Northeast structural genomics consortium (NESG); RT "Crystal structure of northeast structural genomics target sr156."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5- CC phosphate (DXP) to produce the thiazole phosphate moiety of CC thiamine. Sulfur is provided by the thiocarboxylate moiety of the CC carrier protein ThiS. In vitro, sulfur can be provided by H(2)S. CC -!- CATALYTIC ACTIVITY: 1-deoxy-D-xylulose 5-phosphate + 2- CC iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS] CC = 2-((2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene)ethyl CC phosphate + [sulfur-carrier protein ThiS] + 2 H(2)O. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC -!- SUBUNIT: Homotetramer. Forms heterodimers with either ThiH or CC ThiS. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the ThiG family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL009126; CAB13026.1; -; Genomic_DNA. DR PIR; D69845; D69845. DR RefSeq; NP_389051.1; NC_000964.3. DR PDB; 1TYG; X-ray; 3.15 A; A/C=3-255. DR PDB; 1XM3; X-ray; 1.80 A; A/B/C/D=1-255. DR PDBsum; 1TYG; -. DR PDBsum; 1XM3; -. DR ProteinModelPortal; O31618; -. DR SMR; O31618; 2-252. DR IntAct; O31618; 1. DR EnsemblBacteria; EBBACT00000002899; EBBACP00000002899; EBBACG00000002893. DR GeneID; 936422; -. DR GenomeReviews; AL009126_GR; BSU11690. DR KEGG; bsu:BSU11690; -. DR PATRIC; 18974055; VBIBacSub10457_1221. DR GenoList; BSU11690; -. DR eggNOG; COG2022; -. DR HOGENOM; HBG296821; -. DR KO; K03149; -. DR OMA; TAGCFTA; -. DR PhylomeDB; O31618; -. DR ProtClustDB; PRK00208; -. DR BioCyc; BSUB:BSU11690-MONOMER; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR HAMAP; MF_00443; ThiG; 1; -. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR008867; ThiG. DR Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1. DR Pfam; PF05690; ThiG; 1. DR SUPFAM; SSF110399; ThiG; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Reference proteome; KW Schiff base; Thiamine biosynthesis; Transferase. FT CHAIN 1 256 Thiazole synthase. FT /FTId=PRO_0000162788. FT REGION 185 186 DXP binding. FT REGION 207 208 DXP binding. FT ACT_SITE 98 98 Schiff-base intermediate with DXP. FT BINDING 159 159 DXP; via amide nitrogen. FT MUTAGEN 98 98 K->A: No activity; no imine formation FT with DXP. FT MUTAGEN 100 100 E->A: Activity reduced 38-fold. FT MUTAGEN 184 184 D->A: No activity. FT STRAND 4 6 FT STRAND 9 12 FT STRAND 15 18 FT HELIX 25 35 FT STRAND 38 43 FT HELIX 63 65 FT STRAND 66 71 FT HELIX 78 90 FT STRAND 95 99 FT TURN 105 107 FT HELIX 112 124 FT STRAND 129 133 FT HELIX 137 145 FT STRAND 151 153 FT STRAND 155 157 FT HELIX 167 176 FT STRAND 181 185 FT HELIX 190 198 FT STRAND 202 207 FT HELIX 208 211 FT STRAND 213 215 FT HELIX 216 236 SQ SEQUENCE 256 AA; 27022 MW; 39256F75262F97E6 CRC64; MSMLTIGGKS FQSRLLLGTG KYPSFDIQKE AVAVSESDIL TFAVRRMNIF EASQPNFLEQ LDLSKYTLLP NTAGASTAEE AVRIARLAKA SGLCDMIKVE VIGCSRSLLP DPVETLKASE QLLEEGFIVL PYTSDDVVLA RKLEELGVHA IMPGASPIGS GQGILNPLNL SFIIEQAKVP VIVDAGIGSP KDAAYAMELG ADGVLLNTAV SGADDPVKMA RAMKLAVEAG RLSYEAGRIP LKQYGTASSP GEGLPV // ID THIS_BACSU Reviewed; 66 AA. AC O31617; DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 22-FEB-2012, entry version 63. DE RecName: Full=Sulfur carrier protein ThiS; DE AltName: Full=Thiamine biosynthesis protein ThiS; GN Name=thiS; Synonyms=yjbS; OrderedLocusNames=BSU11680; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; 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 [2] RP CHARACTERIZATION. RC STRAIN=168 / CU1065; RX PubMed=14567704; DOI=10.1021/bi034902z; RA Park J.-H., Dorrestein P.C., Zhai H., Kinsland C., McLafferty F.W., RA Begley T.P.; RT "Biosynthesis of the thiazole moiety of thiamin pyrophosphate (vitamin RT B1)."; RL Biochemistry 42:12430-12438(2003). RN [3] RP FUNCTION IN SULFUR TRANSFER TO THIAZOLE. RX PubMed=15489164; DOI=10.1016/j.chembiol.2004.08.009; RA Dorrestein P.C., Zhai H., McLafferty F.W., Begley T.P.; RT "The biosynthesis of the thiazole phosphate moiety of thiamin: the RT sulfur transfer mediated by the sulfur carrier protein ThiS."; RL Chem. Biol. 11:1373-1381(2004). RN [4] RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) IN COMPLEX WITH THIG, AND RP SUBUNIT. RX PubMed=15362849; DOI=10.1021/bi0488911; RA Settembre E.C., Dorrestein P.C., Zhai H., Chatterjee A., RA McLafferty F.W., Begley T.P., Ealick S.E.; RT "Thiamin biosynthesis in Bacillus subtilis: structure of the thiazole RT synthase/sulfur carrier protein complex."; RL Biochemistry 43:11647-11657(2004). CC -!- FUNCTION: Is the sulfur donor in the synthesis of the thiazole CC phosphate moiety of thiamine phosphate. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC -!- SUBUNIT: Forms heterodimers with thiG. CC -!- PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first CC acyl-adenylated (-COAMP) by thiF, then thiocarboxylated (-COSH) by CC thiI (By similarity). CC -!- SIMILARITY: Belongs to the sulfur carrier protein ThiS family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL009126; CAB13025.1; -; Genomic_DNA. DR PIR; C69845; C69845. DR RefSeq; NP_389050.1; NC_000964.3. DR PDB; 1TYG; X-ray; 3.15 A; B/G=1-66. DR PDBsum; 1TYG; -. DR ProteinModelPortal; O31617; -. DR SMR; O31617; 1-65. DR IntAct; O31617; 1. DR EnsemblBacteria; EBBACT00000001881; EBBACP00000001881; EBBACG00000001878. DR GeneID; 939811; -. DR GenomeReviews; AL009126_GR; BSU11680. DR KEGG; bsu:BSU11680; -. DR PATRIC; 18974053; VBIBacSub10457_1220. DR GenoList; BSU11680; -. DR eggNOG; COG2104; -. DR HOGENOM; HBG656610; -. DR KO; K03154; -. DR OMA; RIIQKHE; -. DR ProtClustDB; CLSK887075; -. DR BioCyc; BSUB:BSU11680-MONOMER; -. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR012675; Beta-grasp_ferredoxin-type. DR InterPro; IPR016155; Mopterin_synth/thiamin_S_b. DR InterPro; IPR010035; Thi_S. DR InterPro; IPR003749; ThiS. DR Gene3D; G3DSA:3.10.20.30; Ferredoxin_fold; 1. DR Pfam; PF02597; ThiS; 1. DR SUPFAM; SSF54285; Mo_synth/thiamin_syn_S_b-grasp; 1. DR TIGRFAMs; TIGR01683; ThiS; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Nucleotide-binding; KW Reference proteome; Thiamine biosynthesis. FT CHAIN 1 66 Sulfur carrier protein ThiS. FT /FTId=PRO_0000391751. FT MOD_RES 66 66 1-thioglycine; alternate (By similarity). FT MOD_RES 66 66 Glycyl adenylate; alternate (By FT similarity). FT STRAND 2 4 FT STRAND 12 14 FT HELIX 18 24 FT STRAND 33 36 FT STRAND 39 41 FT TURN 44 48 FT STRAND 53 62 SQ SEQUENCE 66 AA; 7626 MW; 476D61DCC98BAADE CRC64; MLQLNGKDVK WKKDTGTIQD LLASYQLENK IVIVERNKEI IGKERYHEVE LCDRDVIEIV HFVGGG //