Detail Information for IndEnz0002000244
IED ID IndEnz0002000244
Enzyme Type ID protease000244
Protein Name Peptidase E
EC 3.4.13.21
Alpha-aspartyl dipeptidase
Asp-specific dipeptidase
Dipeptidase E
Gene Name pepE SPC_4250
Organism Salmonella paratyphi C (strain RKS4594)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Salmonella Salmonella enterica (Salmonella choleraesuis) Salmonella enterica I Salmonella enterica subsp. enterica serovar Paratyphi C Salmonella paratyphi C (strain RKS4594)
Enzyme Sequence MELLLLSNSTLPGKAWLEHALPLIANQLNGRRSAVFIPFAGVTQTWDEYTDKTAEVLAPLGVNVTGIHRVADPLAAIEKAEIIIVGGGNTFQLLKESRERGLLAPMADRVKRGALYIGWSAGANLACPAIRTTNDMPIVDPNGFDALDLFPLQINPHFTNALPEGHKGETREQRIRELLVVAPELTVIGLPEGNWIQVSNGQAVLGGPNTTWVFKAGEEAVALEAGHRF
Enzyme Length 229
Uniprot Accession Number C0Q494
Absorption
Active Site ACT_SITE 120; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_00510; ACT_SITE 135; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_00510; ACT_SITE 157; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_00510
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides.; EC=3.4.13.21; Evidence={ECO:0000255|HAMAP-Rule:MF_00510};
DNA Binding
EC Number 3.4.13.21
Enzyme Function FUNCTION: Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids. {ECO:0000255|HAMAP-Rule:MF_00510}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1)
Keywords Cytoplasm;Dipeptidase;Hydrolase;Protease;Serine protease
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00510}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 24,739
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda