| IED ID | IndEnz0002016760 |
| Enzyme Type ID | protease016760 |
| Protein Name |
Aminopeptidase N EC 3.4.11.2 Alpha-aminoacylpeptide hydrolase |
| Gene Name | pepN HI_1614 |
| Organism | Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pasteurellales Pasteurellaceae Haemophilus Haemophilus influenzae Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) |
| Enzyme Sequence | MLAKAKYRKDYKQPDFTVTDIYLDFQLDPKHTVVTAITKFQRLNNEATSLCLDGHSFQFSSIKFNGEPFSDYQQDGESLTLDLKDKSADEFEIEIVTFLVPAENTSLQGLYQSGEGICTQCEAEGFRQITYMLDRPDVLARYITKITADKTKYPFLLSNGNRIASGELEDGRHWVEWNDPFPKPSYLFALVAGDFDLLQDKFITKSGREVALELYVDRGNLNRATWAMESLKKAMKWDEDRFNLEYDLDIYMIVAVDFFNMGAMENKGLNIFNSKFVLANPQTATDDDYLAIESVIAHEYFHNWTGNRVTCRDWFQLSLKEGLTVFRDQEFSSDTGSRAVNRINNVKFLRTVQFAEDASPMSHPIRPEKVIEMNNFYTVTVYEKGAEVIRMLHTLLGEQGFQKGMQLYIAENDGKAATCEDFVSAMERANNLDLNQFRRWYSQSGTPELLISDAYDEKTHTYRLTVSQSTPPTADQMEKVNLHIPLKVALYDANGTKQMLQHNGELLSDVLNVTEKDQVFEFHGIYGRPIPALLCDFSAPVKLDYDYKTEQLLGLLKFADNQFIRWDAAQMLFAQELRRNVVRFQQGEALEISPEILTALSYVLNHYEKDIELATLILTLPKEMEFAESFKTIDPDGISAARAFMQAQIAESLKDDFLRVYTHIRLNDYQVTQQDIALRVMRNLCLTYLAYTNLGNNLVQKHYNNANNMTDTLAALSVATKAALLCRDVLLADFEQKWQHDGLVMDKWFALQATRPDDNVLEIIQLLMDHPSFNFNNPNRLRSLVGSFANHNLKAFHNVSGSGYRFLTDVLIRLNESNPQVAARLIEPLIRFSRFDAQRQTLMKRALERLSVVENLSKDLFEKIEKALQ |
| Enzyme Length | 869 |
| Uniprot Accession Number | P45274 |
| Absorption | |
| Active Site | ACT_SITE 299; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | BINDING 122; /note=Substrate; /evidence=ECO:0000250 |
| 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; |
| 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:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (1); Chain (1); Metal binding (3); Region (1); Sequence conflict (3); Site (1) |
| Keywords | Aminopeptidase;Cell inner membrane;Cell membrane;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 99,786 |
| Kinetics | |
| Metal Binding | METAL 298; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 302; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 321; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |