A0A0L0VCP2 · A0A0L0VCP2_9BASI

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

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 site159pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site160pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site187-190pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site243pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site272pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site275pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site297pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site335pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site363pyridoxal 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

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
      PSTG_09626

Organism names

Accessions

  • Primary accession
    A0A0L0VCP2

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue298N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region53-80Disordered
Compositional bias54-75Polar residues
Domain141-325Aminotransferase class V

Sequence similarities

Belongs to the kynureninase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    521
  • Mass (Da)
    57,475
  • Last updated
    2015-11-11 v1
  • Checksum
    D9FD53FFA25C79A3
MSSTPANHAIWARRLSASGCLSLTDPNFAIYLDSIACVGGLRSEFRFPRKECKSNSQQEAASNNTESINQTGTVEEEPNTEDESNACVYLCGNSLGLQNRRTAEMVLAELDVWADQAVQGHFVHSEGRNWKNMTDLVNPILARLVGAAKSTEVACTGSLTTNLHILMTTFYRPTKERYKILCEANCFPSDLYAFTSQIEMHGLDPKEALISLTPRPREFTLRLEDIISAINREGQSIALVIFSGVQFYTGQAFSIKQITAAGHQQGCIVGWDLAHAIGNIPLELNDWQVDFAAWCSYKYLNAGPGAIAGLFVHENWTSDPTKLGGPHGRPRLAGWFGHNPATRFQMPDQYEPMRGAGQFVHSNSDVLSVISLYSSLQLFWSYPGGMSGLRARSEELTGYIEMCLQGLSSYVNPQYAVDYPDSLNEQQSSRARTVGFTIITPSIPAQRGSQLSLMFLPSGKGLVIKIARQLLELGIVADEREPDVIRFSPVPMYNSFEDCRKTVEALNSILETQNLTSAVSS

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0L0VCN0A0A0L0VCN0_9BASIBNA5528

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias54-75Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJIL01000073
EMBL· GenBank· DDBJ
KNE97053.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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