IED ID | IndEnz0002009457 |
Enzyme Type ID | protease009457 |
Protein Name |
Proline iminopeptidase PIP EC 3.4.11.5 Prolyl aminopeptidase PAP |
Gene Name | pip |
Organism | Serratia marcescens |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Yersiniaceae Serratia Serratia marcescens |
Enzyme Sequence | MEQLRGLYPPLAAYDSGWLDTGDGHRIYWELSGNPNGKPAVFIHGGPGGGISPHHRQLFDPERYKVLLFDQRGCGRSRPHASLDNNTTWHLVADIERLREMAGVEQWLVFGGSWGSTLALAYAQTHPERVSEMVLRGIFTLRKQRLHWYYQDGASRFFPEKWERVLSILSDDERKDVIAAYRQRLTSADPQVQLEAAKLWSVWEGETVTLLPSRESASFGEDDFALAFARIENHYFTHLGFLESDDQLLRNVPLIRHIPAVIVHGRYDMACQVQNAWDLAKAWPEAELHIVEGAGHSYDEPGILHQLMIATDRFAGK |
Enzyme Length | 317 |
Uniprot Accession Number | O32449 |
Absorption | |
Active Site | ACT_SITE 113; /note=Nucleophile; ACT_SITE 268; ACT_SITE 296; /note=Proton donor |
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. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Beta strand (12); Chain (1); Domain (1); Helix (17); Turn (2) |
Keywords | 3D-structure;Aminopeptidase;Cytoplasm;Hydrolase;Protease |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (4) |
Cross Reference PDB | 1QTR; 1WM1; 1X2B; 1X2E; |
Mapped Pubmed ID | 12893291; 16452443; |
Motif | |
Gene Encoded By | |
Mass | 36,084 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.11.5; |