P50215 · IDH_SPHYA
- ProteinIsocitrate dehydrogenase [NADP]
- Geneicd
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids406 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and carbon dioxide with the concomitant reduction of NADP+.
Catalytic activity
- D-threo-isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH
Cofactor
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 | 72 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 75 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 77 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 82 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 94 | D-threo-isocitrate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 96 | D-threo-isocitrate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 100 | D-threo-isocitrate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 110 | D-threo-isocitrate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 132 | D-threo-isocitrate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Site | 139 | Critical for catalysis | ||||
Sequence: Y | ||||||
Site | 210 | Critical for catalysis | ||||
Sequence: K | ||||||
Binding site | 250 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 273 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 277 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 308 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 309 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 310 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 313 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 326 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: N |
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
- Short namesIDH
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Sphingobium
Accessions
- Primary accessionP50215
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000083567 | 1-406 | Isocitrate dehydrogenase [NADP] | |||
Sequence: MAKIKVKNPVVEIDGDEMTRIIWEWIRERLILPYLDVDLKYYDLSVEKRDETSDQITIDAANAIKEYGVGVKCATITPDEARVEEFGLKKMWKSPNGTIRNILGGVVFREPIVIKNVPRLVPGWTDPIVVGRHAFGDQYKATDFKVPGAGTLTMKWVGTNGEELEYEVFEFPSAGVAMGMYNLDESIRDFAKASFNYGLNRGWPVYLSTKNTILKAYDGRFKDLFQEVFDAEFADKFKAAGIVYEHRLIDDMVASALKWSGKFVWACKNYDGDVQSDTVAQGFGSLGLMTSVLLSPDGKTVEAEAAHGTVTRHYRQHQQGKATSTNPIASIFAWTQGLSFRGKFDDTPDVVKFAETLEQVCIKTVEGGAMTKDLALLIGPDQAWMTTEQFFEAIRVNLEAEMAKWA |
Interaction
Structure
Sequence
- Sequence statusComplete
- Length406
- Mass (Da)45,483
- Last updated1996-10-01 v1
- Checksum093F7E18303A89E7