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A0A225ZKK0 · A0A225ZKK0_CRYNV

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 site114pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site115pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site142-145pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site232pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site235pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site257pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site286pyridoxal 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
      C356_01807

Organism names

  • Taxonomic identifier
  • Strain
    • c45
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Tremellomycetes > Tremellales > Cryptococcaceae > Cryptococcus > Cryptococcus neoformans species complex

Accessions

  • Primary accession
    A0A225ZKK0

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue258N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain98-357Aminotransferase class V

Sequence similarities

Belongs to the kynureninase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    453
  • Mass (Da)
    50,999
  • Last updated
    2017-10-25 v1
  • MD5 Checksum
    652C5BD2AF3454F538D63BD43CF8427F
MSSDLPTKKDLVKWDQEDALNWTREEYEIPNSKACGGGADGKAIYFCGNSLGLLNKKARQHIMEELDVWSTSSVTGHFSHPYQRPWKHVDEPLTPRLAKLVGAREEEVAHTSTLTSNMHNLFTSFYRPTEKRWKIVIEKGSFPSDWYAVHSHPRLHDKVLRPEQIDNAIIALAPREGEDTLRTEDILKVLDDNKDSVALVWLPLVQYYTGQLFDISSISPKVHEIGALLGLDMAHGIGNVECKLNEWNVDFAVWCTYKYLNAGPGAIGGFYIRSGLEDGGRRLAGWWGNDALTRFHMSPNFQPTPGAKGYQHSCTPVFSSIPLLATLQLIEAVGFSNMVEKARRLTGTLETLLKASRYHVHPADPKGKIGFKIITPAAPYRGTQLSLVILPEEEHVMPKVFDRMLRKGLVGDERKPSVIRLSPVVLYNTFEEVGRAVEIVEEALEEEEEESKR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AMKX01000089
EMBL· GenBank· DDBJ
OWZ54508.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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