IED ID | IndEnz0002012097 |
Enzyme Type ID | protease012097 |
Protein Name |
Proline iminopeptidase PIP EC 3.4.11.5 Prolyl aminopeptidase PAP |
Gene Name | pip pepIP CBO2031 CLC_1977 |
Organism | Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Clostridiaceae Clostridium Clostridium botulinum Clostridium botulinum A Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) |
Enzyme Sequence | MKITEGYMPYLEYKTYYRIVGECTGNKKPLVLLHGGPGSTHNYFEVLDKVAEDGRAVIMYDQLGCGLSATPSRPDLWNAKTWIEELIQLRKHLGLDEIHLLGQSWGGMQAIQYACEYKPEGIKSYILSSTLPAASLWEKEQRRRVAYLPQEMQDAIAKAEKAGDYSSKEYQEAEAEFMLRHCAGAVGPDSPECLRRPKVAGTEAYVTAWGQNEFSPSGTLKNFDFMKEIEDIKEPCLITSGLLDLCSPLVAKTMYDKIPNSEWELFEFSRHMPFVEENEKYIEVLNKWLNKND |
Enzyme Length | 293 |
Uniprot Accession Number | A5I3F5 |
Absorption | |
Active Site | ACT_SITE 104; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P96084; ACT_SITE 244; /evidence=ECO:0000250|UniProtKB:O32449; ACT_SITE 271; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P96084 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5; Evidence={ECO:0000250|UniProtKB:P46542}; |
DNA Binding | |
EC Number | 3.4.11.5 |
Enzyme Function | FUNCTION: Releases the N-terminal proline from various substrates. {ECO:0000250|UniProtKB:P46542}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Domain (1) |
Keywords | Aminopeptidase;Hydrolase;Protease;Reference proteome |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 33,401 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |