IED ID | IndEnz0002016783 |
Enzyme Type ID | protease016783 |
Protein Name |
Putative isoaspartyl peptidase/L-asparaginase EC 3.4.19.5 EC 3.5.1.1 Beta-aspartyl-peptidase Isoaspartyl dipeptidase L-asparagine amidohydrolase Cleaved into: Putative isoaspartyl peptidase/L-asparaginase alpha chain; Putative isoaspartyl peptidase/L-asparaginase beta chain |
Gene Name | DDB_G0279357 |
Organism | Dictyostelium discoideum (Slime mold) |
Taxonomic Lineage | cellular organisms Eukaryota Amoebozoa Evosea Eumycetozoa Dictyostelia (dictyostelid cellular slime molds) Dictyosteliales Dictyosteliaceae Dictyostelium Dictyostelium discoideum (Slime mold) |
Enzyme Sequence | MNKKSVLVIHGGAGVISKSTISKEREEIFLNSLKNILLAGKIILKQGGTSLDVVQEAVRLLEEDPIYNAGKGSVFTELGTNEMDAAIMDGTNLKAGAVGGVSIIRNPIIAARAVMEHTNHCLLVGKGAEEFAKSKNLEIVEPSFFFTQNRYDQLLRAKDEKKLILDHDGENLLEKEKEKEKNNETSTTTTTISVGVDPIDPKYKMGTVGAVCLDSFGNLAAATSTGGMTNKMHGRVGDTPIIGAGVYANKNVAVSSTGTGEAFMRTVAAFDIAAMMEYGSLSLKDASNKVVMEKLITVGDGGVICVDKYGNVEMPFNTEGMYRGYVIIDNNCENDQNDIINVSIYK |
Enzyme Length | 346 |
Uniprot Accession Number | Q54WW4 |
Absorption | |
Active Site | ACT_SITE 207; /note=Nucleophile; /evidence=ECO:0000250 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.; EC=3.4.19.5; CATALYTIC ACTIVITY: Reaction=H2O + L-asparagine = L-aspartate + NH4(+); Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1; |
DNA Binding | |
EC Number | 3.4.19.5; 3.5.1.1 |
Enzyme Function | FUNCTION: Has both L-asparaginase and beta-aspartyl peptidase activity. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine (By similarity). {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (2); Region (2); Site (1) |
Keywords | Autocatalytic cleavage;Hydrolase;Protease;Reference proteome |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | PTM: Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity (By similarity). {ECO:0000250}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 37,216 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:21016 |
Cross Reference Brenda |