| IED ID | IndEnz0002000463 |
| Enzyme Type ID | protease000463 |
| Protein Name |
Peptidase T EC 3.4.11.4 Aminotripeptidase Tripeptidase Tripeptide aminopeptidase |
| Gene Name | pepT BT9727_3488 |
| Organism | Bacillus thuringiensis subsp. konkukian (strain 97-27) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus cereus group Bacillus thuringiensis Bacillus thuringiensis subsp. konkukian Bacillus thuringiensis subsp. konkukian (strain 97-27) |
| Enzyme Sequence | MKQELIERFTRYVKIDTQSNEDSHTVPTTPGQIEFGKLLVEELKEVGLTEVTMDDNGYVMATLPANTDKDVPVIGFLAHLDTATDFTGKNVKPQIHENFDGNAITLNEELNVVLTPEQFPELPSYKGHTIITTDGTTLLGADDKAGLTEIMVAMNYLIHNPQIKHGKVRVAFTPDEEIGRGPAHFDVEAFGASFAYTMDGGPLGGLEYESFNAAGAKLTFNGTNTHPGTAKNKMRNATKLAMEFNGHLPVEEAPEYTEGYEGFYHLLSLNGDVEQSKAYYIIRDFDRKNFEARKNTIENIVKQMQEKYGQDAVVLEMNDQYYNMLEKIEPVREIVDIAYEAMKSLNIEPNIHPIRGGTDGSQLSYMGLPTPNIFTGGENYHGKFEYVSVDVMEKAVQVIIEIARRFEEQA |
| Enzyme Length | 410 |
| Uniprot Accession Number | Q6HF68 |
| Absorption | |
| Active Site | ACT_SITE 81; /evidence=ECO:0000255|HAMAP-Rule:MF_00550; ACT_SITE 176; /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;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 | 45,852 |
| Kinetics | |
| Metal Binding | METAL 79; /note=Zinc 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00550; METAL 142; /note=Zinc 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00550; METAL 142; /note=Zinc 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00550; METAL 177; /note=Zinc 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00550; METAL 199; /note=Zinc 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00550; METAL 381; /note=Zinc 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00550 |
| Rhea ID | |
| Cross Reference Brenda |