ID   THIG_CAMJ8              Reviewed;         258 AA.
AC   A8FM94;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Thiazole synthase {ECO:0000255|HAMAP-Rule:MF_00443};
DE            EC=2.8.1.10 {ECO:0000255|HAMAP-Rule:MF_00443};
GN   Name=thiG {ECO:0000255|HAMAP-Rule:MF_00443}; OrderedLocusNames=C8J_0982;
OS   Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC
OS   11828).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=407148;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81116 / NCTC 11828;
RX   PubMed=17873037; DOI=10.1128/jb.01404-07;
RA   Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M.,
RA   van Vliet A.H.M.;
RT   "The complete genome sequence of Campylobacter jejuni strain 81116
RT   (NCTC11828).";
RL   J. Bacteriol. 189:8402-8403(2007).
CC   -!- FUNCTION: 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:0000255|HAMAP-
CC       Rule:MF_00443}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00443};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00443}.
CC   -!- SUBUNIT: Homotetramer. Forms heterodimers with either ThiH or ThiS.
CC       {ECO:0000255|HAMAP-Rule:MF_00443}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00443}.
CC   -!- SIMILARITY: Belongs to the ThiG family. {ECO:0000255|HAMAP-
CC       Rule:MF_00443}.
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DR   EMBL; CP000814; ABV52581.1; -; Genomic_DNA.
DR   RefSeq; WP_002866076.1; NC_009839.1.
DR   AlphaFoldDB; A8FM94; -.
DR   SMR; A8FM94; -.
DR   KEGG; cju:C8J_0982; -.
DR   HOGENOM; CLU_062233_1_0_7; -.
DR   OMA; PHNFQLI; -.
DR   UniPathway; UPA00060; -.
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   3: Inferred from homology;
KW   Cytoplasm; Schiff base; Thiamine biosynthesis; Transferase.
FT   CHAIN           1..258
FT                   /note="Thiazole synthase"
FT                   /id="PRO_1000124608"
FT   ACT_SITE        100
FT                   /note="Schiff-base intermediate with DXP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT   BINDING         161
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT   BINDING         187..188
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT   BINDING         209..210
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
SQ   SEQUENCE   258 AA;  27620 MW;  41DB27C676E64D36 CRC64;
     MQENLKNDKL KIGKYEFDSR FILGSGKYSL ELIKSAIEEA KTQIITLALR RANTGEIANI
     LDYIPKNITL LPNTSGARNA DEALRIARLS RELGCGELIK IEVISDSRYL LPDNYETIKA
     CELLAKEGFT PLPYMHADLY AARAMRDAGA AAIMPLAAPI GSNKGLCAKE FIQILLNEID
     LPIIVDAGIG SPSQACEAMQ MGVSAVMVNT AIAEAKDVAL MAKAFSLAVN AGRAAFLAGL
     ASVSKAKASS PLTGFLRD