| IED ID | IndEnz0002011063 |
| Enzyme Type ID | protease011063 |
| Protein Name |
Proline iminopeptidase PIP EC 3.4.11.5 Prolyl aminopeptidase PAP |
| Gene Name | pip BBR47_46810 |
| Organism | Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Paenibacillaceae Brevibacillus Brevibacillus brevis (Bacillus brevis) Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599) |
| Enzyme Sequence | MRMQEGYIEVPGGRVWYSRVGEGEKTPLIVLHGGPGNTHDPLKSTLHVLGDDRPVIFYDQLGSGNSDRPTDLTLWKTERFVEELACIRQALDLKEVHILGHSWGTMLAAAYLVDAKPEGVQSIIFSSPCLSAERWKQDADRLIEQLPVDTQQTIATHEEQGTTDSQEYQDAMKEYYKRHVCRLDPMPTVMTESRPKANKEVYMTMWGPSEFCPTGNLKTFDYTPQLHQINIPSLFVCGRYDEATPESTGYYQSLVPKAELHVFENSSHVGYLEETDEYVQVIRRFLQKAESK |
| Enzyme Length | 292 |
| Uniprot Accession Number | C0ZKI1 |
| Absorption | |
| Active Site | ACT_SITE 102; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P96084; ACT_SITE 241; /evidence=ECO:0000250|UniProtKB:O32449; ACT_SITE 268; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P96084 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5; Evidence={ECO:0000250|UniProtKB:P46541}; |
| DNA Binding | |
| EC Number | 3.4.11.5 |
| Enzyme Function | FUNCTION: Releases the N-terminal proline from various substrates. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1) |
| Keywords | Aminopeptidase;Hydrolase;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 33,277 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |