A0A2Z2HPS4 · A0A2Z2HPS4_9EURY
- ProteinDihydroxy-acid dehydratase
- GeneilvD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids574 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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 | 60 | [2Fe-2S] cluster (UniProtKB | ChEBI) | |||
Binding site | 92 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 134 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 135 | Mg2+ (UniProtKB | ChEBI); via carbamate group | |||
Binding site | 459 | Mg2+ (UniProtKB | ChEBI) | |||
Active site | 485 | Proton acceptor | |||
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 lineageArchaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Natrialbaceae > Natrarchaeobaculum
Accessions
- Primary accessionA0A2Z2HPS4
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 135 | N6-carboxylysine | |||
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-25 | Basic and acidic residues | |||
Region | 1-26 | Disordered | |||
Sequence similarities
Belongs to the IlvD/Edd family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length574
- Mass (Da)60,453
- Last updated2018-10-10 v1
- MD5 ChecksumDB55FD67A7A0B44911B72A640C2E50A8
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-25 | Basic and acidic residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP019893 EMBL· GenBank· DDBJ | ARS88573.1 EMBL· GenBank· DDBJ | Genomic DNA |