A0A9P7HTZ0 · A0A9P7HTZ0_9HYPO

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 site158pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site159pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site186-189pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site270pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site273pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site295pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site335pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site363pyridoxal 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
      H9Q72_005457

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • IMI 127659i
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Nectriaceae > Fusarium > Fusarium fujikuroi species complex

Accessions

  • Primary accession
    A0A9P7HTZ0

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue296N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain133-312Aminotransferase class V

Sequence similarities

Belongs to the kynureninase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    487
  • Mass (Da)
    53,552
  • Last updated
    2023-09-13 v1
  • Checksum
    6F48F07972E03B91
MDLSGFVERLRSGAAPKFSSDANSLDFARHLDSQDKLSHLRDEFVLPTKKSLKKKALDGSLPGAANGTNGHSNGNGSAADDQQCLYFVGNSLGAQPKAVREYLNAQLETWASIGVNGHFSTLDNSPLPAWQDLAEDCAVKSADLVGASPHEIVIMNTLTANLHLLMASFYKPNEKRHKVILEWKPFPSDHYAIESQVVWHGLDPEKSMVKIHPNEDHIITTDLILSTIDEHAEDTALLLLPGIQYYSGQLFDIPRITAYAQAKGIVVGWDLAHAAGNVELKLHDWNVDFACWCTYKYINAGPGSIAGAYVHERHGKVELNDATGKATYRPRLMGWYGGDKSVRFNMDNNFIPTSGAGGFQLSNPSAIDLASLSGALSVFNKTTMHDLRSKALVLTAYAEYLLDQILAESSDAELFRIITPRDPLQRGTQLSVLLKDGLLDNVSAALEENAVICDKRKPGVIRVAPVPLYTRFEDVWKFMQILRTALP

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JADFTT010000156
EMBL· GenBank· DDBJ
KAG5766463.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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