| UniProt functional annotation for Q12567 | |||
| UniProt code: Q12567. |
| Organism: | Aspergillus phoenicis (Aspergillus saitoi). | |
| Taxonomy: | Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. | |
| Function: | Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions, but also accepts a lysine residue in the P1 position, leading to the activation of trypsinogen and chymotrypsinogen A. {ECO:0000269|PubMed:13702766, ECO:0000269|PubMed:21699, ECO:0000269|Ref.4}. | |
| Catalytic activity: | Reaction=Hydrolysis of proteins with broad specificity. Generally favors hydrophobic residues in P1 and P1', but also accepts Lys in P1, which leads to activation of trypsinogen. Does not clot milk.; EC=3.4.23.18; Evidence={ECO:0000269|PubMed:21699}; | |
| Biophysicochemical properties: | pH dependence: Optimum pH is 2.9-3.3. {ECO:0000269|Ref.4}; | |
| Subunit: | Monomer. {ECO:0000269|PubMed:5886141}. | |
| Subcellular location: | Secreted {ECO:0000269|Ref.4}. | |
| Similarity: | Belongs to the peptidase A1 family. {ECO:0000255|PROSITE- ProRule:PRU01103}. | |
Annotations taken from UniProtKB at the EBI.