Detail Information for IndEnz0002009332
IED ID IndEnz0002009332
Enzyme Type ID protease009332
Protein Name Proline iminopeptidase
PIP
EC 3.4.11.5
Prolyl aminopeptidase
PAP
Gene Name pip xap
Organism Xanthomonas citri (Xanthomonas campestris pv. citri)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Xanthomonadales Xanthomonadaceae Xanthomonas Xanthomonas citri group Xanthomonas citri (Xanthomonas campestris pv. citri)
Enzyme Sequence MRTLYPEITPYQQGSLKVDDRHTLYFEQCGNPHGKPVVMLHGGPGGGCNDKMRRFHDPAKYRIVLFDQRGSGRSTPHADLVDNTTWDLVADIERLRTHLGVDRWQVFGGSWGSTLALAYAADPSAAGHQLVLRGIFLLRRFELEWFYQEGASRLFPDAWEHYLNAIPPVERADLMSAFHRRLTSDDEATRLAAAKAWSVWEGATSFLHVDEDFVTGHEDAHFALAFARIENHYFVNGGFFEVEDQLLRDAHRIADIPGVIVHGRYDVVCPLQSAWDLHKAWPKAQLQISPASGHSAFEPENVDALVRATDGFA
Enzyme Length 313
Uniprot Accession Number P52279
Absorption
Active Site ACT_SITE 110; /note=Nucleophile; /evidence=ECO:0000269|PubMed:9427736; ACT_SITE 266; /evidence=ECO:0000269|PubMed:9427736; ACT_SITE 294; /note=Proton donor; /evidence=ECO:0000269|PubMed:9427736
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: May be involved in proline metabolism and sensitivity to ascamycin. Has ascamycin dealanylating activity.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Beta strand (12); Chain (1); Domain (1); Helix (17); Sequence conflict (4); Turn (2)
Keywords 3D-structure;Aminopeptidase;Cytoplasm;Direct protein sequencing;Hydrolase;Protease
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 1AZW;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 35,260
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda