Detail Information for IndEnz0002009457
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;