A0A229X5T2 · A0A229X5T2_9EURO

  • Protein
    Kynureninase
  • Gene
    BNA52
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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 site135pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site136pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site163-166pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site248pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site251pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site273pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site313pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site341pyridoxal 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 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
      BNA52
    • Synonyms
      BNA5
    • ORF names
      CDV55_105356
      , CFD26_102949

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • HMR AF 1038
    • HMR AF 23
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Fumigati

Accessions

  • Primary accession
    A0A229X5T2

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue274N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain106-280Aminotransferase class V

Sequence similarities

Belongs to the kynureninase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    464
  • Mass (Da)
    51,224
  • Last updated
    2017-10-25 v1
  • Checksum
    A85A9739181C6A91
MSTNGTLSKPEFPANAASKEYAASLDAADPLAGFREKFIIPSKANIASTKLAKPSLSSEPCIYFCGNSLGIQPKATQKYVQALLDTWSSIGVCGHFTKIEDSPLKEWQNLAEQAAESMSKIVGAAPEEVAAMGTLTMNLHMLLASFYKPTATKRKILMDWKAFPSDHYAIESHIAWHGLDSQETMVLIGPDDGTYEIPTEKILSYIDQHADEAALILLPGIQYYTGQLFDIPKITEYAHSRGLVVGWDLAHAYANVHLKLHDWDVDFATWCTYKYGNAGPGAMAGLFVHEKHGQVDYSEGEDAPKFRHRLTGWYGGDKSVRFKMDNKFKPIPGAGGYQISNPSAIDLASLCAALSVFDETSMAELRKKSVLMTAYLEYLLLKDTTDKSRQFQIITPSDPAARGAQLSLLLKPGLLHKVAHRLQEAGIICDKREPGVVRVAPVPLYNTFTEIWMFVEQLKAALEE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NKHV02000114
EMBL· GenBank· DDBJ
RHZ59562.1
EMBL· GenBank· DDBJ
Genomic DNA
NIDN02000045
EMBL· GenBank· DDBJ
RLL98763.1
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.
FeedbackHelp