H1VHT7 · H1VHT7_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 site130pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site131pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site159-162pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site246pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site249pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site271pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site313pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site341pyridoxal 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
    • Biosynthesis of nicotinic acid protein 5
    • L-kynurenine hydrolase

Gene names

    • Name
      BNA5
    • ORF names
      CH063_10523
      , CH63R_01974

Organism names

Accessions

  • Primary accession
    H1VHT7

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue272N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-26Disordered
Domain194-286Aminotransferase class V

Sequence similarities

Belongs to the kynureninase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    470
  • Mass (Da)
    51,543
  • Last updated
    2012-03-21 v1
  • Checksum
    F2F90446EE3C2745
MDPPSRAHAESLDQKDALRHTRDEFVIPTKQDITSKTLAKKDEPSTASSAGQQEKCTYLCGNSLGLQPKRTAVRIQQYLSTWATQGVQGHFKPLEDSPLPTWLDVDAKAAEMMAPIVGAQVAEVAVMQTLTANLHLLMSAFYKPQEGGRHKIILESKAFPSDHFAVETQIRHHGLSPSKSMICIEPPSASQGPTLTTQHILSTIERHASDTALLLLPGIQYYTGQLLDIPTITAFAHKHSILVIWDLAHAVGNVPLKLHEWDVDAAAWCTYKYINGGPGCIGGAFVNSRHTTVTTSVEDPNSETGYVNRLAGWWGNDKSSRFVMATKFHPAPGASGFQLSNPSVLDTTALCASLEVFEAAGGIGPLREKSLRLTGYLEKMLEAMPEDEKALFRVLTPRRPEERGAQLSLLLADGLLDCVMGYFDEVGVVIDERKPNVIRVAPAPLYNTFVDCFDFVEQFGKALRRARRSG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CACQ02003696
EMBL· GenBank· DDBJ
CCF39790.1
EMBL· GenBank· DDBJ
Genomic DNA
LTAN01000002
EMBL· GenBank· DDBJ
OBR13248.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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