SWISSPROT: A0KFF0_AERHH

ID   A0KFF0_AERHH            Unreviewed;       260 AA.
AC   A0KFF0;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 86.
DE   RecName: Full=Thiazole synthase {ECO:0000256|HAMAP-Rule:MF_00443, ECO:0000256|SAAS:SAAS00958550};
DE            EC=2.8.1.10 {ECO:0000256|HAMAP-Rule:MF_00443, ECO:0000256|SAAS:SAAS00958549};
GN   Name=thiG {ECO:0000256|HAMAP-Rule:MF_00443,
GN   ECO:0000313|EMBL:ABK38057.1};
GN   OrderedLocusNames=AHA_0443 {ECO:0000313|EMBL:ABK38057.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK38057.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK38057.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- FUNCTION: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-
CC       phosphate (DXP) to produce the thiazole phosphate moiety of
CC       thiamine. Sulfur is provided by the thiocarboxylate moiety of the
CC       carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
CC       {ECO:0000256|HAMAP-Rule:MF_00443, ECO:0000256|SAAS:SAAS00958548}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate +
CC         [sulfur-carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH = 2-
CC         [(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate
CC         + [sulfur-carrier protein ThiS]-C-terminal Gly-Gly + 2 H(+) + 2
CC         H2O; Xref=Rhea:RHEA:26297, Rhea:RHEA-COMP:12908, Rhea:RHEA-
CC         COMP:12909, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57792, ChEBI:CHEBI:62899, ChEBI:CHEBI:77846,
CC         ChEBI:CHEBI:90619, ChEBI:CHEBI:90778; EC=2.8.1.10;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00443,
CC         ECO:0000256|SAAS:SAAS01116553};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00443, ECO:0000256|SAAS:SAAS00958556}.
CC   -!- SUBUNIT: Homotetramer. Forms heterodimers with either ThiH or
CC       ThiS. {ECO:0000256|HAMAP-Rule:MF_00443,
CC       ECO:0000256|SAAS:SAAS00958543}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00443,
CC       ECO:0000256|SAAS:SAAS00963437}.
CC   -!- SIMILARITY: Belongs to the ThiG family. {ECO:0000256|HAMAP-
CC       Rule:MF_00443, ECO:0000256|SAAS:SAAS00958557}.
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DR   EMBL; CP000462; ABK38057.1; -; Genomic_DNA.
DR   RefSeq; YP_854972.2; NC_008570.1.
DR   SMR; A0KFF0; -.
DR   STRING; 380703.AHA_0443; -.
DR   EnsemblBacteria; ABK38057; ABK38057; AHA_0443.
DR   GeneID; 4490406; -.
DR   KEGG; aha:AHA_0443; -.
DR   PATRIC; fig|380703.7.peg.433; -.
DR   eggNOG; ENOG4105CA8; Bacteria.
DR   eggNOG; COG2022; LUCA.
DR   HOGENOM; HOG000248049; -.
DR   KO; K03149; -.
DR   OMA; AQYPSPA; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016783; F:sulfurtransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
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;
DR   PRODOM; A0KFF0.
DR   SWISS-2DPAGE; A0KFF0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00443,
KW   ECO:0000256|SAAS:SAAS00963440};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW   Schiff base {ECO:0000256|HAMAP-Rule:MF_00443,
KW   ECO:0000256|SAAS:SAAS00664421};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00443,
KW   ECO:0000256|SAAS:SAAS00958544};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00443,
KW   ECO:0000256|SAAS:SAAS00958551}.
FT   DOMAIN        8    252       ThiG. {ECO:0000259|Pfam:PF05690}.
FT   REGION      187    188       DXP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00443}.
FT   REGION      209    210       DXP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00443}.
FT   ACT_SITE    100    100       Schiff-base intermediate with DXP.
FT                                {ECO:0000256|HAMAP-Rule:MF_00443}.
FT   BINDING     161    161       DXP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00443}.
SQ   SEQUENCE   260 AA;  26901 MW;  BACB5C1480369A83 CRC64;
     MPEADMLKIA DHTFSSRLFT GTGKFARPAL MAAAIEASGS QLVTMAIKRL EPGKAHDDIL
     SPLLQLGVKL LPNTSGAKTA AEAVFAAHLA REALGTNWLK LEIHPDPRYL LPDPIETLKA
     AEQLVKEGFV VLPYCGADPV LCKRLEEVGC AAVMPLGAPI GSNQGLVTRE FLSIIVEQAN
     VPVVVDAGIG APSHAAAAFE LGADAVLVNT AIAVSGDPIA MGRAFALACT AGRSAYEAGL
     GARAQQAQAS SPLTDFLGAL
//