IED ID | IndEnz0013000012 |
Enzyme Type ID | keratinase000012 |
Protein Name |
Subtilisin EC 3.4.21.62 |
Gene Name | apr |
Organism | Bacillus licheniformis |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus licheniformis |
Enzyme Sequence | MMRKKSFWLGMLTAFMLVFTMAFSDSASAAQPAKNVEKDYIVGFKSGVKTASVKKDIIKESGGKVDKQFRIINAAKAKLDKEALKEVKNDPDVAYVEEDHVAHALAQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHPDLNVVGGASFVAGEAYNTDGNGHGTHVAGTVAALDNTTGVLGVAPSVSLYAVKVLNSSGSGSYSGIVSGIEWATTNGMDVINMSLGGASGSTAMKQAVDNAYARGVVVVAAAGNSGSSGNTNTIGYPAKYDSVIAVGAVDSNSNRASFSSVGAELEVMAPGAGVYSTYPTNTYATLNGTSMASPHVAGAAALILSKHPNLSASQVRNRLSSTATYLGSSFYYGKGLINVEAAAQ |
Enzyme Length | 379 |
Uniprot Accession Number | Q6PNN5 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.; EC=3.4.21.62; Evidence={ECO:0000256|ARBA:ARBA00023529}; |
DNA Binding | |
EC Number | 3.4.21.62 |
Enzyme Function | |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Domain (2); Signal peptide (1) |
Keywords | 3D-structure;Hydrolase;Metal-binding;Protease;Serine protease;Signal |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..29; /evidence=ECO:0000256|SAM:SignalP |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 3QTL; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 38,895 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |