Q3TJ51 · Q3TJ51_MOUSE
- ProteinIsocitrate dehydrogenase [NADP]
- GeneIdh1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids414 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
Catalytic activity
- D-threo-isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH
Cofactor
Protein has several cofactor binding sites:
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Binds 1 Mg2+ or Mn2+ ion per subunit.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 75-77 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 77 | D-threo-isocitrate (UniProtKB | ChEBI) | |||
Binding site | 82 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 94-100 | D-threo-isocitrate (UniProtKB | ChEBI) | |||
Binding site | 109 | D-threo-isocitrate (UniProtKB | ChEBI) | |||
Binding site | 132 | D-threo-isocitrate (UniProtKB | ChEBI) | |||
Site | 139 | Critical for catalysis | |||
Site | 212 | Critical for catalysis | |||
Binding site | 252 | Mn2+ (UniProtKB | ChEBI) | |||
Binding site | 260 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 275 | Mn2+ (UniProtKB | ChEBI) | |||
Binding site | 310-315 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 328 | NADP+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | isocitrate dehydrogenase (NADP+) activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | NAD binding | |
Biological Process | glyoxylate cycle | |
Biological Process | isocitrate metabolic process | |
Biological Process | tricarboxylic acid cycle |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameIsocitrate dehydrogenase [NADP]
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ3TJ51
Organism-specific databases
PTM/Processing
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length414
- Mass (Da)46,674
- Last updated2005-10-11 v1
- Checksum3CA44545473F841D
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK167583 EMBL· GenBank· DDBJ | BAE39644.1 EMBL· GenBank· DDBJ | mRNA |