Detail Information for IndEnz0002019117
IED ID IndEnz0002019117
Enzyme Type ID protease019117
Protein Name Probable cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA LPC_0510
Organism Legionella pneumophila (strain Corby)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Legionellales Legionellaceae Legionella Legionella pneumophila Legionella pneumophila (strain Corby)
Enzyme Sequence MNYGLTHTPSLTMSECLVLGVFSDLALPDFATAIDNEQKGLIKKLCQRVPEPGNTVWQTDVEGHSLLIIQCGKKEEFSANSLQKRVGEITEALIKQRFSSATVCLPRLNQESAEWQLEQMIVQIDNLRYQLLDFKTKHAKSHKLESVIFHLPGATEKSLEMAKAIVTGVEFCRDLANMPANICTPTYLGEQAISLSKQFDQISCQVMGPEEIKEMGMGALLAVAQGSDQPPRLIDIHYHGNKNSTPVILVGKGITFDSGGLSIKPANAMDEMKYDMSGAASVLGVIKACALLKLPINLIGIIASAENLISGSAVKSGDIVTTMSGQTVEIINTDAEGRLVLADALTYAERYNPDFVIDIATLTGAIIVALGNIATGYMTRDEQLAKSIERAANESQDKVWRMPLDEAYQDALESPLADMINAGFDRSAGSITAACFLSRFTEKYRWAHLDIAGTAWISGKKRNATGRPVPLLIQLLRHVANSR
Enzyme Length 483
Uniprot Accession Number A5IAU5
Absorption
Active Site ACT_SITE 264; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 338; /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
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 52,613
Kinetics
Metal Binding METAL 252; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 257; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 257; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 275; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 334; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 336; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 336; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181
Rhea ID
Cross Reference Brenda