A0A7W7GDT4 · A0A7W7GDT4_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 site97pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site98pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site125-128pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site194pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site197pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site219pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site249pyridoxal 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
      BJ982_007511

Organism names

  • Taxonomic identifier
  • Strain
    • DSM 45784
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Streptosporangiales > Streptosporangiaceae > Sphaerisporangium

Accessions

  • Primary accession
    A0A7W7GDT4

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue220N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Belongs to the kynureninase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    394
  • Mass (Da)
    42,426
  • Last updated
    2021-06-02 v1
  • Checksum
    548386A8CB8DFC73
MTELDARAAKLDAGDPLGYLRAEFDLDPAVVYLDGNSLGAPPRQVAGRVEEVVRKQWGRRLIRSWPERWWVAPERVGEKIAPLVGAAPGQVVVADSTSVNVFKALVGAVRLAPGRREIVVDATTFPTDGYVAESAAELTGTMVVPAVVDELDDVLSERTAVVLLNQVDYKTGRLHDMAAATEKIHAAGARAVWDLCHSVGVLPIELDALGVDVAVGCTYKFLNGGPGSPAFIYVPRHLQAEFRQPLPGWGGHRDPFAMEPSYDPAPGIARARAGTPDILSLLALDAALEVWDGLDLTAVRAKGLALTGFFMECVDELLGHAVEVVTPRGEWRGHQVSLRHHDARTLVAELTARDVIGDYRPPDVLRFGFAPLYVTYGDALRAARALADLLAETG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACHND010000001
EMBL· GenBank· DDBJ
MBB4705967.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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