B0SCQ5 · ILVC_LEPBA

Function

function

Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 2 magnesium ions per subunit.

Pathway

Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4.
Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site25-28NADP+ (UniProtKB | ChEBI)
Binding site48NADP+ (UniProtKB | ChEBI)
Binding site51NADP+ (UniProtKB | ChEBI)
Binding site53NADP+ (UniProtKB | ChEBI)
Binding site83-86NADP+ (UniProtKB | ChEBI)
Active site108
Binding site134NADP+ (UniProtKB | ChEBI)
Binding site191Mg2+ 1 (UniProtKB | ChEBI)
Binding site191Mg2+ 2 (UniProtKB | ChEBI)
Binding site195Mg2+ 1 (UniProtKB | ChEBI)
Binding site227Mg2+ 2 (UniProtKB | ChEBI)
Binding site231Mg2+ 2 (UniProtKB | ChEBI)
Binding site252substrate

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionketol-acid reductoisomerase activity
Molecular Functionmagnesium ion binding
Molecular FunctionNADP binding
Biological Processisoleucine biosynthetic process
Biological Processvaline biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ketol-acid reductoisomerase (NADP(+))
  • EC number
  • Short names
    KARI
  • Alternative names
    • Acetohydroxy-acid isomeroreductase
      (AHIR
      )
    • Alpha-keto-beta-hydroxylacyl reductoisomerase
    • Ketol-acid reductoisomerase type 1
    • Ketol-acid reductoisomerase type I

Gene names

    • Name
      ilvC
    • Ordered locus names
      LBF_0685

Organism names

Accessions

  • Primary accession
    B0SCQ5

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10001243021-333Ketol-acid reductoisomerase (NADP+)

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-182KARI N-terminal Rossmann
Domain183-331KARI C-terminal knotted

Sequence similarities

Belongs to the ketol-acid reductoisomerase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    333
  • Mass (Da)
    36,156
  • Last updated
    2008-04-08 v1
  • Checksum
    398C0D6E633AB7E9
MANIYYDDSCDLNLLKGKTIAVIGYGSQGHAQAQNMKDSGLKVIIGLRDGSKSVKEAKEAGFEVYNVAEASKKADIIQILAPDTIQADMYKADIEPNLSEGKALVFSHGFNIHYDLITPPKNVDVYMVAPKGPGHLVRRVYTEGGGVPCLIAIYQDATGQAKARALAHASGVGGGRAGILETSFREETETDLFGEQAVLCGGVANLIMSGFETLTEAGYDPEIAYFECLHEVKLITDLIYEGGLARMRFSISDTAEYGDYISGPRVIDAGVKARMKDVLTDIQKDKGAAFAKRWMADTKAGYPEYKKLKEKNAAHPIEAVGTKLRSMMKWLAK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000777
EMBL· GenBank· DDBJ
ABZ93217.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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.
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