A0A364L325 · A0A364L325_9EURO

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 site146pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site147pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site174-177pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site260pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site263pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site285pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site326pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site354pyridoxal 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
      BHQ10_006220

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CIB
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Trichocomaceae > Talaromyces > Talaromyces sect. Talaromyces

Accessions

  • Primary accession
    A0A364L325

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue286N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain212-286Aminotransferase class V
Region400-419Disordered

Sequence similarities

Belongs to the kynureninase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    493
  • Mass (Da)
    55,449
  • Last updated
    2018-11-07 v1
  • Checksum
    031CC8D253005348
MGSRLHFQRIKERPPLPHHDDIRAYKREYAEALDERDPLRSYRDQFIIPSKKDLLRKRLADTEGDDESDPRCTYLCGNSLGLQPKNLRKYLDQYLRSWAIKGVTGHFVSHEDALLPPYLHVDDAGSKLLAPIVGASPSEVAVMGTLTGNIHILMSSFYRPTAERHKIILEGKAFPSDHYAVESQIRLHNFDPATSMVLIEPEDAEKPILSTEQILRVIDENASDTALIFLPGIQFYTGQYFDIKTITAHAHSKGIPIGWDCAHAVGNVELQLHDWDVDFAVWCHYKYVNSGPGAMAGLFVHEKHGIVKLGEETGESPSYHPRLAGWWGHDKETRFQMNNKFVPQEGAAGYQISNPSVLDLSAVASSLEIFNQATMPALRQKSLELTGYLEHLLLKYPLDDPSTSNDKDQRPFTIITPSDPSSRGAQLSILLQPGLLDKVLEILEEEGVVIDERKPNVVRVAPAPLYNTFTDVWEFHRVFVLACKEAVKARDGK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MIKG01000011
EMBL· GenBank· DDBJ
RAO70208.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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