A6W1Q9 · ILVD_MARMS
- ProteinDihydroxy-acid dehydratase
- GeneilvD
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids614 (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 | 81 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 122 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 123 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 124 | Mg2+ (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 193 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 489 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 515 | 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 > Pseudomonadota > Gammaproteobacteria > Oceanospirillales > Oceanospirillaceae > Marinomonas
Accessions
- Primary accessionA6W1Q9
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000073980 | 1-614 | Dihydroxy-acid dehydratase | |||
Sequence: MPVYRSKTTTSGRNMAGARALWRATGMTDDDFQKPIIAVVNSFTQFVPGHVHLKDMGQLVAREIEAAGGVAKEFNTIAVDDGIAMGHDGMLYSLPSRDLIADSVEYMVNAHCADAMVCISNCDKITPGMLMAAMRINIPVIFVSGGPMEAGKTKLSENKLDLVDAMVIAADPTATDERVAEYERSACPTCGSCSGMFTANSMNCLTEALGLSLPGNGTTLATHSDRRRLFLDAGRRIVDITKRYYENDEANWAPRSIASFEAFENAMTLDIAMGGSTNTILHLLAIAREAGVDFSMEDIDRLSRKVPQLCKVAPNSPKYHVEDVHRAGGIFALLGELDRGGILHNQCHTVHSKTMLEALKSWDIMRSPTPEIIEFYKAGPAGIPTQTAFSQSTRWPSLDGDRAEGCIRSIENAFSLEGGLAVLYGNIAVDGCVVKSAGVDESILVFEGRAHVTESQDEAVKNILDDKVEAGDIVIVRYEGPKGGPGMQEMLYPTSYIKSKGLGKACALLTDGRFSGGTSGLSIGHVSPEAAAGGAIGLVENGDRILIDIPNRSINVLLSDEELAKRRAAMEAKGAAAWKPVEMRPRKVSPALKVYAHFATSADKGAVRDISQID | ||||||
Modified residue | 124 | N6-carboxylysine | ||||
Sequence: K |
Interaction
Structure
Sequence
- Sequence statusComplete
- Length614
- Mass (Da)65,903
- Last updated2007-08-21 v1
- ChecksumBE5D57C4014A20F4
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000749 EMBL· GenBank· DDBJ | ABR72638.1 EMBL· GenBank· DDBJ | Genomic DNA |