A0A9X3DDN5 · A0A9X3DDN5_9SPHI

  • Protein
    Kynureninase
  • Gene
    kynU
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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 site105pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site106pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site133-136pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site218pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site221pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site243pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site274pyridoxal 5'-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionkynureninase activity
Molecular Functionpyridoxal phosphate binding
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
    • L-kynurenine hydrolase

Gene names

    • Name
      kynU
    • ORF names
      OQZ29_11565

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 19486
  • Taxonomic lineage
    Bacteria > Bacteroidota > Sphingobacteriia > Sphingobacteriales > Sphingobacteriaceae > Pedobacter

Accessions

  • Primary accession
    A0A9X3DDN5

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue244N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain154-264Aminotransferase class V

Sequence similarities

Belongs to the kynureninase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    431
  • Mass (Da)
    49,073
  • Last updated
    2023-11-08 v1
  • Checksum
    DA79E63A5412D5D8
MKLENTLAFAKEQDEKDELKHFRDQFLFPKYQDKFFIYLCGNSLGLQPKVAKEVINSQLDNWANLAVEGWFDGEEPWMYYHKELKKLMAPIVGALPSEVCPMNTLTVNLHLLMISFYQPQGKRFKIIMEGGAFPSDQYAIESQVRFHGFDPSDAIIEVFPREGEEILRTEDIVAKIKEHGDEIALLLFGGINYYTGQWYDMENITKAGHSIGAMVGWDLAHAAGNVPVKLHDWNVDFACWCSYKYQNAGPGGISGIFVHEKHFENKALNRFAGWWGYQENKRFKMEKGFVPEAGADGWQVSCTQVMPMALYHASLQIFKEAGFLNTLRNKSISLTSYLEFVVNELNIELEKEQYKIITPKNSAERGAQLSIIAARNGKEIFDGLLAHGILGDWREPNVIRLSPVPLYNSFEDIYQTGKALSEVTRKILTTA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAPJUH010000003
EMBL· GenBank· DDBJ
MCX3265387.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help