A0A510DUY9 · A0A510DUY9_9CREN
- ProteinKetol-acid reductoisomerase (NADP(+))
- GeneilvC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids335 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 | 28-31 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: YGNQ | ||||||
Binding site | 56 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 111 | |||||
Sequence: H | ||||||
Binding site | 137 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 194 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 194 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 198 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 230 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 234 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 255 | substrate | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ketol-acid reductoisomerase activity | |
Molecular Function | magnesium ion 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
- Strains
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Sulfolobales > Sulfolobaceae > Sulfuracidifex
Accessions
- Primary accessionA0A510DUY9
- Secondary accessions
Proteomes
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-185 | KARI N-terminal Rossmann | ||||
Sequence: AKIYTDKDASLDALKGKKIAVLGYGNQGRAWALNLRDSGLDVTVGLERQGKSWEKATKDGFTPVKTDEAVRNAEVIIFLVPDMIQRTIWLEKVKPNMKKGADLVFAHGFNIHFRMIEPPADSDVYMVAPKGPGDTVRDYYVAGGGVPVLVAAYQNVSGKAMEKALAVAKGIGATRSGALES | ||||||
Domain | 186-331 | KARI C-terminal knotted | ||||
Sequence: SFKEETETDLVGEQTILVGGIMELMRASFETLVEMGYQPEVAYFETINEVKMIVDIIHSKGLSGMLRAVSDTAKYGGMTVGKKVINEDVRKRIREAAERVRDGQFASEWVEEYNRGMPTVVNGLKEVDNSLEQKVANELRDLIERG |
Sequence similarities
Belongs to the ketol-acid reductoisomerase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length335
- Mass (Da)36,889
- Last updated2019-10-16 v1
- ChecksumE5EDD717F07E845D
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP018929 EMBL· GenBank· DDBJ | BBG23997.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP018930 EMBL· GenBank· DDBJ | BBG26752.1 EMBL· GenBank· DDBJ | Genomic DNA |