| Accession | TIGR02414 |
| Name | pepN_proteo |
| Function | aminopeptidase N |
| Gene Symbol | pepN |
| Trusted Cutoff | 718.20 |
| Domain Trusted Cutoff | 718.20 |
| Noise Cutoff | 403.85 |
| Domain Noise Cutoff | 403.85 |
| Isology Type | equivalog |
| EC Number | 3.4.11.2 |
| HMM Length | 868 |
| Mainrole Category | Protein fate |
| Subrole Category | Degradation of proteins, peptides, and glycopeptides |
| Gene Ontology Term | GO:0004177: aminopeptidase activity molecular_function |
| | GO:0006508: proteolysis biological_process |
| | GO:0008237: metallopeptidase activity molecular_function |
| Author | Haft DH |
| Entry Date | Dec 23 2004 10:57AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | The M1 family of zinc metallopeptidases contains a number of distinct, well-separated clades of proteins with aminopeptidase activity. Several are designated aminopeptidase N, EC 3.4.11.2, after the Escherichia coli enzyme, suggesting a similar activity profile (see SP|P04825 for a description of catalytic activity). This family consists of all aminopeptidases closely related to E. coli PepN and presumed to have similar (not identical) function. Nearly all are found in Proteobacteria, but members are found also in Cyanobacteria, plants, and apicomplexan parasites. This family differs greatly in sequence from the family of aminopeptidases typified by Streptomyces lividans PepN (TIGR02412), from the membrane bound aminopeptidase N family in animals, etc. |
| References | DR SWISSPROT; P04825; Escherichia coli
DR PFAM; PF01433; Peptidase family M1
RM 14663077
RT PepN is the major aminopeptidase in Escherichia coli: insights on substrate specificity and role during sodium-salicylate-induced stress.
RA Chandu D, Nandi D.
RL Microbiology. 2003 Dec;149(Pt 12):3437-47. |
