A0A1J7J0Q0 · A0A1J7J0Q0_9PEZI

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.

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 site133pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site134pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site162-165pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site248pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site251pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site273pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site315pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site343pyridoxal 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

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
      CONLIGDRAFT_652153

Organism names

  • Taxonomic identifier
  • Strain
    • NRRL 30616
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Sordariomycetidae > Coniochaetales > Coniochaetaceae > Coniochaeta

Accessions

  • Primary accession
    A0A1J7J0Q0

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue274N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias1-21Basic and acidic residues
Region1-25Disordered
Domain61-284Aminotransferase class V

Sequence similarities

Belongs to the kynureninase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    473
  • Mass (Da)
    51,765
  • Last updated
    2017-02-15 v1
  • Checksum
    44FCA4DD74C69129
MASSHRRDRARQLDREDPLASTRSEFNIPSKAAIASNRLVDKSAASTTGSASPVDGEASVYLCGNSLGLQPKRTVTRLQQYLSTWATQGVQGHFKPLDDSPLPTWLDADARAAELIAPVVGADKSEVAVMQTLTANLHFLMSAFYRPDINGRHKIILESKAFPSDHFAVETQLRHHGLSPETSMITLKSPHSEDNVLTTDDITSAIAEHADSTALILLPGIQYYTGQLLDIRTITAFAHKHGIFIIWDLAHAVGNVPLALHDWDVDAAAWCTYKYLNGGPGCIGGMFVHSRNSAVSKDITDEKPEEGYQNRLAGWWGNDKKTRFVMANRFHPVGGAAGFQLSNPSILDITSLSASLEVFELAGGVSELRKKSLKLTAFLETLFNEMSAEDKELFRIITPSDPNQRGAQLSVMLSNGLLHTVMKELEARGVIVDERKPDVIRVAPAPLYNKFEDCVDFIEAFSAALAVCRAARS

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-21Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KV875094
EMBL· GenBank· DDBJ
OIW33639.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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