Detail Information for IndEnz0002018578
IED ID IndEnz0002018578
Enzyme Type ID protease018578
Protein Name Probable cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA Rmet_2807
Organism Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Betaproteobacteria Burkholderiales Burkholderiaceae Cupriavidus Cupriavidus metallidurans Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans)
Enzyme Sequence MEFSTKALDLSKAGQNGFLATKTDCLVVGLFEGQSLAGVAKALDVATKGLVARLVKQGDFEGKRGTQLMLHEVAGVGAARVLLVGLGKEADFNDKAFAEAVRTATRALGGTRAASALWCLVQQPPQQRDVAWAIITTITLVREAGYRLLERHPELKRAPRGAGANEKASLRKIVLAVDVGDAKAASQAAVRGTAIANGMELTRDLGNLPSNICTPTYLANTARGIAKRHKLKVEILGRKQIEALNMGAFLAVTKGSVEPPQFIVLRYDGASAKQAPVVLVGKGITFDTGGISLKPGEGMDEMKYDMCGAASVLGTIQAVAEMGLKQNVIAVVPTCENMPSGIATKPGDVVTSMSGQTIEILNTDAEGRLILCDALTYVERFKPAAVIDVATLTGACIIALGHVNSGLYARSDALADQLLGAGRKAMDTAWRLPLDDDYQDQLKSNFADMANIGGRPAGSVTAACFLARYTEKYDWAHLDIAGTAWKSGAAKGATGRPVPLLTQFLMDRAA
Enzyme Length 510
Uniprot Accession Number Q1LJJ6
Absorption
Active Site ACT_SITE 294; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 368; /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;Reference proteome
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 53,736
Kinetics
Metal Binding METAL 282; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 287; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 287; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 305; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 364; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 366; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 366; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181
Rhea ID
Cross Reference Brenda