Detail Information for IndEnz0002019065
IED ID IndEnz0002019065
Enzyme Type ID protease019065
Protein Name Probable cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA Bcer98_3532
Organism Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus cereus group Bacillus cytotoxicus Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98)
Enzyme Sequence MFQVQTELANHGAVIVALFEEETSRFVQELDKAFEGQLQGLLDEKELSTKKKSISKVHSLGKTNVKRYYFVGLGKKEAYTTETLRASLSKTFKTLQAEKIQDAAILLDSFVTEKLDAIDVAHIAAEVYCLGTYRLQTYKTDKKEHVELEKLVVITAEDAKEIEAALTVGYVHGRATNSARTLVNMPPNMLTATKLAEYAVELAEKYDMDYKVLEKEEMEELGMGALLAVNQGSTEPPKMIALIYKGKEEWKDVIGLIGKGITYDTGGYSLKPRDGMVGMKGDMGGAAAVLGAMEIIGELRPEQNVIAIIPSTDNVVSGTAFKPDDVITSMSGKTIEVLNTDAEGRLALADGITYAKKLGANYLVDVATLTGGVIVALGNHTTGAMTNNETLFEQVLEASMETDERIWQLPIFERDKERVRNSKFADLNNSPGRDGHAVMAGTFLGEFAEDTPWVHLDIAGTSDTTSTHDLGPAGATGVMVRTLATLVERFGEE
Enzyme Length 493
Uniprot Accession Number A7GUC8
Absorption
Active Site ACT_SITE 271; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 345; /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 53,721
Kinetics
Metal Binding METAL 259; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 264; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 264; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 282; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 341; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 343; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 343; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181
Rhea ID
Cross Reference Brenda