A0A2R6LWH3 · A0A2R6LWH3_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 site53[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site85Mg2+ (UniProtKB | ChEBI)
Binding site127Mg2+ (UniProtKB | ChEBI)
Binding site128Mg2+ (UniProtKB | ChEBI); via carbamate group
Binding site452Mg2+ (UniProtKB | ChEBI)
Active site478Proton acceptor

GO annotations

AspectTerm
Molecular Function2 iron, 2 sulfur cluster binding
Molecular Functiondihydroxy-acid dehydratase activity
Molecular Functionheme binding
Molecular Functionmagnesium ion binding
Molecular Functionperoxidase activity
Biological Processisoleucine biosynthetic process
Biological Processresponse to oxidative stress
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
      BRD15_12120

Organism names

Accessions

  • Primary accession
    A0A2R6LWH3

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue128N6-carboxylysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain123-414Plant heme peroxidase family profile

Sequence similarities

Belongs to the IlvD/Edd family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    569
  • Mass (Da)
    59,723
  • Last updated
    2018-06-20 v1
  • Checksum
    C7693266BBE545A0
MTQKSERLRSSEVTEGVERAPHRAMFRAMGYDDEDLSSPMVGVANPAADVTPCNVHLDDVAAAAYEGVDSTGGMPIEFGTITISDAISMGTEGMKASLISREVIADSVELVAFGERLDGLVTIGGCDKNMPGMMMAAIRTDLPSVFLYGGSIMPGEHEGREVTIQNVFEGVGAVADGEMSEDELDDLERHACPGAGSCGGMFTANTMASISEALGFAPLGSASPPAEDDDRYEVAERAGELAVEVVEADRRPSEFLSKESFENAIALQVAVGGSTNAVLHLLALAAETGIELDVEAFNEVSARIPKIADLQPGGEKVMNDLHEVGGVPVVLDELYEAGLLHGDALTVTGNTIGEELEARAPPSIADLDAEFLHTVEDPIHERGAIRILTGNLAPEGAVIKITGEDHLRHEGPVRVFERESEAMKYVQEGRVESGDVIVIRNEGPRGGPGMREMLGVTSAVAGQGHAEDVALITDGRFSGATRGFSIGHVAPEAYVGGPIAAIEDGDTVTIDIDNLELSVALSDDEIADRLDARETPEPAYENGVLAKYGATFGSAANGAVTNPGVKRND

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PXSM01000160
EMBL· GenBank· DDBJ
PSQ45262.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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