| IED ID | IndEnz0005000927 |
| Enzyme Type ID | lipase000927 |
| Protein Name |
Phospholipase A1 VesT1.02 EC 3.1.1.32 |
| Gene Name | |
| Organism | Vespa tropica (Greater banded hornet) (Sphex tropica) |
| 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 tropica (Greater banded hornet) (Sphex tropica) |
| Enzyme Sequence | FLPIPYSDDTVKMIILTSENKKHDFYTLDTIKKHNELKESIIKHQVAFITHGFTSSATAEHFLAVAEALLDKGNYLVIMIDWRVAACTNEIAGVKLAYYNYAVSNTRLVGNYIATVTKMLVQKYNVPMANIRLIGHSLGAHISGFAGKKVQELGLGKYSEIIGLDPAGPSFKSQECSQRICETDANYVQIIHTSNHLGTERTLGTVDFYMNNGKNQPGCGLPIIGETCSHTRAVKYFTECIRHECCLIGVPQSKNPQPVSKCTRNECVCVGLNAKTYPKTGSFYVPVESKAPYCNNKGKKI |
| Enzyme Length | 301 |
| Uniprot Accession Number | P0DPT0 |
| Absorption | |
| Active Site | ACT_SITE 137; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 165; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 230; /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:0000269|PubMed:29605550}; |
| DNA Binding | |
| EC Number | 3.1.1.32 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with phospholipase A1 activity (PubMed:29605550). Shows hemolytic activity (By similarity). {ECO:0000250|UniProtKB:P0DMB7, ECO:0000269|PubMed:29605550}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Loses its activity after heat treatment. {ECO:0000269|PubMed:29605550}; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Sequence conflict (1) |
| Keywords | Allergen;Cytolysis;Direct protein sequencing;Disulfide bond;Hemolysis;Hydrolase;Lipid degradation;Lipid metabolism;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29605550}. |
| Modified Residue | |
| Post Translational Modification | PTM: Is not glycosylated. {ECO:0000269|PubMed:29605550}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 33,307 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=214.6 umol/min/ug enzyme {ECO:0000269|PubMed:29605550}; |
| Metal Binding | |
| Rhea ID | RHEA:18689 |
| Cross Reference Brenda | 3.1.1.32; |