Q13584 · Q13584_HUMAN
- ProteinIsocitrate dehydrogenase [NADP]
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids419 (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 | 82-84 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: TIT | ||||||
Binding site | 84 | D-threo-isocitrate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 89 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 101-107 | D-threo-isocitrate (UniProtKB | ChEBI) | ||||
Sequence: SPNGTIR | ||||||
Binding site | 116 | D-threo-isocitrate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 139 | D-threo-isocitrate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Site | 146 | Critical for catalysis | ||||
Sequence: Y | ||||||
Site | 218 | Critical for catalysis | ||||
Sequence: K | ||||||
Binding site | 258 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 266 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 281 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 316-321 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: GTVTRH | ||||||
Binding site | 334 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
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 | NADP 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
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ13584
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 21-408 | Isopropylmalate dehydrogenase-like | ||||
Sequence: HVEAHCLAQRPALAHCDDVTDLDVQLKYFDLGLPNRDQTDDQVTIDSALATQKYSVAVKCATITPDEARVEEFKLKKMWKSPNGTIRNIHGGTVFREPIICKNIPRLVPGWTKPITIGRHAHGDQYKATDFVADRAGTFKMVFTPKDGSGVKEWEVYNFPAGGVGMGMYNTDESISGFAHSCFQYAIQKKWPLYMSTKNTILKAYDGRFKDIFQEIFDKHYKTDFDKNKIWYEHRLIDDMVAQVLKSSGGFVWACKNYDGDVQSDILAQGFGSLGLMTSVLVCPDGKTIEAEAAHGTVTRHYREHQKGRPTSTNPIASIFAWTRGLEHRGKLDGNQDLIRFAQMLEKVCVETVESGAMTKDLAGCIHGLSNVKLNEHFLNTTDFLDTI |
Sequence similarities
Belongs to the isocitrate and isopropylmalate dehydrogenases family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length419
- Mass (Da)46,815
- Last updated1996-11-01 v1
- ChecksumDECFA62AA0DB5E7C