A0A9R1D2G1 · A0A9R1D2G1_9TREE

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 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

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
      D1P53_003932

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MF34
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Tremellomycetes > Tremellales > Cryptococcaceae > Cryptococcus > Cryptococcus gattii species complex

Accessions

  • Primary accession
    A0A9R1D2G1

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
Domain97-360Aminotransferase class V

Sequence similarities

Belongs to the kynureninase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    453
  • Mass (Da)
    50,921
  • Last updated
    2023-09-13 v1
  • Checksum
    47C9C8ECF4E80D19
MSSDLPTKEELVKWDQEDALNWTRGEFEIPNSKACGGEADGKAIYFCGNSLGLLSKKARQHIMEELDVWSTSSVTGHFNHPYQRPWKHVDEPLTPHLAKLVGAREEEIAHTSTLTSNMHNLFTSFYRPTEKRWKIVIEKGSFPSDWYAVHSHPRLHDKVLSPEQIDNAIIALVPREGEDTLRTEDILKVVDDNKDSIAIVWLPVVQYYTGQLFDISSISPKVHEIGALLGLDMAHGIGNVECKLNEWNVDFAVWCTYKYLNAGPAAIGGFYIRSGLDDGGRRLAGWWGNDASTRFHMSPNFQPTPGAKGYQHSCTPVLSSIPLLATLQLIEAAGFSNMVEKGRRLTGSLEALLKASRYYVHPADPKGKIGFKIITPAAPYRGTQLSLVIMPEEEHVMPNVFDRMLRMGLVGDERQPSVIRLSPVVLYNTFEEVGRAVEIVEEALREEEEERKR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VHDQ01000010
EMBL· GenBank· DDBJ
KAE8539994.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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