A0A2G5HGK0 · A0A2G5HGK0_CERBT

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 site154pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site155pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site184-187pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site272pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site275pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site297pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site328pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site356pyridoxal 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
    • Biosynthesis of nicotinic acid protein 5
    • L-kynurenine hydrolase

Gene names

    • Name
      BNA5
    • ORF names
      CB0940_09212

Organism names

Accessions

  • Primary accession
    A0A2G5HGK0

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue298N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Belongs to the kynureninase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    493
  • Mass (Da)
    54,446
  • Last updated
    2018-01-31 v1
  • Checksum
    47D54B362B488B43
MTSTMDATAAIGLLQQGQKPSWPSNAATLEFAESLDNHNDIPKTFRKDFVVPTKSQLKRKTLHDDAQTSAPASSVEDEAIYFCGNSLGLQPKAVSEYMSAYLKTWGSIAVGGHFTNFEDSPLVAYQDMAADCARKMAPIVGAKDAQEVVAMNTLTVNLHLMMAAFYKPDKAAKKTKIMCEWRPFPSDWYAIESQIEWHGLDPKEEMLLVRPDNEKNGEYDMSTEQICNLITQHKDELALILLPGIQYYSGQLLDIPTITAHAHKHGLTIGWDLAHAAGNVELQLHDWDVDFACWCTYKYMNAGAGAIAGVFVHEKHGDSKKNKALKGWYGHDKSSRFLMNNQFVPTPGAGGFQLSNPSVVDLTCLSAALSVYEKTSMKELRRKALLLTAYAEELLGGISKRNVTEGGEAPFKIITPSDPRQRGTQLSVLFKEELMEEVSAALEENGVICDKRKPGCIRVAPVPLYNTFGDVARFMQIIEAALKNKGKASEDSE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LKMD01000106
EMBL· GenBank· DDBJ
PIA91659.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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