| IED ID | IndEnz0002009425 |
| Enzyme Type ID | protease009425 |
| Protein Name |
Cuticle-degrading serine protease EC 3.4.21.- Neutral serine protease Aoz1 Aoz PII |
| Gene Name | |
| Organism | Orbilia oligospora (Nematode-trapping fungus) (Arthrobotrys oligospora) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina Orbiliomycetes Orbiliales Orbiliaceae Orbilia Orbilia oligospora (Nematode-trapping fungus) (Arthrobotrys oligospora) |
| Enzyme Sequence | MLTNGLISLLAIAGLATNAFAGPIRKVSNAGAAGAIADKYIVVLKKGLSDSAVSKHTNRISSFHSNVARDLTGARAHGVGRKFRFSSTGFNGYVGGFDKATLQEILNSPEVDYVEQDTVVTTYAEQTDSTWGLDRISHEDYSAPYTYEYDETAAGAGTTVYVIDTGIRISHDEFQTVNGSSRATWGFNSVDKTDSDGNGHGTHCAGTIAGKTYGVSKKAKVVAVKVLSAGGSGSTAGVVSGMNWVAENATPNFSVASMSLGGSKSTALNAAVDCIFNAGITIVVAAGNENQDAKNVSPASAPNAITVGAIDSSNKIASLSNWGTLIDVFAPGVGVLSSWATSDKETKTISGTSMACPHVAGLAAYYISASEGGADPATITDKITSSRRQWSGHREHPWLPKQDRLQRICLSTHSPKTNHQVTIVAS |
| Enzyme Length | 426 |
| Uniprot Accession Number | G3FNQ9 |
| Absorption | |
| Active Site | ACT_SITE 164; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 200; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 353; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by PMSF, SSI, the peptide Phe-Val and by Phe, but not by EDTA. {ECO:0000269|Ref.1}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Hydrolyzes gelatin, casein, the chromogenic substrate azocoll and the cuticle of the nematode P.redivivus. Immobilizes P.redivivus. {ECO:0000269|Ref.1}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|Ref.1}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-8. {ECO:0000269|Ref.1}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (2); Glycosylation (2); Natural variant (9); Propeptide (1); Signal peptide (1) |
| Keywords | Collagen degradation;Direct protein sequencing;Glycoprotein;Hydrolase;Protease;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | INDUCTION: By easily metabolized forms of nitrogen, including ammonia, nitrate and amino acids, and by glucose. |
| 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 | 44,360 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |