Q0S2H3 · ILVC_RHOJR
- ProteinKetol-acid reductoisomerase (NADP(+))
- GeneilvC
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids337 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Catalytic activity
- (2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-acetolactate + NADPH + H+
Cofactor
Note: Binds 2 magnesium ions per subunit.
Pathway
Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4.
Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 26-29 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 49 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 52 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 54 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 84-87 | NADP+ (UniProtKB | ChEBI) | |||
Active site | 109 | ||||
Binding site | 135 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 192 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 192 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 196 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 228 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 232 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 253 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ketol-acid reductoisomerase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | NADP binding | |
Biological Process | isoleucine biosynthetic process | |
Biological Process | valine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameKetol-acid reductoisomerase (NADP(+))
- EC number
- Short namesKARI
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Nocardiaceae > Rhodococcus
Accessions
- Primary accessionQ0S2H3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000252778 | 1-337 | Ketol-acid reductoisomerase (NADP+) | ||
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 3-183 | KARI N-terminal Rossmann | |||
Domain | 184-329 | KARI C-terminal knotted | |||
Sequence similarities
Belongs to the ketol-acid reductoisomerase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length337
- Mass (Da)36,347
- Last updated2006-09-05 v1
- Checksum83F81AC97EFEDA81
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000431 EMBL· GenBank· DDBJ | ABG98263.1 EMBL· GenBank· DDBJ | Genomic DNA |