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A0A150RYX1 · A0A150RYX1_SORCE

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.

Type
IDPosition(s)Description
Binding site81Mg2+ (UniProtKB | ChEBI)
Binding site123Mg2+ (UniProtKB | ChEBI)
Binding site124Mg2+ (UniProtKB | ChEBI); via carbamate group
Binding site497Mg2+ (UniProtKB | ChEBI)
Active site523Proton 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
      BE17_21055

Organism names

Accessions

  • Primary accession
    A0A150RYX1

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue124N6-carboxylysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region614-633Disordered

Sequence similarities

Belongs to the IlvD/Edd family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    633
  • Mass (Da)
    67,138
  • Last updated
    2016-06-08 v1
  • MD5 Checksum
    F298B52D6FB11460621F10C6BD16244B
MAGYRSRTSTQGRNMAGARALWRATGMKDADFEKPIIAIANSFTQFVPGHVHLHDVGQRAKKVIDAAGGWGVEFNTIAIDDGIAMGHAGMLYSLPSRELIADSVEYMVNAHCADALLCISNCDKITPGMLLAAMRLNIPTVFVSGGPMEAGKIVGTHDRDGKPLIRKLDLIDPMIAASDSKVTDADLAAMERSACPTCGSCSGMFTANSMNCLNEALGLALPGNGTLLATHAARWELFEAAAKRVVALAQKHYVEGDDSVLPRSIATFEAFENAMALDIAMGGSTNTVLHLLATAREAQVDFKMSDIDRMSRKVPNICKVAPSSHYHVEDVHRAGGVLTILGELDRAGLIHREAGTVHARTLGDAIDENDIRRPTATAAAKKRSLAAPGGVPTTVAFSQDKYFADTDDDAEKGCIRDVAHAHSREGGLAVLYGNIAADGCIVKTAGVDESIWKFEGPARVFHSQEAACDAIWNDQVRAGDVVVIVYEGPKGGPGMQEMLYPTSFLKGKGLGKACALVTDGRFSGGTSGLSIGHASPEAAEGGTIGLVEEGDRIRIDIPARTIEVVVSDAELERRRRAAEARGADAFRPNRDRKVSPALRAYALMATSAANGAVRDVNQIEPSRRAGDGAARRS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JEMB01001735
EMBL· GenBank· DDBJ
KYF85320.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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