H1UZE2 · H1UZE2_COLHI

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 site165pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site166pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site193-196pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site277pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site280pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site302pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site340pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site368pyridoxal 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

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
      CH063_05555
      , CH63R_06939

Organism names

Accessions

  • Primary accession
    H1UZE2

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue303N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region64-83Disordered
Domain140-308Aminotransferase class V

Sequence similarities

Belongs to the kynureninase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    493
  • Mass (Da)
    54,519
  • Last updated
    2012-03-21 v1
  • Checksum
    28464F779A75B3B2
MEFTAFAEQIRSGRTAKFPANANTLEFAQQLDAQDSLGHLRNEFIIPTKGSLKKKSLNGTLPDKQNLNGHANGVNGTNGANGSLEDDETPSVYFCGNSLGVPPKAVKEYIHAQLETWASIGVNGHFQGLDNSPLVCWQDMAEDVAKKSAHIVGALPEEVVMMNTLTANLHFLMASFYRPTEKKHKIILEWRPFPSDHYAIESQIQWHGLDPAKSMVQIQPDENFYISTDLILKTIDEHAEETALILLPGIQYYSGQLFDMPRITEYAQSKGIVVGWDLAHAAGNVELKLHDWNVDFAAWCTYKYQNAGPGSMAGAFVHERHGKVDTSEGKPKFRHRLTGWYGGDKSVRFNMDNNFLPTVGAGGFQVSNPSAIDLASLSGALSVFSKTNMTELRTKSLVLTAYAEHLLDTILATEASGEPPFRVLTPRNAHERGAQLSVLLKDGLLERVTEEFVEAGIVCDKRKPGVIRVAPVPLYCTFQDVWKFMDTLKKAIA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CACQ02000721
EMBL· GenBank· DDBJ
CCF33343.1
EMBL· GenBank· DDBJ
Genomic DNA
LTAN01000004
EMBL· GenBank· DDBJ
OBR11247.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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