A0A0L0VCN0 · A0A0L0VCN0_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 site166pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site167pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site194-197pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site250pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site279pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site282pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site304pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site342pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site370pyridoxal 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
    A0A0L0VCN0

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue305N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain147-332Aminotransferase class V

Sequence similarities

Belongs to the kynureninase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    528
  • Mass (Da)
    58,382
  • Last updated
    2015-11-11 v1
  • Checksum
    7039F602B0F6F4DC
MSSTPANHAIWARRLSASGCLSLTDPNFAIYLDSIACVGGLRSEFRFPRKECKSNSQQEYHTFTKEAASNNTESINQTGTVEEEPNTEDESNACVYLCGNSLGLQNRRTAEMVLAELDVWADQAVQGHFVHSEGRNWKNMTDLVNPILARLVGAAKSTEVACTGSLTTNLHILMTTFYRPTKERYKILCEANCFPSDLYAFTSQIEMHGLDPKEALISLTPRPREFTLRLEDIISAINREGQSIALVIFSGVQFYTGQAFSIKQITAAGHQQGCIVGWDLAHAIGNIPLELNDWQVDFAAWCSYKYLNAGPGAIAGLFVHENWTSDPTKLGGPHGRPRLAGWFGHNPATRFQMPDQYEPMRGAGQFVHSNSDVLSVISLYSSLQLFWSYPGGMSGLRARSEELTGYIEMCLQGLSSYVNPQYAVDYPDSLNEQQSSRARTVGFTIITPSIPAQRGSQLSLMFLPSGKGLVIKIARQLLELGIVADEREPDVIRFSPVPMYNSFEDCRKTVEALNSILETQNLTSAVSS

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0L0VCP2A0A0L0VCP2_9BASIBNA5521

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJIL01000073
EMBL· GenBank· DDBJ
KNE97052.1
EMBL· GenBank· DDBJ
Genomic DNA

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