THIG_ERWAM
ID THIG_ERWAM Reviewed; 252 AA.
AC Q9F812; Q9F7Z7;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 86.
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};
OS Erwinia amylovora (Fire blight bacteria).
OG Plasmid pEA29.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=552;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2-95, and Ea88;
RX PubMed=11055941; DOI=10.1128/aem.66.11.4897-4907.2000;
RA McGhee G.C., Jones A.L.;
RT "Complete nucleotide sequence of ubiquitous plasmid pEA29 from Erwinia
RT amylovora strain Ea88: gene organization and intraspecies variation.";
RL Appl. Environ. Microbiol. 66:4897-4907(2000).
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; AF264948; AAG31045.1; -; Genomic_DNA.
DR EMBL; AF264950; AAG31740.1; -; Genomic_DNA.
DR RefSeq; NP_981994.1; NC_005706.1.
DR RefSeq; WP_009351653.1; NZ_RQKG01000022.1.
DR RefSeq; WP_011167228.1; NC_005706.1.
DR AlphaFoldDB; Q9F812; -.
DR SMR; Q9F812; -.
DR GeneID; 8893800; -.
DR OMA; PHNFQLI; -.
DR UniPathway; UPA00060; -.
DR PRO; PR:Q9F812; -.
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; Plasmid; Schiff base; Thiamine biosynthesis; Transferase.
FT CHAIN 1..252
FT /note="Thiazole synthase"
FT /id="PRO_0000162818"
FT ACT_SITE 91
FT /note="Schiff-base intermediate with DXP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT BINDING 152
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT BINDING 179..180
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
FT BINDING 201..202
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00443"
SQ SEQUENCE 252 AA; 27201 MW; FFE858A8D85F5A3D CRC64;
MFYDFVPQSR FLLGTAGYPS PQILQQAIEA SGSEIITVSL RREGSQGGAF RALLTQLNKR
VLPNTAGCHT VKEAVTTAYM ARELFNTRWI KLEVIGHADT LQPDPFALVE AARILCADGF
QVFPYTTEDL ILGEKLLEAG CKLLMPWGAP IGSGQGLRNI EGLRSMRSWF KDIPLIIDAG
IGAPSQAAQA MEMGFDGILL NTAVARAQDP LGMAQAFASA IRAGYDARSA GLIERRDMAT
ASTPIFGMAQ FS
