A0A0U5C1L0 · A0A0U5C1L0_ASPCI

Function

function

Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.

Catalytic activity

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Pathway

Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1.
Cofactor biosynthesis; NAD+ biosynthesis; quinolinate from L-kynurenine: step 2/3.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site147pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site148pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site175-178pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site232pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site261pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site264pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site286pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site327pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site355pyridoxal 5'-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function3-hydroxykynureninase activity
Molecular Functionkynureninase activity
Molecular Functionpyridoxal phosphate binding
Biological Process'de novo' NAD biosynthetic process from tryptophan
Biological Processanthranilate metabolic process
Biological ProcessL-kynurenine catabolic process
Biological Processquinolinate biosynthetic process
Biological Processtryptophan catabolic process to kynurenine

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Kynureninase
  • EC number
  • Alternative names
    • Biosynthesis of nicotinic acid protein 5
    • L-kynurenine hydrolase

Gene names

    • Name
      BNA5
    • ORF names
      ASPCAL00800

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • SF006504
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Nidulantes

Accessions

  • Primary accession
    A0A0U5C1L0

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue287N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the kynureninase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    484
  • Mass (Da)
    54,287
  • Last updated
    2016-03-16 v1
  • Checksum
    4A5A8546D42D40CC
MGSRLRVQQIKNEAPLPYQDDSRAFTREYAASLDAEDPLRHFRDEFIIPSVKDLKRKTLDPSNVSEDSSEPRSIYLCGNSLGLQPRNTRKYIDYYLRTWAVKGVTGHFTHHEDELLPPFVDVDSAGAELMAPIVGALESEVAVMGSLTANLHLLMASFYRPTAERYKVIIEGKAFPSDHYAVESQIHNHNLRSEDALVLIEPQNPDQPILETDHILRVIDEHASSTALLLLSAVQFYTGQYFDVEKITAHAHSKGIVVGWDCAHAAGNVDLKLHDWNVDFAAWCNYKYLNSGPGGMAGIFVHERHGEVKTSKGDGDLQSFHPRLSGWWGGDKATRFLMENHFVPQPGAAGYQVSNPSVLDLNAVAASLELFNRTSMAEIRQKSLKITGYLEHLLLKYPFDGLSEKPFSIITPSNPSERGAQLSLRLAPGLLDKVLEELEEHAVVIDERKPDVIRVAPAPLYNTYEEMWHFCQIFLEACKKAVQE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CDMC01000001
EMBL· GenBank· DDBJ
CEL01212.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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