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UniProtKB - P08200 (IDH_ECOLI)

Entry version 186 (07 Apr 2021)
Sequence version 1 (01 Aug 1988)
Previous versions | rss
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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%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 '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 Publication, Mn2+Note: Binds 1 Mg2+ or Mn2+ ion per subunit.2 Publications

<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

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.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

  1. KM=11.4 µM for isocitrate1 Publication
  2. KM=13 µM for isocitrate1 Publication

    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 sitei104NADPCombined sources3 Publications1
    Binding sitei113SubstrateCombined sources2 Publications1
    Binding sitei115SubstrateCombined sources2 Publications1
    Binding sitei119SubstrateCombined sources2 Publications1
    Binding sitei129SubstrateCombined sources2 Publications1
    Binding sitei153SubstrateCombined sources2 Publications1
    <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 catalysis2 Publications1
    Sitei230Critical for catalysis2 Publications1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 manganeseCombined sources3 Publications1
    Binding sitei352NADP; via amide nitrogen and carbonyl oxygenCombined sources3 Publications1
    Binding sitei391NADPCombined sources3 Publications1
    Binding sitei395NADPCombined sources3 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 – 345NADPCombined sources3 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

    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 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%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:
    Isocitrate dehydrogenase [NADP] (EC:1.1.1.424 Publications)
    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%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:icd
    Synonyms:icdA, icdE
    Ordered Locus Names:b1136, JW1122
    <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

    <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>Mutagenesisi100K → R or E: Abolishes enzymatic activity. 1 Publication1
    Mutagenesisi113S → A or T: Decreased enzyme activity. Loss of phosphorylation. 1 Publication1
    Mutagenesisi113S → D or E: Reduced affinity for isocitrate. 1 Publication1
    Mutagenesisi113S → D: Loss of enzyme activity. 1 Publication1
    Mutagenesisi160Y → F: Nearly abolishes enzyme activity. No significant effect on substrate affinity. 2 Publications1
    Mutagenesisi230K → M: Nearly abolishes enzyme activity and strongly reduces 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    		DB02190, (S)-oxalosuccinic acid
    DB04279, 3-Isopropylmalic Acid
    DB01727, Isocitric Acid
    DB03461, Nicotinamide adenine dinucleotide phosphate

    <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_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 residuei113Phosphoserine2 Publications1
    Modified residuei142N6-acetyllysine1 Publication1
    Modified residuei242N6-succinyllysine1 Publication1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		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%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.

    4 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		4263056, 28 interactors
    850074, 1 interactor

    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    		511145.b1136

    <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

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

    More...    SMRi    		P08200

    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    		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

    Belongs to the isocitrate and isopropylmalate dehydrogenases family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		COG0538, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_031953_7_1_6

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P08200

    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%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.

    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_CP047127.1

    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_CP047127.1

    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[»]
    SMRiP08200
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4263056, 28 interactors
    850074, 1 interactor
    DIPiDIP-10006N
    IntActiP08200, 6 interactors
    STRINGi511145.b1136

    Chemistry databases

    DrugBankiDB02190, (S)-oxalosuccinic acid
    DB04279, 3-Isopropylmalic Acid
    DB01727, Isocitric Acid
    DB03461, Nicotinamide adenine dinucleotide phosphate

    PTM databases

    iPTMnetiP08200

    2D gel databases

    SWISS-2DPAGEiP08200

    Proteomic databases

    jPOSTiP08200
    PaxDbiP08200
    PRIDEiP08200

    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

    Phylogenomic databases

    eggNOGiCOG0538, Bacteria
    HOGENOMiCLU_031953_7_1_6
    InParanoidiP08200
    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

    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 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%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: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: April 7, 2021
    This is version 186 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, 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
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