ID   THIG_VIBA3              Reviewed;         254 AA.
AC   B7VMV3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
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=VS_3094;
OS   Vibrio atlanticus (strain LGP32) (Vibrio splendidus (strain Mel32)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=575788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LGP32;
RA   Mazel D., Le Roux F.;
RT   "Vibrio splendidus str. LGP32 complete genome.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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; FM954972; CAV20361.1; -; Genomic_DNA.
DR   RefSeq; WP_012605073.1; NC_011753.2.
DR   AlphaFoldDB; B7VMV3; -.
DR   SMR; B7VMV3; -.
DR   STRING; 575788.VS_3094; -.
DR   EnsemblBacteria; CAV20361; CAV20361; VS_3094.
DR   KEGG; vsp:VS_3094; -.
DR   PATRIC; fig|575788.5.peg.4270; -.
DR   eggNOG; COG2022; Bacteria.
DR   HOGENOM; CLU_062233_1_0_6; -.
DR   OMA; PHNFQLI; -.
DR   OrthoDB; 784095at2; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000009100; Chromosome 1.
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; Reference proteome; Schiff base; Thiamine biosynthesis;
KW   Transferase.
FT   CHAIN           1..254
FT                   /note="Thiazole synthase"
FT                   /id="PRO_1000196913"
FT   ACT_SITE        95
FT                   /note="Schiff-base intermediate with DXP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT   BINDING         156
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT   BINDING         182..183
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT   BINDING         204..205
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
SQ   SEQUENCE   254 AA;  26695 MW;  2CDE6FBFE7A07251 CRC64;
     MLTIADKTFQ SRLFTGTGKF ANKHLMASAI EASGSQLATM ALKRVDIRSE QDDILQPIID
     AGVNLLPNTS GAKNAKDAIF AAHLAREALG TNWLKLEIHP DPKYLMPDPI ETLKAAEQLV
     KDGFVVLPYC HADPVLCKRL EEVGCAAVMP LGAPIGSNKG IASADFLEII IDQANVPVIV
     DAGIGAPSHA ARAMEMGADA VLVNTAIAAS QQPVEMAIAF KLAVEAGRMA YLAGLAGKVS
     HAVASSPLTS FLDE