A0A7L4PL32 · A0A7L4PL32_9EURY

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 site78Mg2+ (UniProtKB | ChEBI)
Binding site120Mg2+ (UniProtKB | ChEBI)
Binding site121Mg2+ (UniProtKB | ChEBI); via carbamate group
Binding site440Mg2+ (UniProtKB | ChEBI)
Active site466Proton acceptor

GO annotations

AspectTerm
Cellular Componentcytosol
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
      GKC00_01590

Organism names

Accessions

  • Primary accession
    A0A7L4PL32

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue121N6-carboxylysine

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Belongs to the IlvD/Edd family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    549
  • Mass (Da)
    58,943
  • Last updated
    2021-04-07 v1
  • Checksum
    6F83C1BE412C7305
MKSSIIKDDIDKAGARGLLRADGLKDADFKKPFIGVASAYSEIVPGHINLRKLTELVKKGIRDSGGIPFEFGMPGICDGIAMGHQGMRYSLPSRDIIADSVELMVSSHLFDGWIGVTNCDKITPGMLMAAGRVNIPAAMVTGGPMEPGEYNGKRLDLISIFEAIGSFKKGEISEKELKEIEKRSCPGAGACAGLFTANSMACMTEALGLSIPGSATIHANDKRKEDIAYQTGKLIVELVKKDLKPRDIVTKNSFENAIRVDMGIGGSSNTALHLPAVAHAFGLNLPLNLFDKLSKETPHLVNLRPGGPFFMRDFDDAGGIPQILLRLKDKLNLETKTIMGNSLGDVLKKTKMVKSDTIRNTDNPYHKQGGIAILKGNLAPNGSVVKQTAVSDKIMKFEGKAKVFESEEAATKAILAGKIKSGMVVVIRYEGPKGGPGMREMLEPTSLIAGMGLAESVALITDGRFSGGTRGPCIGHISPEAFDKGPIAAVKDGDIIRIDIPKRKLEVALTDKEIEERLKTVKPPKKDIPGMLLRYRKLVSSSDKGAVLE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAAEEM010000050
EMBL· GenBank· DDBJ
NYT03380.1
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