A0A7T7BLW3 · A0A7T7BLW3_PENDI

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 site146pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site147pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site174-177pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site231pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site260pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site263pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site285pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site325pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site353pyridoxal 5'-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionkynureninase activity
Molecular Functionpyridoxal phosphate binding
Molecular Functiontransaminase activity
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
      Pdw03_8516

Organism names

  • Taxonomic identifier
  • Strain
    • PdW03
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Penicillium

Accessions

  • Primary accession
    A0A7T7BLW3

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue286N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Belongs to the kynureninase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    484
  • Mass (Da)
    54,224
  • Last updated
    2021-06-02 v1
  • Checksum
    06143F5EA9F57B29
MGSRQHVRDIKSGSPLPYKDDIRAYKKEYAEALDAQDPLRSFRDEFIIPSKNDLKRKTLAVDDSNEASDEKSIYFCGNSLGVQPRSTQKYIEQYLRTWATKGVTGHFVPHDDQLLPPFVDVDSAASKLMASVVGASQSEVAVMGTLTANLHLLMASFYRPTKEKYKIILEGKAFPSDHYAVESQLRHHNFDPKDGMVLIEPNDLDQPTLGTEQIIKVIDDNASSTALVLLSAIQFYTGQYFDMERITAHAHSKGILIGWDCAHAAGNVDLRLHDWNVDFAAWCNYKYLNSGPGGIAGLFVHERHGSVDEKQPESDGTFRPRLSGWWGGDIKTRFNMENKFLPQPGAAGFQLSNPSVLDINAVMASLEIFNRATMKEIRQKSLNITGYLEHLLMKYPLDAAPEDKPFTLITPSNPAERGAQLSLRLQPGLLDHVLHCLEDNGVVIDERKPDVVRVAPAPLYNTYTEVWEFCQIFLQACKEAVKAR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP060776
EMBL· GenBank· DDBJ
QQK44615.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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