A0A836XKE2 · A0A836XKE2_9GAMM
- ProteinIsocitrate dehydrogenase [NADP]
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids417 (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 | 105 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 114 | substrate | ||||
Sequence: S | ||||||
Binding site | 116 | substrate | ||||
Sequence: N | ||||||
Binding site | 120 | substrate | ||||
Sequence: R | ||||||
Binding site | 130 | substrate | ||||
Sequence: R | ||||||
Binding site | 154 | substrate | ||||
Sequence: R | ||||||
Site | 161 | Critical for catalysis | ||||
Sequence: Y | ||||||
Site | 231 | Critical for catalysis | ||||
Sequence: K | ||||||
Binding site | 308 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 340-346 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: HGTAPKY | ||||||
Binding site | 353 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 392 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 396 | 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
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Cellvibrionales > Porticoccaceae
Accessions
- Primary accessionA0A836XKE2
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 101 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 114 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 143 | N6-acetyllysine | ||||
Sequence: K |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 30-413 | Isopropylmalate dehydrogenase-like | ||||
Sequence: IIPFIEGDGIGIDITPVMVKVIDAAVAKAYDGQKKISWMEVFCGEKAAELYEGDWFPAETLEAVKEYIVSIKGPLTTPVGGGFRSLNVALRQELDLFVCQRPVRWFSGVPSPVKEPNKVDMCIFRENSEDIYAGIEWKAGSDEATKVIKFLQDEMKVTKIRFDTNCGIGVKPVSEEGTKRLVTKAIQYAIDQNKPSVTLVHKGNIMKFTEGAFCDWGYEVARESFGGEPLDGGPWHTVKNPNTGEDIVIKDVIADAMLQQIILRPDEYSVLATLNLNGDYISDALAAQVGGIGIAPGANLSDDIAIFEATHGTAPKYAGQDKVNPGSLILSAEMMLRHLGWGDAADLVIKGIEGAITEKKVTYDFERLMDDAILMSCSEFGDAM |
Sequence similarities
Belongs to the isocitrate and isopropylmalate dehydrogenases family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length417
- Mass (Da)45,546
- Last updated2021-09-29 v1
- ChecksumD248A64B519D2C2B