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Q54KM6 · KAT_DICDI

Function

function

Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond (By similarity).

Catalytic activity

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Pathway

Amino-acid degradation; L-kynurenine degradation; kynurenate from L-kynurenine: step 1/2.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site46substrate
Binding site198substrate
Binding site413substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentmitochondrion
Molecular Functioncysteine-S-conjugate beta-lyase activity
Molecular Functionglutamine-phenylpyruvate transaminase activity
Molecular Functionkynurenine-oxoglutarate transaminase activity
Molecular Functionpyridoxal phosphate binding
Molecular Functiontransaminase activity
Biological Processbiosynthetic process
Biological ProcessL-kynurenine catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Kynurenine--oxoglutarate transaminase
  • EC number
  • Alternative names
    • Glutamine transaminase K (EC:4.4.1.13) . EC:4.4.1.13 (UniProtKB | ENZYME | Rhea)
    • Glutamine--phenylpyruvate transaminase (EC:2.6.1.64) . EC:2.6.1.64 (UniProtKB | ENZYME | Rhea)
    • Kynurenine aminotransferase

Gene names

    • Name
      ccbl
    • Synonyms
      kat
    • ORF names
      DDB_G0287269

Organism names

Accessions

  • Primary accession
    Q54KM6

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00003277251-435Kynurenine--oxoglutarate transaminase
Modified residue262N6-(pyridoxal phosphate)lysine

Proteomic databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    435
  • Mass (Da)
    48,553
  • Last updated
    2005-05-24 v1
  • MD5 Checksum
    1EDB932353353DA16BD051313FE908DE
MLRNTVKRLMTYTFKPSKQTSSFGPSVWLEFSPLAIKYNAVNLGQGFPNFEPPKFVKDAMIKTIEVGGFNQYTRSPGHIRLVKALSSVYSPYFGRELNAMTEIMVGVGASESLFAAISSIVNEGDEVILIEPFFDIYIGPILMAGGIPKFVTLKEEESSQAGSSDKKRSSKHWKINKEELAAAFTDKTKLIILNNPHNPVGKVYSKEELQEIADVVAKHGPNTTVISDEVYEWMTFDGEEHHRFATLPGMWERTITIGSAGKTFSITGWKVGWCIGPSNIIGAIANTHQYVPFSVPTPTQEAVAIALEQPNIKDYFKELATMYQNKRDTLLNSLTQAGLDPVIPQGTYFIMGDTSSIHLQGDQGKDTSITGMGLHLRDWNIARYLTTEYGVTTIPPSAFYCDDHQKIPENFVRFTFCKDDLTLQKAHDNLLKLKK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAFI02000099
EMBL· GenBank· DDBJ
EAL63836.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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