A0A7D9D3L5 · A0A7D9D3L5_9GAMM

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 site219pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site222pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site244pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site275pyridoxal 5'-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
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
      JTBM06_V1_100017

Organism names

  • Taxonomic identifier
  • Strain
    • Gfbio:sag-sample-m06:053724c1-46a9-4a36-b237-ea2bf867836b
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Woeseiales > Woeseiaceae > environmental samples

Accessions

  • Primary accession
    A0A7D9D3L5

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue245N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Belongs to the kynureninase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    424
  • Mass (Da)
    47,917
  • Last updated
    2020-12-02 v1
  • Checksum
    DBD817CBFA64C22A
MTNFESSREYAQSLDATDELRRFRDYFNFPVDKDGRQNIYLCGNSLGLQSKLAVQYIEEELKKWADSCVEGHFTGRRPWVQYHRESTRGLAYLTGARENEVVAMNSLTVNLHLMMTTFYRPDADRYKIIIESTAFPSDRYAVMSQIRLHDFDPADAMLEWEPRDDDELHSDDLQALLDEHGASTALLLLPGVQYYNGQVLDMAGLCRLAKTTGCAIGLDLAHAIGNVPLALHDWAPDFAIWCTYKYLNTGPGSVGGAFVHSRHLDSADRKQLLGWWSNEEATRFKMAPTFVPAEGVDKWQLSCPAVLAQAPLLASLEIFEEAGIDKLRAKSMELTGYLDFLLRQGFAGRIESITPETARGCQLSLVVCDDKVDAKSVFRKLEALNITVDWREPNVIRVAPVPLYNSFEDVYEFTERLEIAMSES

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LR633967
EMBL· GenBank· DDBJ
VUX55757.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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