A2SHM0 · ILVC_METPP

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.

TypeIDPosition(s)Description
Binding site24-27NADP+ (UniProtKB | ChEBI)
Binding site47NADP+ (UniProtKB | ChEBI)
Binding site52NADP+ (UniProtKB | ChEBI)
Active site107
Binding site133NADP+ (UniProtKB | ChEBI)
Binding site190Mg2+ 1 (UniProtKB | ChEBI)
Binding site190Mg2+ 2 (UniProtKB | ChEBI)
Binding site194Mg2+ 1 (UniProtKB | ChEBI)
Binding site226Mg2+ 2 (UniProtKB | ChEBI)
Binding site230Mg2+ 2 (UniProtKB | ChEBI)
Binding site251substrate

GO annotations

AspectTerm
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
      Mpe_A2103

Organism names

Accessions

  • Primary accession
    A2SHM0

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10000505331-338Ketol-acid reductoisomerase (NADP+)

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-181KARI N-terminal Rossmann
Domain182-327KARI C-terminal knotted

Sequence similarities

Belongs to the ketol-acid reductoisomerase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    338
  • Mass (Da)
    36,526
  • Last updated
    2007-03-06 v1
  • Checksum
    FBADDD177A49613B
MKVYYDKDADLSLIKGKSVAIIGYGSQGHAHAQNLNDSGVKVTVGLRRGGASWNKVEKAGLKVAEVADAVKSADVVMILLPDEQIASVYSAEVAPNIKQGASLAFAHGFNVHYGQVVPREDLDVWMVAPKAPGHTVRNTYTQGGGVPHLIAVHADKTGKARDLALSYAAANGGGKAGIIETNFREETETDLFGEQAVLCGGTVELIKAGFETLVEAGYAPEMAYFECLHELKLIVDLIYEGGIANMNYSISNNAEYGEYVTGPRVVTEDTKAAMRQCLKDIQTGEYAKSFILENRAGAPTLLSRRRLTAEHDIEVVGEKLRAMMPWIKANKLVDKSRN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000555
EMBL· GenBank· DDBJ
ABM95059.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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