A0A5N8YBG6 · A0A5N8YBG6_9CHLR
- Protein3-isopropylmalate dehydrogenase
- GeneleuB
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids369 (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: GPKWDNPLAPHRPE | ||||||
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 | 191 | Important for catalysis | ||||
Sequence: K | ||||||
Binding site | 223 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 223 | substrate | ||||
Sequence: D | ||||||
Binding site | 247 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 251 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 291-303 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GSAPDIAGQGKAN |
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
- Strain
- Taxonomic lineageBacteria > Chloroflexota > Dehalococcoidia > SAR202 cluster
Accessions
- Primary accessionA0A5N8YBG6
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-363 | Isopropylmalate dehydrogenase-like | ||||
Sequence: NIALLPGDGVGPEVVAEGVRALKRVEELTDATFNLEYGQVGGIAIDEKGTPLPNEALELARRSDAILFGAVGGPKWDNPLAPHRPEDAILGLRKALGFFANLRPVKVIPALLNSSSVKPSVLEGVDMLVVRELTGGLYFARPKKRWQTSRGRRGVDTLRYTEAEIERVLRVGFELARRRRKKLTSVDKANVLESSRLWREIAIELSGQYPDVELEHMLVDSCAMALVRTPIRFDVLVAENLFGDILTDEAAILAGSLGMLPSSSLAGIPREDTGGHRRTLGLYEPIHGSAPDIAGQGKANPIATILSVALMLRYSLGHPNAASALEAAVESVLNQGYRTQDIAEEGSRDVLTTAEMGQRI |
Sequence similarities
Family and domain databases
Sequence
- Sequence statusComplete
- Length369
- Mass (Da)40,089
- Last updated2020-04-22 v1
- ChecksumC1E4489837A13B1F
Keywords
- Technical term