THIE_ECOLI
ID THIE_ECOLI Reviewed; 211 AA.
AC P30137; Q2M8T0;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Thiamine-phosphate synthase;
DE Short=TP synthase;
DE Short=TPS;
DE EC=2.5.1.3 {ECO:0000269|Ref.5};
DE AltName: Full=Thiamine-phosphate pyrophosphorylase;
DE Short=TMP pyrophosphorylase;
DE Short=TMP-PPase;
GN Name=thiE; OrderedLocusNames=b3993, JW3957;
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 FUNCTION, CATALYTIC ACTIVITY, AND KINETIC PARAMETERS.
RA Backstrom A.D., Austin R., McMordie S., Begley T.P.;
RT "Biosynthesis of thiamin I: the function of the thiE gene product.";
RL J. Am. Chem. Soc. 117:2351-2352(1995).
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).
RN [7]
RP FUNCTION IN THIAMINE METABOLISM.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15292217; DOI=10.1074/jbc.m404284200;
RA Lawhorn B.G., Gerdes S.Y., Begley T.P.;
RT "A genetic screen for the identification of thiamin metabolic genes.";
RL J. Biol. Chem. 279:43555-43559(2004).
CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole
CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine
CC pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
CC {ECO:0000269|PubMed:15292217, ECO:0000269|Ref.5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl
CC phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2
CC H(+) = CO2 + diphosphate + thiamine phosphate; Xref=Rhea:RHEA:47844,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, ChEBI:CHEBI:62899; EC=2.5.1.3;
CC Evidence={ECO:0000269|Ref.5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-
CC methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate
CC + thiamine phosphate; Xref=Rhea:RHEA:47848, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, ChEBI:CHEBI:37575,
CC ChEBI:CHEBI:57841, ChEBI:CHEBI:62890; EC=2.5.1.3;
CC Evidence={ECO:0000269|Ref.5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 4-methyl-
CC 5-(2-phosphooxyethyl)-thiazole + H(+) = diphosphate + thiamine
CC phosphate; Xref=Rhea:RHEA:22328, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, ChEBI:CHEBI:57841,
CC ChEBI:CHEBI:58296; EC=2.5.1.3; Evidence={ECO:0000269|Ref.5};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 uM for HMP-PP {ECO:0000269|Ref.5};
CC KM=2 uM for THZ-P {ECO:0000269|Ref.5};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine
CC and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
CC -!- MASS SPECTROMETRY: Mass=23014.8; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10082377};
CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family.
CC {ECO:0000305}.
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DR EMBL; M88701; AAB95617.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43091.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76967.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77326.1; -; Genomic_DNA.
DR PIR; S35118; S35118.
DR RefSeq; NP_418421.1; NC_000913.3.
DR RefSeq; WP_000284615.1; NZ_SSZK01000047.1.
DR AlphaFoldDB; P30137; -.
DR SMR; P30137; -.
DR BioGRID; 4259333; 19.
DR DIP; DIP-10983N; -.
DR IntAct; P30137; 4.
DR STRING; 511145.b3993; -.
DR SWISS-2DPAGE; P30137; -.
DR PaxDb; P30137; -.
DR PRIDE; P30137; -.
DR EnsemblBacteria; AAC76967; AAC76967; b3993.
DR EnsemblBacteria; BAE77326; BAE77326; BAE77326.
DR GeneID; 58463415; -.
DR GeneID; 948491; -.
DR KEGG; ecj:JW3957; -.
DR KEGG; eco:b3993; -.
DR PATRIC; fig|1411691.4.peg.2718; -.
DR EchoBASE; EB1545; -.
DR eggNOG; COG0352; Bacteria.
DR HOGENOM; CLU_018272_3_3_6; -.
DR InParanoid; P30137; -.
DR OMA; ITAFQFR; -.
DR PhylomeDB; P30137; -.
DR BioCyc; EcoCyc:THIE-MON; -.
DR BioCyc; MetaCyc:THIE-MON; -.
DR SABIO-RK; P30137; -.
DR UniPathway; UPA00060; UER00141.
DR PRO; PR:P30137; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IDA:EcoCyc.
DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IBA:GO_Central.
DR GO; GO:0009228; P:thiamine biosynthetic process; IDA:EcoCyc.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00564; TMP_TenI; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00097; TMP_synthase; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036206; ThiamineP_synth_sf.
DR InterPro; IPR022998; ThiamineP_synth_TenI.
DR InterPro; IPR034291; TMP_synthase.
DR Pfam; PF02581; TMP-TENI; 1.
DR SUPFAM; SSF51391; SSF51391; 1.
DR TIGRFAMs; TIGR00693; thiE; 1.
PE 1: Evidence at protein level;
KW Magnesium; Metal-binding; Reference proteome; Thiamine biosynthesis;
KW Transferase.
FT CHAIN 1..211
FT /note="Thiamine-phosphate synthase"
FT /id="PRO_0000157010"
FT BINDING 37..41
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000250"
FT BINDING 134..136
FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT ylidene]ethyl phosphate"
FT /ligand_id="ChEBI:CHEBI:62899"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT ylidene]ethyl phosphate"
FT /ligand_id="ChEBI:CHEBI:62899"
FT /evidence="ECO:0000250"
FT BINDING 186..187
FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT ylidene]ethyl phosphate"
FT /ligand_id="ChEBI:CHEBI:62899"
FT /evidence="ECO:0000250"
SQ SEQUENCE 211 AA; 23015 MW; C731953E46BC33E1 CRC64;
MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA DVVAAIALGR
RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA AGLRLGVSTH DDMEIDVALA
ARPSYIALGH VFPTQTKQMP SAPQGLEQLA RHVERLADYP TVAIGGISLA RAPAVIATGV
GSIAVVSAIT QAADWRLATA QLLEIAGVGD E
