Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A5D0ILQ9 · A0A5D0ILQ9_9FLAO

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 site103pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site104pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site131-134pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site216pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site219pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site241pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site272pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site300pyridoxal 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
    • L-kynurenine hydrolase

Gene names

    • Name
      kynU
    • ORF names
      FUA24_05450

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • B011
  • Taxonomic lineage
    Bacteria > Bacteroidota > Flavobacteriia > Flavobacteriales > Flavobacteriaceae

Accessions

  • Primary accession
    A0A5D0ILQ9

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue242N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Belongs to the kynureninase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    419
  • Mass (Da)
    47,805
  • Last updated
    2019-11-13 v1
  • MD5 Checksum
    FC46CA49E64103A3B80B70FA6372C44A
MLGLDFALEQDKKDVLKPYKDQFYIPKDKHGNNLIYMTGNSLGLQPKSTKHYINQELTDWAALGVEGHFEAKNPWLPYHEFLTESMAKVVGAKPIEVVVMNTLTTNLHLMMVSFYKPTKTRYKILIESDAFPSDKYAVESQLRHHGFDHNEGLILWQPRDNEELLRYEDLEAILDTQGDEIALIMIGGINYYTGQYFNLKRITELGHKHGCKVGFDCAHGAGNVKLNLHDSGADFAVWCTYKYLNSGPGSLAGCFVHERHAHNKDLNRFTGWWSHNKATRFTMRDEFDQLPGAEGWQLSNPPILSMAAIKASLDIFHEVGIDALVEKSKQLTGYFEFLLKELGDDIIRIITPKHPEERGCQLSIQVKNADKTLHHKLTEAGVITDWREPDVIRCAPVPLYNSFEDVYVLVEKLKTILNE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VSDQ01000409
EMBL· GenBank· DDBJ
TYA84464.1
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.
Help