THIG_SULSY
ID THIG_SULSY Reviewed; 267 AA.
AC B2V959;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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};
GN OrderedLocusNames=SYO3AOP1_0852;
OS Sulfurihydrogenibium sp. (strain YO3AOP1).
OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae;
OC Sulfurihydrogenibium; unclassified Sulfurihydrogenibium.
OX NCBI_TaxID=436114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YO3AOP1;
RX PubMed=19136599; DOI=10.1128/jb.01645-08;
RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(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; CP001080; ACD66482.1; -; Genomic_DNA.
DR RefSeq; WP_012459556.1; NC_010730.1.
DR AlphaFoldDB; B2V959; -.
DR SMR; B2V959; -.
DR STRING; 436114.SYO3AOP1_0852; -.
DR EnsemblBacteria; ACD66482; ACD66482; SYO3AOP1_0852.
DR KEGG; sul:SYO3AOP1_0852; -.
DR eggNOG; COG2022; Bacteria.
DR HOGENOM; CLU_062233_1_0_0; -.
DR OMA; PHNFQLI; -.
DR OrthoDB; 784095at2; -.
DR UniPathway; UPA00060; -.
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..267
FT /note="Thiazole synthase"
FT /id="PRO_1000196908"
FT ACT_SITE 107
FT /note="Schiff-base intermediate with DXP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT BINDING 168
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT BINDING 194..195
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT BINDING 216..217
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
SQ SEQUENCE 267 AA; 28708 MW; 9490E1AE530B5DB5 CRC64;
MFDLEKFLEN DKLVIGGKEF KSRLIVGSGK YKDFQQTKEA TEASGAEMIT VAVRRVNITD
PNQDNLLNYI DTSKIMILPN TAGCYTAEEA ILTAKLAREA LGHGFVKLEV IGDQKTLYPD
MIETLKAAEI LVKEGFTVLP YITDDPVMAK RFEDIGCAAV MPLAAPIGSG LGLQNPYNIL
FIKEAVKIPV IVDAGIGTAS DAAIVMELGV DGVLMNTAIA QAKDPIKMAV AMKHAVIAGR
LAYLAGRIPK KMYASASSPM EGVIGRN