A0A1I5CX70 · A0A1I5CX70_9FLAO

  • Protein
    Kynureninase
  • Gene
    kynU
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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 site107pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site108pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site135-138pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site220pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site223pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site245pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site276pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site304pyridoxal 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
      SAMN04487989_10660

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 23925
  • Taxonomic lineage
    Bacteria > Bacteroidota > Flavobacteriia > Flavobacteriales > Flavobacteriaceae > Bizionia

Accessions

  • Primary accession
    A0A1I5CX70

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue246N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the kynureninase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    422
  • Mass (Da)
    48,099
  • Last updated
    2017-11-22 v1
  • Checksum
    ECF48927578BBDCB
MSNYKTGLDFAKKQDANDPLSSYREQFHIPKDKHNNELIYLCGNSLGLQPKSTKNYINQELEDWANLGVEGHTHAKNPWLPYHEFLTTSMSKVVGAKPIEVVVMNTLTANLHFMMVSFYKPTTTRYKIIIEADAFPSDKYAVESQLRHHGYDDKEGLILWKAREGEELLRYEDLETILDKHGDEVALVMIGGVNYYTGQFFDLKRITKLGHKHGCMVGFDCAHGAGNVELNLHDSGADFAVWCTYKYLNSGPGSLGGCFVHERHAHNKTLNRFTGWWSHNKETRFKMRDEFDVIPGAEGWQLSNPPILSMAAIKASLDIFEEVGIKKLNQKSKDLTAYFEFLLKELGQDTIRIITPNNPDARGCQLSIQVKNADRALHDKLTEAGVISDWREPDVIRCAPVPLYNSYQDIYHMVEKLKNILK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FOVN01000006
EMBL· GenBank· DDBJ
SFN91539.1
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