A6QIQ2 · ILVC_STAAE

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 site52NADP+ (UniProtKB | ChEBI)
Binding site82-85NADP+ (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
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
      NWMN_1962

Organism names

Accessions

  • Primary accession
    A6QIQ2

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10000723261-334Ketol-acid reductoisomerase (NADP+)

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
    334
  • Mass (Da)
    36,956
  • Last updated
    2007-08-21 v1
  • Checksum
    33E0B8FC772DE52E
MTTVYYDQDVKTDALQGKKIAVVGYGSQGHAHAQNLKDNGYDVVIGIRPGRSFDKAKEDGFDVFPVAEAVKQADVIMVLLPDEIQGDVYKNEIEPNLEKHNALAFAHGFNIHFGVIQPPADVDVFLVAPKGPGHLVRRTFVEGSAVPSLFGIQQGASGQARNIALSYAKGIGATRAGVIETTFKEETETDLFGEQAVLCGGVSKLIQSGFETLVEAGYQPELAYFEVLHEMKLIVDLMYEGGMENVRYSISNTAEFGDYVSGPRVITPDVKENMKAVLTDIQNGNFSNRFIEDNKNGFKEFYKLREEQHGHQIEKVGRELREMMPFIKSKSIEK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP009351
EMBL· GenBank· DDBJ
BAF68234.1
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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