ID   THIG_BACCQ              Reviewed;         256 AA.
AC   B9J523;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 61.
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=BCQ_0823;
OS   Bacillus cereus (strain Q1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=361100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q1;
RX   PubMed=19060151; DOI=10.1128/jb.01629-08;
RA   Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA   Xue Y., Zhu Y., Jin Q.;
RT   "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT   with industrial applications.";
RL   J. Bacteriol. 191:1120-1121(2009).
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; CP000227; ACM11253.1; -; Genomic_DNA.
DR   RefSeq; WP_000931987.1; NC_011969.1.
DR   AlphaFoldDB; B9J523; -.
DR   SMR; B9J523; -.
DR   EnsemblBacteria; ACM11253; ACM11253; BCQ_0823.
DR   KEGG; bcq:BCQ_0823; -.
DR   HOGENOM; CLU_062233_1_0_9; -.
DR   OMA; PHNFQLI; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000000441; 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..256
FT                   /note="Thiazole synthase"
FT                   /id="PRO_1000196838"
FT   ACT_SITE        96
FT                   /note="Schiff-base intermediate with DXP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT   BINDING         157
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT   BINDING         183..184
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT   BINDING         205..206
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
SQ   SEQUENCE   256 AA;  27229 MW;  AD6EB081F2D3F57C CRC64;
     MLNIGPFSFH SRLLLGTGKF PDFDVQQKAI DVSEAEILTF AVRRMDIFDA KQPNLLERLD
     VKKYTLLPNT AGAKNAEEAV RIAKLAKASG LCDMIKVEVI GDDRTLLPDP VETLKASEML
     LEEGFIVLPY TSDDVVLARK LQELGVHAIM PGASPIGSGL GIVNPLNLSF IIEQATLPVI
     VDAGIGSPAD AAFAMELGAD GVLLNTAVSG AKDPIKMAQA MKLSIEAGRL GFEAGRIARK
     RCATASSPLE GMSVVE