A0AAD4LV49 · A0AAD4LV49_9AGAM

  • 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

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 site99pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site100pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site127-130pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site183pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site212pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site215pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site237pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site265pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site293pyridoxal 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

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
      EDB92DRAFT_1931792

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • QP
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Russulales > Russulaceae > Lactarius

Accessions

  • Primary accession
    A0AAD4LV49

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue238N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain154-259Aminotransferase class V

Sequence similarities

Belongs to the kynureninase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    445
  • Mass (Da)
    49,690
  • Last updated
    2024-05-29 v1
  • Checksum
    25B485BD8F91E718
MDSPSRRHFIIPTNTDIGASRVRGEEPCTYLCGNSLGLLPKPAEVLVQEELRVWGSRAVQGHHDHPLGREWVKITDHVNPLLGDLLGAREAEVACMGTLTANLHLMMNTFYRPTPDRYKLLCEGKAFPSDQYAFASQVQLHGFKPEDAIIEMNPRQGEFTLREEDILEVIEKHGSSITLVIFSGVQYYTGQWFPMQSITKAAKAQGCICGWDLAHAIGNVPLSLHDWDVDWAVWCSYKYLNSGPGNIAGLYVHEKWDEKPRYAGWWGHDPATRFLMPPIFSPIRGAQGLQLSNPSVLGVASLLGSLQVFKEAGMMGRLRERSVELTAHLEGLLTRSAYFVPPHEAAVKLPLCVGSTDSVQYRRPAFTIITPTAANSRGSQLSLLFFSSDTELMQKVHERLGSYGVMTDERHPNVIRLAPTALYNTIEDCENAAKYLEEVLKELDN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAKELL010000001
EMBL· GenBank· DDBJ
KAH9001216.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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