Detail Information for IndEnz0002010510
IED ID IndEnz0002010510
Enzyme Type ID protease010510
Protein Name Prolyl endopeptidase
PE
EC 3.4.21.26
Post-proline cleaving enzyme
Gene Name
Organism Aeromonas hydrophila
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Aeromonadales Aeromonadaceae Aeromonas Aeromonas hydrophila
Enzyme Sequence MSGKARLHYPVTRQSEQLDHYFGQAVADPYRWLEDDRSPETEAWVKAQNRVTQDYLAQIPFRDAIKGKLATSWNYAKEGAPFREGRYHYFFKNDGLQNQNVLCGQLAGKPAEVFLDPNLLSPDGTTALDQLSFSRDGKTLAYSLSLAGSDWREIHLMDVESKQPLETPLRDVKFSGISWLGNEGFFYSSYDKPDGSELSARTDQHKLYFHRLGTAQEEDRLVFGAIPAQRHRYVGATVTEDDRYLLISAADSTSGNRLYVKDLTREGAPLLTVQGDLAADVSLVDNKGSRLYLLTNRDAPNRRLVTVEADNPGPEQWRDLIPERQQVLTVHSGGGYLFAEYMVDATARVEQFDHDGKRVREVGLPGLGSVSGFNGKQDDPALYFGFENYAQPPTLYKFEPNSGAISLYRASAAPFKPEDYVSEQRFYRSKDGTRVPLIISYRKGLKLDGSNPTILYGYGGFDVSLTPSFSVSVANWLDLGGVYAVANLRGGGEYGQAWHLAGTRMNKQNVFDDFIAAAEYLKAEGYTRTDRLAIRGGSNGGLLVGAVMTQRPDLMRVACQAVGVLDMLRYHTFTAGAGWAYDYGTSADSEAMFDYLKGYSPLHSVRAGVSYPSTLVTTADHDDRVVPAHSFKFAATLQADDAGPHPQLIRIETNAGHGAGTPVAKLIEQSADIYAFTLFEMGYRQLPRQP
Enzyme Length 690
Uniprot Accession Number Q06903
Absorption
Active Site ACT_SITE 538; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10084; ACT_SITE 657; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10084
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.; EC=3.4.21.26;
DNA Binding
EC Number 3.4.21.26
Enzyme Function FUNCTION: Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. Has an absolute requirement for an X-Pro bond in the trans configuration immediately preceding the Pro-Y scissible bond.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Initiator methionine (1)
Keywords Direct protein sequencing;Hydrolase;Protease;Serine protease
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 76,515
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda