A0A101FKT4 · A0A101FKT4_9BACT
- ProteinDihydroxy-acid dehydratase
- GeneilvD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids554 (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 | 78 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 120 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 121 | Mg2+ (UniProtKB | ChEBI); via carbamate group | |||
Binding site | 442 | Mg2+ (UniProtKB | ChEBI) | |||
Active site | 468 | Proton acceptor | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
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
- Taxonomic lineageBacteria > Synergistota > Synergistia > Synergistales
Accessions
- Primary accessionA0A101FKT4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 121 | N6-carboxylysine | |||
Interaction
Structure
Sequence
- Sequence statusComplete
- Length554
- Mass (Da)58,808
- Last updated2016-04-13 v1
- MD5 ChecksumDD308A7E87617E7EE2A027A3343720B6
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LGFQ01000108 EMBL· GenBank· DDBJ | KUK38869.1 EMBL· GenBank· DDBJ | Genomic DNA |