Detail Information for IndEnz0002016759
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