Detail Information for IndEnz0002016760
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