| IED ID | IndEnz0005000767 |
| Enzyme Type ID | lipase000767 |
| Protein Name |
Phospholipase A1 1 EC 3.1.1.32 EC 3.1.1.4 Allergen Dol m I allergen Dol m 1 Fragment |
| Gene Name | |
| Organism | Dolichovespula maculata (Bald-faced hornet) (Vespula maculata) |
| 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) Dolichovespula Dolichovespula maculata (Bald-faced hornet) (Vespula maculata) |
| Enzyme Sequence | RLIMFVGDPSSSNELDRFSVCPFSNDTVKMIFLTRENRKHDFYTLDTMNRHNEFKKSIIKRPVVFITHGFTSSATEKNFVAMSEALMHTGDFLIIMVDWRMAACTDEYPGLKYMFYKAAVGNTRLVGNFIAMIAKKLVEQYKVPMTNIRLVGHSLGAHISGFAGKRVQELKLGKFSEIIGLDPAGPSFKKNDCSERICETDAHYVQILHTSSNLGTERTLGTVDFYINNGSNQPGCRYIIGETCSHTRAVKYFTECIRRECCLIGVPQSKNPQPVSKCTRNECVCVGLNAKKYPKRGSFYVPVEAEAPYCNNNGKII |
| Enzyme Length | 317 |
| Uniprot Accession Number | Q06478 |
| Absorption | |
| Active Site | ACT_SITE 154; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:A0A0M3KKW3; ACT_SITE 182; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 246; /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:0000305|PubMed:8458431}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000305|PubMed:8458431}; |
| DNA Binding | |
| EC Number | 3.1.1.32; 3.1.1.4 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with phospholipase A1 (EC 3.1.1.32) and phospholipase A2 (EC 3.1.1.4) activities. Shows hemolytic activity (By similarity). {ECO:0000250|UniProtKB:P0DMB7, ECO:0000305|PubMed:8458431}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Glycosylation (2); Natural variant (1); Non-terminal residue (1); Propeptide (1); Signal peptide (1) |
| Keywords | Allergen;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8458431}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL <1..7; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 35,708 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=280 umol/min/mg enzyme toward egg yolk {ECO:0000269|PubMed:8458431}; |
| Metal Binding | |
| Rhea ID | RHEA:18689; RHEA:15801 |
| Cross Reference Brenda |