4 experimentally studied proteins
23 sequences in Swiss-Prot
3,107 unique sequences in UniRef100
Eukaryotic aspartylglucosaminidases
| Fam ? Class - Clan - Family | Alt ? Alternative historical name / classification | AN ? UniProt accession number | Name ? UniProt entry name, only given here for Swiss-Prot entries | EC | Organism | Cell-Loc | AAs | Structure | PDB | Km i for Asn [mM] | Vmax i for Asn [μmol/min/mg] | Kcat i for Asn [s-1] |
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| Fam ? Class - Clan - Family | Alt ? Alternative historical name / classification | AN ? UniProt accession number | Name ? UniProt entry name, only given here for Swiss-Prot entries | EC | Organism | Cell-Loc | AAs | Structure | PDB | Km i for Asn [mM] | Vmax i for Asn [μmol/min/mg] | Kcat i for Asn [s-1] |
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Clan 1 contains five families that are to an extent phylogenetically distinct from the other clans, they have aspartylglucosaminidase (AGA) activity in addition to l‑asparaginase activity.
Family 2 is well-studied and contains sequences of eukaryotic origin. One protein structure has been solved, the lysosomal Homo sapiens AGA (P20933), its Km for l‑asparagine is about four times higher than for aspartylglucosamines.
1Varadi, M et al. AlphaFold Protein Structure Database in 2024: providing structure coverage for over 214 million protein sequences. Nucleic Acids Research (2024). Licensed under CC BY 4.0.
2Suzek, B.E. et al. UniRef: comprehensive and non-redundant UniProt reference clusters. Bioinformatics (2007). Licensed under CC BY 4.0. Added classification code to sequence headers.
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