ID   THIG_ANASK              Reviewed;         257 AA.
AC   B4UIG2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=AnaeK_1335;
OS   Anaeromyxobacter sp. (strain K).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter;
OC   unclassified Anaeromyxobacter.
OX   NCBI_TaxID=447217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikiva G.,
RA   Beliaev A.;
RT   "Complete sequence of Anaeromyxobacter sp. K.";
RL   Submitted (AUG-2008) 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}.
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; CP001131; ACG72567.1; -; Genomic_DNA.
DR   RefSeq; WP_012525390.1; NC_011145.1.
DR   AlphaFoldDB; B4UIG2; -.
DR   SMR; B4UIG2; -.
DR   EnsemblBacteria; ACG72567; ACG72567; AnaeK_1335.
DR   KEGG; ank:AnaeK_1335; -.
DR   HOGENOM; CLU_062233_1_0_7; -.
DR   OMA; PHNFQLI; -.
DR   OrthoDB; 784095at2; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000001871; 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   3: Inferred from homology;
KW   Cytoplasm; Schiff base; Thiamine biosynthesis; Transferase.
FT   CHAIN           1..257
FT                   /note="Thiazole synthase"
FT                   /id="PRO_1000124597"
FT   ACT_SITE        98
FT                   /note="Schiff-base intermediate with DXP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT   BINDING         159
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT   BINDING         185..186
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT   BINDING         207..208
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
SQ   SEQUENCE   257 AA;  26926 MW;  BBCC9A1B97D6BB6F CRC64;
     MADTWSIGAH AFTSRLLVGT GKYPDFPTMQ RALAASGAEV VTVAVRRLDL SKKGEESLLA
     WIPKGMKLLP NTAACFTAEE AIRTARLGRE LEMGDLVKLE VIGDRRTLFP DVEGLIQAAK
     VLVKEGFTVL PYTNDDPVTA KKLEDAGCAA VMPLGAPIGS GLGLRNPYNL RIIMETVQVP
     VLVDAGVGTA SDAALAMELG AVAVLMNTAI AEAKDPVLMA EAMRAGVEGG RKAFLAGRIP
     MKLHAAASSP MSGLIGS