IED ID | IndEnz0002016758 |
Enzyme Type ID | protease016758 |
Protein Name |
Aminopeptidase N EC 3.4.11.2 Alpha-aminoacylpeptide hydrolase |
Gene Name | pepN CC_2481 |
Organism | Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Alphaproteobacteria Caulobacterales Caulobacteraceae Caulobacter Caulobacter vibrioides (Caulobacter crescentus) Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus) |
Enzyme Sequence | MRTDTPQAVNLADYRPFPFAIETTRLVFDLHPTRTRVSAELSVRRTGGKNEPLVLNGERLKLVSIAIDGRPLAAGEYGVDAERLTIAEAPDAFVLTTEVEIDPSSNKALMGLYMSGGRFCTQCEAEGFRTITYFPDRPDVLSRYSVRIEADGKFPHLLSNGNPVASGSLDGGRHFAEWSDPFPKPSYLFALVAGDLDVLADKFITMSGREVALRVFVDPGQASRAAYALDSLKRAMKWDEEAFGREYDLDLFMIVAVRDFNFGAMENKGLNIFNSSLLLADPQTATDLDYERIEAVVAHEYFHNWTGNRITCRDWFQLCLKEGFTVFRDQGLSADMRGAAVQRIKDVRALRARQFAEDAGPLAHPVRPSSYLKIDNFYTATIYEKGAEIIRMLKAILGAPAFRKGCDLYFQRHDGEATTVEAFIACFAEASGRDLSGFFGWYEQAGTPSVTIETAYDAAAGALTLTLTQSTSPTPGQPDKKPLPIPIAIGLLAADGRVLRDTEIVLLDQAQMTVRWDSIPEPPVLSALRGFSAPVNLSTDARPSDRYVLFGSDTDLFNRWEAGQTLARDLILTRAAGAPDEVGEERYADALGRALVDDAAEPAFKALLLALPSEPDLALMFEAADPAALHAARDHLRTRIAVHLGDLLRRLHGEMQINGEFSSDAAAAGRRALRNACAEALSADPHAENLARLLGHFGAARNMTDMIGGLYPMVAMGGVPREKALESFHHAWRTEPLVLDKWFAVQGRDPNPDALERVIALTQHPDFEPTNPNRLRALVSTFANFNPARFHDPSGAGYAFLADEILKVDAFNPMTAARLVEPLGGWRRYKPELGDLMRAQLERIVAHPNLSKNVLELASKALG |
Enzyme Length | 863 |
Uniprot Accession Number | P37893 |
Absorption | |
Active Site | ACT_SITE 300; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
Activity Regulation | |
Binding Site | BINDING 124; /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. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Binding site (1); Chain (1); Metal binding (3); Region (1); Site (1) |
Keywords | Aminopeptidase;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 94,880 |
Kinetics | |
Metal Binding | METAL 299; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 303; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 322; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
Rhea ID | |
Cross Reference Brenda |