Detail Information for IndEnz0002003918
IED ID IndEnz0002003918
Enzyme Type ID protease003918
Protein Name Probable cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA SCO2179 SC5F7.22
Organism Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces Streptomyces albidoflavus group Streptomyces coelicolor Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Enzyme Sequence MTALTLSTAAAPGLRADAIVIGVAKGAGGPSVAPGAEAVDKAYDGRLAAVLETLGASGAEGEVTKLPAPSGFKAPVVVAVGLGAEPEKDAGFDPEALRRAAGAAARALAGAKKAAFALPLAEAADAGVVAEGLLLGAYSFDAYKASAKEAKEAKGAKAKANGNGKAPLAEAALLGGKPRDKAYKAAIERATAVAEELNRARDLVNTPPNDLDPEAFAAVAQAAAKEHGIKVQVLDEKALVKGGYGGILGVGAGSASGPRLVKLSYTSPKAKKSLAFVGKGITYDSGGISLKPAGHNETMKCDMAGAAAVFAAVVAAARLGLEVNVTGWLALAENMPSGSATRPGDVLRMYSGKTVEVLNTDAEGRLVLADALWAASQDEPDAIIDVATLTGAMMLALGSRTYGIMANDDAFRSAVHEAAEESGEPAWPMPLPEHLRKGMDSPTADIANMGERMGGGLVAGLFLREFVGEGITWAHLDIAGPAFNEGGPFGYTPKGGTGTAVRTLVRVAELAAAGELG
Enzyme Length 517
Uniprot Accession Number Q9S2Q7
Absorption
Active Site ACT_SITE 291; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 365; /evidence=ECO:0000255|HAMAP-Rule:MF_00181
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.; EC=3.4.11.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00181}; CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.; EC=3.4.11.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00181};
DNA Binding
EC Number 3.4.11.1; 3.4.11.10
Enzyme Function FUNCTION: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. {ECO:0000255|HAMAP-Rule:MF_00181}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Metal binding (7)
Keywords Aminopeptidase;Cytoplasm;Hydrolase;Manganese;Metal-binding;Protease;Reference proteome
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00181}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 51,997
Kinetics
Metal Binding METAL 279; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 284; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 284; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 302; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 361; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 363; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 363; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181
Rhea ID
Cross Reference Brenda