Detail Information for IndEnz0005000802
IED ID IndEnz0005000802
Enzyme Type ID lipase000802
Protein Name Phospholipase A1
EC 3.1.1.32
Allergen Sol i I
Venom allergen 1
Venom allergen I
allergen Sol i 1
Gene Name
Organism Solenopsis invicta (Red imported fire ant) (Solenopsis wagneri)
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 Formicoidea Formicidae Myrmicinae Solenopsidini Solenopsis Solenopsis invicta (Red imported fire ant) (Solenopsis wagneri)
Enzyme Sequence MRKFAAIFVVFFVQCTHLYSLAQARAEPDPGVVEYLKQSCVYGNSSYINVYLYNSRFQGKNLGNQQSCQDINASLPVVFITHGFTSSAQVSTFKDLANAFVQKGHTAFIVDWSEAACTDGLPGVQFAEYNAAASNTYDIGQLMAKYTVDLMNKCKIPLNNIQYVGHSLGSHVCGFAAKHVKKLINKTMPYILALDPADPSFGSNKCGERICKSDAKRIVVFKTSILGIGENIIGHLLIVFDGGKSQPACSWYDVPCSHSESIVYATGMVSGRCQHLAVPWTAQQRINPIQWKFWRVFTSNIPAYPTSDTTNCVVLNTNVFKNDNTFEGEYHAFPDCARNLFKCRQQ
Enzyme Length 346
Uniprot Accession Number Q68KK0
Absorption
Active Site ACT_SITE 167; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:A0A0M3KKW3; ACT_SITE 195; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 258; /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:15753912};
DNA Binding
EC Number 3.1.1.32
Enzyme Function FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with phospholipase A1 activity. Shows hemolytic activity (Probable). {ECO:0000305|PubMed:15753912}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Glycosylation (3); Propeptide (1); Sequence conflict (8); Signal peptide (1)
Keywords Allergen;Cytolysis;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemolysis;Hydrolase;Lipid degradation;Lipid metabolism;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15753912, ECO:0000269|PubMed:8588684}.
Modified Residue
Post Translational Modification PTM: Contains six disulfide bonds. {ECO:0000250}.; PTM: N-glycosylated; contains mannose. {ECO:0000269|PubMed:15753912}.
Signal Peptide SIGNAL 1..26; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 38,417
Kinetics
Metal Binding
Rhea ID RHEA:18689
Cross Reference Brenda