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Protein

Isocitrate lyase

Gene

aceA

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

Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates.5 Publications

<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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 PublicationNote: Divalent metal cations. Can also use Mn2+ ion.1 Publication

<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

Activated by phosphorylation on histidine. Competitively inhibited by 3-phosphosglycerate, oxalate, malate, chloride, phosphate and sulfate ions, and uncompetitively inhibited by succinate and phosphoenolpyruvate (PEP).3 Publications

<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 28.5 sec(-1) for isocitrate lyase activity with threo-D-isocitrate as substrate (at pH 7.3).1 Publication
  1. KM=0.076 µM for threo-D-isocitrate (at pH 7.3)1 Publication
  2. KM=8 µM for threo-D-isocitrate (at pH 7.5 and 25 degrees Celsius)1 Publication
  3. KM=32 µM for isocitrate (at pH 6.8)1 Publication
  4. KM=63 µM for isocitrate (at pH 7.3)1 Publication
  5. KM=130 µM for glyoxylate (at pH 7.3)1 Publication
  6. KM=590 µM for succinate (at pH 7.3)1 Publication

    pH dependencei

    Optimum pH is 7.3.1 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: glyoxylate cycle

    This protein is involved in step 1 of the subpathway that synthesizes (S)-malate from isocitrate.1 Publication
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Isocitrate lyase (aceA)
    2. Malate synthase A (aceB), Malate synthase G (glcB)
    This subpathway is part of the pathway glyoxylate cycle, which is itself part of Carbohydrate metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-malate from isocitrate, the pathway glyoxylate cycle and in Carbohydrate metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi157Magnesium1 Publication1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei195Proton acceptor1 Publication1
    <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 sitei232Substrate1 Publication1
    Binding sitei351SubstrateBy similarity1

    <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

    • cation binding Source: EcoliWiki
    • isocitrate lyase activity Source: EcoliWiki
    • metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    • glyoxylate cycle Source: EcoliWiki
    • tricarboxylic acid cycle Source: UniProtKB-KW

    <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 functionLyase
    Biological processGlyoxylate bypass, Tricarboxylic acid cycle
    LigandMagnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:ISOCIT-LYASE-MONOMER
    MetaCyc:ISOCIT-LYASE-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    4.1.3.1 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P0A9G6

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

    More...
    UniPathwayi
    UPA00703;UER00719

    <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:
    Isocitrate lyase1 Publication (EC:4.1.3.13 Publications)
    Short name:
    ICL1 Publication
    Alternative name(s):
    Isocitrase1 Publication
    Isocitratase1 Publication
    <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:aceA1 Publication
    Synonyms:icl
    Ordered Locus Names:b4015, JW3975
    <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
    EG10022 aceA

    <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

    • cytosol Source: UniProtKB

    <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>Mutagenesisi195C → A: Large decrease in activity. 1 Publication1
    Mutagenesisi195C → S: Large decrease in activity. 1 Publication1
    Mutagenesisi219A → C: Isocitrate lyase activity is reduced compared to the wild-type. 1 Publication1

    <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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <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_00000687742 – 434Isocitrate lyaseAdd BLAST433

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P0A9G6

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

    More...
    PaxDbi
    P0A9G6

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0A9G6

    2D gel databases

    Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

    More...
    SWISS-2DPAGEi
    P0A9G6

    <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

    Homotetramer.4 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4263469, 7 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-35893N

    Protein interaction database and analysis system

    More...
    IntActi
    P0A9G6, 3 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    316385.ECDH10B_4204

    <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

    1434
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P0A9G6

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

    More...
    SMRi
    P0A9G6

    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
    P0A9G6

    <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

    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>Regioni91 – 93Substrate binding1 Publication3
    Regioni196 – 197Substrate bindingBy similarity2
    Regioni317 – 321Substrate bindingBy similarity5

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4108I9X Bacteria
    COG2224 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000238475

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0A9G6

    KEGG Orthology (KO)

    More...
    KOi
    K01637

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0A9G6

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00377 ICL_PEPM, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR039556 ICL/PEPM
    IPR006254 Isocitrate_lyase
    IPR018523 Isocitrate_lyase_ph_CS
    IPR015813 Pyrv/PenolPyrv_Kinase-like_dom

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR21631 PTHR21631, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00463 ICL, 2 hits

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF001362 Isocit_lyase, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51621 SSF51621, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01346 isocit_lyase, 2 hits

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00161 ISOCITRATE_LYASE, 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.

    <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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A9G6-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKTRTQQIEE LQKEWTQPRW EGITRPYSAE DVVKLRGSVN PECTLAQLGA
    60 70 80 90 100
    AKMWRLLHGE SKKGYINSLG ALTGGQALQQ AKAGIEAVYL SGWQVAADAN
    110 120 130 140 150
    LAASMYPDQS LYPANSVPAV VERINNTFRR ADQIQWSAGI EPGDPRYVDY
    160 170 180 190 200
    FLPIVADAEA GFGGVLNAFE LMKAMIEAGA AAVHFEDQLA SVKKCGHMGG
    210 220 230 240 250
    KVLVPTQEAI QKLVAARLAA DVTGVPTLLV ARTDADAADL ITSDCDPYDS
    260 270 280 290 300
    EFITGERTSE GFFRTHAGIE QAISRGLAYA PYADLVWCET STPDLELARR
    310 320 330 340 350
    FAQAIHAKYP GKLLAYNCSP SFNWQKNLDD KTIASFQQQL SDMGYKFQFI
    360 370 380 390 400
    TLAGIHSMWF NMFDLANAYA QGEGMKHYVE KVQQPEFAAA KDGYTFVSHQ
    410 420 430
    QEVGTGYFDK VTTIIQGGTS SVTALTGSTE ESQF
    Length:434
    Mass (Da):47,522
    Last modified:July 19, 2005 - 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:iF66449CCD1E168E9
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti101 – 117LAASM…PANSV → WRPACIRISRSIRQTRC in CAA30416 (PubMed:3290857).CuratedAdd BLAST17
    Sequence conflicti215A → P in CAA30416 (PubMed:3290857).Curated1
    Sequence conflicti293P → R in AAA24009 (PubMed:2836370).Curated1
    Sequence conflicti338Q → E in CAA30416 (PubMed:3290857).Curated1
    Sequence conflicti419 – 434TSSVT…EESQF → DVFSHRADRLH (PubMed:3049537).CuratedAdd BLAST16

    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
    X12431 Genomic DNA Translation: CAA30974.1
    X07543 Genomic DNA Translation: CAA30416.1
    M22621 Genomic DNA Translation: AAC13650.1
    U00006 Genomic DNA Translation: AAC43109.1
    U00096 Genomic DNA Translation: AAC76985.1
    AP009048 Genomic DNA Translation: BAE78017.1
    M20714 Genomic DNA Translation: AAA24009.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S05692 WZECIC

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_418439.1, NC_000913.3
    WP_000857856.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC76985; AAC76985; b4015
    BAE78017; BAE78017; BAE78017

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    948517

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW3975
    eco:b4015

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.2698

    <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
    X12431 Genomic DNA Translation: CAA30974.1
    X07543 Genomic DNA Translation: CAA30416.1
    M22621 Genomic DNA Translation: AAC13650.1
    U00006 Genomic DNA Translation: AAC43109.1
    U00096 Genomic DNA Translation: AAC76985.1
    AP009048 Genomic DNA Translation: BAE78017.1
    M20714 Genomic DNA Translation: AAA24009.1
    PIRiS05692 WZECIC
    RefSeqiNP_418439.1, NC_000913.3
    WP_000857856.1, NZ_LN832404.1

    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
    1IGWX-ray2.10A/B/C/D1-434[»]
    ProteinModelPortaliP0A9G6
    SMRiP0A9G6
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4263469, 7 interactors
    DIPiDIP-35893N
    IntActiP0A9G6, 3 interactors
    STRINGi316385.ECDH10B_4204

    2D gel databases

    SWISS-2DPAGEiP0A9G6

    Proteomic databases

    EPDiP0A9G6
    PaxDbiP0A9G6
    PRIDEiP0A9G6

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76985; AAC76985; b4015
    BAE78017; BAE78017; BAE78017
    GeneIDi948517
    KEGGiecj:JW3975
    eco:b4015
    PATRICifig|1411691.4.peg.2698

    Organism-specific databases

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

    More...
    EchoBASEi
    EB0021
    EcoGeneiEG10022 aceA

    Phylogenomic databases

    eggNOGiENOG4108I9X Bacteria
    COG2224 LUCA
    HOGENOMiHOG000238475
    InParanoidiP0A9G6
    KOiK01637
    PhylomeDBiP0A9G6

    Enzyme and pathway databases

    UniPathwayi
    UPA00703;UER00719

    BioCyciEcoCyc:ISOCIT-LYASE-MONOMER
    MetaCyc:ISOCIT-LYASE-MONOMER
    BRENDAi4.1.3.1 2026
    SABIO-RKiP0A9G6

    Miscellaneous databases

    EvolutionaryTraceiP0A9G6

    Protein Ontology

    More...
    PROi
    PR:P0A9G6

    Family and domain databases

    CDDicd00377 ICL_PEPM, 1 hit
    InterProiView protein in InterPro
    IPR039556 ICL/PEPM
    IPR006254 Isocitrate_lyase
    IPR018523 Isocitrate_lyase_ph_CS
    IPR015813 Pyrv/PenolPyrv_Kinase-like_dom
    PANTHERiPTHR21631 PTHR21631, 1 hit
    PfamiView protein in Pfam
    PF00463 ICL, 2 hits
    PIRSFiPIRSF001362 Isocit_lyase, 1 hit
    SUPFAMiSSF51621 SSF51621, 1 hit
    TIGRFAMsiTIGR01346 isocit_lyase, 2 hits
    PROSITEiView protein in PROSITE
    PS00161 ISOCITRATE_LYASE, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    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 nameiACEA_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: P0A9G6
    Secondary accession number(s): P05313, Q2M6T9
    <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: July 19, 2005
    Last sequence update: July 19, 2005
    Last modified: December 5, 2018
    This is version 109 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, Direct protein sequencing, Reference proteome

    Documents

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