1 experimentally studied proteins
0 sequences in Swiss-Prot
1,153 unique sequences in UniRef100
Mostly fungal asparaginases, like the Rhizomucor miehei L-asparaginase with a Km in the micromolar range
Additional ankyrin repeats
Clan 5: Family 14, Family 15, Family 16, Family 17, Family 18
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] | |
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1-5-15 | RmAI | W0G253 | 3.5.1.1 | Rhizomucor miehei | - | 682 | Homo dimer i Determined by gel filtration. Has additional ankyrin repeats. | - | 0.133 i brenda-enzymes.org | 3380.0 | 676 |
Clan 5 is the clan that holds many of the historical bacterial "type I" L-asparaginases as well as L-asparaginases from fungi and metazoans, including humans.
Family 15 is similar to Family 14, as most of the sequences also contain ankyrin repeats, however, these L-asparaginases are mostly of fungal origin and lack the extra alpha helix. Many AlphaFold structures seem to have an additional beta sheet instead. At least one protein was studied experimentally: the Rhizomucor miehei RmAI (W0G253) with a relatively high affinity to L-asparagine and negligible L-glutaminase activity.