Detail Information for IndEnz0002010675
IED ID IndEnz0002010675
Enzyme Type ID protease010675
Protein Name Proline iminopeptidase
PIP
EC 3.4.11.5
Prolyl aminopeptidase
PAP
Gene Name pip pepI CD630_30410
Organism Clostridioides difficile (strain 630) (Peptoclostridium difficile)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Peptostreptococcaceae Clostridioides Clostridioides difficile (Peptoclostridium difficile) Clostridioides difficile (strain 630) (Peptoclostridium difficile)
Enzyme Sequence MKITEGYMPFKGFKTYYRIVGENTEGKKPLVLLHGGPGSTHNYFEVLDKIAESGRQVIMYDQIGCGNSFVEGHPELFNADTWIEELIELRKHLGLDEIHLLGQSWGGMQAIWYAIEYKPKGIKSYILSSTLSSAKLWEKEQKRRISYMSEVDQKALLDAVNTGDYSSKEYNDALERFMEMYCAGEVTEDSPECLRRPKKSGSEAYIVGWGQNEFSPTGTLSGYEFTDRLHEIKEPCLVTSGAIDLCSPYIAKTMYDRIPNSKWELFEYSRHMPFVEENEKYIKVLTEWLNAND
Enzyme Length 293
Uniprot Accession Number Q184M8
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 33,663
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda