Detail Information for IndEnz0005000768
IED ID IndEnz0005000768
Enzyme Type ID lipase000768
Protein Name Phospholipase A1 1
EC 3.1.1.32
allergen Pol d 1
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 MNFKYSILFICFVKVLDNCYAADDLTTLRNGTLDRGITPDCTFNEKDIELHVYSRDKRNGIILKKEILKNYDLFQKSQISHQIAILIHGFLSTGNNENFDAMAKALIEIDNFLVISVDWKKGACNAFASTNDVLGYSQAVGNTRHVGKYVADFTKLLVEQYKVPMSNIRLIGHSLGAHTSGFAGKEVQRLKLGKYKEIIGLDPAGPSFLTNKCPNRLCETDAEYVQAIHTSAILGVYYNVGSVDFYVNYGKSQPGCSEPSCSHTKAVKYLTECIKRECCLIGTPWKSYFSTPKPISQCKRDTCVCVGLNAQSYPAKGSFYVPVDKDAPYCHNEGIKL
Enzyme Length 337
Uniprot Accession Number Q6Q252
Absorption
Active Site ACT_SITE 174; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:A0A0M3KKW3; ACT_SITE 202; /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: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); Propeptide (1); Signal peptide (1)
Keywords Allergen;Cytolysis;Direct protein sequencing;Disulfide bond;Hemolysis;Hydrolase;Lipid degradation;Lipid metabolism;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16196201}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..21; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 37,559
Kinetics
Metal Binding
Rhea ID RHEA:18689
Cross Reference Brenda 3.1.1.32;