Detail Information for IndEnz0002009308
IED ID IndEnz0002009308
Enzyme Type ID protease009308
Protein Name Proline iminopeptidase
PIP
EC 3.4.11.5
Prolyl aminopeptidase
PAP
Gene Name pip pepI LCRIS_00081
Organism Lactobacillus crispatus (strain ST1)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Lactobacillaceae Lactobacillus Lactobacillus crispatus Lactobacillus crispatus (strain ST1)
Enzyme Sequence MEVIEGKMPFMGYETYYRIVGRRSEKTPLVLLHGGPGSSHNYFEVLDKLAEIDNRRIIMYDQLGCGKSSIPDDHPELYTKETWVKELMALREHLALRKIHLLGQSWGGMLALIYMCDYHPVGIQSLILSSTLSSASLWSKELHRMIKYLPIEEQAAIHRAELTSNFNDPDYLKANEHFMNQHAIDMTKTWPECVMRKKCGGIVAYETAWGPNEYTPEGNLHDYEYTEKLGKIKIPTLITSGTDDLCTPYVAKTMQDHLAGSKWQLFENCGHMSFVEKTDEYVEMLRKWLDQHD
Enzyme Length 293
Uniprot Accession Number D5H0J3
Absorption
Active Site ACT_SITE 105; /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:P52278};
DNA Binding
EC Number 3.4.11.5
Enzyme Function FUNCTION: Releases the N-terminal proline from various substrates. {ECO:0000250|UniProtKB:P52278}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Domain (1)
Keywords Aminopeptidase;Hydrolase;Protease
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell envelope {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 33,827
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda