Q81F27 · ILVC2_BACCR
- ProteinKetol-acid reductoisomerase (NADP(+)) 2
- GeneilvC2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids335 (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 + H+ + NADPH
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 | 24-27 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: YGSQ | ||||||
Binding site | 47 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 51 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 81-84 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: DEQQ | ||||||
Active site | 106 | |||||
Sequence: H | ||||||
Binding site | 132 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 189 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 189 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 193 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 225 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 229 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 250 | substrate | ||||
Sequence: S |
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(+)) 2
- EC number
- Short namesKARI 2
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus > Bacillus cereus group
Accessions
- Primary accessionQ81F27
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000151275 | 1-335 | Ketol-acid reductoisomerase (NADP+) 2 | |||
Sequence: MKTYYEKDANVELLQGKTVAVVGYGSQGHAQAQNLRDSGVEVVVGVRPGKSYEVAKADGFEVMSVSEAVRTAQVVQMLLPDEQQAHVYKAEVEENLREGQMLLFSHGFNIHFGQINPPSYVDVAMVAPKSPGHLVRRVFQEGNGVPALVAVHQDATGTALHVALAYAKGVGCTRAGVIETTFQEETETDLFGEQAVLCGGVTALVKAGFETLTEGGYRPEIAYFECLHELKLIVDLMYEGGLTTMRHSISDTAEFGDYVTGSRIVTDETKKEMKRVLTEIQQGEFAKKWILENQAGRPTYNAMKKAEQNHQLEKVGAELREMMSWIHAPKELVKK |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-180 | KARI N-terminal Rossmann | ||||
Sequence: MKTYYEKDANVELLQGKTVAVVGYGSQGHAQAQNLRDSGVEVVVGVRPGKSYEVAKADGFEVMSVSEAVRTAQVVQMLLPDEQQAHVYKAEVEENLREGQMLLFSHGFNIHFGQINPPSYVDVAMVAPKSPGHLVRRVFQEGNGVPALVAVHQDATGTALHVALAYAKGVGCTRAGVIET | ||||||
Domain | 181-326 | KARI C-terminal knotted | ||||
Sequence: TFQEETETDLFGEQAVLCGGVTALVKAGFETLTEGGYRPEIAYFECLHELKLIVDLMYEGGLTTMRHSISDTAEFGDYVTGSRIVTDETKKEMKRVLTEIQQGEFAKKWILENQAGRPTYNAMKKAEQNHQLEKVGAELREMMSWI |
Sequence similarities
Belongs to the ketol-acid reductoisomerase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length335
- Mass (Da)36,921
- Last updated2003-06-01 v1
- Checksum07741D1B931B3E9F
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE016877 EMBL· GenBank· DDBJ | AAP08753.1 EMBL· GenBank· DDBJ | Genomic DNA |