14 experimentally studied proteins
1 sequences in Swiss-Prot
7,894 unique sequences in UniRef100
Bacterial L-asparaginases
Bacillus lichenformis L-asparaginase, a dimeric enzyme with a Km in potentially the in the micromolar range
| 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] | |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 1-2-5 | - | A0A3Q8UES2 | 3.5.1.1 | Bacillus cereus | - | 325 | Homo dimer i Determined by gel filtration chromatography | - | 9.38 | - | 63.6 | ||
| 1-2-5 | BlA, type I | P30363 | ASPG_BACLI | 3.5.1.1 | Bacillus licheniformis | Cytoplasm | 322 | - | - | - | - | - | |
| 1-2-5 | i Very similar sequence to ASPG_BACLI, but not identical | A0A6I7U6Y2 | 3.5.1.1 | Bacillus licheniformis | - | 322 | Homo dimer | 7CB4 PDBs | 2.96 | - | - | ||
| 1-2-5 | i Very similar sequence to ASPG_BACLI, but not identical | A0A3G1GZN5 | 3.5.1.1 | Bacillus licheniformis | - | 322 | - | - | 0.0106 | - | 23.96 | ||
| 1-2-5 | - | Q5KXR8 | 3.5.1.1 | Geobacillus kaustophilus | - | 323 | - | - | 0.487 | 243.9 | - | ||
| 1-2-5 | - | A0A7U9P5Z0 | 3.5.1.1 | Geobacillus thermopakistaniensis | - | 323 | i "Biochemical characterization revealed that ASNaseGt existed in an oligomeric form in solution which can be converted to the most active tetrameric form by the addition of thiol reducers." | - | 0.35 | 2735 | 1595 | ||
| 1-2-5 | - | F0TGT0 | 3.5.1.1 | Lactobacillus acidophilus | - | 331 | - | - | 6.23 | - | 0.51 | ||
| 1-2-5 | - | A0AAD1ETD3 | 3.5.1.1 | Lactobacillus casei | - | 324 | - | - | 0.0123 i Sequence may not be exact match | - | - | ||
| 1-2-5 | - | F9URL2 | 3.5.1.1 | Lactobacillus plantarum | - | 324 | - | - | 7.85 | - | 2.33 | ||
| 1-2-5 | - | Q38YS9 | 3.5.1.1 | Latilactobacillus sakei | - | 324 | Homo dimer i Determined by gel filtration | - | 7.64 | - | 4.09 | ||
| 1-2-5 | - | I6ZQC6 | 3.5.1.1 | Melioribacter roseus | - | 326 | - | - | 2.7 | 163 | 96 | ||
| 1-2-5 | i brenda-enzymes.org, archived id J9H7D1 | A0A9X4QZ02 | 3.5.1.1 | Staphylococcus sp. | - | 324 | Homo dimer i Size-exclusion chromatography determined | - | 2.2 | - | 4.65 | ||
| 1-2-5 | - | A0A062WR39 | 3.5.1.1 | Streptococcus pneumoniae | - | 320 | Monomer i Context unknown, paper to be published | 9D91 i Paper to be published | - | - | - | ||
| 1-2-5 | - | Q5M2S9 | 3.5.1.1 | Streptococcus thermophilus | - | 322 | - | - | 2.34 | - | 101 |
| 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] | |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 1-2-5 | BlA, type I | P30363 | ASPG_BACLI | 3.5.1.1 | Bacillus licheniformis | Cytoplasm | 322 | - | - | - | - | - |
Clan 2 is closest to Clan 1 on the tree, but there is a distinct phylogenetic gap. The sequences are also predominantly of bacterial origin, however, this clan is not as well studied as Clan 1.
One protein structure has been solved in Family 5: the Bacillus licheniformis BlA (closest in Swiss-Prot: P30363, actual: A0A6I7U6Y2). The authors report that the native form is homo dimeric and despite similar overall folded topology, there are notable structural differences to other L-asparaginases with solved structures: a longer loop near the active site, a unique linker loop and a different β-hairpin structure in the N-terminal domain. To an extent, these specificities are present throughout Clan 2 in predicted AlphaFold structures, too. The BlA and similar sequences have caused issues in the historical classification, as they show similarities to both "type I" and "type II" L-asparaginases.
