| IED ID | IndEnz0002013665 |
| Enzyme Type ID | protease013665 |
| Protein Name |
Aminopeptidase YpdF EC 3.4.11.- |
| Gene Name | ypdF b2385 JW2382 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MTLLASLRDWLKAQQLDAVLLSSRQNKQPHLGISTGSGYVVISRESAHILVDSRYYVEVEARAQGYQLHLLDATNTLTTIVNQIIADEQLQTLGFEGQQVSWETAHRWQSELNAKLVSATPDVLRQIKTPEEVEKIRLACGIADRGAEHIRRFIQAGMSEREIAAELEWFMRQQGAEKASFDTIVASGWRGALPHGKASDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVNGEGVSAESHLLFNVYQIVLQAQLAAISAIRPGVRCQQVDDAARRVITEAGYGDYFGHNTGHAIGIEVHEDPRFSPRDTTTLQPGMLLTVEPGIYLPGQGGVRIEDVVLVTPQGAEVLYAMPKTVLLTGEA |
| Enzyme Length | 361 |
| Uniprot Accession Number | P76524 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.11.- |
| Enzyme Function | FUNCTION: Hydrolyzes the N-terminal methionine when the next amino acid is alanine, proline or serine. The substrate preference for methionyl aminopeptidase activity is Pro > Ala > Ser. Also able to hydrolyze the Xaa-Pro peptide bond when the first amino acid is alanine, asparagine or methionine. {ECO:0000269|PubMed:15901689}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (18); Chain (1); Helix (12); Turn (4) |
| Keywords | 3D-structure;Aminopeptidase;Hydrolase;Protease;Reference proteome |
| Interact With | P0A6F5 |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5CNX; |
| Mapped Pubmed ID | 16606699; 24561554; 30536999; |
| Motif | |
| Gene Encoded By | |
| Mass | 39,624 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.9; |