| IED ID | IndEnz0002014216 |
| Enzyme Type ID | protease014216 |
| Protein Name |
Aminopeptidase N EC 3.4.11.2 Alpha-aminoacylpeptide hydrolase |
| Gene Name | pepN b0932 JW0915 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MTQQPQAKYRHDYRAPDYQITDIDLTFDLDAQKTVVTAVSQAVRHGASDAPLRLNGEDLKLVSVHINDEPWTAWKEEEGALVISNLPERFTLKIINEISPAANTALEGLYQSGDALCTQCEAEGFRHITYYLDRPDVLARFTTKIIADKIKYPFLLSNGNRVAQGELENGRHWVQWQDPFPKPCYLFALVAGDFDVLRDTFTTRSGREVALELYVDRGNLDRAPWAMTSLKNSMKWDEERFGLEYDLDIYMIVAVDFFNMGAMENKGLNIFNSKYVLARTDTATDKDYLDIERVIGHEYFHNWTGNRVTCRDWFQLSLKEGLTVFRDQEFSSDLGSRAVNRINNVRTMRGLQFAEDASPMAHPIRPDMVIEMNNFYTLTVYEKGAEVIRMIHTLLGEENFQKGMQLYFERHDGSAATCDDFVQAMEDASNVDLSHFRRWYSQSGTPIVTVKDDYNPETEQYTLTISQRTPATPDQAEKQPLHIPFAIELYDNEGKVIPLQKGGHPVNSVLNVTQAEQTFVFDNVYFQPVPALLCEFSAPVKLEYKWSDQQLTFLMRHARNDFSRWDAAQSLLATYIKLNVARHQQGQPLSLPVHVADAFRAVLLDEKIDPALAAEILTLPSVNEMAELFDIIDPIAIAEVREALTRTLATELADELLAIYNANYQSEYRVEHEDIAKRTLRNACLRFLAFGETHLADVLVSKQFHEANNMTDALAALSAAVAAQLPCRDALMQEYDDKWHQNGLVMDKWFILQATSPAANVLETVRGLLQHRSFTMSNPNRIRSLIGAFAGSNPAAFHAEDGSGYLFLVEMLTDLNSRNPQVASRLIEPLIRLKRYDAKRQEKMRAALEQLKGLENLSGDLYEKITKALA |
| Enzyme Length | 870 |
| Uniprot Accession Number | P04825 |
| Absorption | |
| Active Site | ACT_SITE 298; /note="Proton acceptor"; /evidence="ECO:0000305|PubMed:16885166, ECO:0000305|PubMed:18416562, ECO:0000305|PubMed:19622865" |
| Activity Regulation | |
| Binding Site | BINDING 121; /note=Substrate |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.; EC=3.4.11.2; Evidence={ECO:0000269|PubMed:16885166, ECO:0000269|PubMed:18416562, ECO:0000269|PubMed:19622865}; |
| DNA Binding | |
| EC Number | 3.4.11.2 |
| Enzyme Function | FUNCTION: Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation. {ECO:0000269|PubMed:16885166, ECO:0000269|PubMed:18416562, ECO:0000269|PubMed:19622865, ECO:0000305|PubMed:20067529}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (31); Binding site (1); Chain (1); Helix (38); Initiator methionine (1); Metal binding (3); Region (1); Sequence conflict (1); Site (1); Turn (7) |
| Keywords | 3D-structure;Aminopeptidase;Cell inner membrane;Cell membrane;Direct protein sequencing;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | P19318; Itself |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (42) |
| Cross Reference PDB | 2DQ6; 2DQM; 2HPO; 2HPT; 2ZXG; 3B2P; 3B2X; 3B34; 3B37; 3B3B; 3KED; 3PUU; 3QJX; 4Q4E; 4Q4I; 4XMT; 4XMU; 4XMV; 4XMW; 4XMX; 4XMZ; 4XN1; 4XN2; 4XN4; 4XN5; 4XN7; 4XN8; 4XN9; 4XNA; 4XNB; 4XND; 4XO3; 4XO4; 4XO5; 5MFR; 5MFS; 5MFT; 5YO1; 5YQ1; 5YQ2; 5YQB; 6G8B; |
| Mapped Pubmed ID | 12482750; 15690043; 16606699; 16938892; 17196937; 22025387; 24561554; 25644575; 28383176; 30275593; 355237; 792681; |
| Motif | |
| Gene Encoded By | |
| Mass | 98,919 |
| Kinetics | |
| Metal Binding | METAL 297; /note=Zinc; catalytic; METAL 301; /note=Zinc; catalytic; METAL 320; /note=Zinc; catalytic |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.2; |