Q9JS61 · ILVD_NEIMB

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.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
[2Fe-2S] cluster (UniProtKB | Rhea| CHEBI:190135 )

Note: Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

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 site122[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site123Mg2+ (UniProtKB | ChEBI)
Binding site124Mg2+ (UniProtKB | ChEBI); via carbamate group
Binding site198[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site494Mg2+ (UniProtKB | ChEBI)
Active site520Proton acceptor

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function2 iron, 2 sulfur cluster binding
Molecular Functiondihydroxy-acid dehydratase activity
Molecular Functionhydro-lyase 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
      ilvD1
    • Ordered locus names
      NMB1150
    • Name
      ilvD2
    • Ordered locus names
      NMB1188

Organism names

Accessions

  • Primary accession
    Q9JS61

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001034841-619Dihydroxy-acid dehydratase
Modified residue124N6-carboxylysine

Proteomic databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the IlvD/Edd family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    619
  • Mass (Da)
    66,786
  • Last updated
    2000-10-01 v1
  • Checksum
    1346AE03A24DD58F
MPEYRSKTSTHGRNMAGARALWRATGVMETDFGKPIIAVANSFTQFVPGHVHLHNMGQLVAREIEKAGAIAKEFNTIAIDDGIAMGHSGMLYSLPSRDLIADSIEYMVNAHCADALVCISNCDKITPGMLIAAMRLNIPTIFVSGGPMEAGKVIGVANIQPERRLDLIDAMIESADDNVSNRQVEEVEQNACPTCGSCSGMFTANSMNCLTEALGLSLPGNGSYLATHAGRKELFLEAGRMIVEITKRYYEQNDETVLPRSIATKKAFENAMTMDIAMGGSTNTILHLLAVANEAGVDFKMADIDRLSRVVPCICKTAPNNHDYYMEDVHRAGGIFAILKELDKAGKLHTDVHTIHAPTLKDAIEQWDVTNPENTRAIERFKAAPGGVRTTQAFSQNRMWKTLDLDREKGCIRDVAHAYSQDGGLAVLFGNIAERGCVVKTAGVDESILKFTGRARVFESQEDAVEGILGNQIVAGDIVIIRYEGPKGGPGMQEMLYPTSYLKSKGLGKACALLTDGRFSGGTSGLSIGHASPEAAEGGAIGLVHEGDTVEIDIPNRSIHLAISDEELAARRAEMEARGSKAWKPKNRDRYVSAALRAYGAMATSADKGAVRDVAQIER

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE002098
EMBL· GenBank· DDBJ
AAF41537.1
EMBL· GenBank· DDBJ
Genomic DNA
AE002098
EMBL· GenBank· DDBJ
AAF41572.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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