A0A5S6PWW5 · A0A5S6PWW5_BRUMA

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.

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 site474pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site475pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site502-505pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site558pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site590pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site612pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site642pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site670pyridoxal 5'-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function3-hydroxykynureninase activity
Molecular Functionkynureninase activity
Molecular Functionmetal ion binding
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
    • L-kynurenine hydrolase

Gene names

    • Name
      Bma-kynu-1

Organism names

  • Taxonomic identifier
  • Strain
    • FR3
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Spirurina > Spiruromorpha > Filarioidea > Onchocercidae > Brugia

Accessions

  • Primary accession
    A0A5S6PWW5

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue613N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain103-161FLYWCH-type
Region227-251Disordered
Compositional bias229-251Polar residues

Sequence similarities

Belongs to the kynureninase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    808
  • Mass (Da)
    91,568
  • Last updated
    2020-02-26 v1
  • Checksum
    657F8A28924E5D71
MDLLSQLVACKQSSNETDQEEINFSTTTTTTTAAIATNISLNRNEGLKMMESDVNKIAVNTMKSNVVCKMEEANLESNDSPKFGIVESFMLKMAPDSGVQIFRSKKGFEKLAYDGFLYNLDKRHQKYVLWRCEMSKKPGYKCSGRVRMTEDSLEMYSSHSHPPNPLKVVADILKARLYAAAEDPTNSSKFLYHEAVHLASFAGSSGLPKLGSMQRVISRKRRHTQKLLEESLNPTSSSYDSSSITSTSTSNDGNCSISDLLQTAERLQFLFTPSGGFKEIEPERTRDTSAEYCTDECSNMKKSKANMDDRKVELLPLQSFFADASISDEKTECSFKPSRSKRMEIQIHLQRVAQDIGISDLTSFDLAEALDDADPLKFLRNEFAYPKMRTLPHVDLLLVNANDDAIYMCGNSLGLMPKGTKHLMDEQFEKWANMGVFGHLQEPLAWAKSDQSILDSIAELVGAQRTEVALMNSLTVNLHILLTAFYKPTPKRHKIFIESKAFPSDHYAIESQIRLKGFAVEESLICMHPRTGDDCIRNEDIIALIEEQGDTIAIIWFSAIHYYTGQLFDIRKITKSGHDKGCLVGWNLAHAFANIPLSLHEWDVDFACWCTYKYSCSGAGGIGGFFVHKRFETDKRERMVGWWGHKEETRFFMNNQLELENGAAGYRISNPPMMLMVPLIAFLDVLSKTTMQDLRTKSLLLTGYLEYLINHFLSPSSLNRRTKKIMCTIMTPSDPEQRGCQLSLKFNIDISLVYRELVKRGVVIDKRYPDVIRVTPVHLYNSYTDVHRFMRALLDSLIVVEGDYEKLL

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A5S6PWD9A0A5S6PWD9_BRUMABma-kynu-1654

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias229-251Polar residues

Keywords

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp