A0A416KEQ0 · A0A416KEQ0_9FIRM

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.

TypeIDPosition(s)Description
Binding site26-29NADP+ (UniProtKB | ChEBI)
Binding site49NADP+ (UniProtKB | ChEBI)
Binding site59NADP+ (UniProtKB | ChEBI)
Active site114
Binding site140NADP+ (UniProtKB | ChEBI)
Binding site197Mg2+ 2 (UniProtKB | ChEBI)
Binding site197Mg2+ 1 (UniProtKB | ChEBI)
Binding site201Mg2+ 1 (UniProtKB | ChEBI)
Binding site233Mg2+ 2 (UniProtKB | ChEBI)
Binding site237Mg2+ 2 (UniProtKB | ChEBI)
Binding site258substrate

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionisomerase activity
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

Gene names

    • Name
      ilvC
    • ORF names
      DWY95_09675

Organism names

Accessions

  • Primary accession
    A0A416KEQ0

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-188KARI N-terminal Rossmann
Domain189-337KARI C-terminal knotted

Sequence similarities

Belongs to the ketol-acid reductoisomerase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    339
  • Mass (Da)
    37,174
  • Last updated
    2019-05-08 v1
  • Checksum
    66CEF35C9826AB4D
MAIKKYYDSDCNLGVLDGKTVAVIGFGSQGHAHSENLAESGVNVVVGLRKGSAHWEKASEFAATHDNFKVMEVEEAAKAGDVVMMLVPDELCADIYNKQVAPYMTEGKALAFAHGFNIHFKTITAPKNVDVIMIAPKGPGHIVRRLYTEGEGCPSLICVEQDYTGKAKDIALAYASGIGAGRAGILQTTFKEETETDLFGEQAVLCGGVSELIHAGFDTLVEAGYEPEMAYFETCHEMKLIVDLINEGGFSKMRYSISNTAEYGDYRTGKRLITAETRKEMKKVLTEIQDGTFASEFLTEMSPNGGRKVHFLAKRRMEAELPIEKVGAELRSMMSWLKK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QUFG01000006
EMBL· GenBank· DDBJ
RHQ26375.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp