THIG_ECOLI
ID THIG_ECOLI Reviewed; 256 AA.
AC P30139; P76779; Q2M8S7;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Thiazole synthase;
DE EC=2.8.1.10;
GN Name=thiG; OrderedLocusNames=b3991, JW5549;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8432721; DOI=10.1128/jb.175.4.982-992.1993;
RA Vander Horn P.B., Backstrom A.D., Stewart V., Begley T.P.;
RT "Structural genes for thiamine biosynthetic enzymes (thiCEFGH) in
RT Escherichia coli K-12.";
RL J. Bacteriol. 175:982-992(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-7, FUNCTION, MASS SPECTROMETRY, SUBUNIT, AND
RP INTERACTION WITH THIH.
RX PubMed=12650933; DOI=10.1016/s0014-5793(03)00204-7;
RA Leonardi R., Fairhurst S.A., Kriek M., Lowe D.J., Roach P.L.;
RT "Thiamine biosynthesis in Escherichia coli: isolation and initial
RT characterisation of the ThiGH complex.";
RL FEBS Lett. 539:95-99(2003).
RN [6]
RP MASS SPECTROMETRY.
RX PubMed=10082377; DOI=10.1002/pro.5560070815;
RA Kelleher N.L., Taylor S.V., Grannis D., Kinsland C., Chiu H.-J.,
RA Begley T.P., McLafferty F.W.;
RT "Efficient sequence analysis of the six gene products (7-74 kDa) from the
RT Escherichia coli thiamin biosynthetic operon by tandem high-resolution mass
RT spectrometry.";
RL Protein Sci. 7:1796-1801(1998).
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:0000269|PubMed:12650933}.
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;
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC -!- SUBUNIT: Homotetramer. Forms heterodimers with either ThiH or ThiS.
CC {ECO:0000269|PubMed:12650933}.
CC -!- INTERACTION:
CC P30139; P0A6R3: fis; NbExp=3; IntAct=EBI-547059, EBI-550170;
CC P30139; P30140: thiH; NbExp=2; IntAct=EBI-547059, EBI-1125553;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MASS SPECTROMETRY: Mass=26893.3; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12650933};
CC -!- MASS SPECTROMETRY: Mass=26896.5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10082377};
CC -!- SIMILARITY: Belongs to the ThiG family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC43089.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M88701; AAB95621.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43089.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76965.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77329.1; -; Genomic_DNA.
DR PIR; B65206; B65206.
DR RefSeq; NP_418418.2; NC_000913.3.
DR RefSeq; WP_000944104.1; NZ_SSZK01000047.1.
DR AlphaFoldDB; P30139; -.
DR SMR; P30139; -.
DR BioGRID; 4262656; 16.
DR ComplexPortal; CPX-2135; thiG-thiH thiazole phosphate synthase complex.
DR DIP; DIP-6868N; -.
DR IntAct; P30139; 10.
DR STRING; 511145.b3991; -.
DR PaxDb; P30139; -.
DR PRIDE; P30139; -.
DR EnsemblBacteria; AAC76965; AAC76965; b3991.
DR EnsemblBacteria; BAE77329; BAE77329; BAE77329.
DR GeneID; 948493; -.
DR KEGG; ecj:JW5549; -.
DR KEGG; eco:b3991; -.
DR PATRIC; fig|1411691.4.peg.2721; -.
DR EchoBASE; EB1547; -.
DR eggNOG; COG2022; Bacteria.
DR HOGENOM; CLU_062233_1_0_6; -.
DR InParanoid; P30139; -.
DR OMA; PHNFQLI; -.
DR PhylomeDB; P30139; -.
DR BioCyc; EcoCyc:THIG-MON; -.
DR BioCyc; MetaCyc:THIG-MON; -.
DR BRENDA; 2.8.1.10; 2026.
DR UniPathway; UPA00060; -.
DR PRO; PR:P30139; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1902508; C:2-iminoacetate synthase complex; IPI:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1990107; F:thiazole synthase activity; IEA:RHEA.
DR GO; GO:0009228; P:thiamine biosynthetic process; IMP:EcoCyc.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Reference proteome; Schiff base;
KW Thiamine biosynthesis; Transferase.
FT CHAIN 1..256
FT /note="Thiazole synthase"
FT /id="PRO_0000162815"
FT ACT_SITE 95
FT /note="Schiff-base intermediate with DXP"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000250"
FT BINDING 182..183
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000250"
FT BINDING 204..205
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000250"
SQ SEQUENCE 256 AA; 26896 MW; 8B0BDEE617104E38 CRC64;
MLRIADKTFD SHLFTGTGKF ASSQLMVEAI RASGSQLVTL AMKRVDLRQH NDAILEPLIA
AGVTLLPNTS GAKTAEEAIF AAHLAREALG TNWLKLEIHP DARWLLPDPI ETLKAAETLV
QQGFVVLPYC GADPVLCKRL EEVGCAAVMP LGAPIGSNQG LETRAMLEII IQQATVPVVV
DAGIGVPSHA AQALEMGADA VLVNTAIAVA DDPVNMAKAF RLAVEAGLLA RQSGPGSRSY
FAHATSPLTG FLEASA
