Detail Information for IndEnz0002019084
IED ID IndEnz0002019084
Enzyme Type ID protease019084
Protein Name Probable cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA Cpar_1121
Organism Chlorobaculum parvum (strain DSM 263 / NCIMB 8327) (Chlorobium vibrioforme subsp. thiosulfatophilum)
Taxonomic Lineage cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Chlorobi Chlorobia Chlorobiales Chlorobiaceae Chlorobaculum Chlorobaculum parvum Chlorobaculum parvum (strain DSM 263 / NCIMB 8327) (Chlorobium vibrioforme subsp. thiosulfatophilum)
Enzyme Sequence MRLTVTAKEGGSIKADALVLFISTKDLKKEAGKLLRSLGADEGALKDFKASAGELVMAYRAASGKSPLRLLLAGIGDGLKLEEFRKAAEAAARKAVDLKIGILALDCSGAAQWAKQLKCKSDELAAVLAGAAQYGAYRFDRLKSGKLDKKKDESKPKGISELVFAGCGTQLGAIENGANAGMIVGSCQNAARDLVNLPGNHLSAEDLADAAREAGKRGGFEVTVFDKKKITELKMGGLLAVNKGSEQPPTFTIMDYKPEGKAKKTIALVGKGVTFDSGGISLKPAQGMEEMKSDMAGAACVIEAVEAAARLALPVRVIGFVPSTDNMPSGSAQMPGDVITTMSGITVEVGNTDAEGRLILADALTYAKQEYNPDVMIDLATLTGACIVALGYPVAGLFSNDEALADRLFKSGQASGEKVWQLPLWDEYAELIKSDVADVHNTGGRGAGSITAAKFLEKFIDGHKHWAHVDIAGPAFPTKGGSKVSGATGFGVRLLVDLLQSWS
Enzyme Length 503
Uniprot Accession Number B3QNM5
Absorption
Active Site ACT_SITE 283; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 357; /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 52,622
Kinetics
Metal Binding METAL 271; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 276; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 276; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 294; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 353; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 355; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 355; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181
Rhea ID
Cross Reference Brenda