| IED ID | IndEnz0002012720 |
| Enzyme Type ID | protease012720 |
| Protein Name |
Xaa-Pro dipeptidyl-peptidase EC 3.4.14.11 X-Pro dipeptidyl-peptidase X-prolyl-dipeptidyl aminopeptidase X-PDAP |
| Gene Name | pepX LVIS_1782 |
| Organism | Levilactobacillus brevis (strain ATCC 367 / BCRC 12310 / CIP 105137 / JCM 1170 / LMG 11437 / NCIMB 947 / NCTC 947) (Lactobacillus brevis) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Lactobacillaceae Levilactobacillus Levilactobacillus brevis (Lactobacillus brevis) Levilactobacillus brevis (strain ATCC 367 / BCRC 12310 / CIP 105137 / JCM 1170 / LMG 11437 / NCIMB 947 / NCTC 947) (Lactobacillus brevis) |
| Enzyme Sequence | MRNQQFAIRPTTLDQARVELQQIHFLDDTNLSFTTPSDLLRDFYDRSWPEYTTSSVVAQQLSNLMATPETDGLTYLTTHEQVPVDVFYNLALQRLGFAVDLDFQLTDPLAAMTKIQLPVADHEGTTFTLNELMNAWYVLLTTHNKTGQTFLDQLTTHGYFAPLIHDNSVPKPLIFNGKAQAVFDTTQLIHEVVYVESPQDTDHDGHRDLLKAEIIRPAETANGLKVPVLYTASPYNQGTNDEAGEALTHNVNVPLTAKQPAATTLADVTAESVTTPLPDARPVTATTHTAAETFAREQSYTLNDYFLARGFAVVYAAGIGTKDSDGLRTTGDPEETTSTIAIIEWLAGNRTAFTTRNATQAIPAWWSNHQVAMTGRSYLGTLATAAATTGVAGLKTVISEAAISNWYDYYRDGGLVVAPGGFPGEDADVLAEETFSRQLLAGDYHRIQEKWQHQLAAITQNQDRVTGNYNRFWDARNYLKNAKNIKADLLLVHGLNDWNVKPRNVNNLWRAVRDLPVTKKLILHQGQHIYINAFRSIDYTDIVNLWLTHELLGVDNHAETLLPNVIIQDNVTPETWQAYPDWDAPSNPVQHFNLQADELVAPSDHIPAAATSFNDQLPVDQFNHYTHHIDEWQADLLGDKHNAMFKHRLLFKSAVLTDDLVLDGRPTIDLQVAVNQPLGLLSFQLVDYGDAKRLGVSPTPLRIRLDEGYRWREDNLREFTVAATTPWKMITKGHRNLQNRTNAYQVDELKPNTFYDLSVTLQPTHYRLLAGHQLGLVIYATDFGMTVRGNQDLQYSIQLGQSALHVPFITD |
| Enzyme Length | 811 |
| Uniprot Accession Number | Q03PM5 |
| Absorption | |
| Active Site | ACT_SITE 377; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_00698; ACT_SITE 497; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_00698; ACT_SITE 528; /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;Reference proteome;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 | 90,917 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |