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UniProtKB - P0A9J8 (CMPDT_ECOLI)

Entry version 129 (10 Feb 2021)
Sequence version 1 (01 Apr 1988)
Previous versions | rss
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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%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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%5Fsection">'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), 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), 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <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
    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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

    <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

    • cytoplasm Source: GO_Central
    Complete GO annotation on QuickGO ...

    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%5Fand%5Fbiotech%5Fsection">'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

    Drug and drug target database

    More...    DrugBanki    		DB08648, (1R,3S,5S,8R)-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid

    <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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001191851 – 386Bifunctional chorismate mutase/prephenate dehydrataseAdd BLAST386

    Proteomic databases

    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%5Fsection">'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%5Fsection">'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

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

    More...    SMRi    		P0A9J8

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Protein Data Bank in Europe - Knowledge Base

    More...    PDBe-KBi    		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%5Fand%5Fdomains%5Fsection">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    		COG0077, Bacteria
    COG1605, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_035008_1_0_6

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P0A9J8

    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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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_SSUR01000056.1

    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    		58463063
    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_SSUR01000056.1

    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[»]
    SMRiP0A9J8
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4263461, 19 interactors
    DIPiDIP-36017N
    IntActiP0A9J8, 17 interactors
    STRINGi511145.b2599

    Chemistry databases

    BindingDBiP0A9J8
    ChEMBLiCHEMBL3341586
    DrugBankiDB08648, (1R,3S,5S,8R)-8-Hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid

    Proteomic databases

    jPOSTiP0A9J8
    PaxDbiP0A9J8
    PRIDEiP0A9J8

    Genome annotation databases

    EnsemblBacteriaiAAC75648; AAC75648; b2599
    BAA16484; BAA16484; BAA16484
    GeneIDi58463063
    947081
    KEGGiecj:JW2580
    eco:b2599
    PATRICifig|1411691.4.peg.4140

    Organism-specific databases

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

    More...    EchoBASEi    		EB0701

    Phylogenomic databases

    eggNOGiCOG0077, Bacteria
    COG1605, Bacteria
    HOGENOMiCLU_035008_1_0_6
    InParanoidiP0A9J8
    PhylomeDBiP0A9J8

    Enzyme and pathway databases

    UniPathwayiUPA00120;UER00203
    UPA00121;UER00345
    BioCyciEcoCyc:CHORISMUTPREPHENDEHYDRAT-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

    More...    ProtoNeti    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		Search...

    <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%5Fand%5Fisoforms">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: February 10, 2021
    This is version 129 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, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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