Detail Information for IndEnz0002000541
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