B4RG67 · ILVC_PHEZH
- ProteinKetol-acid reductoisomerase (NADP(+))
- GeneilvC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids339 (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 | 24-27 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: YGSQ | ||||||
Binding site | 48 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 51 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 53 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 83-86 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: DELQ | ||||||
Active site | 108 | |||||
Sequence: H | ||||||
Binding site | 134 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 191 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 191 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 195 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 227 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 231 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 252 | substrate | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Caulobacterales > Caulobacteraceae > Phenylobacterium
Accessions
- Primary accessionB4RG67
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000124317 | 1-339 | Ketol-acid reductoisomerase (NADP+) | |||
Sequence: MRVYYDRDADLSRILDKKIAIVGYGSQGRAHALNLVDSGVKNVAVALRPGSATAKKVEADGLKVMSVAEASAWADAIMILAPDELQAQIYRDEIAPNIKDGAALLFAHGLNVHFGLIEPKKTVDVLMVAPKGPGHTVRGEYQKGGGVPCLIAVHHDATGGAMDFGLAYASAIGGGRSGVIETNFREECETDLFGEQAVLCGGLVELIRAGFETLVEAGYAPEMAYFECLHEVKLIVDLIYEGGIANMNYSISNTAEYGEYVTGPRIVTSETKAEMKRVLEDIQSGRFVRDFMQENAVGAPSFKATRRRNAEHPIEEVGGRLRAMMPWITKNKLVDTERN |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-182 | KARI N-terminal Rossmann | ||||
Sequence: MRVYYDRDADLSRILDKKIAIVGYGSQGRAHALNLVDSGVKNVAVALRPGSATAKKVEADGLKVMSVAEASAWADAIMILAPDELQAQIYRDEIAPNIKDGAALLFAHGLNVHFGLIEPKKTVDVLMVAPKGPGHTVRGEYQKGGGVPCLIAVHHDATGGAMDFGLAYASAIGGGRSGVIET | ||||||
Domain | 183-328 | KARI C-terminal knotted | ||||
Sequence: NFREECETDLFGEQAVLCGGLVELIRAGFETLVEAGYAPEMAYFECLHEVKLIVDLIYEGGIANMNYSISNTAEYGEYVTGPRIVTSETKAEMKRVLEDIQSGRFVRDFMQENAVGAPSFKATRRRNAEHPIEEVGGRLRAMMPWI |
Sequence similarities
Belongs to the ketol-acid reductoisomerase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length339
- Mass (Da)36,775
- Last updated2008-09-23 v1
- ChecksumF9DD1F0D12105AC2
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000747 EMBL· GenBank· DDBJ | ACG77191.1 EMBL· GenBank· DDBJ | Genomic DNA |