A0A013S2F9 · A0A013S2F9_9GAMM

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.
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 site97pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site98pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site129-132pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site201pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site204pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site226pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site256pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site282pyridoxal 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
    • ORF names
      J690_1825

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 742879
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Moraxellales > Moraxellaceae > Acinetobacter > Acinetobacter calcoaceticus/baumannii complex

Accessions

  • Primary accession
    A0A013S2F9

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue227N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Belongs to the kynureninase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    416
  • Mass (Da)
    47,823
  • Last updated
    2014-06-11 v1
  • Checksum
    98A6E79A66F797D7
MITHEQCLYWDQEDELKKFKDEFALPENIIYLDGNSLGARPKKSLEVAQHIIAKEWGEDLINSWNKADWWGLPTRLGDKVAQLIGAEKGEVVISDSTTLNLFKVLSAAVKIQAEKFPECKIIVAEKDAFPTDIYIIEGFIDLIHQGYQVELIDGTDDLSRVLAKDVAVVVLSHVNYRTGYFYDMESINQQIHAKDALIIWDLCHSVGAVPMDLNQSNSDFAIGCTYKYLNGGPGSPALLWVNRKHRDQFWQPLSGWWSHKKPFDMAQHYEPANSIRRYLCGTQPIISMSLIECGIDIFLQADMQQIREKSLKLTDLFIQLVQQECAQFGFELITPLNHKYRGSHVSYRHEFGYEIIQALIARGVIGDYREPEVLRFGITPLYLGFEDIWNAVQQLKQIMLNSEWKNERYLVRSEVT

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JFYC01000006
EMBL· GenBank· DDBJ
EXS28549.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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