IED ID | IndEnz0010000791 |
Enzyme Type ID | esterase000791 |
Protein Name |
Putative Xaa-Pro dipeptidyl-peptidase X-Pro dipeptidyl-peptidase EC 3.4.14.11 X-prolyl-dipeptidyl aminopeptidase X-PDAP |
Gene Name | RB9674 |
Organism | Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1) |
Taxonomic Lineage | cellular organisms Bacteria PVC group Planctomycetes Planctomycetia Pirellulales Pirellulaceae Rhodopirellula Rhodopirellula baltica Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1) |
Enzyme Sequence | MTKLVRSRLDLTWVFTTMKRLRLPVLAVLFLAISPVQGGEIQIPVIKDGEAQVIKELEDSDYWIRHDLWVETEFDLDGDGKLDRMHVSVTRPTQTDTQSLKLPVIYNSSPYFAGTTGGDESYFWDARQELGDEPPKRSAAPAIEREGTRPIISKRHVKDWLPRGFVVVHSSAPGTGLSQGCPTVGDDPEALAPKAVIDWLCGRAKGFTEPFGGEPVEAYWSSGKVGMTGTSYNGTIPLAAATTGVEGLEVIIPVAPNTSYYHYYRSNGLVRHPGGYLGEDIDILYDFIHSGGDEETRAYCDCHIRDEQMMANQDRATGDYNDFWYSRDYLNRVDGVKAAVLMAHAFNDWNVVPEHSIRIYEALKKNGVETQLFMHQGGHGGPPPISMMNRWFTHYLYGEDNGVEKGSKSWIVREKDERTKPTEYPQYPHPEAKDVVVYPVPGAPQRGRLQTAPLTEPITETLVDNFSFAGETLAQAEYTEHRLIYTTPELSEAVHLSGTPRIKLRLACDRPAANLSVWLVSLPWNTQKNSKITDNIITRGWADPQNIESMRESKPLVPGQFYDIEFDLQPDDQVIAKGQQIGLMVFSSDRDYTLHPTPGTKLTIDLQHTQLSLPVVGGTIPLESQD |
Enzyme Length | 626 |
Uniprot Accession Number | P59825 |
Absorption | |
Active Site | ACT_SITE 231; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 348; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 379; /note=Charge relay system; /evidence=ECO:0000250 |
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; |
DNA Binding | |
EC Number | 3.4.14.11 |
Enzyme Function | |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1) |
Keywords | Aminopeptidase;Hydrolase;Protease;Reference proteome;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 | 70,020 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |