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J2QYQ6 · J2QYQ6_9PSED

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 site97pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site98pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site129-132pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site172pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site201pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site204pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site226pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site256pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site282pyridoxal 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
    • L-kynurenine hydrolase

Gene names

    • Name
      kynU
    • ORF names
      PMI26_01002

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • GM33
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas

Accessions

  • Primary accession
    J2QYQ6

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue227N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Belongs to the DegT/DnrJ/EryC1 family.
Belongs to the kynureninase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    416
  • Mass (Da)
    45,705
  • Last updated
    2012-10-03 v1
  • MD5 Checksum
    62A40199422CB2BED73DF89BF2F91EEC
MTTRNSCLALDAQDALAPLRQQFALPEGIIYLDGNSLGARPVAALARAQAVVAEEWGNGLIRSWNSAGWRELSERLGDRLAGLIGAGAGEVVVTDTTSINLFKVLSAALRVQATRSPQRRVIVSESSNFPTDLYIAEGLAQMLQQGYTLRLVDSPEALPQAIDQDTAVVMLTHVNYKTGYMHDMQALTALTHECGALTIWDLAHSAGAVPVDLHQAGADYAIGCTYKYLNGGPGSQAFVWVSPSLCDLVPQPLSGWFGHSRQFAMESHYEPSSGIARYLCGTQPITSLAMVECGLDVFAQTDMASLRRKSLALTDLFIELVEQRCAAHELKLITPREHVRRGSHVSFEHPEGYAVIQALIDRGVIGDYREPRIMRFGFTPLYTTFTEVWDAVQILGEILDRNTWSQARYQVRHSVT

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AKJO01000028
EMBL· GenBank· DDBJ
EJM47556.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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.
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