UniProt ID: Q5BKW9 |
FUNCTION: Has both L-asparaginase and beta-aspartyl peptidase activity. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine. {ECO:0000250}. CATALYTIC ACTIVITY: Reaction=H2O + L-asparagine = L-aspartate + NH4(+); Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1; Evidence={ECO:0000250|UniProtKB:Q7L266}; CATALYTIC ACTIVITY: Reaction=Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.; EC=3.4.19.5; Evidence={ECO:0000250|UniProtKB:Q7L266}; SUBUNIT: Heterodimer of an alpha and beta chain produced by autocleavage. {ECO:0000250}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7L266}. PTM: Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity. {ECO:0000250|UniProtKB:Q7L266}. DISRUPTION PHENOTYPE: Abnormal and deformed fish at 6 dpf. {ECO:0000269|PubMed:27106100}. SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}. |
UniProt ID: B2GNT8 |
CATALYTIC ACTIVITY: Reaction=Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.; EC=3.4.19.5; Evidence={ECO:0000256|ARBA:ARBA00000306}; CATALYTIC ACTIVITY: Reaction=H2O + L-asparagine = L-aspartate + NH4(+); Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1; Evidence={ECO:0000256|ARBA:ARBA00000667}; SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000256|ARBA:ARBA00010872}. |
This information was provided by UniProt through a collaboration with ZFIN. (1) |