A0A194RL00 · A0A194RL00_PAPMA

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 site91pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site198pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site201pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site223pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site252pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site280pyridoxal 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

    • ORF names
      RR48_07237

Organism names

  • Taxonomic identifier
  • Strain
    • Ya'a_city_454_Pm
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Lepidoptera > Glossata > Ditrysia > Papilionoidea > Papilionidae > Papilioninae > Papilio

Accessions

  • Primary accession
    A0A194RL00

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue224N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the kynureninase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    402
  • Mass (Da)
    46,081
  • Last updated
    2016-10-05 v1
  • Checksum
    AE91FEA41122DF8C
MLDRLDPLRQFRQRFYQTKGEIYLCGHTLGLASIDAEKSLNDLLELWKKEGVSIWMKNNRKYVKYSSLLAELIAPLIKVQPDEIVISGSCTSNIHVAMCTLYKPTSRKYKVLVDDINFSSDRYAVDSQVRLKNLDPRDAVKVVHCQGSFMDEDLIINSMTEDVALLLLPVVYYKTSQVLEMKRICEKANELDIIIGLDVSHAIGVIDLDLQVLNIDFAVWCTYKYLNGGPGSCAGLYINKKHFHLMPGLAGWYGNKDETRLQFKQEFDHQKNANGWQIGTPCLFSMAPLQGSLEIFNEAGIKNIRKKSLRITAYLMYLIDKKLVRYGFNVGNLREDEKRGGHVCVVHVDARRISLALKSRGIVTDFREPDIMRVAPIALYNTYEEVYKFVEILLDIMKRKTY

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KQ459995
EMBL· GenBank· DDBJ
KPJ18513.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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