A0A1W2THV6 · A0A1W2THV6_ROSNE

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 site137pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site138pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site166-169pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site252pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site255pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site277pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site319pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site347pyridoxal 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
      SAMD00023353_2800690

Organism names

Accessions

  • Primary accession
    A0A1W2THV6

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue278N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain116-288Aminotransferase class V

Sequence similarities

Belongs to the kynureninase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    476
  • Mass (Da)
    52,474
  • Last updated
    2017-06-07 v1
  • Checksum
    40A4F5556DDC7FFC
MALPADASHLSGLYARAEALDREDSLGHLRDEFHIPTKADIRRKTLLANDRSTDVHADETTPCAYLCGNSLGVQPKRTATRIQQYLATWATQGVHGHFKPLEDSPLPTWLDADHRAAKMMAPIVGAEETEVIVMQTLTANLHFLMSAFYRPDPNGRHKIILESKAFPSDHFAVLSQIRHHGLSPETSMVTIESPFTEDPIISTYDIQSLISKHAADTALILLPGIQYYTGQLLDIPTITAYARDHGIFIIWDLAHAAGNVPLSLHDWDVDAAAWCTYKYLNGGPGCIGGAFVHSRNSPISSPVVPGESEQGYRNRLSGWWGNDKGTRFQMENKFLPAQGAASFQLSNPSILDITSVCASLEIFELAGGMLPLREKSKRLTAFLEECLSSLSDDVENMFRIITPRDPDQRGSQLSLLLKDGLLADTMHSLEAQGVVVDQRKPNVIRVAPAPIYNNFGDCIYFAKAFESALLAAQKEK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DF977473
EMBL· GenBank· DDBJ
GAP87732.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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