Detail Information for IndEnz0002001233
IED ID IndEnz0002001233
Enzyme Type ID protease001233
Protein Name Putative proline iminopeptidase
PIP
EC 3.4.11.5
Prolyl aminopeptidase
PAP
Gene Name pip MPN_022 MP132
Organism Mycoplasma pneumoniae (strain ATCC 29342 / M129)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Tenericutes Mollicutes Mycoplasmatales Mycoplasmataceae Mycoplasma Mycoplasma pneumoniae Mycoplasma pneumoniae (strain ATCC 29342 / M129)
Enzyme Sequence MNTSPKQSGYLKVGNGHEVYFWTAGNPQGKSALYVHGGPGSGTDAGCLKYFDLDTTYVILLDQRGCGQSKAVNPLLHNTTQDLVGDLEALRQHLKLERWTLFGGSWGSTLALVYAITHPQVVEQVFLRALFLGREQDWAEMLLGLGKLFYPYEHQTLLKAIPQACRTDFTKFTNYFYEVLQGNDSALKTQLANAWVKWENTLLSPISYVKDEKAEDANFTFKLALLECHYAKHHSFLKPNFILENVAVLKDKPVHLIHGRFDLVCPLSQALELKRALPTLNLYVTNNAGHSGSDPNNLTTIKHLLKTQL
Enzyme Length 309
Uniprot Accession Number P75092
Absorption
Active Site ACT_SITE 105; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 262; /evidence=ECO:0000250; ACT_SITE 290; /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: Specifically catalyzes the removal of N-terminal proline residues from peptides. {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Domain (1)
Keywords Aminopeptidase;Cytoplasm;Hydrolase;Protease;Reference proteome
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 19965468;
Motif
Gene Encoded By
Mass 34,690
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda