Detail Information for IndEnz0002007554
IED ID IndEnz0002007554
Enzyme Type ID protease007554
Protein Name Proline iminopeptidase
PIP
EC 3.4.11.5
Prolyl aminopeptidase
PAP
Gene Name pip PD_0727
Organism Xylella fastidiosa (strain Temecula1 / ATCC 700964)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Xanthomonadales Xanthomonadaceae Xylella Xylella fastidiosa Xylella fastidiosa (strain Temecula1 / ATCC 700964)
Enzyme Sequence MRTLYPEVTPFDHGMLCVDDSHRLYYEQCGNPHGKPVVILHGGPGGGCNDKMRRFHDPDKYRIVLFDQRGAGRSMPHANLTNNTTWDLVADIEKLRVALGITRWQVFGGSWGSTLALAYAQTHPEQTTELVLRGIFMLRRWELEWFYQEGASRLFPDAWDRYIAAIPPVERHDLISAFHRRLTSDDEATRLAAAQAWSLWEGATSCLYMDQDFIASHENPHFALAFARIENHYFVNGGFFEVEDQLLRDAQRIANIPGVIVHGRYDVVCPLQNAWDLHKAWPKASLKITPGAGHSAFEPQNIDALVCATDSFV
Enzyme Length 313
Uniprot Accession Number Q87DF8
Absorption
Active Site ACT_SITE 110; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 266; /evidence=ECO:0000250; ACT_SITE 294; /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
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 -
Motif
Gene Encoded By
Mass 35,519
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda