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UniProtKB - P08200 (IDH_ECOLI)

Entry version 188 (23 Feb 2022)
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 bindingi307MagnesiumCombined 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

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.1.1.42, 2026
2.7.11.5, 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
BRENDAi1.1.1.42, 2026
2.7.11.5, 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

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: February 23, 2022
This is version 188 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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