| IED ID | IndEnz0002016759 |
| Enzyme Type ID | protease016759 |
| Protein Name |
Aminopeptidase N AP-N EC 3.4.11.2 Membrane glycoprotein H11 Microsomal aminopeptidase |
| Gene Name | |
| Organism | Haemonchus contortus (Barber pole worm) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Strongylida Trichostrongyloidea Haemonchidae Haemonchus Haemonchus contortus (Barber pole worm) |
| Enzyme Sequence | MTSQGRTRTLLNLTPIRLIVALFLVAAAVGLSIGLTYYFTRKAFDTSEKPGKDDTGGKDKDNSPSAAELLLPSNIKPLSYDLTIKTYLPGYVDFPPEKNLTFDGRVEISMVVIEPTKSIVLNSKKISVIPQECELVSGDKKLEIESVKEHPRLEKVEFLIKSQLEKDQQILLKVGYIGLISNSFGGIYQTTYTTPDGTPKIAAVSQNEPIDARRMVPCMDEPKYKANWTVTVIHPKGTKAVSNGIEVNGDGEISGDWITSKFLTTPRMSSYLLAVMVSEFEYIEGETKTGVRFRIWSRPEAKKMTQYALQSGIKCIEFYEDFFDIRFPLKKQDMIALPDFSAGAMENWGLITYRENSLLYDDRFYAPMNKQRIARIVAHELAHQWFGDLVTMKWWDNLWLNEGFARFTEFIGAGQITQDDARMRNYFLIDVLERALKADSVASSHPLSFRIDKAAEVEEAFDDITYAKGASVLTMLRALIGEEKHKHAVSQYLKKFSYSNAEATDLWAVFDEVVTDVEGPDGKPMKTTEFASQWTTQMGFPVISVAEFNSTTLKLTQSRYEANKDAVEKEKYRHPKYGFKWDIPLWYQEGDKKEIKRTWLRRDEPLYLHVSDAGAPFVVNADRYGFYRQNHDANGWKKIIKQLKDNHEVYSPRTRNAIISDAFAAAATDAIEYETVFELLNYAEKETEYLPLEIAMSGISSILKYFGTEPEAKPAQTYMMNILKPMYEKSSIDFIANNYRNDKLFFQINLQKDVIDMFCALGSQDCRKKYKKLFDDEVMNKCRDGQAATECVRIAAPLRSSVYCYGVKEGGDYASDKVMELYTAETLALEKDFLRLALGCHKDVTALKGLLLRALDRNSSFVRMQDIPSAFNDVAANPIGGEFIFNFLIERWPDIIESIGTKHTYVEKVIPACTSGIRSQQQIDQLKNLQKNGMNARQFGAFDKAIERAQNRVDWIKKHFQKLAAFFKKATL |
| Enzyme Length | 972 |
| Uniprot Accession Number | Q10737 |
| Absorption | |
| Active Site | ACT_SITE 380; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | BINDING 208; /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 | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (1); Chain (1); Compositional bias (1); Disulfide bond (2); Glycosylation (4); Initiator methionine (1); Metal binding (3); Region (2); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Aminopeptidase;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Signal-anchor;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 110,674 |
| Kinetics | |
| Metal Binding | METAL 379; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 383; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 402; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |