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Protein

Isocitrate dehydrogenase [NADP] cytoplasmic

Gene

IDH1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH.

GO - Molecular functioni

  1. isocitrate dehydrogenase (NADP+) activity Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB

GO - Biological processi

  1. 2-oxoglutarate metabolic process Source: UniProtKB
  2. isocitrate metabolic process Source: UniProtKB
  3. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Isocitrate dehydrogenase [NADP] cytoplasmic (EC:1.1.1.42)
Short name:
IDH
Alternative name(s):
Cytosolic NADP-isocitrate dehydrogenase
IDP
NADP(+)-specific ICDH
Oxalosuccinate decarboxylase
Gene namesi
Name:IDH1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›13›13Isocitrate dehydrogenase [NADP] cytoplasmicPRO_0000083579Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Sequencei

Sequence statusi: Fragment.

P20304-1 [UniParc]FASTAAdd to Basket

« Hide

        10 
DLAGEIHGLS NVK
Length:13
Mass (Da):1,353
Last modified:February 1, 1991 - v1
Checksum:i1B640F0E9F7C71E0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei13 – 131

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "Isolation of the glutamyl peptide labeled by the nucleotide analogue 2-(4-bromo-2,3-dioxobutylthio)-1,N(6)-ethenoadenosine 2',5'-biphosphate in the active site of NADP+-specific isocitrate dehydrogenase."
    Bailey J.M., Colman R.F.
    J. Biol. Chem. 262:12620-12626(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "Characterization of an active site peptide modified by the substrate analogue 3-bromo-2-ketoglutarate on a single chain of dimeric NADP+-dependent isocitrate dehydrogenase."
    Ehrlich R.S., Colman R.F.
    J. Biol. Chem. 262:12614-12619(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.

Entry informationi

Entry nameiIDHC_PIG
AccessioniPrimary (citable) accession number: P20304
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: January 7, 2015
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.