Detail Information for IndEnz0002018757
IED ID IndEnz0002018757
Enzyme Type ID protease018757
Protein Name Probable cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA PMM1332
Organism Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 / MED4)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Cyanobacteria/Melainabacteria group Cyanobacteria Synechococcales Prochlorococcaceae Prochlorococcus Prochlorococcus marinus Prochlorococcus marinus subsp. pastoris Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 / MED4)
Enzyme Sequence MQFSTFQQDLNTWQGSSLIFGIVEEDLKNQLQKINFIIDSKLLLEKINQKKFNGEKGKILNFDFFDQRLQTLKIIGLGESKNINSNDIKNSLADVIRKSSDKEEKISILFPWELINSPEEIQSFGESARLSAYKDNRFNSKRDDKKVLNEIEFLNLNKFKNINFNETEYICEGVELARRLVAAPPNSLTPLEMSIQASKIAKDHGLEIKILEKNECEDLGMGAYLAVAKGSDLEPKFIHLTLKSTSPVKEKIALVGKGLTFDSGGYNLKVGASQIEMMKYDMGGSAAVLGAAKALGAIKPDGLEIHFIVAACENMINGSAVHPGDVIKASNGKTIEINNTDAEGRLTLADALTYASNLKPDSIIDLATLTGAIVVALGNDVAGFWTNNNMMASDLKTASSQAGEELWQMPLQKSYKDGLKSHIADMKNTGPRAGGSITAALFLEEFFDKNIKWAHIDIAGTCWTDKNRGIHPSGATGYGVKTLVQWIKNKR
Enzyme Length 491
Uniprot Accession Number Q7V0D4
Absorption
Active Site ACT_SITE 269; /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 54,029
Kinetics
Metal Binding METAL 257; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 262; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 262; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 281; /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