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A0A5E8B471 · A0A5E8B471_9ASCO

  • Protein
    Kynureninase
  • Gene
    BNA5
  • 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.

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 site126pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site127pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site154-157pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site210pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site241pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site244pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site266pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site296pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site324pyridoxal 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
      SAPINGB_P000312

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Dipodascaceae > Saprochaete

Accessions

  • Primary accession
    A0A5E8B471

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue267N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Belongs to the kynureninase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    458
  • Mass (Da)
    50,271
  • Last updated
    2019-11-13 v1
  • MD5 Checksum
    398412E097C7783C3F7438F0701F36CF
MASVPLTRQAAQALDSQYPSHAHLFAIPTLASLGLTKPTSGTQDSSSPSIYFCGNSLGLMPKATRAAVDAELNAWAARGVVAHFRRNDATGDGLEPWVSIDKPLAPLLAAVVGADGEDEVAAMNTLTGNLHTLLAAFYKPTQARYKILFEDKAFPSDLYAFQGQAEMHGLNPETALVPLKPRVGEYTLRTEDILAAIDEHKDSLAAVVFSGIQFYTGQYFDMETITSYAHAASPDIVVGWDLAHAAGNVDVRLHDWGVDFACFCSYKYLNSGPGGIGGIFVHRKHAKDKRARQAGWWGNNESTRFAMLPDFDAIPGAQGFRMSNPSVLNTVCLYESLKLFEKAGGIGVLRARSISMTTFLYRLLAESKFYVPVTEFDEDKKPSFTIITPEDPVQRGAQLSLLFSRDTMEHVFEELDARGIIGDERRPSVIRLAPNHFYNTHEEVYQVVKALNEIMSGL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CABVLU010000001
EMBL· GenBank· DDBJ
VVT44125.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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