| IED ID | IndEnz0002000473 |
| Enzyme Type ID | protease000473 |
| Protein Name |
Peptidase T EC 3.4.11.4 Aminotripeptidase Tripeptidase Tripeptide aminopeptidase |
| Gene Name | pepT BT_4583 |
| Organism | Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) |
| Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Bacteroidia Bacteroidales Bacteroidaceae Bacteroides Bacteroides thetaiotaomicron Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) |
| Enzyme Sequence | MTLVDRFLKYVSFDTQSDESTGLTPSTPKQMVFAEYLKTELESLGLEDITLDEHGYLFATLPANIDKKVPTIGFIAHMDTSPDMTGKDVTPRIVKGYDGTDIVLCAEENIILSPAQFPELLDHKGEDLIVTNGKTLLGADDKAGIAEIVSAIVYLKEHPEIKHGKIRIGFNPDEEIGEGAHKFDVGKFGCEWAYTMDGGEVGELEFENFNAAAAKITFKGRNVHPGYAKNKMINSIRVANQFIAMLPSTETPEQTEGYEGFYHLISIQGDVEQSTVSYIIRDHDRAKFEKRKEEIKRLVAQVNTEYGEGTATLELRDQYYNMREKIEPVMHIIDTAFAAMEAVGVKPNVKPIRGGTDGAQLSFKGLPCPNIFAGGLNFHGRYEFVPIQNMEKAMNVIVKIAELVASK |
| Enzyme Length | 407 |
| Uniprot Accession Number | Q89YZ7 |
| Absorption | |
| Active Site | ACT_SITE 79; /evidence=ECO:0000255|HAMAP-Rule:MF_00550; ACT_SITE 174; /note=Proton acceptor; /evidence=ECO:0000255|HAMAP-Rule:MF_00550 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of the N-terminal residue from a tripeptide.; EC=3.4.11.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00550}; |
| DNA Binding | |
| EC Number | 3.4.11.4 |
| Enzyme Function | FUNCTION: Cleaves the N-terminal amino acid of tripeptides. {ECO:0000255|HAMAP-Rule:MF_00550}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (6) |
| Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00550}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 45,178 |
| Kinetics | |
| Metal Binding | METAL 77; /note=Zinc 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00550; METAL 140; /note=Zinc 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00550; METAL 140; /note=Zinc 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00550; METAL 175; /note=Zinc 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00550; METAL 197; /note=Zinc 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00550; METAL 379; /note=Zinc 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00550 |
| Rhea ID | |
| Cross Reference Brenda |