Detail Information for IndEnz0002008561
IED ID IndEnz0002008561
Enzyme Type ID protease008561
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