A0A9N8IJG9 · A0A9N8IJG9_STAAU

  • Protein
    Ketol-acid reductoisomerase (NADP(+))
  • Gene
    ilvC
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

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

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)
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 ProcessL-valine 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

Gene names

    • Name
      ilvC
    • ORF names
      SAMEA70153168_01881

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MOS114
  • Taxonomic lineage
    Bacteria > Bacillati > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus

Accessions

  • Primary accession
    A0A9N8IJG9

Proteomes

Subcellular Location

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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    334
  • Mass (Da)
    37,030
  • Last updated
    2023-09-13 v1
  • MD5 Checksum
    664A780908D121AF9F9F7B55D9C46F40
MTTVYYDQDVKTDALQGKKIAVVGYGSQGHAHAQNLKDNGYDVVIGIRPGRSFDKAKEDGFDVFPVAEADKQADVIMVLLPDEIQGDVYKNEIEPNLEKHNALAFAHGFNIHFGVIQPPADVDVFLVAPKGPGHLVRRTFVEGSAVPSLFGIQQDASGQARNIALSYAKGIGATRAGVIETTFKEETETDLFGEQAVLCGGVSKLIQSGFETLVEAGYQPELAYFEVLHEMKLIVDLMYEGGMENVRYSISNTAEFGDYVSGPRVITPDVKENMKAVLTDIQNGNFSNRFIEDNKNGFKEFYKLREEQHGHQIEKVGRELREMMPFIKSKSIEK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CAIIGN010000007
EMBL· GenBank· DDBJ
CAC8242821.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice.
Help