A0A0F0HK53 · A0A0F0HK53_9ACTN

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 site102pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site103pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site131-134pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site200pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site203pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site225pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site255pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site281pyridoxal 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
      UK14_02880

Organism names

  • Taxonomic identifier
  • Strain
    • NRRL F-4428
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    A0A0F0HK53

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue226N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Belongs to the kynureninase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    399
  • Mass (Da)
    41,694
  • Last updated
    2015-06-24 v1
  • Checksum
    E77E7F3155DD2CD6
MPGGAADLRDRAAALDAADELAKLRERFVLPDGVVYLDGNSLGALPAGVAATTADVVARQWGELLIRSWEESGWWTAPERTGDKIAPLVGAAAGQVVVGDSTSVNLFKALVGAARLAAPGRTRMLVDAATFPTDGYIAQSAARLTGLTVVPVDPSHAAEAMDADTAVVLLNHVDYRTGRLHDLPALTAAARAAGAVTVWDLCHSAGALPVGLDAHGVDLAVGCTYKYLNGGPGAPAYLYIATRHQDAFDSPLPGWNGHADPFAMTPAYEAAPGASRARVGTPDILSMLALEAALDAWDGVCVEAVRAKSLALTDFFLECVAAYVPQGLVEPVTPAEHEHRGSQVSLRTGNAREVMGELISRGVIGDFRAPDVLRFGFTPLYVGFADVERAARTLGHIFG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JYJI01000011
EMBL· GenBank· DDBJ
KJK54183.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
Help