| IED ID | IndEnz0002000555 |
| Enzyme Type ID | protease000555 |
| Protein Name |
Peptidase T EC 3.4.11.4 Aminotripeptidase Tripeptidase Tripeptide aminopeptidase |
| Gene Name | pepT EFER_1291 |
| Organism | Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia fergusonii Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73) |
| Enzyme Sequence | MDKLLERFLNYVSLDTQSKAGVRQVPSTEGQWKLLHLLKEQLEEMGLINVTLSEKGTLMATLPANVPGDIPAIGFISHVDTSPDCSGKNVNPQIVENYRGGDIALGVGDEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGIAEIMTALAVLQQKNIPHGDIRVAFTPDEEVGKGAKHFDVDAFDARWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVMVNALSLAARIHAEVPADESPEMTEGYEGFYHLASMKGTVERADMHYIIRDFDRKQFEARKRKMMEIAKKVGKGLHPDCYIELVIEDSYYNMREKVAEHPHILDIAQQAMRDCGIEPQLKPIRGGTDGAQLSFMGLPCPNLFTGGYNYHGKHEFVTLEGMEKAVRVIVRIAELTAKQN |
| Enzyme Length | 408 |
| Uniprot Accession Number | B7LQ18 |
| Absorption | |
| Active Site | ACT_SITE 80; /evidence=ECO:0000255|HAMAP-Rule:MF_00550; ACT_SITE 173; /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 | 44,794 |
| Kinetics | |
| Metal Binding | METAL 78; /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 174; /note=Zinc 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00550; METAL 196; /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 |