| IED ID | IndEnz0005000775 |
| Enzyme Type ID | lipase000775 |
| Protein Name |
Phospholipase A1 2 EC 3.1.1.32 allergen Pol d 1 Fragment |
| Gene Name | |
| Organism | Polistes dominula (European paper wasp) (Vespa dominula) |
| 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) Polistinae (paper wasps) Polistini Polistes Polistes dominula (European paper wasp) (Vespa dominula) |
| Enzyme Sequence | ADDLTTLRNGTLDRGITPDCTFNEKDIELHVYSRDKRNGIILKKEILKNYDLFQKSQISHQIAILIHGFLSTGNNENFDAMAKALIEIDNFLVISVDWKKGACNAFASTNDVLGYSQAVGNTRHVGKYVADFTKLLVEQYKVPMSNIRLIGHSLGAHTSGFAGKEVQRLKLGKYKEIIGLDPAGPSFLTNKCPNRLCETDAEYVQAIHTSAILGVYYNVGSVDFYVNYGKSQPGCSEPSCSHTKAVKYLTECIKRECCLIGTPWKSYFSTPKPISQCKRDTCVCVGLNAQSYPAKGSFYVPVEKDAPYCHNEGIKL |
| Enzyme Length | 316 |
| Uniprot Accession Number | Q6Q251 |
| Absorption | |
| Active Site | ACT_SITE 153; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:A0A0M3KKW3; ACT_SITE 181; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 242; /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:P0DMB7}; |
| 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). {ECO:0000250|UniProtKB:P0DMB7}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Non-terminal residue (1); 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:0000305|PubMed:16196201}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL <1..4; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 35,059 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:18689 |
| Cross Reference Brenda |