| IED ID | IndEnz0002006693 |
| Enzyme Type ID | protease006693 |
| Protein Name |
Basic phospholipase A2 beta-bungarotoxin A2 chain Beta-BuTX A2 chain svPLA2 EC 3.1.1.4 Phosphatidylcholine 2-acylhydrolase Fragment |
| Gene Name | |
| Organism | Bungarus candidus (Malayan krait) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Lepidosauria (lepidosaurs) Squamata (squamates) Bifurcata (split-tongued squamates) Unidentata Episquamata Toxicofera Serpentes (snakes) Colubroidea Elapidae Bungarinae Bungarus Bungarus candidus (Malayan krait) |
| Enzyme Sequence | AVCVSLLGAANIPPHPFNLINFMKMIRYTIPCEKTWGEYVDYGCYCGVGGSGRPIDALDRCCYVHDNCYGDAEKKHKCNPKMQSYSYKLTKRTTSAMVPQVLVHVLSVIVTARQPSASAILNTSSGTRILTPRDIADDI |
| Enzyme Length | 139 |
| Uniprot Accession Number | Q8AY47 |
| Absorption | |
| Active Site | ACT_SITE 65; /evidence=ECO:0000255|PROSITE-ProRule:PRU10035 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | 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:0000255|PROSITE-ProRule:PRU10035}; |
| DNA Binding | |
| EC Number | 3.1.1.4 |
| Enzyme Function | FUNCTION: Snake venom phospholipase A2 (PLA2) that shows presynaptic neurotoxicity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (2); Metal binding (4); Non-terminal residue (1); Propeptide (1); Signal peptide (1) |
| Keywords | Calcium;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Neurotoxin;Presynaptic neurotoxin;Secreted;Signal;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL <1..9; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 15,318 |
| Kinetics | |
| Metal Binding | METAL 45; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 47; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 49; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 66; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | RHEA:15801 |
| Cross Reference Brenda |