Detail Information for IndEnz0002000234
IED ID IndEnz0002000234
Enzyme Type ID protease000234
Protein Name Peptidase E
EC 3.4.13.21
Alpha-aspartyl dipeptidase
Asp-specific dipeptidase
Dipeptidase E
Gene Name pepE alr7184
Organism Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Cyanobacteria/Melainabacteria group Cyanobacteria Nostocales Nostocaceae Nostoc unclassified Nostoc Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Enzyme Sequence MSKRLLLLSNSTNIGEEYLFYARQEIKNFLGSSVKKIAFIPFAAVTSTYQHYSEKVRKVFQDIGYEFDAIHLVESSHELIKNAEAVVVGGGNTFHLIHCLHETKLLDDIRNKVSNGTPYIGWSAGSNVACPTIKTSNDMPIIEPISFQGLNLVPFQINPHYTNAVIPNHNGETREQRLEDFLVLNPDIYVVGLPEGTMLKIEDSSIRLIGNKTIYLFKFGEEKQEYYPHDNLDFLLERASFT
Enzyme Length 242
Uniprot Accession Number P58493
Absorption
Active Site ACT_SITE 123; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_00510; ACT_SITE 138; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_00510; ACT_SITE 160; /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); Frameshift (1)
Keywords Cytoplasm;Dipeptidase;Hydrolase;Plasmid;Protease;Reference proteome;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 Plasmid pCC7120alpha
Mass 27,458
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda