Detail Information for IndEnz0005000800
IED ID IndEnz0005000800
Enzyme Type ID lipase000800
Protein Name Phospholipase A1
EC 3.1.1.32
allergen Poly p 1
Gene Name
Organism Polybia paulista (Neotropical social wasp) (Swarm-founding polistine 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) Polistinae (paper wasps) Epiponini Polybia Polybia paulista (Neotropical social wasp) (Swarm-founding polistine wasp)
Enzyme Sequence MNFKYSILFICFGTLDRGLIPECPFNEYDILFFVYTRQQRDGIVLTEETLQNYDLFKKSTISRQVVFIDHGFLSNGNNENFIAMAKALIEKDNFLVISVDWKKGACNAFASTLDYLGYSTAVGNTRHVGKYVADFTKLLVEQYKVSMSNIRLIGHSLGAHTSGFAGKEVQELKLNKYSNIDGLDPAGPSFDSNDCPERLCETDAEYVQIIHTSNILGVYSKIGTVDFYMNYGSHQPGCGRFFSPSCSHTKAVKYLTECIKHECCLIGTPWKKYFSTPKPISQCTKDTCVCVGLNAKSYPARGSFYVPVEATAPYCHNEGIKL
Enzyme Length 322
Uniprot Accession Number A2VBC4
Absorption
Active Site ACT_SITE 156; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:A0A0M3KKW3; ACT_SITE 184; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 248; /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:0000269|PubMed:17761205};
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 (PubMed:17761205). Shows hemolytic activity (PubMed:17761205). {ECO:0000269|PubMed:17761205}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (6); 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:17761205}.
Modified Residue
Post Translational Modification PTM: Contains six disulfide bonds. {ECO:0000269|PubMed:17761205}.; PTM: Is not glycosylated. {ECO:0000269|PubMed:17761205}.
Signal Peptide SIGNAL 1..18; /evidence=ECO:0000269|PubMed:17761205
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 36,082
Kinetics
Metal Binding
Rhea ID RHEA:18689
Cross Reference Brenda 3.1.1.32;