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Protein

P-protein

Gene

pheA

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

Functioni

Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.1 Publication

Catalytic activityi

Chorismate = prephenate.
Prephenate = phenylpyruvate + H2O + CO2.

Enzyme regulationi

Inhibited by L-phenylalanine.1 Publication

Kineticsi

  1. KM=45 µM for chorismate (at pH 7.8 and at 37 degrees Celsius, PubMed:4261395)2 Publications
  2. KM=100 µM for prephenate (at pH 7.8 and at 37 degrees Celsius, PubMed:4261395)2 Publications
  3. KM=147 µM for chorismate (at pH 4.9)2 Publications
  4. KM=296 µM for chorismate (at pH 7.5)2 Publications

    Temperature dependencei

    Optimum temperature is 7.3 degrees Celsius for chorismate mutase.2 Publications

    Pathway:iL-phenylalanine biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes phenylpyruvate from prephenate.
    Proteins known to be involved in this subpathway in this organism are:
    1. P-protein (pheA)
    This subpathway is part of the pathway L-phenylalanine biosynthesis, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes phenylpyruvate from prephenate, the pathway L-phenylalanine biosynthesis and in Amino-acid biosynthesis.

    Pathway:iprephenate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes prephenate from chorismate.
    Proteins known to be involved in this subpathway in this organism are:
    1. P-protein (pheA), T-protein (tyrA)
    This subpathway is part of the pathway prephenate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes prephenate from chorismate, the pathway prephenate biosynthesis and in Metabolic intermediate biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei11 – 111Substrate
    Binding sitei28 – 281Substrate
    Binding sitei39 – 391Substrate
    Binding sitei48 – 481Substrate
    Binding sitei52 – 521Substrate
    Binding sitei84 – 841Substrate
    Binding sitei88 – 881Substrate
    Sitei278 – 2781Essential for prephenate dehydratase activitySequence Analysis

    GO - Molecular functioni

    • amino acid binding Source: InterPro
    • chorismate mutase activity Source: EcoCyc
    • prephenate dehydratase activity Source: EcoCyc

    GO - Biological processi

    • chorismate metabolic process Source: InterPro
    • L-phenylalanine biosynthetic process Source: EcoCyc
    • tyrosine biosynthetic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase, Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Phenylalanine biosynthesis

    Enzyme and pathway databases

    BioCyciEcoCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER.
    ECOL316407:JW2580-MONOMER.
    MetaCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER.
    BRENDAi5.4.99.5. 2026.
    SABIO-RKP0A9J8.
    UniPathwayiUPA00120; UER00203.
    UPA00121; UER00345.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    P-protein
    Including the following 2 domains:
    Chorismate mutase (EC:5.4.99.5)
    Short name:
    CM
    Prephenate dehydratase (EC:4.2.1.51)
    Short name:
    PDT
    Gene namesi
    Name:pheA
    Ordered Locus Names:b2599, JW2580
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10707. pheA.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi11 – 111R → A: Important decrease in catalytic efficiency and affinity. 1 Publication
    Mutagenesisi11 – 111R → K: Important decrease in catalytic efficiency and affinity. 1 Publication
    Mutagenesisi28 – 281R → A: Important decrease in catalytic efficiency and affinity. 1 Publication
    Mutagenesisi28 – 281R → K: Important decrease in catalytic efficiency and affinity. 1 Publication
    Mutagenesisi39 – 391K → A: Important decrease in catalytic efficiency and affinity. 1 Publication
    Mutagenesisi39 – 391K → Q: Important decrease in catalytic efficiency and affinity. 1 Publication
    Mutagenesisi39 – 391K → R: Important decrease in catalytic efficiency and affinity. 1 Publication
    Mutagenesisi52 – 521E → A: Important decrease in catalytic efficiency and affinity. 1 Publication
    Mutagenesisi52 – 521E → D: Important decrease in catalytic efficiency and affinity. 1 Publication
    Mutagenesisi52 – 521E → Q: Important decrease in catalytic efficiency and affinity. 1 Publication
    Mutagenesisi88 – 881Q → A: Important decrease in catalytic efficiency and affinity. 1 Publication
    Mutagenesisi88 – 881Q → E: Important decrease in catalytic efficiency and affinity. 1 Publication
    Mutagenesisi88 – 881Q → K: Important decrease in catalytic efficiency and affinity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 386386P-proteinPRO_0000119185Add
    BLAST

    Proteomic databases

    PaxDbiP0A9J8.
    PRIDEiP0A9J8.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    DIPiDIP-36017N.
    IntActiP0A9J8. 17 interactions.
    MINTiMINT-1248118.
    STRINGi511145.b2599.

    Structurei

    Secondary structure

    1
    386
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 4136Combined sources
    Helixi49 – 6517Combined sources
    Helixi70 – 9324Combined sources
    Helixi96 – 994Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ECMX-ray2.20A/B1-109[»]
    ProteinModelPortaliP0A9J8.
    SMRiP0A9J8. Positions 6-100, 106-375.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A9J8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 9292Chorismate mutasePROSITE-ProRule annotationAdd
    BLAST
    Domaini105 – 285181Prephenate dehydratasePROSITE-ProRule annotationAdd
    BLAST
    Domaini299 – 37678ACTPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni286 – 386101Regulatory (Phe-binding)Add
    BLAST

    Sequence similaritiesi

    Contains 1 ACT domain.PROSITE-ProRule annotation
    Contains 1 chorismate mutase domain.PROSITE-ProRule annotation
    Contains 1 prephenate dehydratase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0077.
    HOGENOMiHOG000018972.
    InParanoidiP0A9J8.
    KOiK14170.
    OMAiHSHRPIR.
    OrthoDBiEOG6WHNT1.
    PhylomeDBiP0A9J8.

    Family and domain databases

    Gene3Di1.20.59.10. 1 hit.
    InterProiIPR002912. ACT_dom.
    IPR008242. Chor_mutase/pphenate_deHydtase.
    IPR002701. Chorismate_mutase.
    IPR020822. Chorismate_mutase_type_II.
    IPR010952. CM_P_1.
    IPR001086. Preph_deHydtase.
    IPR018528. Preph_deHydtase_CS.
    [Graphical view]
    PfamiPF01817. CM_2. 1 hit.
    PF00800. PDT. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001500. Chor_mut_pdt_Ppr. 1 hit.
    SMARTiSM00830. CM_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF48600. SSF48600. 1 hit.
    TIGRFAMsiTIGR01797. CM_P_1. 1 hit.
    PROSITEiPS51671. ACT. 1 hit.
    PS51168. CHORISMATE_MUT_2. 1 hit.
    PS00857. PREPHENATE_DEHYDR_1. 1 hit.
    PS00858. PREPHENATE_DEHYDR_2. 1 hit.
    PS51171. PREPHENATE_DEHYDR_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0A9J8-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTSENPLLAL REKISALDEK LLALLAERRE LAVEVGKAKL LSHRPVRDID
    60 70 80 90 100
    RERDLLERLI TLGKAHHLDA HYITRLFQLI IEDSVLTQQA LLQQHLNKIN
    110 120 130 140 150
    PHSARIAFLG PKGSYSHLAA RQYAARHFEQ FIESGCAKFA DIFNQVETGQ
    160 170 180 190 200
    ADYAVVPIEN TSSGAINDVY DLLQHTSLSI VGEMTLTIDH CLLVSGTTDL
    210 220 230 240 250
    STINTVYSHP QPFQQCSKFL NRYPHWKIEY TESTSAAMEK VAQAKSPHVA
    260 270 280 290 300
    ALGSEAGGTL YGLQVLERIE ANQRQNFTRF VVLARKAINV SDQVPAKTTL
    310 320 330 340 350
    LMATGQQAGA LVEALLVLRN HNLIMTRLES RPIHGNPWEE MFYLDIQANL
    360 370 380
    ESAEMQKALK ELGEITRSMK VLGCYPSENV VPVDPT
    Length:386
    Mass (Da):43,111
    Last modified:April 1, 1988 - v1
    Checksum:i4B0960854C75A4F1
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M10431 Genomic DNA. Translation: AAA24330.1.
    U00096 Genomic DNA. Translation: AAC75648.1.
    AP009048 Genomic DNA. Translation: BAA16484.1.
    M58024 Genomic DNA. Translation: AAA62784.1.
    V00314 Genomic DNA. Translation: CAA23601.1.
    PIRiA30261. KMECPW.
    RefSeqiNP_417090.1. NC_000913.3.
    WP_000200120.1. NZ_CP010445.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75648; AAC75648; b2599.
    BAA16484; BAA16484; BAA16484.
    GeneIDi947081.
    KEGGieco:b2599.
    PATRICi32120597. VBIEscCol129921_2697.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M10431 Genomic DNA. Translation: AAA24330.1.
    U00096 Genomic DNA. Translation: AAC75648.1.
    AP009048 Genomic DNA. Translation: BAA16484.1.
    M58024 Genomic DNA. Translation: AAA62784.1.
    V00314 Genomic DNA. Translation: CAA23601.1.
    PIRiA30261. KMECPW.
    RefSeqiNP_417090.1. NC_000913.3.
    WP_000200120.1. NZ_CP010445.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ECMX-ray2.20A/B1-109[»]
    ProteinModelPortaliP0A9J8.
    SMRiP0A9J8. Positions 6-100, 106-375.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-36017N.
    IntActiP0A9J8. 17 interactions.
    MINTiMINT-1248118.
    STRINGi511145.b2599.

    Proteomic databases

    PaxDbiP0A9J8.
    PRIDEiP0A9J8.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75648; AAC75648; b2599.
    BAA16484; BAA16484; BAA16484.
    GeneIDi947081.
    KEGGieco:b2599.
    PATRICi32120597. VBIEscCol129921_2697.

    Organism-specific databases

    EchoBASEiEB0701.
    EcoGeneiEG10707. pheA.

    Phylogenomic databases

    eggNOGiCOG0077.
    HOGENOMiHOG000018972.
    InParanoidiP0A9J8.
    KOiK14170.
    OMAiHSHRPIR.
    OrthoDBiEOG6WHNT1.
    PhylomeDBiP0A9J8.

    Enzyme and pathway databases

    UniPathwayiUPA00120; UER00203.
    UPA00121; UER00345.
    BioCyciEcoCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER.
    ECOL316407:JW2580-MONOMER.
    MetaCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER.
    BRENDAi5.4.99.5. 2026.
    SABIO-RKP0A9J8.

    Miscellaneous databases

    EvolutionaryTraceiP0A9J8.
    PROiP0A9J8.

    Family and domain databases

    Gene3Di1.20.59.10. 1 hit.
    InterProiIPR002912. ACT_dom.
    IPR008242. Chor_mutase/pphenate_deHydtase.
    IPR002701. Chorismate_mutase.
    IPR020822. Chorismate_mutase_type_II.
    IPR010952. CM_P_1.
    IPR001086. Preph_deHydtase.
    IPR018528. Preph_deHydtase_CS.
    [Graphical view]
    PfamiPF01817. CM_2. 1 hit.
    PF00800. PDT. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001500. Chor_mut_pdt_Ppr. 1 hit.
    SMARTiSM00830. CM_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF48600. SSF48600. 1 hit.
    TIGRFAMsiTIGR01797. CM_P_1. 1 hit.
    PROSITEiPS51671. ACT. 1 hit.
    PS51168. CHORISMATE_MUT_2. 1 hit.
    PS00857. PREPHENATE_DEHYDR_1. 1 hit.
    PS00858. PREPHENATE_DEHYDR_2. 1 hit.
    PS51171. PREPHENATE_DEHYDR_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Nucleotide sequence and transcription of the phenylalanine and tyrosine operons of Escherichia coli K12."
      Hudson G.S., Davidson B.E.
      J. Mol. Biol. 180:1023-1051(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
      Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
      , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
      DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
      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. "pheAo mutants of Escherichia coli have a defective pheA attenuator."
      Gavini N., Davidson B.E.
      J. Biol. Chem. 265:21532-21535(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
    6. "Nucleotide sequence of the leader region of the phenylalanine operon of Escherichia coli."
      Zurawski G.R., Brown K., Killingly D., Yanofsky C.
      Proc. Natl. Acad. Sci. U.S.A. 75:4271-4275(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
    7. "Chorismate mutase-prephenate dehydratase from Escherichia coli K-12. II. Kinetic properties."
      Dopheide T.A., Crewther P., Davidson B.E.
      J. Biol. Chem. 247:4447-4452(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A CHORISMATE MUTASE AND PREPHENATE DEHYDRATASE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    8. "Analysis of active site residues in Escherichia coli chorismate mutase by site-directed mutagenesis."
      Liu D.R., Cload S.T., Pastor R.M., Schultz P.G.
      J. Am. Chem. Soc. 118:1789-1790(1996)
      Cited for: MUTAGENESIS OF ARG-11; ARG-28; LYS-39; GLU-52 AND GLN-88, BIOPHYSICOCHEMICAL PROPERTIES.
    9. "Chorismate mutase-prephenate dehydratase from Escherichia coli. Study of catalytic and regulatory domains using genetically engineered proteins."
      Zhang S., Pohnert G., Kongsaeree P., Wilson D.B., Clardy J., Ganem B.
      J. Biol. Chem. 273:6248-6253(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN.
    10. "Atomic structure of the buried catalytic pocket of Escherichial coli chorismate mutase."
      Lee A.Y., Karplus P.A., Ganem B., Clardy J.
      J. Am. Chem. Soc. 117:3627-3628(1995)
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-109 IN COMPLEX WITH SUBSTRATE ANALOGS, SUBUNIT.

    Entry informationi

    Entry nameiPHEA_ECOLI
    AccessioniPrimary (citable) accession number: P0A9J8
    Secondary accession number(s): P07022, P78204
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: April 1, 1988
    Last modified: July 22, 2015
    This is version 92 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

    3D-structure, Complete proteome, Multifunctional enzyme, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.