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A0A2Z2HPS4 · A0A2Z2HPS4_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.

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.

Type
IDPosition(s)Description
Binding site60[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site92Mg2+ (UniProtKB | ChEBI)
Binding site134Mg2+ (UniProtKB | ChEBI)
Binding site135Mg2+ (UniProtKB | ChEBI); via carbamate group
Binding site459Mg2+ (UniProtKB | ChEBI)
Active site485Proton 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
      B1756_01565

Organism names

  • Taxonomic identifier
  • Strain
    • JW/NM-HA 15
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Natrialbaceae > Natrarchaeobaculum

Accessions

  • Primary accession
    A0A2Z2HPS4

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue135N6-carboxylysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for compositional bias, region.

Type
IDPosition(s)Description
Compositional bias1-25Basic and acidic residues
Region1-26Disordered

Sequence similarities

Belongs to the IlvD/Edd family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    574
  • Mass (Da)
    60,453
  • Last updated
    2018-10-10 v1
  • MD5 Checksum
    DB55FD67A7A0B44911B72A640C2E50A8
MSSDEPFDYGKDESLQSHEVTQGAEKAPHRAMFRAMGFDDDDLSSPMIGVANPAADITPCNVHLDEVAESALEGVDEAGGMPIEFGTITISDAISMGTEGMKASLISREVIADSVELVAFGERMDGLVTIGGCDKNMPGMMMAAIRTDLPSVFLYGGSIMPGEHDGREVTIQNVFEGVGAVADGEMAPEELDEMERHACPGAGSCGGMFTANTMSSISEALGFAPLGSASPPAEADDRYEIARESGELAVDAVERGFRPSDFLSRESFENAIALQVAVGGSTNAVLHLLAMAAEAGVDLEIEEFNDISARTPKIADLQPGGEKVMNDLHEIGGVPVVLRELLEADLLHGDALTVTGETMAEAIERVDPPRVSDIDAEFLHSVDEPIHERGAIRILTGNLAPEGAVIKITGDDHLRHEGPVRIFEDEESAMAYVQDGNVETGDVIGIRNEGPRGGPGMREMLGVTSAVAGQGHAEDVALFTDGRFSGATRGFSIGHVAPEAYVGGPIAALEDGDTVTIDIDELELSVDLTDDEIEERLADHDPEPTYDAGVLAKYGQAFDSASNGAVTNPAAKQD

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-25Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP019893
EMBL· GenBank· DDBJ
ARS88573.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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