A0A263NLH2 · A0A263NLH2_9PSED
- Protein3-isopropylmalate dehydrogenase
- GeneleuB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids360 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Catalytic activity
- (2R,3S)-3-isopropylmalate + NAD+ = 4-methyl-2-oxopentanoate + CO2 + NADH
Cofactor
Protein has several cofactor binding sites:
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Binds 1 Mg2+ or Mn2+ ion per subunit.
Pathway
Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 76-89 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GPKWDKIERDIRPE | ||||||
Binding site | 96 | substrate | ||||
Sequence: R | ||||||
Binding site | 106 | substrate | ||||
Sequence: R | ||||||
Binding site | 134 | substrate | ||||
Sequence: R | ||||||
Site | 141 | Important for catalysis | ||||
Sequence: Y | ||||||
Site | 192 | Important for catalysis | ||||
Sequence: K | ||||||
Binding site | 224 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 224 | substrate | ||||
Sequence: D | ||||||
Binding site | 248 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 252 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 282-294 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GSAPDIAGQGIAN |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 3-isopropylmalate dehydrogenase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | NAD binding | |
Biological Process | L-leucine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name3-isopropylmalate dehydrogenase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionA0A263NLH2
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-353 | Isopropylmalate dehydrogenase-like | ||||
Sequence: QILILPGDGIGPEIMAEAVKVLELANSKYSLGFELSHDVIGGAAIDKHGVPLADETLDRARAADAVLLGAVGGPKWDKIERDIRPERGLLKIRAQLGLFGNLRPAILYPQLADASSLKPEVVAGLDILIVRELTGGIYFGSPRGVRTLENGERQAYDTLPYSESEIRRIARVGFDMARVRGKKVCSVDKANVLASSQLWREIVEEVAKDYPDVELSHMYVDNAAMQLVRAPKQFDVIVTDNLFGDILSDQASMLTGSIGMLPSASLDTHNKGMYEPCHGSAPDIAGQGIANPLATILSVSMMLRYSFNLSDAADAIEKAVSLVLDQGLRTGDIWSQGCTKIGTQEMGDAV |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length360
- Mass (Da)38,785
- Last updated2017-12-20 v1
- Checksum814D52CCFCF2B682