1 experimentally studied protein
0 sequences in Swiss-Prot
2,941 unique sequences in UniRef100
Bacterial and some fungal l‑asparaginases
Homo dimeric structure
Contains the Rhizobium etli "type V" l‑asparaginase isoenzyme
Clan 3: Family 3
| 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 3 and Family 3 have l‑asparaginases of both bacterial and fungal origin. The crystal structure of the inducible thermolabile allosteric Rhizobium etli ReAV (Q2K0Z2) has been solved, a homo dimer with a millimolar Km for l‑asparagine.
