Detail Information for IndEnz0005000808
IED ID IndEnz0005000808
Enzyme Type ID lipase000808
Protein Name Phospholipase A1
EC 3.1.1.32
allergen Ves s 1
Gene Name
Organism Vespula squamosa (Southern 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 squamosa (Southern yellow jacket) (Wasp)
Enzyme Sequence GSKCPFSDDTVAMVIVTRENRNRDFYTLQTLRNHDEFKKKAITRPVVFITHGFTSSATVESFVDLQTAILEXXXXKVTVSDWRVAACNRTTGLLYYVTAVSNTRLVGRYIATVTKKLVTDYNVSMADIRLIGHSLGAHVSGFAGKEVQKLKLEKYSEIIGLDPAGPSFESNDCAERLCKTDAHYVQIIHTSKKFGIEKSIGHVDFYVNQGNNQPGCGIIPLKDVCSHSRAITYMTECIKRECCLIGIPQSKSSKSISSCTRQECVCVGLKAKSYPNTGSFYVPVESTAPFCNNKGKII
Enzyme Length 298
Uniprot Accession Number P0CH86
Absorption
Active Site ACT_SITE 134; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:A0A0M3KKW3; ACT_SITE 162; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 227; /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:P0DMB4};
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 (By similarity). Shows hemolytic activity (By similarity). {ECO:0000250|UniProtKB:P0DMB4}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (6); Glycosylation (2)
Keywords Allergen;Cytolysis;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemolysis;Hydrolase;Lipid degradation;Lipid metabolism;Secreted
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15753912}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 32,934
Kinetics
Metal Binding
Rhea ID RHEA:18689
Cross Reference Brenda