Detail Information for IndEnz0002014025
IED ID IndEnz0002014025
Enzyme Type ID protease014025
Protein Name Probable cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA BC_4921
Organism Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus cereus group Bacillus cereus Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711)
Enzyme Sequence MFQVQKELAGHEAVIVALFEEEKMSSFVQELDKAFEGQLQVLLEEKELSTKKKAISKVHSLGKTNVKRYYFVGLGKKESYTTETLRAALGKAFKTLQAAKVQDAAILLDSFVTEKLDAIDVAHIAAEVQGLGTYELQTYKSDKKDRVELEKFMAITSEDAQEIEAALTVGYVHGRATNSARTLVNMPPNVLTATKLAEYAVELAEKYDMDYKVLEKEEMEDLGMGALLAVNQGSVEPPKMIALIYKGKEEWKDVIGFVGKGITYDTGGYSLKPREGMVGMKGDMGGAAAVLGAMEIIGELRPEQNVIAVIPSTDNVVSGTAFKPDDVITSMSGKTIEVLNTDAEGRLALADGITYAKKLGANYLVDVATLTGGVIVALGNYTTGAMTNNEELFEQVLEASMETDEPIWQLPIFDRDKERVRNSKFADLNNSPGREGHAVMAGTFLGEFAEDTPWVHLDIAGTSETKGAHDLGPAGATGAMVRTLATLVERFGEE
Enzyme Length 494
Uniprot Accession Number Q816E3
Absorption
Active Site ACT_SITE 272; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 346; /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 53,617
Kinetics
Metal Binding METAL 260; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 265; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 265; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 283; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 342; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 344; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 344; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181
Rhea ID
Cross Reference Brenda