Detail Information for IndEnz0002014086
IED ID IndEnz0002014086
Enzyme Type ID protease014086
Protein Name Probable cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA TC_0315
Organism Chlamydia muridarum (strain MoPn / Nigg)
Taxonomic Lineage cellular organisms Bacteria PVC group Chlamydiae Chlamydiia Chlamydiales Chlamydiaceae Chlamydia/Chlamydophila group Chlamydia Chlamydia muridarum Chlamydia muridarum (strain MoPn / Nigg)
Enzyme Sequence MVLLYSQASWDKRSKADALVLPFWMKNVKAQEAAVVDEDYKLVYQNALQNFSGKKGEAVFLFGNDKTKEQKIVLLGLGKSEEVSGTAILDAYAHVTTVLRKAKCKTVNILLPTISQLRFSVEEFLTNLAAGVLSLNYNYPTYHKVDASLPLLEKVTVLGIVPKVGDKIFRKEESLFEGVYLTRDLVNTNADEVTPEKLAAVAKGLAGEFASLDVKILDRKAILKEKMGLLAAVAKGSAVEPRFIVLDYQGKPKSKDRTVLIGKGVTFDSGGLDLKPGKAMITMKEDMAGAATVLGIFSALASLELPINVTGIIPATENAIGSAAYKMGDVYVGMSGLSVEIGSTDAEGRLILADAITYALKYCAPTRIIDFATLTGAMVVSLGEAVAGFFANNDVLARDLAEAASETGEALWRMPLVEKYDRALHSDIADMKNIGSNRAGSITAALFLQRFLEDNPVAWAHLDIAGTAYHEKEELPYPKYATGFGVRCLIYYMNKFLSK
Enzyme Length 499
Uniprot Accession Number P38019
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 54,109
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