IED ID | IndEnz0002001233 |
Enzyme Type ID | protease001233 |
Protein Name |
Putative proline iminopeptidase PIP EC 3.4.11.5 Prolyl aminopeptidase PAP |
Gene Name | pip MPN_022 MP132 |
Organism | Mycoplasma pneumoniae (strain ATCC 29342 / M129) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Tenericutes Mollicutes Mycoplasmatales Mycoplasmataceae Mycoplasma Mycoplasma pneumoniae Mycoplasma pneumoniae (strain ATCC 29342 / M129) |
Enzyme Sequence | MNTSPKQSGYLKVGNGHEVYFWTAGNPQGKSALYVHGGPGSGTDAGCLKYFDLDTTYVILLDQRGCGQSKAVNPLLHNTTQDLVGDLEALRQHLKLERWTLFGGSWGSTLALVYAITHPQVVEQVFLRALFLGREQDWAEMLLGLGKLFYPYEHQTLLKAIPQACRTDFTKFTNYFYEVLQGNDSALKTQLANAWVKWENTLLSPISYVKDEKAEDANFTFKLALLECHYAKHHSFLKPNFILENVAVLKDKPVHLIHGRFDLVCPLSQALELKRALPTLNLYVTNNAGHSGSDPNNLTTIKHLLKTQL |
Enzyme Length | 309 |
Uniprot Accession Number | P75092 |
Absorption | |
Active Site | ACT_SITE 105; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 262; /evidence=ECO:0000250; ACT_SITE 290; /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 | 19965468; |
Motif | |
Gene Encoded By | |
Mass | 34,690 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |