Q0IDM2 · Q0IDM2_SYNS3
- ProteinIsocitrate dehydrogenase [NADP]
- Geneicd
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids482 (go to sequence)
- Protein existenceInferred from homology
- 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 | 114 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 123 | D-threo-isocitrate (UniProtKB | ChEBI) | |||
Binding site | 125 | D-threo-isocitrate (UniProtKB | ChEBI) | |||
Binding site | 129 | D-threo-isocitrate (UniProtKB | ChEBI) | |||
Binding site | 139 | D-threo-isocitrate (UniProtKB | ChEBI) | |||
Binding site | 163 | D-threo-isocitrate (UniProtKB | ChEBI) | |||
Site | 170 | Critical for catalysis | |||
Site | 247 | Critical for catalysis | |||
Binding site | 372 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 417 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 456 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 460 | 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 | 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
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Synechococcales > Synechococcaceae > Synechococcus
Accessions
- Primary accessionQ0IDM2
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 110 | N6-succinyllysine | |||
Modified residue | 123 | Phosphoserine | |||
Modified residue | 152 | N6-acetyllysine | |||
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 38-478 | Isopropylmalate dehydrogenase-like | |||
Sequence similarities
Belongs to the isocitrate and isopropylmalate dehydrogenases family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length482
- Mass (Da)53,127
- Last updated2006-10-03 v1
- Checksum86A645DB97E388D4
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000435 EMBL· GenBank· DDBJ | ABI45038.1 EMBL· GenBank· DDBJ | Genomic DNA |