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Protein

Thiamine-phosphate synthase

Gene

thiE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).2 Publications

Catalytic activityi

4-amino-2-methyl-5-diphosphomethylpyrimidine + 2-((2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate = diphosphate + thiamine phosphate + CO2.1 Publication
4-amino-2-methyl-5-diphosphomethylpyrimidine + 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate = diphosphate + thiamine phosphate + CO2.1 Publication
4-amino-2-methyl-5-diphosphomethylpyrimidine + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate.1 Publication

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Kineticsi

  1. KM=1 µM for HMP-PP1 Publication
  2. KM=2 µM for THZ-P1 Publication

    Pathwayi: thiamine diphosphate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole.
    Proteins known to be involved in this subpathway in this organism are:
    1. Thiamine-phosphate synthase (thiE)
    This subpathway is part of the pathway thiamine diphosphate biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole, the pathway thiamine diphosphate biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei69 – 691HMP-PPBy similarity
    Metal bindingi70 – 701MagnesiumBy similarity
    Metal bindingi89 – 891MagnesiumBy similarity
    Binding sitei108 – 1081HMP-PPBy similarity
    Binding sitei137 – 1371HMP-PPBy similarity
    Binding sitei166 – 1661THZ-P; via amide nitrogenBy similarity

    GO - Molecular functioni

    • magnesium ion binding Source: EcoCyc
    • metal ion binding Source: EcoCyc
    • thiamine-phosphate diphosphorylase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    • thiamine biosynthetic process Source: EcoCyc
    • thiamine diphosphate biosynthetic process Source: UniProtKB-UniPathway
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Thiamine biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:THIE-MONOMER.
    ECOL316407:JW3957-MONOMER.
    MetaCyc:THIE-MONOMER.
    UniPathwayiUPA00060; UER00141.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thiamine-phosphate synthase (EC:2.5.1.31 Publication)
    Short name:
    TP synthase
    Short name:
    TPS
    Alternative name(s):
    Thiamine-phosphate pyrophosphorylase
    Short name:
    TMP pyrophosphorylase
    Short name:
    TMP-PPase
    Gene namesi
    Name:thiE
    Ordered Locus Names:b3993, JW3957
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11586. thiE.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 211211Thiamine-phosphate synthasePRO_0000157010Add
    BLAST

    Proteomic databases

    EPDiP30137.
    PaxDbiP30137.

    2D gel databases

    SWISS-2DPAGEP30137.

    Interactioni

    Protein-protein interaction databases

    BioGridi4259333. 19 interactions.
    DIPiDIP-10983N.
    IntActiP30137. 4 interactions.
    MINTiMINT-1247897.
    STRINGi511145.b3993.

    Structurei

    3D structure databases

    ProteinModelPortaliP30137.
    SMRiP30137. Positions 20-202.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni37 – 415HMP-PP bindingBy similarity
    Regioni134 – 1363THZ-P bindingBy similarity
    Regioni186 – 1872THZ-P bindingBy similarity

    Sequence similaritiesi

    Belongs to the thiamine-phosphate synthase family.Curated

    Phylogenomic databases

    eggNOGiENOG4108UV6. Bacteria.
    COG0352. LUCA.
    HOGENOMiHOG000155781.
    InParanoidiP30137.
    KOiK00788.
    OMAiDSVEWIA.
    OrthoDBiEOG6XWV53.
    PhylomeDBiP30137.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_00097. TMP_synthase.
    InterProiIPR013785. Aldolase_TIM.
    IPR022998. ThiaminP_synth_SF.
    IPR003733. TMP_synthase.
    [Graphical view]
    PfamiPF02581. TMP-TENI. 1 hit.
    [Graphical view]
    SUPFAMiSSF51391. SSF51391. 1 hit.
    TIGRFAMsiTIGR00693. thiE. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P30137-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MYQPDFPPVP FRSGLYPVVD SVQWIERLLD AGVRTLQLRI KDRRDEEVEA
    60 70 80 90 100
    DVVAAIALGR RYNARLFIND YWRLAIKHQA YGVHLGQEDL QATDLNAIRA
    110 120 130 140 150
    AGLRLGVSTH DDMEIDVALA ARPSYIALGH VFPTQTKQMP SAPQGLEQLA
    160 170 180 190 200
    RHVERLADYP TVAIGGISLA RAPAVIATGV GSIAVVSAIT QAADWRLATA
    210
    QLLEIAGVGD E
    Length:211
    Mass (Da):23,015
    Last modified:April 1, 1993 - v1
    Checksum:iC731953E46BC33E1
    GO

    Mass spectrometryi

    Molecular mass is 23014.8 Da from positions 1 - 211. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M88701 Genomic DNA. Translation: AAB95617.1.
    U00006 Genomic DNA. Translation: AAC43091.1.
    U00096 Genomic DNA. Translation: AAC76967.1.
    AP009048 Genomic DNA. Translation: BAE77326.1.
    PIRiS35118.
    RefSeqiNP_418421.1. NC_000913.3.
    WP_000284615.1. NZ_CP014272.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76967; AAC76967; b3993.
    BAE77326; BAE77326; BAE77326.
    GeneIDi948491.
    KEGGiecj:JW3957.
    eco:b3993.
    PATRICi32123509. VBIEscCol129921_4107.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M88701 Genomic DNA. Translation: AAB95617.1.
    U00006 Genomic DNA. Translation: AAC43091.1.
    U00096 Genomic DNA. Translation: AAC76967.1.
    AP009048 Genomic DNA. Translation: BAE77326.1.
    PIRiS35118.
    RefSeqiNP_418421.1. NC_000913.3.
    WP_000284615.1. NZ_CP014272.1.

    3D structure databases

    ProteinModelPortaliP30137.
    SMRiP30137. Positions 20-202.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259333. 19 interactions.
    DIPiDIP-10983N.
    IntActiP30137. 4 interactions.
    MINTiMINT-1247897.
    STRINGi511145.b3993.

    2D gel databases

    SWISS-2DPAGEP30137.

    Proteomic databases

    EPDiP30137.
    PaxDbiP30137.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76967; AAC76967; b3993.
    BAE77326; BAE77326; BAE77326.
    GeneIDi948491.
    KEGGiecj:JW3957.
    eco:b3993.
    PATRICi32123509. VBIEscCol129921_4107.

    Organism-specific databases

    EchoBASEiEB1545.
    EcoGeneiEG11586. thiE.

    Phylogenomic databases

    eggNOGiENOG4108UV6. Bacteria.
    COG0352. LUCA.
    HOGENOMiHOG000155781.
    InParanoidiP30137.
    KOiK00788.
    OMAiDSVEWIA.
    OrthoDBiEOG6XWV53.
    PhylomeDBiP30137.

    Enzyme and pathway databases

    UniPathwayiUPA00060; UER00141.
    BioCyciEcoCyc:THIE-MONOMER.
    ECOL316407:JW3957-MONOMER.
    MetaCyc:THIE-MONOMER.

    Miscellaneous databases

    PROiP30137.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_00097. TMP_synthase.
    InterProiIPR013785. Aldolase_TIM.
    IPR022998. ThiaminP_synth_SF.
    IPR003733. TMP_synthase.
    [Graphical view]
    PfamiPF02581. TMP-TENI. 1 hit.
    [Graphical view]
    SUPFAMiSSF51391. SSF51391. 1 hit.
    TIGRFAMsiTIGR00693. thiE. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Structural genes for thiamine biosynthetic enzymes (thiCEFGH) in Escherichia coli K-12."
      Vander Horn P.B., Backstrom A.D., Stewart V., Begley T.P.
      J. Bacteriol. 175:982-992(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
      Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
      Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Biosynthesis of thiamin I: the function of the thiE gene product."
      Backstrom A.D., Austin R., McMordie S., Begley T.P.
      J. Am. Chem. Soc. 117:2351-2352(1995)
      Cited for: FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS.
    6. "Efficient sequence analysis of the six gene products (7-74 kDa) from the Escherichia coli thiamin biosynthetic operon by tandem high-resolution mass spectrometry."
      Kelleher N.L., Taylor S.V., Grannis D., Kinsland C., Chiu H.-J., Begley T.P., McLafferty F.W.
      Protein Sci. 7:1796-1801(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY.
    7. "A genetic screen for the identification of thiamin metabolic genes."
      Lawhorn B.G., Gerdes S.Y., Begley T.P.
      J. Biol. Chem. 279:43555-43559(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THIAMINE METABOLISM.
      Strain: K12 / MG1655 / ATCC 47076.

    Entry informationi

    Entry nameiTHIE_ECOLI
    AccessioniPrimary (citable) accession number: P30137
    Secondary accession number(s): Q2M8T0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: May 11, 2016
    This is version 136 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.