A0A193BUE2 · A0A193BUE2_AMYOR

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 site493Mg2+ (UniProtKB | ChEBI)
Active site519Proton 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
      SD37_09100

Organism names

Accessions

  • Primary accession
    A0A193BUE2

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue124N6-carboxylysine

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the IlvD/Edd family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    614
  • Mass (Da)
    65,132
  • Last updated
    2016-10-05 v1
  • Checksum
    C802804BBD4D9D98
MPQLRSRTTTHGRNAAGARSLWRATGMTDSDFGKPIVAIANSYTQFVPGHVHLKDLGEIVADAVKEAGGVAREFHTIAVDDGIAMGHSGMLYSLPSREIIADSVEYMVNAHQADALVCISNCDKITPGMLNAAMRLNIPVVFVSGGPMEAGKAVVVGGVAQAPTDLITAIAASASSEVDEDGLSIVERSACPTCGSCSGMFTANSMNCLTEALGLSLPGNGSTLATHAARRALFSDAGRTVVELCKRWYEQDDETALPRSIASKKAFENAMALDMAMGGSTNTVLHILAAAQEGEVDFTIDDIDAIGRRVPCLSKVAPNSDYHMEDVHRAGGIPAILGELYRGGLLNTDVHSVHSPDLESWLSTWDIRAKEPSARAIELFHAAPGGVRTTEAFSTENRWSSLDTDAENGCIHDVEHAYTKDGGLAILRGNLAENGAVIKSAGIDEELWHFEGPARVLESQEEAVSAILKKEIQPGEVLVIRYEGPAGGPGMQEMLHPTAFLKGSGLGKKCALITDGRFSGGSSGISVGHISPEAAAGGTIGLVQNGDRILLDVHERRLELLVDEDVLAERRAKMEASERPWQPVSRNRPITAALRAYARMATSADTGAVRDPNK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP016174
EMBL· GenBank· DDBJ
ANN15793.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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