Detail Information for IndEnz0002014102
IED ID IndEnz0002014102
Enzyme Type ID protease014102
Protein Name Probable cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA GWCH70_2878
Organism Geobacillus sp. (strain WCH70)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Geobacillus unclassified Geobacillus Geobacillus sp. (strain WCH70)
Enzyme Sequence MFTIKQQLSLDTTHEVLVVGMFEKNQPLDGIIAECDRRLGGQVSVLLKEGDISAKKKQISKVHTLNQAGVKRLYFVGLGKEEELTFDLLREAFGKLFKTLKQAKRTEAAIALDTFVTKDIDANDAAHALSEAYYLATYEFPGYKQKKNEPEKRIESITIYTEADQAEIEASVFVGSVYGKATNSARTLVNTPSNLLTAADLANYAVELANKYEFEYEILEKDDMEKLGMGAFLAVNQGSKNPPKMIVLKYQGKETWENVIGLVGKGVTFDTGGYSLKPRESMVDMKTDMAGAAAVLGAMEIIGELRPEQNVVAVIPATDNMISGEAFKPDDVITSMSGKTIEVKNTDAEGRLILADAITYAKHHGASYLIDVATLTGGVIVALGVHTTGAMTNNEALFEQVLEASAETGEFIWRLPITEKDKERVRSSKIADLNNSPGREGHAIMGGAFLGEFAEDTPWVHLDIAGTSVTSKEHDLGPSGATGVMVRTLATLVERFE
Enzyme Length 497
Uniprot Accession Number C5D720
Absorption
Active Site ACT_SITE 277; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 351; /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 54,103
Kinetics
Metal Binding METAL 265; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 270; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 270; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 288; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 347; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 349; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 349; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181
Rhea ID
Cross Reference Brenda