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A0A371MDW3 · A0A371MDW3_9EURY

  • Protein
    Ketol-acid reductoisomerase (NADP(+))
  • Gene
    ilvC
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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 site29-32NADP+ (UniProtKB | ChEBI)
Binding site52NADP+ (UniProtKB | ChEBI)
Binding site55NADP+ (UniProtKB | ChEBI)
Binding site57NADP+ (UniProtKB | ChEBI)
Active site111
Binding site137NADP+ (UniProtKB | ChEBI)
Binding site194Mg2+ 2 (UniProtKB | ChEBI)
Binding site194Mg2+ 1 (UniProtKB | ChEBI)
Binding site198Mg2+ 1 (UniProtKB | ChEBI)
Binding site230Mg2+ 2 (UniProtKB | ChEBI)
Binding site234Mg2+ 2 (UniProtKB | ChEBI)
Binding site255substrate

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
      C5B91_05965

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Atlit-10N
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Haloferacaceae > Haloferax

Accessions

  • Primary accession
    A0A371MDW3

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain6-185KARI N-terminal Rossmann
Domain186-331KARI C-terminal knotted
Region328-349Disordered
Compositional bias330-349Acidic residues

Sequence similarities

Belongs to the ketol-acid reductoisomerase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    349
  • Mass (Da)
    38,010
  • Last updated
    2018-11-07 v1
  • MD5 Checksum
    A41A0C47AD26FE25944B9C155F81CDE2
MTELTTEVYYDDDADRSQIDDKTVAVIGYGSQGHAHAQNLADSGVDVVVGLRANSSSRDAAEADGLCVKEPAEAAAEGDIVSVLVPDTVQPAVFEEIRDSLEAGDTLQFAHGFNIHYNQIRPPENVDVTMVAPKSPGHLVRRNYEANEGTPGLIAVYQDVTGDAKEEALAYAHGLGCTRAGVIETTFQEETETDLFGEQAVLCGGVTSLVKQGYETLVDAGYSPEMAYFECLNELKLIVDLMYEGGLGEMWDSVSDTAEFGGLTRGDRVVDEHARENMEEILEEVQDGTFAREWILENQAGRPSYSQLKDAEENHHIEQVGAPLRDLFAWADDEEEEADAEKAEAPADD

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias330-349Acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PSYX01000001
EMBL· GenBank· DDBJ
RDZ61041.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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