Q8PM33 · KYNU_XANAC

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 site105pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site106pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site133-136pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site218pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site221pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site243pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site273pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site301pyridoxal 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

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
      XAC1601

Organism names

Accessions

  • Primary accession
    Q8PM33

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00003570141-423Kynureninase
Modified residue244N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Structure

Family & Domains

Sequence similarities

Belongs to the kynureninase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    423
  • Mass (Da)
    45,845
  • Last updated
    2002-10-01 v1
  • Checksum
    D05719233F2F29BC
MTDPLSRAHAAALDAADPLRNLRDAFVFPQHGDDDQTYFVGNSLGLQPRAARAMVDEVLDQWGALAVEGHFTGPTQWLTYHQLVGDALARVVGAQPGEVVAMNTLSVNLHLMMASFYRPTAERGAILIEAGAFPSDRHAVESQLRLHGLDPATHLIEVEADEPNGTVSMSAIAEAIAQHGPHLALVLWPGIQYRTGQAFDLAEIVRLARAQGAAVGLDLAHAVGNLPLTLHDDGVDFAVWCHYKYLNAGPGAVGGCFVHARHATSDLPRMAGWWGHEQQTRFRMDPQFVPSPGAEGWQLSNPPVLALAPLRASLALFDQAGMAALRAKSEQLTGHLEQMIHARVPQVLQIVTPVEPARRGCQLSLRVAGGRARGRALFEHLHAAGVLGDWREPDVIRIAPVPLYNRFSDLHTFVEQVEAWAAA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE008923
EMBL· GenBank· DDBJ
AAM36469.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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