THIG_ERWPE
ID THIG_ERWPE Reviewed; 252 AA.
AC Q8GEI4; C8ZLR4;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 106.
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=EpC_pEp360130;
OS Erwinia pyrifoliae (strain DSM 12162 / Ep1/96).
OG Plasmid pEP36.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634499;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 12162 / Ep1/96;
RX PubMed=12450843; DOI=10.1128/aem.68.12.6182-6192.2002;
RA McGhee G.C., Schnabel E.L., Maxson-Stein K., Jones B., Stromberg V.K.,
RA Lacy G.H., Jones A.L.;
RT "Relatedness of chromosomal and plasmid DNAs of Erwinia pyrifoliae and
RT Erwinia amylovora.";
RL Appl. Environ. Microbiol. 68:6182-6192(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12162 / Ep1/96;
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(2010).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN04534.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY123045; AAN04534.1; ALT_INIT; Genomic_DNA.
DR EMBL; FP236829; CAX53415.1; -; Genomic_DNA.
DR RefSeq; NP_758746.1; NC_004445.1.
DR RefSeq; WP_012814638.1; NC_013263.1.
DR AlphaFoldDB; Q8GEI4; -.
DR SMR; Q8GEI4; -.
DR KEGG; epy:EpC_pEp360130; -.
DR HOGENOM; CLU_062233_1_0_6; -.
DR OMA; PHNFQLI; -.
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; Plasmid; Schiff base; Thiamine biosynthesis; Transferase.
FT CHAIN 1..252
FT /note="Thiazole synthase"
FT /id="PRO_0000162820"
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; 27355 MW; 561772A042A9DCDB CRC64;
MFYDFVPQSR FLLGTAGYPS PQILQQAVMA SESEIITVSL RREGSQGGAF RELLTQLNKR
ILPNTAGCHT VKEAVTTAHM ARELFNTRWI KLEVIGHADT LQPDPFALVE AARILCADGF
QVFPYTTEDL ILGEKLLEAG CELLMPWGAP IGSGQGLRNI EGLRSMRLWF KDIPLIIDAG
IGAPSQAAQA MEMGFDGILL NTAVARAQDP LRMAQAFAAA VRAGYDAHGA GLIERRDMAT
ASTPIFGMAQ FS
