A0A210Q8V9 · A0A210Q8V9_MIZYE

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

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 site153pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site154pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site181-184pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site237pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site266pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site269pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site291pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site321pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site349pyridoxal 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
    • L-kynurenine hydrolase

Gene names

    • Name
      KYNU
    • ORF names
      KP79_PYT23621

Organism names

Accessions

  • Primary accession
    A0A210Q8V9

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue292N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain215-386Aminotransferase class V

Sequence similarities

Belongs to the kynureninase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    497
  • Mass (Da)
    56,106
  • Last updated
    2017-09-27 v1
  • Checksum
    6CB863332B71EADF
MNKIMSDDERCRVAKKAKVDALHPCDELKRIAKELDCEMTEKEFAKHMDNIDPLQSLRQDFYYPKMKEVLGTDLSLVDPDEDCVYFCGNSLGLCPKNTKKYMDVELNKWAKIGVQGHLQGEGMPWAKCDECLDADMAKLVGGRPGEVAIMNGLTVNLHLLLISFYRPTAKRHKIMCESKAFPSDHYTFQSQIKLHGFDPETSLLCVEPRKGEMTLRSEDILAKIEEEGESIAVICFSGVQYYTGQVMDMPTITRAGHAKGCYVGFDLAHAAGNVPLYLHDWDIDFACWCTYKYINSSAGCLACIFLHDKHKHNDFPKLLGWWGHNPNTRFNMDNELDLCPGAYGYRISNPAGLLCPPLKASLEIFNKTSMEEIRAKSKLLTAYLEYCIVEKYGQTNGIAEGTLEPIDGDFKHVHVHIFTPSDPEQRGAQLSLSFSVNISYVFKELEKRGVICDERKPSVIRVSPAPLYCSFQDVQRFMEYLDQALKAAAITAALDKE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NEDP02004556
EMBL· GenBank· DDBJ
OWF45173.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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