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Protein

Tautomerase PptA

Gene

pptA

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

Functioni

Can use enol isomers of phenylpyruvate, 2-hydroxy-2,4-pentadienoate and (p-hydroxyphenyl)pyruvate as substrates.1 Publication

Enzyme regulationi

Inhibited by (E)-2-fluoro-p-hydroxycinnamate.1 Publication

Kineticsi

  1. KM=205 µM for enol isomers of phenylpyruvate1 Publication
  2. KM=220 µM for 2-hydroxy-2,4-pentadienoate1 Publication
  3. KM=180 µM for (p-hydroxyphenyl)pyruvate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei2 – 21Proton acceptor; via imino nitrogen

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11761-MONOMER.
    ECOL316407:JW1456-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tautomerase PptA (EC:5.3.2.-)
    Gene namesi
    Name:pptA
    Synonyms:ydcE
    Ordered Locus Names:b1461, JW1456
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11761. pptA.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Chemistry

    DrugBankiDB03793. Benzoic Acid.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved
    Chaini2 – 7776Tautomerase PptAPRO_0000209526Add
    BLAST

    Proteomic databases

    PaxDbiP31992.
    PRIDEiP31992.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi4262891. 27 interactions.
    IntActiP31992. 14 interactions.
    STRINGi511145.b1461.

    Structurei

    Secondary structure

    1
    77
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 97Combined sources
    Helixi15 – 3319Combined sources
    Helixi37 – 393Combined sources
    Beta strandi41 – 466Combined sources
    Helixi49 – 513Combined sources
    Helixi52 – 587Combined sources
    Turni59 – 668Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GYJX-ray2.10A/B2-77[»]
    1GYXX-ray1.35A/B2-77[»]
    1GYYX-ray1.35A/B2-77[»]
    ProteinModelPortaliP31992.
    SMRiP31992. Positions 2-77.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP31992.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105KZK. Bacteria.
    COG1942. LUCA.
    HOGENOMiHOG000077848.
    KOiK01821.
    OMAiIKCFPRD.
    OrthoDBiEOG6X6RJ5.

    Family and domain databases

    HAMAPiMF_00718. Tautomerase_PptA.
    InterProiIPR004370. 4-oxalocrotonate_tautomerase.
    IPR014347. Tautomerase/MIF_sf.
    IPR017284. Tautomerase_PptA.
    [Graphical view]
    PfamiPF01361. Tautomerase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037799. Tautomer_YdcE_prd. 1 hit.
    SUPFAMiSSF55331. SSF55331. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P31992-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPHIDIKCFP RELDEQQKAA LAADITDVII RHLNSKDSSI SIALQQIQPE
    60 70
    SWQAIWDAEI APQMEALIKK PGYSMNA
    Length:77
    Mass (Da):8,673
    Last modified:January 23, 2007 - v3
    Checksum:iD32FF4023FE556CA
    GO

    Mass spectrometryi

    Molecular mass is 8540 Da from positions 2 - 77. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X60998 Genomic DNA. Translation: CAA43312.1.
    U00096 Genomic DNA. Translation: AAC74543.1.
    AP009048 Genomic DNA. Translation: BAA15092.1.
    PIRiH64898.
    RefSeqiNP_415978.1. NC_000913.3.
    WP_001120143.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74543; AAC74543; b1461.
    BAA15092; BAA15092; BAA15092.
    GeneIDi945731.
    KEGGiecj:JW1456.
    eco:b1461.
    PATRICi32118214. VBIEscCol129921_1527.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X60998 Genomic DNA. Translation: CAA43312.1.
    U00096 Genomic DNA. Translation: AAC74543.1.
    AP009048 Genomic DNA. Translation: BAA15092.1.
    PIRiH64898.
    RefSeqiNP_415978.1. NC_000913.3.
    WP_001120143.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GYJX-ray2.10A/B2-77[»]
    1GYXX-ray1.35A/B2-77[»]
    1GYYX-ray1.35A/B2-77[»]
    ProteinModelPortaliP31992.
    SMRiP31992. Positions 2-77.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4262891. 27 interactions.
    IntActiP31992. 14 interactions.
    STRINGi511145.b1461.

    Chemistry

    DrugBankiDB03793. Benzoic Acid.

    Proteomic databases

    PaxDbiP31992.
    PRIDEiP31992.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74543; AAC74543; b1461.
    BAA15092; BAA15092; BAA15092.
    GeneIDi945731.
    KEGGiecj:JW1456.
    eco:b1461.
    PATRICi32118214. VBIEscCol129921_1527.

    Organism-specific databases

    EchoBASEiEB1711.
    EcoGeneiEG11761. pptA.

    Phylogenomic databases

    eggNOGiENOG4105KZK. Bacteria.
    COG1942. LUCA.
    HOGENOMiHOG000077848.
    KOiK01821.
    OMAiIKCFPRD.
    OrthoDBiEOG6X6RJ5.

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11761-MONOMER.
    ECOL316407:JW1456-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP31992.
    PROiP31992.

    Family and domain databases

    HAMAPiMF_00718. Tautomerase_PptA.
    InterProiIPR004370. 4-oxalocrotonate_tautomerase.
    IPR014347. Tautomerase/MIF_sf.
    IPR017284. Tautomerase_PptA.
    [Graphical view]
    PfamiPF01361. Tautomerase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037799. Tautomer_YdcE_prd. 1 hit.
    SUPFAMiSSF55331. SSF55331. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Rhs elements of Escherichia coli K-12: complex composites of shared and unique components that have different evolutionary histories."
      Zhao S., Sandt C.H., Feulner G., Vlazny D.A., Gray J.A., Hill C.W.
      J. Bacteriol. 175:2799-2808(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    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. "The crystal structure of YdcE, a 4-oxalocrotonate tautomerase homologue from Escherichia coli, confirms the structural basis for oligomer diversity."
      Almrud J.J., Kern A.D., Wang S.C., Czerwinski R.M., Johnson W.H. Jr., Murzin A.G., Hackert M.L., Whitman C.P.
      Biochemistry 41:12010-12024(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH INHIBITOR, FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MASS SPECTROMETRY.
      Strain: K12.

    Entry informationi

    Entry nameiPPTA_ECOLI
    AccessioniPrimary (citable) accession number: P31992
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: January 23, 2007
    Last modified: January 20, 2016
    This is version 124 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    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.