Detail Information for IndEnz0002012097
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