A0A0C2IQ67 · A0A0C2IQ67_9PEZI

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 site130pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site131pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site159-162pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site245pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site248pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site270pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site312pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site340pyridoxal 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
      SPBR_04920

Organism names

  • Taxonomic identifier
  • Strain
    • 5110
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Sordariomycetidae > Ophiostomatales > Ophiostomataceae > Sporothrix

Accessions

  • Primary accession
    A0A0C2IQ67

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue271N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain107-289Aminotransferase class V

Sequence similarities

Belongs to the kynureninase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    473
  • Mass (Da)
    51,534
  • Last updated
    2015-04-01 v1
  • MD5 Checksum
    209566C67164D92D337F9C6BA15C8296
MSLLIPARERARSLDRKDELRRFRSEFAIPSTSQIHSDTLTLPSDNTGAPTVPRRSIYLCGNSLGLQPMRTATRIQQHLSTWAAQGVQGHFKPLADSPLPTWLDADAKAAEMIAPIVGAETSEVAVMQTLTANLHLLLSAFYRPETRGRHKIILESKAFPSDHFAVETQIRHHGLSVATSMVVVDMPSSENPSTATHDVMATISRHAVDTAVLLLPGIQYYSGEFLDIPVITDFAHAHGIFVIWDLAHAVGNVPLRLHDWDVDAAVWCSYKYLNSGPGGIGGLFVHTRHSQVTRSIIDDQPHTGFPNRLAGWWGNDKATRFAMTTKFHPVPGAAGFQLSNPSILDITSLCASLEVFREAGGVDALRKKSVGLTGFLEALLNSLPSELRSKFRILTPSVPAHRGAQLSLLIGDGLLDSVMDVLLARSVIADERKPNVIRVAPAPLYNSYEDCVDFVEAFEDALKKAGAPSPGVN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AWTV01000010
EMBL· GenBank· DDBJ
KIH87192.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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