| IED ID | IndEnz0002007468 |
| Enzyme Type ID | protease007468 |
| Protein Name |
Proline iminopeptidase PIP EC 3.4.11.5 Prolyl aminopeptidase PAP |
| Gene Name | pip |
| Organism | Neisseria gonorrhoeae |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Betaproteobacteria Neisseriales Neisseriaceae Neisseria Neisseria gonorrhoeae |
| Enzyme Sequence | MYEIKQPFHSGYLQVSEIHQIYWEESGNPDGVPVIFLHGGPGAGASPECRGFFNPDVFRIVIIDQRGCGRSHPYACAEDNTTWDLVADIEKVREMLGIGKWLVFGGSWGSTLSLAYAQTHPERVKGLVLRGIFLCRPSETAWLNEAGGVSRIYPEQWQKFVAPIAENRRNRLIEAYHGLLFHQDEEVCLSAAKAWADWESYLIRFEPEGVDEDAYASLAIARLENHYFVNGGWLQGDKAILNNIGKIRHIPTVIVQGRYDLCTPMQSAWELSKAFPEAELRVVQAGHCAFDPPLADALVQAVEDILPRLL |
| Enzyme Length | 310 |
| Uniprot Accession Number | P42786 |
| Absorption | |
| Active Site | ACT_SITE 107; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 260; /evidence=ECO:0000250; ACT_SITE 287; /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: Hydrolyzes peptides having the structure Pro-Y-Z to yield free proline. Also hydrolyzes the dipeptide Pro-Gly. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1) |
| Keywords | Aminopeptidase;Cytoplasm;Direct protein sequencing;Hydrolase;Protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 34,792 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |