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P0A9J8

- PHEA_ECOLI

UniProt

P0A9J8 - PHEA_ECOLI

Protein

P-protein

Gene

pheA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (01 Apr 1988)
      Previous versions | rss
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    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

    Pathwayi

    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

    1. amino acid binding Source: InterPro
    2. chorismate mutase activity Source: EcoCyc
    3. prephenate dehydratase activity Source: EcoCyc

    GO - Biological processi

    1. chorismate metabolic process Source: InterPro
    2. L-phenylalanine biosynthetic process Source: EcoCyc
    3. tyrosine biosynthetic process Source: EcoCyc

    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.
    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10707. pheA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A9J8.

    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 – 4136
    Helixi49 – 6517
    Helixi70 – 9324

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ECMX-ray2.20A/B1-109[»]
    ProteinModelPortaliP0A9J8.
    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.
    KOiK14170.
    OMAiIDVQANL.
    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

    MTSENPLLAL REKISALDEK LLALLAERRE LAVEVGKAKL LSHRPVRDID    50
    RERDLLERLI TLGKAHHLDA HYITRLFQLI IEDSVLTQQA LLQQHLNKIN 100
    PHSARIAFLG PKGSYSHLAA RQYAARHFEQ FIESGCAKFA DIFNQVETGQ 150
    ADYAVVPIEN TSSGAINDVY DLLQHTSLSI VGEMTLTIDH CLLVSGTTDL 200
    STINTVYSHP QPFQQCSKFL NRYPHWKIEY TESTSAAMEK VAQAKSPHVA 250
    ALGSEAGGTL YGLQVLERIE ANQRQNFTRF VVLARKAINV SDQVPAKTTL 300
    LMATGQQAGA LVEALLVLRN HNLIMTRLES RPIHGNPWEE MFYLDIQANL 350
    ESAEMQKALK ELGEITRSMK VLGCYPSENV VPVDPT 386
    Length:386
    Mass (Da):43,111
    Last modified:April 1, 1988 - v1
    Checksum:i4B0960854C75A4F1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_490822.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75648; AAC75648; b2599.
    BAA16484; BAA16484; BAA16484.
    GeneIDi12934467.
    947081.
    KEGGiecj:Y75_p2547.
    eco:b2599.
    PATRICi32120597. VBIEscCol129921_2697.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi A30261. KMECPW.
    RefSeqi NP_417090.1. NC_000913.3.
    YP_490822.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ECM X-ray 2.20 A/B 1-109 [» ]
    ProteinModelPortali P0A9J8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-36017N.
    IntActi P0A9J8. 17 interactions.
    MINTi MINT-1248118.
    STRINGi 511145.b2599.

    Proteomic databases

    PaxDbi P0A9J8.
    PRIDEi P0A9J8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75648 ; AAC75648 ; b2599 .
    BAA16484 ; BAA16484 ; BAA16484 .
    GeneIDi 12934467.
    947081.
    KEGGi ecj:Y75_p2547.
    eco:b2599.
    PATRICi 32120597. VBIEscCol129921_2697.

    Organism-specific databases

    EchoBASEi EB0701.
    EcoGenei EG10707. pheA.

    Phylogenomic databases

    eggNOGi COG0077.
    HOGENOMi HOG000018972.
    KOi K14170.
    OMAi IDVQANL.
    OrthoDBi EOG6WHNT1.
    PhylomeDBi P0A9J8.

    Enzyme and pathway databases

    UniPathwayi UPA00120 ; UER00203 .
    UPA00121 ; UER00345 .
    BioCyci EcoCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER.
    ECOL316407:JW2580-MONOMER.
    MetaCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER.
    SABIO-RK P0A9J8.

    Miscellaneous databases

    EvolutionaryTracei P0A9J8.
    PROi P0A9J8.

    Gene expression databases

    Genevestigatori P0A9J8.

    Family and domain databases

    Gene3Di 1.20.59.10. 1 hit.
    InterProi IPR002912. 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 ]
    Pfami PF01817. CM_2. 1 hit.
    PF00800. PDT. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001500. Chor_mut_pdt_Ppr. 1 hit.
    SMARTi SM00830. CM_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48600. SSF48600. 1 hit.
    TIGRFAMsi TIGR01797. CM_P_1. 1 hit.
    PROSITEi PS51671. 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 ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 85 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