| IED ID | IndEnz0002000601 |
| Enzyme Type ID | protease000601 |
| Protein Name |
Aspergillopepsin-1 EC 3.4.23.18 Aspartic protease pepA Aspergillopepsin I Aspergillopeptidase A Proctase B |
| Gene Name | prtB pepA AN6888 |
| Organism | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Enzyme Sequence | MVVFSKVAAAAFGLSAVASAMPAAPPRQGFTINQLTRAIPKRTINLPAIYANALSKYGGNVPPHIQDAMAHGSAVTTPEQYDVEYLTPVAVGGTTMNLDFDTGSADLWVFSNELPSSQTTGHSVYKPSDNGTRMSGYSWEISYGDGSSAGGDVYRDTVTVGGVTAPGQAVEAASHISEQFTRDQNNDGLLGLAFSSINTVQPKSQTTFFDSVKSQLESPLFAVTLKHQAPGSYDFGYIDQSKYTGELTYTDVDNSQGFWMFSATAGETDFDAIADTGTTLIMIDQSIAEDYYSQVPLAFNNFFYGGWTFPCSAELPSFTVTINGYDAVVPGEHIKYAPVTDGSSTCFGGIQDNQGLPFSILGDVFLKSQYVVFDSEGPQLGFAPQA |
| Enzyme Length | 386 |
| Uniprot Accession Number | O93885 |
| Absorption | |
| Active Site | ACT_SITE 101; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103; ACT_SITE 275; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | 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:0000250|UniProtKB:Q12567}; |
| DNA Binding | |
| EC Number | 3.4.23.18 |
| Enzyme Function | 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:0000250|UniProtKB:Q12567}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Propeptide (1); Signal peptide (1) |
| Keywords | Aspartyl protease;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Signal;Zymogen |
| Interact With | |
| Induction | INDUCTION: Expressed, albeit at a very low level. {ECO:0000269|PubMed:10882536}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q12567}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 41,194 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |