Detail Information for IndEnz0002018610
IED ID IndEnz0002018610
Enzyme Type ID protease018610
Protein Name Probable cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA APJL_1116
Organism Actinobacillus pleuropneumoniae serotype 3 (strain JL03)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pasteurellales Pasteurellaceae Actinobacillus Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae) Actinobacillus pleuropneumoniae serovar 3 Actinobacillus pleuropneumoniae serotype 3 (strain JL03)
Enzyme Sequence MEFSVKNGSVEKQRTACLVVGVYEPRRLSAAAEQLDKLSEGYISTLLRRGDLEGKAGQTLLLHNVPNVPADRVLLVGCGKERELTERQYKQIIQKMVQAVSETGSMEVVCFLTELHVKGRTSYWNVRFAIEAIQESLYSYNDFKSIKPEVRREFRRVIFNVANRKDLADAERALEQGKAISTGVAFAKNVANCPPNVCNPAYLAELAKGLAAEYDNIRTTVIDEAEMAALGMNAYLAVSRGSQNPAYLSVIEYKNHPNPDAKPIVLVGKGLTFDSGGISIKPSDSMDEMKYDMGGAASVYGTMKALAEMKLPLNVIGVLAGCENMPDGNAYRPGDILTTMNGLTVEVLNTDAEGRLVLCDTLTYVERFEPELVIDMATLTGACMIALGAHNSGLMSTSNVLANDLLNAAEQADDKAWRLPLGEEYQEQLKSNFADLANIGGRLGGAITAGQLLSNFTKKYVWAHLDIAGTAWKSGVAKGATGRPVSLLSQFLINKANNQ
Enzyme Length 499
Uniprot Accession Number B0BQ37
Absorption
Active Site ACT_SITE 281; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 355; /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 54,202
Kinetics
Metal Binding METAL 269; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 274; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 274; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 292; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 351; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 353; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 353; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181
Rhea ID
Cross Reference Brenda