Detail Information for IndEnz0002019087
IED ID IndEnz0002019087
Enzyme Type ID protease019087
Protein Name Probable cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA CPn_0385 CP_0370 CpB0397
Organism Chlamydia pneumoniae (Chlamydophila pneumoniae)
Taxonomic Lineage cellular organisms Bacteria PVC group Chlamydiae Chlamydiia Chlamydiales Chlamydiaceae Chlamydia/Chlamydophila group Chlamydia Chlamydia pneumoniae (Chlamydophila pneumoniae)
Enzyme Sequence MVLFHAQASGRNRVKADAIVLPFWHFKDAKNAASFEAEFEPSYLPALENFQGKTGEIELLYSSPKAKEKRIVLLGLGKNEELTSDVVFQTYATLTRVLRKAKCSTVNIILPTISELRLSAEEFLVGLSSGILSLNYDYPRYNKVDRNLETPLSKVTVIGIVPKMADAIFRKEAAIFEGVYLTRDLVNRNADEITPKKLAEVALNLGKEFPSIDTKVLGKDAIAKEKMGLLLAVSKGSCVDPHFIVVRYQGRPKSKDHTVLIGKGVTFDSGGLDLKPGKSMLTMKEDMAGGATVLGILSALAVLELPINVTGIIPATENAIDGASYKMGDVYVGMSGLSVEICSTDAEGRLILADAITYALKYCKPTRIIDFATLTGAMVVSLGEEVAGFFSNNDVLAEDLLEASAETSEPLWRLPLVKKYDKTLHSDIADMKNLGSNRAGAITAALFLQRFLEESSVAWAHLDIAGTAYHEKEEDRYPKYASGFGVRSILYYLENSLSK
Enzyme Length 499
Uniprot Accession Number Q9Z8F8
Absorption
Active Site ACT_SITE 275; /evidence=ECO:0000255; ACT_SITE 349; /evidence=ECO:0000255
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; CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.; EC=3.4.11.10;
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 (By similarity). {ECO:0000250}.
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:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 54,510
Kinetics
Metal Binding METAL 263; /note=Manganese 2; /evidence=ECO:0000250; METAL 268; /note=Manganese 1; /evidence=ECO:0000250; METAL 268; /note=Manganese 2; /evidence=ECO:0000250; METAL 286; /note=Manganese 2; /evidence=ECO:0000250; METAL 345; /note=Manganese 1; /evidence=ECO:0000250; METAL 347; /note=Manganese 1; /evidence=ECO:0000250; METAL 347; /note=Manganese 2; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda