| IED ID | IndEnz0002008533 |
| Enzyme Type ID | protease008533 |
| Protein Name |
Alkaline protease 1 ALP EC 3.4.21.63 Aspergillopeptidase B Aspergillus proteinase B Elastase Elastinolytic serine proteinase Oryzin |
| Gene Name | alp1 alk1 alp AFUB_068800 |
| Organism | Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus) |
| Enzyme Sequence | MLSIKRTLLLLGAVLPAVFGAPVQETRRAAQKIPGKYIVTFKPGTDTATIESHTLWATDLHKRNLERRDTTSGEPPVGIEKSYKIKDFAAYAGSFDDATIEEIRKSADVAHVEEDQIWYLDALTTQKGAPWGLGSISHKGQASTDYIYDTSAGAGTYAYVVDSGINVNHVEFESRASLAYNAAGGSHVDSIGHGTHVAGTIGGKTYGVAKKTNLLSVKVFQGESSSTSIILDGFNWAVNDIVSKGRTKKAAINMSLGGGYSYAFNNAVENAFDEGVLSVVAAGNENSDASNTSPASAPNALTVAAINKSNARASFSNYGSVVDIFAPGQDILSAWIGSTTATNTISGTSMATPHIVGLSVYLMGLENLSGPAAVTARIKELATNGVVTNVKGSPNKLAYNGNA |
| Enzyme Length | 403 |
| Uniprot Accession Number | B0Y708 |
| Absorption | |
| Active Site | ACT_SITE 162; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 193; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 349; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides.; EC=3.4.21.63; |
| DNA Binding | |
| EC Number | 3.4.21.63 |
| Enzyme Function | FUNCTION: Secreted alkaline protease that allows assimilation of proteinaceous substrates (By similarity). Acts as a significant virulence factor in invasive aspergillosis. Involved in immune evasion from the human and mice complement systems during infection. Efficiently cleaves important components of the complement cascade such as such as C3, C4, C5, and C1q, as well as IgG, which leads to down-regulation of complement activation at the hyphal surface (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (2); Glycosylation (3); Propeptide (1); Signal peptide (1) |
| Keywords | Glycoprotein;Hydrolase;Protease;Secreted;Serine protease;Signal;Virulence;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 42,190 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |