IED ID | IndEnz0002000541 |
Enzyme Type ID | protease000541 |
Protein Name |
Peptidase T EC 3.4.11.4 Aminotripeptidase Tripeptidase Tripeptide aminopeptidase |
Gene Name | pepT b1127 JW1113 |
Organism | Escherichia coli (strain K12) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
Enzyme Sequence | MDKLLERFLNYVSLDTQSKAGVRQVPSTEGQWKLLHLLKEQLEEMGLINVTLSEKGTLMATLPANVPGDIPAIGFISHVDTSPDCSGKNVNPQIVENYRGGDIALGIGDEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGIAEIMTALAVLQQKKIPHGDIRVAFTPDEEVGKGAKHFDVDAFDARWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVMVNALSLAARIHAEVPADESPEMTEGYEGFYHLASMKGTVERADMHYIIRDFDRKQFEARKRKMMEIAKKVGKGLHPDCYIELVIEDSYYNMREKVVEHPHILDIAQQAMRDCDIEPELKPIRGGTDGAQLSFMGLPCPNLFTGGYNYHGKHEFVTLEGMEKAVQVIVRIAELTAQRK |
Enzyme Length | 408 |
Uniprot Accession Number | P29745 |
Absorption | |
Active Site | ACT_SITE 80; /evidence=ECO:0000250; ACT_SITE 173; /note=Proton acceptor; /evidence=ECO:0000250 |
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; |
DNA Binding | |
EC Number | 3.4.11.4 |
Enzyme Function | FUNCTION: Cleaves the N-terminal amino acid of tripeptides. {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (18); Chain (1); Helix (13); Metal binding (6); Turn (7) |
Keywords | 3D-structure;Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
Interact With | P0A7C6; P0A858 |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 1VIX; |
Mapped Pubmed ID | 15690043; 16606699; 16858726; 24561554; |
Motif | |
Gene Encoded By | |
Mass | 44,923 |
Kinetics | |
Metal Binding | METAL 78; /note=Zinc 1; /evidence=ECO:0000269|PubMed:16021622; METAL 140; /note=Zinc 1; /evidence=ECO:0000269|PubMed:16021622; METAL 140; /note=Zinc 2; /evidence=ECO:0000269|PubMed:16021622; METAL 174; /note=Zinc 2; /evidence=ECO:0000269|PubMed:16021622; METAL 196; /note=Zinc 1; /evidence=ECO:0000269|PubMed:16021622; METAL 379; /note=Zinc 2; /evidence=ECO:0000269|PubMed:16021622 |
Rhea ID | |
Cross Reference Brenda |