C7R815 · C7R815_KANKD

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 site106pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site107pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site134-137pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site219pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site222pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site244pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site275pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site303pyridoxal 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
    • Ordered locus names
      Kkor_0377

Organism names

Accessions

  • Primary accession
    C7R815

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue245N6-(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
    425
  • Mass (Da)
    48,321
  • Last updated
    2009-10-13 v1
  • Checksum
    7B50E691B06ED267
MNNLFSLEHAQQLDQQDPLHHMRDQFHIPKQDNGDDEIYLCGNSLGLQPKRTQEYLNYELNQWQKLGVKGHFSGDFPWMPYHEFLTEESAKLVGAKNTEVVCMNSLTANLHFMMVSFYRPSKTRNKILIEDHAFPSDHYAVESQIRFHGFDPDQAMLLAKPREGEETLRTEDLLNLIEMHGDEIALIMLPGVQYYTGQVLDMKTITEAGHAKGCMVGFDLAHATGNIPMNLHDWNVDFAAWCTYKYLNSGPGSVAGCFVHEKHHSNLELPRFAGWWGHDKESRFRMENRFVPMQSAEAWQVSNPPILSLAAIRASLDTVKEAGGIDALREKSLKLTRYLRDLLEQELSEEINILTPADNSASGCQLSLTVNLHVLDGKTVFDRIEAAGVTCDFRHPNVIRVAPVPLYNSFEDAYRFVSILKDSLQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001707
EMBL· GenBank· DDBJ
ACV25797.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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