A0A9X4NII1 · A0A9X4NII1_9LACT
- ProteinDihydroxy-acid dehydratase
- GeneilvD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids570 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
Catalytic activity
- (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2OThis reaction proceeds in the forward direction.
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Pathway
Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 3/4.
Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 3/4.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 61 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 94 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 136 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 137 | Mg2+ (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 459 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 485 | Proton acceptor | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | dihydroxy-acid dehydratase 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 nameDihydroxy-acid dehydratase
- EC number
- Short namesDAD
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Lactococcus
Accessions
- Primary accessionA0A9X4NII1
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 137 | N6-carboxylysine | ||||
Sequence: K |
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length570
- Mass (Da)60,692
- Last updated2023-11-08 v1
- ChecksumB2701C3043AB6508