A0A1Y2T8U4 · A0A1Y2T8U4_SYMTR
- ProteinKetol-acid reductoisomerase (NADP(+))
- GeneilvC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids338 (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 | 25-28 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: FGSQ | ||||||
Binding site | 48 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 51 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 108 | |||||
Sequence: H | ||||||
Binding site | 134 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 191 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 191 | Mg2+ 1 (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 | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | isomerase activity | |
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
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Symbiobacteriaceae > Symbiobacterium
Accessions
- Primary accessionA0A1Y2T8U4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-182 | KARI N-terminal Rossmann | ||||
Sequence: TRLYYESDANLAVLQGKKIAVIGFGSQGHAHALNLKDSGLDVTVGLREGSPRWAQAEEAGLRVAPVAAAAEEADVIMLLINDEQQGQVFAEQIRPHLRPGKALGFGHGFAVHFGQVRPPADVDVFMIAPKGPGHLVRRQYLEGRGVPCLMAIHQDATGRCRDVALAWAKGIGGTRAGVIET | ||||||
Domain | 183-328 | KARI C-terminal knotted | ||||
Sequence: TFKEECESDLFGEQAVLCGGLTQLVKYGFEVLTEAGYAPEIAYFECLHELKLIVDLMYEGGMAAMRYSISDTAEYGDYVSGPRVIGPEVKERMKQILAEIQNGTFAKDWILENQVGRPRFTALRRQNAAHPIEQVGARLRAMMPWL |
Sequence similarities
Belongs to the ketol-acid reductoisomerase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length338
- Mass (Da)36,865
- Last updated2017-08-30 v1
- Checksum0842BFD3343586B4