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MGP005537

UniProt Annotations

Entry Information
Gene Namecysteine conjugate-beta lyase 2
Protein EntryKAT3_HUMAN
UniProt IDQ6YP21
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q6YP21-1; Sequence=Displayed; Name=2; IsoId=Q6YP21-2; Sequence=VSP_025603, VSP_025604; Note=No experimental confirmation available.; Name=3; IsoId=Q6YP21-3; Sequence=VSP_042841;
Catalytic ActivityAn L-cysteine-S-conjugate + H(2)O = RSH + NH(3) + pyruvate.
Catalytic ActivityL-kynurenine + 2-oxoglutarate = 4-(2- aminophenyl)-2,4-dioxobutanoate + L-glutamate.
Catalytic ActivityL-kynurenine + glyoxylate = 4-(2-aminophenyl)- 2,4-dioxobutanoate + glycine.
CautionThe first non-coding exon of CCBL2 is in common with that of RBMXL1. {ECO:0000305}.
CofactorName=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250};
FunctionCatalyzes the irreversible transamination of the L- tryptophan metabolite L-kynurenine to form kynurenic acid (KA). May catalyze 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). Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2- oxoglutarate as amino group acceptor (in vitro) (By similarity). {ECO:0000250}.
Sequence CautionSequence=AAC72959.1; Type=Frameshift; Positions=336; Evidence={ECO:0000305}; Sequence=AAH00819.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; Sequence=CAG29278.1; Type=Frameshift; Positions=336; Evidence={ECO:0000305}; Sequence=CAI21695.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; Sequence=CAI21696.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; Sequence=CAI41339.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; Sequence=CAI41340.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
SimilarityBelongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000305}.
SubunitHomodimer. {ECO:0000250}.
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