GenomeNet

Database: UniProt
Entry: O31618
LinkDB: O31618
Original site: O31618 
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   02-JUN-2021, entry version 137.
DE   RecName: Full=Thiazole synthase;
DE            EC=2.8.1.10 {ECO:0000269|PubMed:14567704};
GN   Name=thiG; Synonyms=yjbT; OrderedLocusNames=BSU11690;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
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., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., 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., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., 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 sulfur
RT   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 SCHIFF
RP   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 B1):
RT   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: identification
RT   of the product of the thiazole synthase-catalyzed 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 ASP-184,
RP   SUBUNIT, AND REACTION MECHANISM.
RX   PubMed=15362849; DOI=10.1021/bi0488911;
RA   Settembre E.C., Dorrestein P.C., Zhai H., Chatterjee A., McLafferty F.W.,
RA   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-phosphate
CC       (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is
CC       provided by the thiocarboxylate moiety of the carrier protein ThiS. In
CC       vitro, sulfur can be provided by H(2)S. {ECO:0000269|PubMed:14567704}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + [sulfur-
CC         carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH = 2-[(2R,5Z)-2-
CC         carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-
CC         carrier protein ThiS]-C-terminal Gly-Gly + 2 H(+) + 2 H2O;
CC         Xref=Rhea:RHEA:26297, Rhea:RHEA-COMP:12908, Rhea:RHEA-COMP:12909,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57792,
CC         ChEBI:CHEBI:62899, ChEBI:CHEBI:77846, ChEBI:CHEBI:90619,
CC         ChEBI:CHEBI:90778; EC=2.8.1.10;
CC         Evidence={ECO:0000269|PubMed:14567704};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC   -!- SUBUNIT: Homotetramer. Forms heterodimers with either ThiH or ThiS.
CC       {ECO:0000269|PubMed:15362849}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ThiG family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL009126; CAB13026.1; -; Genomic_DNA.
DR   PIR; D69845; D69845.
DR   RefSeq; NP_389051.1; NC_000964.3.
DR   RefSeq; WP_010886483.1; NZ_JNCM01000035.1.
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   SMR; O31618; -.
DR   IntAct; O31618; 2.
DR   MINT; O31618; -.
DR   STRING; 224308.BSU11690; -.
DR   PaxDb; O31618; -.
DR   PRIDE; O31618; -.
DR   EnsemblBacteria; CAB13026; CAB13026; BSU_11690.
DR   GeneID; 936422; -.
DR   KEGG; bsu:BSU11690; -.
DR   eggNOG; COG2022; Bacteria.
DR   InParanoid; O31618; -.
DR   OMA; PHNFQLI; -.
DR   PhylomeDB; O31618; -.
DR   BioCyc; BSUB:BSU11690-MONOMER; -.
DR   BioCyc; MetaCyc:BSU11690-MONOMER; -.
DR   BRENDA; 2.8.1.10; 658.
DR   UniPathway; UPA00060; -.
DR   EvolutionaryTrace; O31618; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:1990107; F:thiazole synthase activity; IEA:RHEA.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04728; ThiG; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00443; ThiG; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR033983; Thiazole_synthase_ThiG.
DR   InterPro; IPR008867; ThiG.
DR   PANTHER; PTHR34266; PTHR34266; 1.
DR   Pfam; PF05690; ThiG; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Reference proteome; Schiff base;
KW   Thiamine biosynthesis; Transferase.
FT   CHAIN           1..256
FT                   /note="Thiazole synthase"
FT                   /id="PRO_0000162788"
FT   REGION          185..186
FT                   /note="DXP binding"
FT   REGION          207..208
FT                   /note="DXP binding"
FT   ACT_SITE        98
FT                   /note="Schiff-base intermediate with DXP"
FT   BINDING         159
FT                   /note="DXP; via amide nitrogen"
FT   MUTAGEN         98
FT                   /note="K->A: No activity; no imine formation with DXP."
FT                   /evidence="ECO:0000269|PubMed:15012138"
FT   MUTAGEN         100
FT                   /note="E->A: Activity reduced 38-fold."
FT                   /evidence="ECO:0000269|PubMed:15362849"
FT   MUTAGEN         184
FT                   /note="D->A: No activity."
FT                   /evidence="ECO:0000269|PubMed:15362849"
FT   STRAND          4..6
FT                   /evidence="ECO:0007829|PDB:1XM3"
FT   STRAND          9..12
FT                   /evidence="ECO:0007829|PDB:1XM3"
FT   STRAND          15..18
FT                   /evidence="ECO:0007829|PDB:1XM3"
FT   HELIX           25..35
FT                   /evidence="ECO:0007829|PDB:1XM3"
FT   STRAND          38..43
FT                   /evidence="ECO:0007829|PDB:1XM3"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:1TYG"
FT   HELIX           57..60
FT                   /evidence="ECO:0007829|PDB:1TYG"
FT   HELIX           63..65
FT                   /evidence="ECO:0007829|PDB:1XM3"
FT   STRAND          66..71
FT                   /evidence="ECO:0007829|PDB:1XM3"
FT   HELIX           78..90
FT                   /evidence="ECO:0007829|PDB:1XM3"
FT   STRAND          95..99
FT                   /evidence="ECO:0007829|PDB:1XM3"
FT   TURN            105..107
FT                   /evidence="ECO:0007829|PDB:1XM3"
FT   HELIX           112..124
FT                   /evidence="ECO:0007829|PDB:1XM3"
FT   STRAND          129..133
FT                   /evidence="ECO:0007829|PDB:1XM3"
FT   HELIX           137..145
FT                   /evidence="ECO:0007829|PDB:1XM3"
FT   STRAND          151..153
FT                   /evidence="ECO:0007829|PDB:1XM3"
FT   STRAND          155..157
FT                   /evidence="ECO:0007829|PDB:1XM3"
FT   HELIX           167..176
FT                   /evidence="ECO:0007829|PDB:1XM3"
FT   STRAND          181..185
FT                   /evidence="ECO:0007829|PDB:1XM3"
FT   HELIX           190..198
FT                   /evidence="ECO:0007829|PDB:1XM3"
FT   STRAND          202..207
FT                   /evidence="ECO:0007829|PDB:1XM3"
FT   HELIX           208..211
FT                   /evidence="ECO:0007829|PDB:1XM3"
FT   STRAND          213..215
FT                   /evidence="ECO:0007829|PDB:1XM3"
FT   HELIX           216..236
FT                   /evidence="ECO:0007829|PDB:1XM3"
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
//
DBGET integrated database retrieval system