| IED ID | IndEnz0005000807 |
| Enzyme Type ID | lipase000807 |
| Protein Name |
Probable phospholipase A1 magnifin EC 3.1.1.32 |
| Gene Name | |
| Organism | Vespa magnifica (Hornet) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Hymenoptera Apocrita (wasps ants and bees) Aculeata Vespoidea Vespidae (wasps) Vespinae (hornets and yellowjackets) Vespa Vespa magnifica (Hornet) |
| Enzyme Sequence | MNLKYLLLFFCLVQVLHYCYSHGDPSLSNELDRGLIPKCKLVPEQISFVLSTRENQNGVFLTLDNLSKGGILPKSDLSSIPVIFLIHGFISSANNSNYVDMTKALLEKNDCMVISIDWRDGACTHEFKILKFIGYPNAVKNTRAVGKYIADFTKLLMQKYKVSLANIRLIGHSLGAQIAGFAGKEYQKFKLGKYPEIIGLDPAGPLFKSNDCSERICETDAHYVQIIHTSNNLGTERTLGTVDFYVNNGYNQPGCYLSFLGEACSHTRAVKYFTECIRHECCLIGVPQSKNPQPVSKCTRKECVCIGLNAKTYPKTGSFYVPVESKAPYCNNKGKKI |
| Enzyme Length | 337 |
| Uniprot Accession Number | P0CH47 |
| Absorption | |
| Active Site | ACT_SITE 173; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:A0A0M3KKW3; ACT_SITE 201; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 266; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000250|UniProtKB:P0DMB4}; |
| DNA Binding | |
| EC Number | 3.1.1.32 |
| Enzyme Function | FUNCTION: Has phospholipase activity, probably a phospholipase A1 activity as suggested by sequence similarity. In vivo, induces dose-dependently platelet aggregation at nanomolar concentration and induces thrombosis in vivo (PubMed:18023835). {ECO:0000250|UniProtKB:P0DMB4, ECO:0000269|PubMed:18023835}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Propeptide (1); Signal peptide (1) |
| Keywords | Allergen;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Hydrolase;Lipid degradation;Lipid metabolism;Platelet aggregation activating toxin;Secreted;Signal;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18023835}. |
| 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 | 37,617 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:18689 |
| Cross Reference Brenda |