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Protein

Isocitrate dehydrogenase [NADP]

Gene

icd

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

<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+, Mn2+Note: Binds 1 Mg2+ or Mn2+ ion per subunit.

<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

Inhibition of this enzyme by phosphorylation regulates the branch point between the Krebs cycle and the glyoxylate bypass, which is an alternate route that accumulates carbon for biosynthesis when acetate is the sole carbon source for growth.

<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

  1. KM=11.4 µM for isocitrate1 Publication

    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 sitei104NADP3 Publications1
    Binding sitei113Substrate1 Publication1
    Binding sitei115Substrate1
    Binding sitei119Substrate1
    Binding sitei129Substrate1
    Binding sitei153Substrate1
    <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>Sitei160Critical for catalysis1
    Sitei230Critical for catalysis1
    <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 bindingi307Magnesium or manganese3 Publications1
    Binding sitei352NADP; via amide nitrogen and carbonyl oxygen3 Publications1
    Binding sitei391NADP3 Publications1
    Binding sitei395NADP3 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi339 – 345NADP3 Publications7

    <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

    • isocitrate dehydrogenase (NADP+) activity Source: UniProtKB
    • magnesium ion binding Source: InterPro
    • NAD binding Source: InterPro

    GO - Biological processi

    • electron transport chain Source: EcoliWiki
    • glyoxylate cycle Source: UniProtKB-KW
    • response to oxidative stress Source: EcoCyc
    • 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 functionOxidoreductase
    Biological processGlyoxylate bypass, Tricarboxylic acid cycle
    LigandMagnesium, Manganese, Metal-binding, NADP

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:ISOCITDEH-SUBUNIT
    MetaCyc:ISOCITDEH-SUBUNIT

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.1.1.42 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P08200

    <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 dehydrogenase [NADP] (EC:1.1.1.42)
    Short name:
    IDH
    Alternative name(s):
    IDP
    NADP(+)-specific ICDH
    Oxalosuccinate decarboxylase
    <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:icd
    Synonyms:icdA, icdE
    Ordered Locus Names:b1136, JW1122
    <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
    EG10489 icd

    <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

    <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>Mutagenesisi100K → R or E: Abolishes enzymatic activity. 1 Publication1
    Mutagenesisi113S → D or E: Reduced affinity for isocitrate. 1 Publication1
    Mutagenesisi160Y → F: Large decrease in activity and a small increase in substrate affinity. 2 Publications1
    Mutagenesisi230K → M: Decrease in activity and substrate affinity. 2 Publications1
    Mutagenesisi242K → E: Strongly impairs enzymatic activity. 1 Publication1
    Mutagenesisi242K → R: Impairs enzymatic activity. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB03461 2'-Monophosphoadenosine 5'-Diphosphoribose
    DB02190 2-Oxalosuccinic Acid
    DB04279 3-Isopropylmalic Acid
    DB01848 Isocitrate Calcium Complex
    DB01727 Isocitric 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000835511 – 416Isocitrate dehydrogenase [NADP]Add BLAST416

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei100N6-succinyllysine1 Publication1
    Modified residuei113Phosphoserine1 Publication1
    Modified residuei142N6-acetyllysine1 Publication1
    Modified residuei242N6-succinyllysine1 Publication1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Phosphorylation state of this enzyme is controlled by isocitrate dehydrogenase kinase/phosphatase (AceK).1 Publication
    Succinylation probably inhibits enzymatic activity.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P08200

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

    More...
    PaxDbi
    P08200

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P08200

    2D gel databases

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

    More...
    SWISS-2DPAGEi
    P08200

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P08200

    <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.4 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    aceKP110715EBI-369069,EBI-1112800

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4263056, 28 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-10006N

    Protein interaction database and analysis system

    More...
    IntActi
    P08200, 6 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    316385.ECDH10B_1208

    <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

    1416
    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
    P08200

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

    More...
    SMRi
    P08200

    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
    P08200

    <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

    <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
    ENOG4108HMX Bacteria
    COG0538 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000021113

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P08200

    KEGG Orthology (KO)

    More...
    KOi
    K00031

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P08200

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR019818 IsoCit/isopropylmalate_DH_CS
    IPR004439 Isocitrate_DH_NADP_dimer_prok
    IPR024084 IsoPropMal-DH-like_dom

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR43504 PTHR43504, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00180 Iso_dh, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM01329 Iso_dh, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00183 prok_nadp_idh, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00470 IDH_IMDH, 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.

    P08200-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MESKVVVPAQ GKKITLQNGK LNVPENPIIP YIEGDGIGVD VTPAMLKVVD
    60 70 80 90 100
    AAVEKAYKGE RKISWMEIYT GEKSTQVYGQ DVWLPAETLD LIREYRVAIK
    110 120 130 140 150
    GPLTTPVGGG IRSLNVALRQ ELDLYICLRP VRYYQGTPSP VKHPELTDMV
    160 170 180 190 200
    IFRENSEDIY AGIEWKADSA DAEKVIKFLR EEMGVKKIRF PEHCGIGIKP
    210 220 230 240 250
    CSEEGTKRLV RAAIEYAIAN DRDSVTLVHK GNIMKFTEGA FKDWGYQLAR
    260 270 280 290 300
    EEFGGELIDG GPWLKVKNPN TGKEIVIKDV IADAFLQQIL LRPAEYDVIA
    310 320 330 340 350
    CMNLNGDYIS DALAAQVGGI GIAPGANIGD ECALFEATHG TAPKYAGQDK
    360 370 380 390 400
    VNPGSIILSA EMMLRHMGWT EAADLIVKGM EGAINAKTVT YDFERLMDGA
    410
    KLLKCSEFGD AIIENM
    Length:416
    Mass (Da):45,757
    Last modified:August 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:i9A02E707C3B4FDD9
    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
    J02799 Genomic DNA Translation: AAA24006.1
    U00096 Genomic DNA Translation: AAC74220.1
    AP009048 Genomic DNA Translation: BAA35958.1
    AF017587 Genomic DNA Translation: AAC45887.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A28482 DCECIS

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_415654.1, NC_000913.3
    WP_000444484.1, NZ_CP010440.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC74220; AAC74220; b1136
    BAA35958; BAA35958; BAA35958

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    945702

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW1122
    eco:b1136

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|511145.12.peg.1183

    <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
    J02799 Genomic DNA Translation: AAA24006.1
    U00096 Genomic DNA Translation: AAC74220.1
    AP009048 Genomic DNA Translation: BAA35958.1
    AF017587 Genomic DNA Translation: AAC45887.1
    PIRiA28482 DCECIS
    RefSeqiNP_415654.1, NC_000913.3
    WP_000444484.1, NZ_CP010440.1

    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
    1AI2X-ray1.90A1-416[»]
    1AI3X-ray1.90A1-416[»]
    1BL5X-ray2.50A3-416[»]
    1CW1X-ray2.10A1-416[»]
    1CW4X-ray2.10A1-416[»]
    1CW7X-ray2.60A1-416[»]
    1GROX-ray2.50A1-416[»]
    1GRPX-ray2.50A1-416[»]
    1HJ6X-ray2.00A1-416[»]
    1IDCX-ray2.50A1-416[»]
    1IDDX-ray2.50A1-416[»]
    1IDEX-ray2.50A1-416[»]
    1IDFX-ray2.50A1-416[»]
    1IKAX-ray2.70A1-416[»]
    1ISOX-ray1.90A1-416[»]
    1P8FX-ray1.85A1-416[»]
    1PB1X-ray1.70A1-416[»]
    1PB3X-ray1.70A1-416[»]
    1SJSX-ray2.42A1-416[»]
    3ICDX-ray2.50A1-416[»]
    3LCBX-ray2.90C/D1-416[»]
    4AJ3X-ray1.90A1-416[»]
    4AJAX-ray1.80A1-416[»]
    4AJBX-ray1.90A1-416[»]
    4AJCX-ray2.30A1-416[»]
    4AJRX-ray2.69A1-416[»]
    4AJSX-ray1.80A1-416[»]
    4BNPX-ray2.00A1-416[»]
    4ICDX-ray2.50A1-416[»]
    4P69X-ray3.30C/D2-416[»]
    5ICDX-ray2.50A1-416[»]
    6ICDX-ray2.80A1-416[»]
    7ICDX-ray2.40A1-416[»]
    8ICDX-ray2.50A1-416[»]
    9ICDX-ray2.50A1-416[»]
    ProteinModelPortaliP08200
    SMRiP08200
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4263056, 28 interactors
    DIPiDIP-10006N
    IntActiP08200, 6 interactors
    STRINGi316385.ECDH10B_1208

    Chemistry databases

    DrugBankiDB03461 2'-Monophosphoadenosine 5'-Diphosphoribose
    DB02190 2-Oxalosuccinic Acid
    DB04279 3-Isopropylmalic Acid
    DB01848 Isocitrate Calcium Complex
    DB01727 Isocitric Acid

    PTM databases

    iPTMnetiP08200

    2D gel databases

    SWISS-2DPAGEiP08200

    Proteomic databases

    EPDiP08200
    PaxDbiP08200
    PRIDEiP08200

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74220; AAC74220; b1136
    BAA35958; BAA35958; BAA35958
    GeneIDi945702
    KEGGiecj:JW1122
    eco:b1136
    PATRICifig|511145.12.peg.1183

    Organism-specific databases

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

    More...
    EchoBASEi
    EB0484
    EcoGeneiEG10489 icd

    Phylogenomic databases

    eggNOGiENOG4108HMX Bacteria
    COG0538 LUCA
    HOGENOMiHOG000021113
    InParanoidiP08200
    KOiK00031
    PhylomeDBiP08200

    Enzyme and pathway databases

    BioCyciEcoCyc:ISOCITDEH-SUBUNIT
    MetaCyc:ISOCITDEH-SUBUNIT
    BRENDAi1.1.1.42 2026
    SABIO-RKiP08200

    Miscellaneous databases

    EvolutionaryTraceiP08200

    Protein Ontology

    More...
    PROi
    PR:P08200

    Family and domain databases

    InterProiView protein in InterPro
    IPR019818 IsoCit/isopropylmalate_DH_CS
    IPR004439 Isocitrate_DH_NADP_dimer_prok
    IPR024084 IsoPropMal-DH-like_dom
    PANTHERiPTHR43504 PTHR43504, 1 hit
    PfamiView protein in Pfam
    PF00180 Iso_dh, 1 hit
    SMARTiView protein in SMART
    SM01329 Iso_dh, 1 hit
    TIGRFAMsiTIGR00183 prok_nadp_idh, 1 hit
    PROSITEiView protein in PROSITE
    PS00470 IDH_IMDH, 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 nameiIDH_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: P08200
    <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: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: December 5, 2018
    This is version 172 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. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
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