| IED ID | IndEnz0002012049 |
| Enzyme Type ID | protease012049 |
| Protein Name |
Aminopeptidase YpdE EC 3.4.11.- |
| Gene Name | ypdE b2384 JW2381 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MDLSLLKALSEADAIASSEQEVRQILLEEADRLQKEVRFDGLGSVLIRLNESTGPKVMICAHMDEVGFMVRSISREGAIDVLPVGNVRMAARQLQPVRITTREECKIPGLLDGDRQGNDVSAMRVDIGARSYDEVMQAGIRPGDRVTFDTTFQVLPHQRVMGKAFDDRLGCYLLVTLLRELHDAELPAEVWLVASSSEEVGLRGGQTATRAVSPDVAIVLDTACWAKNFDYGAANHRQIGNGPMLVLSDKSLIAPPKLTAWVETVAAEIGVPLQADMFSNGGTDGGAVHLTGTGVPTVVMGPATRHGHCAASIADCRDILQMQQLLSALIQRLTRETVVQLTDFR |
| Enzyme Length | 345 |
| Uniprot Accession Number | P77585 |
| Absorption | |
| Active Site | ACT_SITE 198; /note=Proton acceptor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.11.- |
| Enzyme Function | FUNCTION: Has a broad aminopeptidase activity on non-blocked peptides by progressively cleaving amino acids off the peptide substrate. Aminopeptidase activity stops at the residue before the first proline in the peptide. Cannot cleave when proline is the first N-terminal residue. {ECO:0000269|PubMed:15901689}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (6) |
| Keywords | Aminopeptidase;Cobalt;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16606699; 24561554; |
| Motif | |
| Gene Encoded By | |
| Mass | 37,409 |
| Kinetics | |
| Metal Binding | METAL 62; /note=Divalent metal cation 1; /evidence=ECO:0000250; METAL 166; /note=Divalent metal cation 1; /evidence=ECO:0000250; METAL 166; /note=Divalent metal cation 2; /evidence=ECO:0000250; METAL 199; /note=Divalent metal cation 2; /evidence=ECO:0000250; METAL 221; /note=Divalent metal cation 1; /evidence=ECO:0000250; METAL 308; /note=Divalent metal cation 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |