| IED ID | IndEnz0002012476 |
| Enzyme Type ID | protease012476 |
| Protein Name |
Snake venom metalloproteinase Batx-1 SVMP EC 3.4.24.- Batx-I Fragment |
| Gene Name | |
| Organism | Bothrops atrox (Barba amarilla) (Fer-de-lance) |
| 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 Viperidae Crotalinae (pit vipers) Bothrops Bothrops atrox (Barba amarilla) (Fer-de-lance) |
| Enzyme Sequence | YIELAVVADHGIFTKYNSNLNTIR |
| Enzyme Length | 24 |
| Uniprot Accession Number | P0DJE1 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA, and o-phenanthroline, but not inhibited by PMSF, pepstatin A, and aprotinin. {ECO:0000269|PubMed:20600221}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Zinc metalloproteinase that exhits a weak hemorrhagic activity. Degrades preferentially the Aalpha- (FGA) and Bbeta-chains (FGB) of fibrinogen, and partially degrades gamma-chain (FGG) at higher concentration. Induces a mild myotoxicity, but lacks coagulant activity on human plasma or bovin fibrinogen and defibrinating activity. {ECO:0000269|PubMed:20600221}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (1); Metal binding (1); Non-terminal residue (2) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Myotoxin;Protease;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: The N-terminus is blocked.; PTM: Contains 3 disulfide bonds. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 2,752 |
| Kinetics | |
| Metal Binding | METAL 3; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |