THIG_PELUB
ID THIG_PELUB Reviewed; 257 AA.
AC Q4FMP0;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=SAR11_0730;
OS Pelagibacter ubique (strain HTCC1062).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Pelagibacterales;
OC Pelagibacteraceae; Candidatus Pelagibacter.
OX NCBI_TaxID=335992;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC1062;
RX PubMed=16109880; DOI=10.1126/science.1114057;
RA Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D.,
RA Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M.,
RA Carrington J.C., Mathur E.J.;
RT "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL Science 309:1242-1245(2005).
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; CP000084; AAZ21549.1; -; Genomic_DNA.
DR RefSeq; WP_006997183.1; NC_007205.1.
DR AlphaFoldDB; Q4FMP0; -.
DR SMR; Q4FMP0; -.
DR STRING; 335992.SAR11_0730; -.
DR EnsemblBacteria; AAZ21549; AAZ21549; SAR11_0730.
DR GeneID; 66295233; -.
DR KEGG; pub:SAR11_0730; -.
DR eggNOG; COG2022; Bacteria.
DR HOGENOM; CLU_062233_1_0_5; -.
DR OMA; PHNFQLI; -.
DR OrthoDB; 784095at2; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000002528; 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; Reference proteome; Schiff base; Thiamine biosynthesis;
KW Transferase.
FT CHAIN 1..257
FT /note="Thiazole synthase"
FT /id="PRO_0000236350"
FT ACT_SITE 100
FT /note="Schiff-base intermediate with DXP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT BINDING 161
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT BINDING 187..188
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT BINDING 209..210
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; 27819 MW; A17924AC64B2FE34 CRC64;
MVNDKLIIDK KKFNSRLIVG TGKYKSMAEC AKAIKLSGAE IVTVAVRRVN ISDKKKPLLM
DYIDPKKITY LPNTAGCFNS EEALRTLRLA REIGGWKLVK LEVLGDKKNL FPDMIETLKS
TEVLTREGFR VMVYCNDDPL MAKRLENVGA CAIMPLAAPI GSGLGIQNTT NIKIIRSQTK
LPLIIDAGLG QASDAAIAME LGCDGVLANT AIAKAKKPFQ MALAFKNGVI AGRQSYLAGR
IEKSIYGSAS SPKTGII
