ID   THIG_NEIMF              Reviewed;         262 AA.
AC   A1KWF0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=NMC2052;
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS   15464 / FAM18).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=272831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA   Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA   Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA   Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(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; AM421808; CAM11207.1; -; Genomic_DNA.
DR   RefSeq; WP_002221723.1; NC_008767.1.
DR   AlphaFoldDB; A1KWF0; -.
DR   SMR; A1KWF0; -.
DR   EnsemblBacteria; CAM11207; CAM11207; NMC2052.
DR   KEGG; nmc:NMC2052; -.
DR   HOGENOM; CLU_062233_1_0_4; -.
DR   OMA; PHNFQLI; -.
DR   OrthoDB; 784095at2; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000002286; 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..262
FT                   /note="Thiazole synthase"
FT                   /id="PRO_1000026017"
FT   REGION          243..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        97
FT                   /note="Schiff-base intermediate with DXP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT   BINDING         158
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   262 AA;  28067 MW;  15DD6603380324A9 CRC64;
     MLTLYGETFP SRLLLGTAAY PTPEILKQSI QTAQPAMITV SLRRAGSGGE AHGQGFWSLL
     QETGVPVLPN TAGCQSVQEA VTTAQMAREV FETDWIKLEL IGDDDTLQPD VFQLVEAAEI
     LIKDGFKVLP YCTEDLIACR RLLDAGCQAL MPWAAPIGTG LGAVHAYALN VLRERLPDTP
     LIIDAGLGLP SQAAQVMEWG FDGVLLNTAV SRSGDPVNMA RAFALAVESG RLAFEAGPVE
     ARDKAQASTP TVGQPFWHSA EY