| IED ID | IndEnz0002003014 |
| Enzyme Type ID | protease003014 |
| Protein Name |
Dipeptidyl-peptidase 7 DPP7 EC 3.4.14.- |
| Gene Name | dpp7 BF9343_2924 |
| Organism | Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow) |
| Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Bacteroidia Bacteroidales Bacteroidaceae Bacteroides Bacteroides fragilis Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow) |
| Enzyme Sequence | MNRLKLYLLALTALAVCSAKADEGMWLLQLMQQQHSIDMMKKQGLKLEAQDLYNPNGVSLKDAVGIFGGGCTGEIISPEGLILTNHHCGYASIQQHSSVEHDYLTDGFWATSRDKELPTPGLKFTFIERIEDITDIVNLRIAAKEITESESFSSTFLNKLAKELFEKSDLKGKKGIVPQALPFYAGNKFYMFYKKVYPDVRMVAAPPSSIGKFGGETDNWMWPRHTGDFSMFRIYADANGEPAEYSASNVPLKTKKHLNISIKGLKEGDYAMIMGFPGSTSRYLTVSEVKERMEASNAPRIRIRGTRQDVLKEAMNASDKVRIQYANKYAGSSNYWKNSIGMNKAIIDNNVLGTKAEQEAKFAKFAKEKNNTDYMNVVAKIDEAVAKTSPIKYQQTCLTETFFGGIEFGSPFMVMDKLKEALEQKNDSSIEANIKVLKEVFNDIHNKDYDHEVDRKVAKALLPLYAEMIPAGQRPAIYDVIEKEYKGDYNAYVDAMYDTSILANQANFDKFIKKPTVKAIEKDIATQYSRAKFDKYTNLAEQMGKLPEELALLHKTYIRGLGEMKLPVPSYPDANFTIRLTYGNVKPYSPKDGVYYKYYTTTDGILEKENPEDREFVVPAKLKELIEKKDFGRYALPNGEMPVCFLSTNDITGGNSGSPVLNENGELIGCAFDGNWESLSGDINFDNNLQRCINLDIRYVLFILEKLGGCGHLINEMTIVE |
| Enzyme Length | 721 |
| Uniprot Accession Number | Q5LB17 |
| Absorption | |
| Active Site | ACT_SITE 87; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:V5YM14; ACT_SITE 228; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:V5YM14; ACT_SITE 656; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:V5YM14 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.14.- |
| Enzyme Function | FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Most potently cleaves the synthetic substrate Met-Leu-methylcoumaryl-7-amide (Met-Leu-MCA), followed by Leu-Arg-, and to a much lesser extent Lys-Ala-, Leu-Asp-, Leu-Glu-, Leu-Lys, and Val-Arg-MCA, while this enzyme does not hydrolyze Gly-Arg-, Gly-Gly-, Lys-Lys-, or Gly-Pro-MCA. {ECO:0000269|PubMed:23246913}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Signal peptide (1); Site (1) |
| Keywords | Aminopeptidase;Hydrolase;Protease;Reference proteome;Serine protease;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 81,134 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |