IED ID | IndEnz0002009050 |
Enzyme Type ID | protease009050 |
Protein Name |
Proline iminopeptidase PIP EC 3.4.11.5 Prolyl aminopeptidase PAP |
Gene Name | pip pap |
Organism | Aeromonas sobria |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Aeromonadales Aeromonadaceae Aeromonas Aeromonas sobria |
Enzyme Sequence | MSSPLHYVLDGIHCEPHFFTVPLDHQQPDDEETITLFGRTLCRKDRLDDELPWLLYLQGGPGFGAPRPSANGGWIKRALQEFRVLLLDQRGTGHSTPIHAELLAHLNPRQQADYLSHFRADSIVRDAELIREQLSPDHPWSLLGQSFGGFCSLTYLSLFPDSLHEVYLTGGVAPIGRSADEVYRATYQRVADKNRAFFARFPHAQAIANRLATHLQRHDVRLPNGQRLTVEQLQQQGLDLGASGAFEELYYLLEDAFIGEKLNPAFLYQVQAMQPFNTNPVFAILHELIYCEGAASHWAAERVRGEFPALAWAQGKDFAFTGEMIFPWMFEQFRELIPLKEAAHLLAEKADWGPLYDPVQLARNKVPVACAVYAEDMYVEFDYSRETLKGLSNSRAWITNEYEHNGLRVDGEQILDRLIRLNRDC |
Enzyme Length | 425 |
Uniprot Accession Number | P46547 |
Absorption | |
Active Site | ACT_SITE 146; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 351; /evidence=ECO:0000250; ACT_SITE 404; /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: Higher activity toward long peptides. Acts on hydroxyproline beta-naphthylamide with almost as high an activity as on proline beta-naphthylamide. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Domain (1); Initiator methionine (1) |
Keywords | Aminopeptidase;Cytoplasm;Direct protein sequencing;Hydrolase;Protease |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 48,406 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |