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B0XS72 · KYNU1_ASPFC

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 site169pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site170pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site197-200pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site283pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site286pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site308pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site349pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site377pyridoxal 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 1
  • EC number
  • Alternative names
    • Biosynthesis of nicotinic acid protein 5-1
    • L-kynurenine hydrolase 1

Gene names

    • Name
      bna5-1
    • ORF names
      AFUB_026170

Organism names

Accessions

  • Primary accession
    B0XS72

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00003569631-509Kynureninase 1
Modified residue309N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Structure

Family & Domains

Sequence similarities

Belongs to the kynureninase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    509
  • Mass (Da)
    57,148
  • Last updated
    2008-04-08 v1
  • MD5 Checksum
    06322C02C435E6FC96621F9A51837C79
MGSRLHVQVIHGGPPLPYKDDIRAFGKEYAEQLDAQDPLRRFRDEFIIPSKKDLKRKTLFPNDGMYSCGHPICFANTSCACVHAAETEETSDEKCIYLCGNSLGLQPRSTRKYIDHYLRTWATKGVTGHFVPHDDQLLPPFVDVDEAGAKLMAPIVGALKSEVAVMGTLTANLHLLMASFYRPTPERNKIIIEGKAFPSDHYAVESQIRHHNLDPKDAMVLIEPEDLDRPILDTKYILRVIDENAHSTALILLPAIQFYTGQYFDIQRITAHAQSKGILVGWDCAHAAGNVDLRLHDWNVDFAAWCTYKYLNAGPGGMAALFVHERHGRVDIEQAASGKEAFHPRFSGWWGGDKQTRFLMNNHFVPQQGAAGFQLSNPSVLDMNAVVASLELFNQTSMAEIRKKSLNLTGYLEHLLLRDPQTENSEKRPFSIITPSNPAERGAQLSIRLQPGLLDRVLESLNEDAVIIDERKPDVIRVAPAPLYNTYAEVWRFAQLFHLACDKALCGRK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DS499595
EMBL· GenBank· DDBJ
EDP54558.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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