IED ID | IndEnz0005000810 |
Enzyme Type ID | lipase000810 |
Protein Name |
Phospholipase A1 EC 3.1.1.32 EC 3.1.1.4 Allergen Ves v I allergen Ves v 1 |
Gene Name | |
Organism | Vespula vulgaris (Yellow jacket) (Wasp) |
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) Vespula Vespula vulgaris (Yellow jacket) (Wasp) |
Enzyme Sequence | MEENMNLKYLLLFVYFVQVLNCCYGHGDPLSYELDRGPKCPFNSDTVSIIIETRENRNRDLYTLQTLQNHPEFKKKTITRPVVFITHGFTSSASETNFINLAKALVDKDNYMVISIDWQTAACTNEAAGLKYLYYPTAARNTRLVGQYIATITQKLVKHYKISMANIRLIGHSLGAHASGFAGKKVQELKLGKYSEIIGLDPARPSFDSNHCSERLCETDAEYVQIIHTSNYLGTEKTLGTVDFYMNNGKNQPGCGRFFSEVCSHSRAVIYMAECIKHECCLIGIPKSKSSQPISSCTKQECVCVGLNAKKYPSRGSFYVPVESTAPFCNNKGKII |
Enzyme Length | 336 |
Uniprot Accession Number | P49369 |
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 265; /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:8828537}; 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:8828537}; |
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. {ECO:0000250|UniProtKB:P0DMB7, ECO:0000305|PubMed:8828537}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Disulfide bond (6); Propeptide (1); Sequence conflict (1); Signal peptide (1) |
Keywords | Allergen;Direct protein sequencing;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Secreted;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8828537}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 37,676 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:18689; RHEA:15801 |
Cross Reference Brenda |