Detail Information for IndEnz0002006726
IED ID IndEnz0002006726
Enzyme Type ID protease006726
Protein Name Xaa-Pro dipeptidyl-peptidase
EC 3.4.14.11
X-Pro dipeptidyl-peptidase
X-prolyl-dipeptidyl aminopeptidase
X-PDAP
Gene Name pepX Spy49_1451
Organism Streptococcus pyogenes serotype M49 (strain NZ131)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Streptococcus Streptococcus pyogenes Streptococcus pyogenes serotype M49 Streptococcus pyogenes serotype M49 (strain NZ131)
Enzyme Sequence MRYNQFSYIPTSLERAAEELKELGFDLDLQKTAKANLESFLRKLFFHYPDSVYPLSHLIAKNDMDALSFFQSEQELSKEVFDLLALQVLGFIPGVDFTEADAFLDKLAFPIHFDETEIIKHIHHLLATRCKSGMTLIDDLVSQGMLTMDNDYHFFNGKSLATFDTSQLIREVVYVEAPLDTDQDGQLDLIKVNIIRPQSQKPLPTLMTPSPYHQGINEVANDKKLYRMEKELVVKKRRQITVEDRDFIPLETQPCKLPIGQNLESFSYINSYSLNDYFLARGFANIYVSGVGTAGSTGFMTSGDYAQIESFKAVIDWLNGRATAYTSHSKTHQVRADWANGLVCTTGKSYLGTMSTGLATTGVDGLAMIIAESAISSWYNYYRENGLVCSPGGYPGEDLDVLTELTYSRNLLAGDYLRHNDRYQELLNQQSQALDRQSGDYNQFWHDRNYLKNAHQIKCDVVYTHGLQDWNVKPRQVYEIVNALPSTINKHLFLHQGEHVYMHNWQSIDFRESMNALLCQKLLGLANDFSLPEMIWQDNTCPQNWQERKVFGTSTIKELDLGQELLLIDNHYGEDEFKAYGKDFRAFKAALFKGKANQALVDILLEEDLLINGEIVLQLKVKSSENKGLLSAQILDYGKKKRLGDLPIALTQSSIDNGQNFSREPLKELPFRENSYRVISKGFMNLQNRNNLSSIETIPNNKWMTVRLPLQPTIYHLEKGDTLRVILYTTDFEHTVRDNSNYALTIDLSQSQLIVPIASN
Enzyme Length 760
Uniprot Accession Number B5XI61
Absorption
Active Site ACT_SITE 349; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_00698; ACT_SITE 469; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_00698; ACT_SITE 499; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_00698
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolyzes Xaa-Pro-|- bonds to release unblocked, N-terminal dipeptides from substrates including Ala-Pro-|-p-nitroanilide and (sequentially) Tyr-Pro-|-Phe-Pro-|-Gly-Pro-|-Ile.; EC=3.4.14.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00698};
DNA Binding
EC Number 3.4.14.11
Enzyme Function FUNCTION: Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. {ECO:0000255|HAMAP-Rule:MF_00698}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1)
Keywords Aminopeptidase;Cytoplasm;Hydrolase;Protease;Serine protease
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00698}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 86,703
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda