| IED ID | IndEnz0002005194 |
| Enzyme Type ID | protease005194 |
| Protein Name |
Microbial collagenase EC 3.4.24.3 |
| Gene Name | |
| Organism | Vibrio alginolyticus |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Vibrionales Vibrionaceae Vibrio Vibrio harveyi group Vibrio alginolyticus |
| Enzyme Sequence | MELKILSVAIATTLTSTGVFALSEPVSQVTEQHAHSAHTHGVEFNRVEYQPTATLPIQPSKATRVQSLESLDESSTACDLEALVTESSNQLISEILSQGATCVNQLFSAESRIQESVFSSDHMYNIAKHTTTLAKGYTGGGSDELETLFLYLRAGYYAEFYNDNISFIEWVTPAVKESVDAFVNTASFYENSDRHGKVLSEVIITMDSAGLQHAYLPQVTQWLTRWNDQYAQHWYMRNAVNGVFTILFGGQWNEQFVQIIGNQTDLAKALGDFALRASSIGAEDEFMAANAGRELGRLTKYTGNASSVVKSQLSRIFEQYEMYGRGDAVWLAAADTASYYADCSEFGICNFETELKGLVLSQTYTCSPTIRILSQNMTQEQHAAACSKMGYEEGYFHQSLETGEQPVKDDHNTQLQVNIFDSSTDYGKYAGPIFDISTDNGGMYLEGDPSQPGNIPNFIAYEASYANADHFVWNLEHEYVHYLDGRFDLYGGFSHPTEKIVWWSEGIAEYVAQENDNQAALETILDGSTYTLSEIFETTYDGFDVDRIYRWGYLAVRFMFENHKDDVNQMLVETRQGNWINYKATITQWANLYQSEFEQWQQTLVSNGAPNAVITANSKGKVGESITFSSENSTDPNGKIVSVLWDFGDGSTSTQTKPTHQYGSEGEYSVSLSVTDSEGLTATATHTVVISALGGNDTLPQDCAVQSKVSGGRLTAGEPVCLANQQTIWLSVPAVNESSNLAITTGNGTGNLKLEYSNSGWPDDTNLHGWSDNIGNGECITLSNQSNYWGYVKVSGDFENAAIVVDFDAQKCRQ |
| Enzyme Length | 814 |
| Uniprot Accession Number | P43154 |
| Absorption | |
| Active Site | ACT_SITE 478; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Digestion of native collagen in the triple helical region at Xaa-|-Gly bonds. With synthetic peptides, a preference is shown for Gly at P3 and P1', Pro and Ala at P2 and P2', and hydroxyproline, Ala or Arg at P3'.; EC=3.4.24.3; |
| DNA Binding | |
| EC Number | 3.4.24.3 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (1); Metal binding (2); Propeptide (1); Signal peptide (1) |
| Keywords | Collagen degradation;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytic cleavage might yield three different active forms. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 89,963 |
| Kinetics | |
| Metal Binding | METAL 477; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 481; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.3; |