Detail Information for IndEnz0002018710
IED ID IndEnz0002018710
Enzyme Type ID protease018710
Protein Name Probable cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA Bamb_2515
Organism Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD))
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Betaproteobacteria Burkholderiales Burkholderiaceae Burkholderia Burkholderia cepacia complex Burkholderia ambifaria Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD))
Enzyme Sequence MDFSIKGCDWSKGEAKGFLTGKSDCIVLGIFEAQTLSGAALDIDTATKGLISRVVKAGDMDGKRGKTLFLHEVSGIGASRVLLVGLGKQDAFNQKAYTDAVTAAWRALLSTKIVQVTFTLAQLPVDERSSDWGVRAAILALRNETYRFTQMKSKPEPASHTLKRVVFSVDPVDEKAAKLAVKQAVALANGMDLTRDLGNLPGNVCTPTYLGNTAKKIAKDWGLKAEVLGLKQIQALNMGSFLSVARASVEPPQFIVLHYQGAAAKAAPVVLVGKGITFDTGGISLKPGEAMDEMKYDMCGAGSVLGTMRAVAEMGLKINVVAIVPTCENMPGGNATKPGDIVTSMKGLTIEVLNTDAEGRLILCDALTYAERFKPAAVIDVATLTGACVIALGTHNSGLFSKDDALAGELLDASREANDPAWRMPLDDEYQDQLKSNFADIANIGGRPAGAVTAACFLSRFTDSYPWAHLDIAGTAWKGGAAKGATGRPVPLLAQFLIDRAGQ
Enzyme Length 503
Uniprot Accession Number Q0BCQ2
Absorption
Active Site ACT_SITE 286; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 360; /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 53,123
Kinetics
Metal Binding METAL 274; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 279; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 279; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 297; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 356; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 358; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 358; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181
Rhea ID
Cross Reference Brenda