| IED ID | IndEnz0005000776 |
| Enzyme Type ID | lipase000776 |
| Protein Name |
Phospholipase A1 2 EC 3.1.1.32 Allergen Ves a 1.02 Vespapase allergen Vesp a 1 |
| Gene Name | |
| Organism | Vespa affinis (Lesser banded 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 affinis (Lesser banded hornet) |
| Enzyme Sequence | MMNLKYLLFFCLVQALHYCYAYGDPSLSNELDRFNPCPYSDDTVKMIILTRENKKHDFYTLNTIKNHNEFKKSTIKHQVVFITHGFTSTATAENFLAMAEALLDKGNYLVILIDWRVAACTNEMAGVKLAYYSYAASNTRLVGNYIATVTKMLVQQYNVPMANIRLVGHSLGAHTSGFAGKKVQELRLGKYSEIIGLDPAGPSFKSQECSQRICETDANYVQIIHTSNHLGTLVTLGTVDFYMNNGYNQPGCGLPIIGETCSHTRAVKYFTECIRHECCLIGVPQSKNPQPVSKCTRNQCVCVGLNAKTYPKTGSFYVPVESKAPYCNNKGKII |
| Enzyme Length | 334 |
| Uniprot Accession Number | P0DMB5 |
| Absorption | |
| Active Site | ACT_SITE 170; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:A0A0M3KKW3; ACT_SITE 198; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 263; /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:23159790}; |
| DNA Binding | |
| EC Number | 3.1.1.32 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with phospholipase A1 (EC 3.1.1.32) activity. Shows hemolytic activity (By similarity). Shows a phospholipase A1 enzymatic activity of 6.3 U/ml. {ECO:0000250|UniProtKB:P0DMB7, ECO:0000269|PubMed:23159790}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Loses its activity after heat treatment. {ECO:0000269|PubMed:23159790}; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Propeptide (1); Signal peptide (1) |
| Keywords | Allergen;Cytolysis;Disulfide bond;Hemolysis;Hydrolase;Lipid degradation;Lipid metabolism;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23159790}. |
| Modified Residue | |
| Post Translational Modification | PTM: Not glycosylated. {ECO:0000269|PubMed:23159790}. |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 37,303 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:18689 |
| Cross Reference Brenda |