A0A1J9PH62 · A0A1J9PH62_9BURK
- ProteinIsocitrate dehydrogenase [NADP]
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids418 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
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 | 106 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 115 | substrate | ||||
Sequence: S | ||||||
Binding site | 117 | substrate | ||||
Sequence: N | ||||||
Binding site | 121 | substrate | ||||
Sequence: R | ||||||
Binding site | 131 | substrate | ||||
Sequence: R | ||||||
Binding site | 155 | substrate | ||||
Sequence: R | ||||||
Site | 162 | Critical for catalysis | ||||
Sequence: Y | ||||||
Site | 232 | Critical for catalysis | ||||
Sequence: K | ||||||
Binding site | 309 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 341-347 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: HGTAPKY | ||||||
Binding site | 354 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 393 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 397 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R |
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
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Burkholderia > Burkholderia cepacia complex
Accessions
- Primary accessionA0A1J9PH62
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 102 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 115 | Phosphoserine | ||||
Sequence: S |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 30-414 | Isopropylmalate dehydrogenase-like | ||||
Sequence: IIPYIEGDGTGFDITPVMIKVVDAAVAHAYKGKRKIHWMEIFAGEKATKVYGPDVWLPDETLQVLKEYVVSIKGPLTTPVGGGIRSLNVALRQELDLYVCLRPVQYFKGVPSPVREPQKIDMVIFRENSEDIYAGIEWAAGSEQAKKVIKFLQDEMGVKKIRFPETSGIGVKPVSTEGTERLVRKAIQYAIDNDRKSVTLVHKGNIMKFTEGLFRDAGYALAQKEFGGELIDGGPWMRVKNPRTGNEIVIKDSIADAFLQQILLRPAEYDVIATLNLNGDYISDALAAQVGGIGIAPGANLSDSVAMFEATHGTAPKYAGKDYVNPGSEILSAEMMLRHLGWTEAADTIIASMEKSILQKRVTYDFARLMEGATQVSCSGFGEVL |
Sequence similarities
Belongs to the isocitrate and isopropylmalate dehydrogenases family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length418
- Mass (Da)45,947
- Last updated2017-02-15 v1
- Checksum5A882546B871A338