A0A4R5LI39 · A0A4R5LI39_9BURK

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

[2Fe-2S] cluster (UniProtKB | Rhea| CHEBI:190135 )

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.

TypeIDPosition(s)Description
Binding site50[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site82Mg2+ (UniProtKB | ChEBI)
Binding site108[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site124Mg2+ (UniProtKB | ChEBI)
Binding site125Mg2+ (UniProtKB | ChEBI); via carbamate group
Binding site447Mg2+ (UniProtKB | ChEBI)
Active site473Proton acceptor

GO annotations

AspectTerm
Molecular Function2 iron, 2 sulfur cluster binding
Molecular Functiondihydroxy-acid dehydratase activity
Molecular Functionmagnesium ion binding
Biological Processisoleucine biosynthetic process
Biological Processvaline biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Dihydroxy-acid dehydratase
  • EC number
  • Short names
    DAD

Gene names

    • Name
      ilvD
    • ORF names
      E1N52_08280

Organism names

  • Taxonomic identifier
  • Strain
    • CNPSo 3008
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Paraburkholderia

Accessions

  • Primary accession
    A0A4R5LI39

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue125N6-carboxylysine

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Belongs to the IlvD/Edd family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    557
  • Mass (Da)
    59,108
  • Last updated
    2019-07-31 v1
  • Checksum
    55C1C28CCB350B37
MPYNRRSKHITQGVARSPNRSMYYALGYEKADFDKPMIGVANGHSTITPCNAGLQRLTDAAVDAIKHADANPQTFGTPTISDGMSMGTEGMKYSLVSREVIADCIETCVQGQWMDGVVVIGGCDKNMPGGMIALARINVPGIYVYGGTIRPGNWKGKALTIVSAFEAVGEFTAGRMTEEDFEGVEKNACPSTGSCGGMYTANTMSSSFEALGMSLMYSSTMANPDQEKVDSAAESARVLVEAVKQDLKPRDIITKQSIENAVALIMATGGSTNAVLHYLAIAHAAEIEWTIDDFERMRKKVPVICDLKPSGQYVATDLHEAGGIPQVLKILLDAGLLHGDCITITGKTIAEELKDVPSTPRADQKVIFPISQALYKEGHLAILKGNLATHGAVAKITGLKNPVITGPARVFDDEQSAMEAILADRIKAGDVVVLRYLGPKGGPGMPEMLAPTSAIIGKGLGESVGLITDGRFSGGTWGMVVGHVAPEAFEGGTIALVQEGDSITIDAHKLLLQLNVDDAELARRRAAWKQPAPRYTRGVMAKYAALARPANQGAVTG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SMOD01000005
EMBL· GenBank· DDBJ
TDG09120.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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