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A0AA39XNV9 · A0AA39XNV9_9PEZI

  • Protein
    Kynureninase
  • Gene
    BNA5
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

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

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 site155pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site156pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site183-186pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site270pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site273pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site295pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site334pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site362pyridoxal 5'-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionkynureninase activity
Molecular Functionpyridoxal phosphate binding
Molecular Functiontransferase activity
Biological Process'de novo' NAD biosynthetic process from tryptophan
Biological Processanthranilate metabolic 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
      B0T17DRAFT_628423

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • SMH3391-2
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Sordariomycetidae > Sordariales > Lasiosphaeriaceae > Bombardia

Accessions

  • Primary accession
    A0AA39XNV9

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue296N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain128-303Aminotransferase class V

Sequence similarities

Belongs to the kynureninase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    492
  • Mass (Da)
    53,652
  • Last updated
    2024-01-24 v1
  • MD5 Checksum
    A4F973D67E9AF7F165A5B9C0320AD7E0
MPFVSFVKALRAGQSVQFPLEAKSLEYARGLDAEDDLGHLRDQFLIPTRGSLKKKALNGTLLGKGPNGATTNQDQDDNTPSIYFVGNSLGAQPKAVRSYLEAHLETWASVGVNGHFTQYDNSPLVSWQDMAEDCATKSAAIVGASPGEIVIMNSLTANLHLMMASFYRPTEKRHKIILEWKPFPSDWYAIQSQITLHGFSPATSMVEVQPDPSPNNFYISTATILSTIDAHADSAALLLLPGIQYYTGQLFDMPLITRYAQDRGIVVGWDLAHAAGNVELALHDWNVDFAVWCTYKYLNAGPGAIAGAFVHERHGKVGRDGSGKAEFRPRLSGWYGADKSVRFNMEKEFQPTAGAGGFQLSNPSAVDLASLSAALGVFGMTSMARLRDKALVLTAYAEWLLDGVLAGDGNGGDGGPPFRIITPRSPLERGTQLSILFGEGLLERVSKRLVENGVVFDVRKPDVIRIAPVPMYCTFVDVWKFGDIFKEAMNSK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAULSR010000001
EMBL· GenBank· DDBJ
KAK0637486.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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