A0A9E7W235 · A0A9E7W235_9MICO

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.

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 site115pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site116pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site147-150pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site193pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site222pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site225pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site247pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site277pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site303pyridoxal 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 Processquinolinate biosynthetic process
Biological Processtryptophan catabolic process

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
      LJ362_16100

Organism names

  • Taxonomic identifier
  • Strain
    • JSBI002
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Micrococcales > Brevibacteriaceae > Brevibacterium

Accessions

  • Primary accession
    A0A9E7W235

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue248N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for compositional bias, region.

TypeIDPosition(s)Description
Compositional bias1-24Polar residues
Region1-27Disordered

Sequence similarities

Belongs to the kynureninase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    437
  • Mass (Da)
    47,566
  • Last updated
    2023-05-03 v1
  • Checksum
    8F5A1AAD5444B1C8
MTTPDRTATSANSTGSPSSITRADCKQRDANDPLRDCREEFLLPEGTIYLDGNSLGPRTKGAAERAQEVITDEWGTGLIGSWNTAGWWDLPAKLGEKVAGLVGGGAGSTVVTDTTSINLFKAASAALKMQAEDSSDRRVILTQRENFPSDIYMLEGLAEQLGDGYEVRLVDDEEVTAGFPTTMSDEVALVVLTHVNYRTGRLFDMGTTTSAIHSGGAMVIWDLCHSAGALPIDLAGTGADMAIGCTYKFLNGGPGSPAFIWVAEALQNRFSQPLSGWWSHAQPFDMAPDYRPADGIRRYLTGTQGILSMSVAELGLDIHSRVDMEQVREKSLALSDLFIDLVDERLADHPVEVVTPREHAHRGSQVSIRHPEGFAVMSALIERGIIGDYREPEVLRFGLTPLYIGFTEVWNTVEALRDILDNRLWDTPAHKVRGAVT

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-24Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP110341
EMBL· GenBank· DDBJ
UZD62157.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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