Detail Information for IndEnz0002019088
IED ID IndEnz0002019088
Enzyme Type ID protease019088
Protein Name Probable cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA DVU_0415
Organism Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria delta/epsilon subdivisions Deltaproteobacteria Desulfovibrionales Desulfovibrionaceae Desulfovibrio Desulfovibrio vulgaris Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough)
Enzyme Sequence MDIRFQAGGHAAWRAGAVMVFVFKDEPLAEVDSQLVEAAPWLTIAPAGNDFRAAKDEVAVLHGPPAFDIPRVVAVGLGKREDCTLERIRLAAAAGIRRCRDLRVENVGVVAAQLGRMAPTEHDALRVAEEVVCGALLGLYRYDRFRTVKDDERAEDPRWLALLCEGKNVPDDLHGAARKGEAVALGMGVARDLVNGPANIVTPAFLASEAEALGRKHGFRVEVLGRDELSSMGMGAFASVFRGAEEEARLIVIEHAPAGTEEQQPLVFVGKGVTFDTGGISLKPAAKMHEMKGDMAGAAAILGLFAALGERDLPRRVVGVLPCTENMPDGRATRPGDVVTTLSGKTVEILNTDAEGRLLLCDALTYAQRRWQPEALVDLATLTGACVVALGTEVAGLFCDDAALADAIASRGETVGDLFWPLPLWKSYAENLKSDVADLANVGPREGGAVNAALFLRQFIDDGVRWAHLDIAGPAFTAKKSALCPGGGTGFAVRTLFELVSEGIPAA
Enzyme Length 507
Uniprot Accession Number Q72F03
Absorption
Active Site ACT_SITE 283; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 357; /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 53,772
Kinetics
Metal Binding METAL 271; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 276; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 276; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 294; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 353; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 355; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 355; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181
Rhea ID
Cross Reference Brenda