IED ID | IndEnz0002000754 |
Enzyme Type ID | protease000754 |
Protein Name |
Peptidase T EC 3.4.11.4 Aminotripeptidase Tripeptidase Tripeptide aminopeptidase |
Gene Name | pepT SGO_1312 |
Organism | Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Streptococcus Streptococcus gordonii Streptococcus gordonii str. Challis Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288) |
Enzyme Sequence | MKYPNLLERFLTYVKVNTRSDETSTTTPSTQSQMDFANNILIPEMKRVGLENVYYLPNGFAIGTLPANDPSFTLKIGFISHMDTADFNAENVQPQVIENYDGGVIPLGQSGFNLDPADFASLHKYKGQTLITTDGTTLLGADDKSGIAEIMTAIEYLSAHPEIKHGEIRVGFGPDEEIGIGADKFDAENFDVDFAYTVDGGPLGELQYETFSAAGAELTFQGRNVHPGTAKDQMINALQLAIDFHNQLPEADRPEKTEGYQGFYHLMNLTGTVEEAQASYIIRDFETDAFENRKAAMQAIADKMNQELGRERVILTLKDQYYNMKQVIEKDMTPIHIAKAVMESLDIQPIIEPIRGGTDGSKISFMGIPTPNLFAGGENMHGRFEYVSLETMERAVDTIIGIVSYQEK |
Enzyme Length | 408 |
Uniprot Accession Number | A8AXT3 |
Absorption | |
Active Site | ACT_SITE 83; /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;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 | 45,229 |
Kinetics | |
Metal Binding | METAL 81; /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 |