IED ID | IndEnz0002013151 |
Enzyme Type ID | protease013151 |
Protein Name |
Snake venom metalloproteinase H1 SVMP EC 3.4.24.- Fragment |
Gene Name | |
Organism | Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus) |
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) Deinagkistrodon Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus) |
Enzyme Sequence | FPYQGSSIILESGNVNDYEVVYPRKVTALPKGAVQQKYEDAMQYEFKVNGEPVVLHLEKNKGLFSKDYSEIHYSPDGRRITTHPLVEDHCYYRGHIRNDADSTASISACNGLKGHFKLRGETYLIEPMKISNSEAHAVYKYENVEKEDEAHKMCGVTQNWESYEPIKKASQLIVSTEFQRYMEIVIVVDHSMYTKYKGDSDKIKAWVYEMINTISESYRYLYIDIIVSALEMWSEKDLINVETSAENTLKSFGEWRAKDLIHRISHDNAQLLTATDFDGPTIGLAYVASMCDPKRSVGVVQDHSSVNHLVAITLAHEIAHNLGVHHDEGSCSCGSGYTCIMSPVINSEVIKYFSDCSYIQCREYISKENPPCILNKPLRTDTVSTPVSGNELLEAGKDYD |
Enzyme Length | 400 |
Uniprot Accession Number | Q9IAY3 |
Absorption | |
Active Site | ACT_SITE 317; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.24.- |
Enzyme Function | FUNCTION: Snake venom metalloproteinase that impairs hemostasis in the envenomed animal. {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Disulfide bond (3); Domain (1); Metal binding (12); Non-terminal residue (1); Propeptide (2); Signal peptide (1) |
Keywords | Calcium;Disulfide bond;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Toxin;Zinc;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL <1..6; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 45,306 |
Kinetics | |
Metal Binding | METAL 183; /note=Calcium 1; /evidence=ECO:0000250; METAL 267; /note=Calcium 1; /evidence=ECO:0000250; METAL 316; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 320; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 326; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 372; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 375; /note=Calcium 1; /evidence=ECO:0000250; METAL 387; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 390; /note=Calcium 2; /evidence=ECO:0000250; METAL 392; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 394; /note=Calcium 2; /evidence=ECO:0000250; METAL 400; /note=Calcium 2; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |