A0AAF0GX79 · A0AAF0GX79_RHIRD

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.

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 site81Mg2+ (UniProtKB | ChEBI)
Binding site123Mg2+ (UniProtKB | ChEBI)
Binding site124Mg2+ (UniProtKB | ChEBI); via carbamate group
Binding site491Mg2+ (UniProtKB | ChEBI)
Active site517Proton 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
      CFBP5506_07240

Organism names

Accessions

  • Primary accession
    A0AAF0GX79

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue124N6-carboxylysine

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Belongs to the IlvD/Edd family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    611
  • Mass (Da)
    65,010
  • Last updated
    2024-05-29 v1
  • Checksum
    8AEB86C0ED5F21D6
MPAYRSRTTTHGRNMAGARGLWRATGMKDSDFGKPIIAVVNSFTQFVPGHVHLKDLGQLVAREIEAAGGVAKEFNTIAVDDGIAMGHDGMLYSLPSREIIADSVEYMVNAHCADAMVCISNCDKITPGMLNAAMRLNIPAVFVSGGPMEAGKVVLHGKTVALDLVDAMVAAADDKISDEDVKVIERSACPTCGSCSGMFTANSMNCLTEALGLSLPGNGSTLATHSDRKRLFVEAGHLIVDLARRYYEQEDETVLPRTIANKAAFENAMSLDIAMGGSTNTVLHILAAAHEGGVDFGMEDIDRLSRKVPCLSKVAPAKQDVHMEDVHRAGGIMRILGELERGGLINRDTYTVHEATLGDAIDRWDITRTNSETVREFFKAAPGGVPTQVAFSQSSRWDDLDTDSDNGVIRSVEKPFSKDGGLAVLYGNIALDGCIVKTAGVDESILKFTGPAVVYESQDAAVKGILGNEVKAGDVVVIRYEGPKGGPGMQEMLYPTSYLKSKGLGKACALITDGRFSGGTSGLSIGHASPEAAQGGAIGLVRQGDMIEIDIPNRTINLKVSDAELASRRAEQEEKGWKPEAPRKRNVTTALKAYAAFAASADKGAVRILPE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP122962
EMBL· GenBank· DDBJ
WGM58143.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp