Detail Information for IndEnz0002019120
IED ID IndEnz0002019120
Enzyme Type ID protease019120
Protein Name Probable cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA Mpe_A1942
Organism Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Betaproteobacteria Burkholderiales Burkholderiales genera incertae sedis Methylibium Methylibium petroleiphilum Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1)
Enzyme Sequence MDFRILATSTSSLSKVSADALLIVVAGDPKQQGLDDPLDRVLSDAIAAGDLAFKAGRTLYLHRPLGVKAARVVFAVAGDAGPKAFKSAVAAGLGLIKPLGVKHLAVAASGAIEDSHAEAAAAAASDATYSYRHTKPSASPAPALQKITLLVDKAEAKAAQTGLSRGAAIALGVALARECANRPGNHCTPSFLAAEARKLAKLPRIKVDVLDRKACEKLGMGSFLAVAQGSDEPPKFIVLRYDGASRSDAPVVLVGKGITFDTGGISIKPAAEMDEMKYDMGGAASVLGSFRAVAELQPQVNVVGLIPSCENMPSGRAIKPGDVVTSMSGQTIEVLNTDAEGRLILCDALTYAERFKPAVVIDIATLTGACVIALGHHRSGLFSADDALADALLDAGSAGLDPAWRMPLDDEYEEALRSNFADMGNVGGRAGGAITAAMFLKKFTAKYRWAHLDIAGTAWKSGAAKGATGRPVPLLTHFVLSRTR
Enzyme Length 484
Uniprot Accession Number A2SH61
Absorption
Active Site ACT_SITE 268; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 342; /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 50,148
Kinetics
Metal Binding METAL 256; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 261; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 261; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 279; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 338; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 340; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 340; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181
Rhea ID
Cross Reference Brenda