| IED ID | IndEnz0002011668 |
| Enzyme Type ID | protease011668 |
| Protein Name |
Probable proline iminopeptidase PIP EC 3.4.11.5 Prolyl aminopeptidase PAP |
| Gene Name | SCO1989 SC7H2.03c |
| Organism | Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces Streptomyces albidoflavus group Streptomyces coelicolor Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) |
| Enzyme Sequence | MSLYPEIEPYDHGMLDVGDGNHVYWETCGNPHGKPAVVLHGGPGSRASPGLRRYFDPAAYRIVLLDQRGAGRSLPRASAPDTDMSVNTTAHLMADLERLRVHLGIERWLVWGVSWGSVLGLRYAQTHPGVVTELVLTGVATGSNAEVALLTRGLGNIFPEAHERFLAELPPDARDGNLPAAYNRLLESPDPAVRERAARAWTDWETATIPAPPGSVARYQDPDFRMGFARTVTHYWGNDHFLGDGNDEGVVIRDAHLLKGIPGTLVQGSLDFGNLLGIVWRLHHAWPDSDLVIVDEAGHDAGTTGDEALLAATDKYARGGTAE |
| Enzyme Length | 323 |
| Uniprot Accession Number | Q9S2L4 |
| Absorption | |
| Active Site | ACT_SITE 114; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 271; /evidence=ECO:0000250; ACT_SITE 299; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5; |
| DNA Binding | |
| EC Number | 3.4.11.5 |
| Enzyme Function | FUNCTION: Specifically catalyzes the removal of N-terminal proline residues from peptides. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1) |
| Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 35,040 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |