ID   THIG_ECOLI              Reviewed;         256 AA.
AC   P30139; P76779; Q2M8S7;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 3.
DT   04-NOV-2026, entry version 186.
DE   RecName: Full=Thiazole synthase;
DE            EC=2.8.1.10;
GN   Name=thiG; OrderedLocusNames=b3991, JW5549;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=8432721; DOI=10.1128/jb.175.4.982-992.1993;
RA   Vander Horn P.B., Backstrom A.D., Stewart V., Begley T.P.;
RT   "Structural genes for thiamine biosynthetic enzymes (thiCEFGH) in
RT   Escherichia coli K-12.";
RL   J. Bacteriol. 175:982-992(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA   Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT   "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT   from 89.2 to 92.8 minutes.";
RL   Nucleic Acids Res. 21:5408-5417(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   PROTEIN SEQUENCE OF 1-7, FUNCTION, MASS SPECTROMETRY, SUBUNIT, AND
RP   INTERACTION WITH THIH.
RX   PubMed=12650933; DOI=10.1016/s0014-5793(03)00204-7;
RA   Leonardi R., Fairhurst S.A., Kriek M., Lowe D.J., Roach P.L.;
RT   "Thiamine biosynthesis in Escherichia coli: isolation and initial
RT   characterisation of the ThiGH complex.";
RL   FEBS Lett. 539:95-99(2003).
RN   [6]
RP   MASS SPECTROMETRY.
RX   PubMed=10082377; DOI=10.1002/pro.5560070815;
RA   Kelleher N.L., Taylor S.V., Grannis D., Kinsland C., Chiu H.-J.,
RA   Begley T.P., McLafferty F.W.;
RT   "Efficient sequence analysis of the six gene products (7-74 kDa) from the
RT   Escherichia coli thiamin biosynthetic operon by tandem high-resolution mass
RT   spectrometry.";
RL   Protein Sci. 7:1796-1801(1998).
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:12650933}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[ThiS sulfur-carrier protein]-C-terminal-Gly-
CC         aminoethanethioate + 2-iminoacetate + 1-deoxy-D-xylulose 5-phosphate
CC         = [ThiS sulfur-carrier protein]-C-terminal Gly-Gly + 2-[(2R,5Z)-2-
CC         carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 2 H2O + H(+);
CC         Xref=Rhea:RHEA:26297, Rhea:RHEA-COMP:12909, Rhea:RHEA-COMP:19908,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57792,
CC         ChEBI:CHEBI:62899, ChEBI:CHEBI:77846, ChEBI:CHEBI:90778,
CC         ChEBI:CHEBI:232372; EC=2.8.1.10;
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC   -!- SUBUNIT: Homotetramer. Forms heterodimers with either ThiH or ThiS.
CC       {ECO:0000269|PubMed:12650933}.
CC   -!- INTERACTION:
CC       P30139; P0A6R3: fis; NbExp=3; IntAct=EBI-547059, EBI-550170;
CC       P30139; P30140: thiH; NbExp=2; IntAct=EBI-547059, EBI-1125553;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MASS SPECTROMETRY: Mass=26893.3; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:12650933};
CC   -!- MASS SPECTROMETRY: Mass=26896.5; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10082377};
CC   -!- SIMILARITY: Belongs to the ThiG family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC43089.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M88701; AAB95621.1; -; Genomic_DNA.
DR   EMBL; U00006; AAC43089.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC76965.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77329.1; -; Genomic_DNA.
DR   PIR; B65206; B65206.
DR   RefSeq; NP_418418.2; NC_000913.3.
DR   RefSeq; WP_000944104.1; NZ_CP009789.1.
DR   SMR; P30139; -.
DR   BioGRID; 4262656; 19.
DR   ComplexPortal; CPX-2135; thiG-thiH thiazole phosphate synthase complex.
DR   DIP; DIP-6868N; -.
DR   IntAct; P30139; 10.
DR   STRING; 511145.b3991; -.
DR   PaxDb; 511145-b3991; -.
DR   EnsemblBacteria; AAC76965; AAC76965; b3991.
DR   GeneID; 948493; -.
DR   KEGG; ecj:JW5549; -.
DR   KEGG; eco:b3991; -.
DR   KEGG; ecoc:C3026_21555; -.
DR   PATRIC; fig|1411691.4.peg.2721; -.
DR   EchoBASE; EB1547; -.
DR   eggNOG; COG2022; Bacteria.
DR   HOGENOM; CLU_062233_1_0_6; -.
DR   InParanoid; P30139; -.
DR   OMA; AACIMPL; -.
DR   OrthoDB; 9805935at2; -.
DR   PhylomeDB; P30139; -.
DR   BioCyc; EcoCyc:THIG-MONOMER; -.
DR   BioCyc; MetaCyc:THIG-MONOMER; -.
DR   BRENDA; 2.8.1.10; 2026.
DR   UniPathway; UPA00060; -.
DR   PRO; PR:P30139; -.
DR   CDD; cd04728; ThiG; 1.
DR   FunFam; 3.20.20.70:FF:000049; Thiazole synthase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 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; THIAZOLE SYNTHASE; 1.
DR   PANTHER; PTHR34266:SF2; THIAZOLE SYNTHASE; 1.
DR   Pfam; PF05690; ThiG; 1.
DR   SUPFAM; SSF110399; ThiG-like; 1.
DR   GO; GO:1902508; C:2-iminoacetate synthase complex; IPI:ComplexPortal.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:1990107; F:thiazole synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IMP:EcoCyc.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IDA:ComplexPortal.
DR   Proteomes; UP000000625; Chromosome.
DR   AlphaFoldDB; P30139; -.
DR   FunCoup; P30139; 482.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Reference proteome; Schiff base;
KW   Thiamine biosynthesis; Transferase.
FT   CHAIN           1..256
FT                   /note="Thiazole synthase"
FT                   /id="PRO_0000162815"
FT   ACT_SITE        95
FT                   /note="Schiff-base intermediate with DXP"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000250"
FT   BINDING         182..183
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000250"
FT   BINDING         204..205
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   256 AA;  26896 MW;  8B0BDEE617104E38 CRC64;
     MLRIADKTFD SHLFTGTGKF ASSQLMVEAI RASGSQLVTL AMKRVDLRQH NDAILEPLIA
     AGVTLLPNTS GAKTAEEAIF AAHLAREALG TNWLKLEIHP DARWLLPDPI ETLKAAETLV
     QQGFVVLPYC GADPVLCKRL EEVGCAAVMP LGAPIGSNQG LETRAMLEII IQQATVPVVV
     DAGIGVPSHA AQALEMGADA VLVNTAIAVA DDPVNMAKAF RLAVEAGLLA RQSGPGSRSY
     FAHATSPLTG FLEASA
//