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Entry version 117 (10 Apr 2019)
Sequence version 1 (01 Apr 1988)
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Protein

Bifunctional chorismate mutase/prephenate dehydratase

Gene

pheA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Both activities are inhibited by L-phenylalanine.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 72 sec(-1) at pH 7.5. kcat is 31 sec(-1) at pH 4.9.1 Publication
  1. KM=45 µM for chorismate (at pH 7.8 and at 37 degrees Celsius)1 Publication
  2. KM=1.0 mM for prephenate (at pH 7.8 and at 37 degrees Celsius)1 Publication
  3. KM=147 µM for chorismate (at pH 4.9)1 Publication
  4. KM=296 µM for chorismate (at pH 7.5)1 Publication

    pH dependencei

    Optimum pH is 7.3 for chorismate mutase activity.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-phenylalanine biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes phenylpyruvate from prephenate.Curated
    Proteins known to be involved in this subpathway in this organism are:
    1. Bifunctional chorismate mutase/prephenate dehydratase (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.

    Pathwayi: prephenate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes prephenate from chorismate.Curated
    Proteins known to be involved in this subpathway in this organism are:
    1. Bifunctional chorismate mutase/prephenate dehydratase (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)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei11Substrate1 Publication1
    Binding sitei28Substrate1 Publication1
    Binding sitei39Substrate1 Publication1
    Binding sitei48Substrate1 Publication1
    Binding sitei52Substrate1 Publication1
    Binding sitei84Substrate1 Publication1
    Binding sitei88Substrate1 Publication1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei278Essential for prephenate dehydratase activitySequence analysis1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    • chorismate metabolic process Source: InterPro
    • L-phenylalanine biosynthetic process Source: EcoCyc
    • tyrosine biosynthetic process Source: EcoCyc

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionIsomerase, Lyase, Multifunctional enzyme
    Biological processAmino-acid biosynthesis, Aromatic amino acid biosynthesis, Phenylalanine biosynthesis

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER
    ECOL316407:JW2580-MONOMER
    MetaCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    5.4.99.5 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P0A9J8

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00120;UER00203

    UPA00121;UER00345

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Bifunctional chorismate mutase/prephenate dehydrataseCurated
    Alternative name(s):
    Chorismate mutase-prephenate dehydratase1 Publication
    P-protein1 Publication
    Including the following 2 domains:
    Chorismate mutase1 Publication (EC:5.4.99.51 Publication)
    Short name:
    CMCurated
    Prephenate dehydratase1 Publication (EC:4.2.1.511 Publication)
    Short name:
    PDTCurated
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:pheA1 Publication
    Ordered Locus Names:b2599, JW2580
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    Escherichia coli strain K12 genome database

    More...
    EcoGenei
    EG10707 pheA

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi11R → A or K: Important decrease in catalytic efficiency and affinity. 1 Publication1
    Mutagenesisi28R → A or K: Important decrease in catalytic efficiency and affinity. 1 Publication1
    Mutagenesisi39K → A, Q or R: Important decrease in catalytic efficiency and affinity. 1 Publication1
    Mutagenesisi52E → A, D or Q: Important decrease in catalytic efficiency and affinity. 1 Publication1
    Mutagenesisi88Q → A, E or K: Important decrease in catalytic efficiency and affinity. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3341586

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001191851 – 386Bifunctional chorismate mutase/prephenate dehydrataseAdd BLAST386

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P0A9J8

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P0A9J8

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P0A9J8

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0A9J8

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4263461, 19 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-36017N

    Protein interaction database and analysis system

    More...
    IntActi
    P0A9J8, 17 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b2599

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P0A9J8

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1386
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1ECMX-ray2.20A/B1-109[»]
    5VHTX-ray2.00A/B1-92[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P0A9J8

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P0A9J8

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P0A9J8

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 92Chorismate mutasePROSITE-ProRule annotationAdd BLAST92
    Domaini105 – 285Prephenate dehydratasePROSITE-ProRule annotationAdd BLAST181
    Domaini299 – 376ACTPROSITE-ProRule annotationAdd BLAST78

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni286 – 386Regulatory (Phe-binding)1 PublicationAdd BLAST101

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105CQC Bacteria
    COG0077 LUCA
    COG1605 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000018972

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0A9J8

    KEGG Orthology (KO)

    More...
    KOi
    K14170

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0A9J8

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.20.59.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR002912 ACT_dom
    IPR008242 Chor_mutase/pphenate_deHydtase
    IPR036263 Chorismate_II_sf
    IPR036979 CM_dom_sf
    IPR002701 CM_II_prokaryot
    IPR010952 CM_P_1
    IPR001086 Preph_deHydtase
    IPR018528 Preph_deHydtase_CS

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01817 CM_2, 1 hit
    PF00800 PDT, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF001500 Chor_mut_pdt_Ppr, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00830 CM_2, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF48600 SSF48600, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01797 CM_P_1, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    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

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4B0960854C75A4F1
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    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

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A30261 KMECPW

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_417090.1, NC_000913.3
    WP_000200120.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC75648; AAC75648; b2599
    BAA16484; BAA16484; BAA16484

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    947081

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW2580
    eco:b2599

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.4140

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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_LN832404.1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1ECMX-ray2.20A/B1-109[»]
    5VHTX-ray2.00A/B1-92[»]
    ProteinModelPortaliP0A9J8
    SMRiP0A9J8
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4263461, 19 interactors
    DIPiDIP-36017N
    IntActiP0A9J8, 17 interactors
    STRINGi511145.b2599

    Chemistry databases

    BindingDBiP0A9J8
    ChEMBLiCHEMBL3341586

    Proteomic databases

    EPDiP0A9J8
    jPOSTiP0A9J8
    PaxDbiP0A9J8
    PRIDEiP0A9J8

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75648; AAC75648; b2599
    BAA16484; BAA16484; BAA16484
    GeneIDi947081
    KEGGiecj:JW2580
    eco:b2599
    PATRICifig|1411691.4.peg.4140

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...
    EchoBASEi
    EB0701
    EcoGeneiEG10707 pheA

    Phylogenomic databases

    eggNOGiENOG4105CQC Bacteria
    COG0077 LUCA
    COG1605 LUCA
    HOGENOMiHOG000018972
    InParanoidiP0A9J8
    KOiK14170
    PhylomeDBiP0A9J8

    Enzyme and pathway databases

    UniPathwayi
    UPA00120;UER00203

    UPA00121;UER00345

    BioCyciEcoCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER
    ECOL316407:JW2580-MONOMER
    MetaCyc:CHORISMUTPREPHENDEHYDRAT-MONOMER
    BRENDAi5.4.99.5 2026
    SABIO-RKiP0A9J8

    Miscellaneous databases

    EvolutionaryTraceiP0A9J8

    Protein Ontology

    More...
    PROi
    PR:P0A9J8

    Family and domain databases

    Gene3Di1.20.59.10, 1 hit
    InterProiView protein in InterPro
    IPR002912 ACT_dom
    IPR008242 Chor_mutase/pphenate_deHydtase
    IPR036263 Chorismate_II_sf
    IPR036979 CM_dom_sf
    IPR002701 CM_II_prokaryot
    IPR010952 CM_P_1
    IPR001086 Preph_deHydtase
    IPR018528 Preph_deHydtase_CS
    PfamiView protein in Pfam
    PF01817 CM_2, 1 hit
    PF00800 PDT, 1 hit
    PIRSFiPIRSF001500 Chor_mut_pdt_Ppr, 1 hit
    SMARTiView protein in SMART
    SM00830 CM_2, 1 hit
    SUPFAMiSSF48600 SSF48600, 1 hit
    TIGRFAMsiTIGR01797 CM_P_1, 1 hit
    PROSITEiView protein in PROSITE
    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

    ProtoNet; Automatic hierarchical classification of proteins

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    ProtoNeti
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    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCMPDT_ECOLI
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0A9J8
    Secondary accession number(s): P07022, P78204
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: April 1, 1988
    Last modified: April 10, 2019
    This is version 117 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
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