| IED ID | IndEnz0002004435 |
| Enzyme Type ID | protease004435 |
| Protein Name |
Probable isoaspartyl peptidase/L-asparaginase GA20639 EC 3.4.19.5 EC 3.5.1.1 Beta-aspartyl-peptidase GA20639 Isoaspartyl dipeptidase GA20639 L-asparagine amidohydrolase GA20639 Cleaved into: Probable isoaspartyl peptidase/L-asparaginase GA20639 alpha chain; Probable isoaspartyl peptidase/L-asparaginase GA20639 beta chain |
| Gene Name | GA20639 |
| Organism | Drosophila pseudoobscura pseudoobscura (Fruit fly) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora obscura group pseudoobscura subgroup Drosophila pseudoobscura Drosophila pseudoobscura pseudoobscura (Fruit fly) |
| Enzyme Sequence | MPRPVLLIHGGAGDIPDSRIAGKFKGIKEALRCAWGSLVPASGAKGGALDAVETAVRSMELDENFNAGYGSCLNTDGQVEMEASLMEGQDLRAGCVTLLRDVMHPITVARRLMEKQRHTFIGGEAAQELALSTGSERLPANALVTEGARFTLQQFKEQLTQGKDPFFARTELAAEQKTDPSGETVGAVAMDHNGQIVVGTSTGGITGKWPGRIGDTPILGSGTYADNARGGVSTTGHGETIMRYNLAQRILAAIEHKGMSAQAAADQECREMTRRIGGTGGAIVVGHAGDLGISFTSQRMAWGYIQDDTIFYGIEGQVVHQEPLS |
| Enzyme Length | 325 |
| Uniprot Accession Number | Q29I93 |
| Absorption | |
| Active Site | ACT_SITE 184; /note=Nucleophile; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | 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; Evidence={ECO:0000250|UniProtKB:Q7L266}; CATALYTIC ACTIVITY: Reaction=Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.; EC=3.4.19.5; Evidence={ECO:0000250|UniProtKB:Q7L266}; |
| 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. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Region (2) |
| 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. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 34,399 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:21016 |
| Cross Reference Brenda |