| IED ID | IndEnz0002014345 |
| Enzyme Type ID | protease014345 |
| Protein Name |
N 4 - beta-N-acetylglucosaminyl -L-asparaginase EC 3.5.1.26 Aspartylglucosaminidase AGA Glycosylasparaginase N4- N-acetyl-beta-glucosaminyl -L-asparagine amidase Cleaved into: Glycosylasparaginase alpha chain AGA subunit alpha p18 ; Glycosylasparaginase beta chain AGA subunit beta p30 Fragments |
| Gene Name | |
| Organism | Asobara tabida (Parasitic wasp) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Hymenoptera Apocrita (wasps ants and bees) Parasitoida Ichneumonoidea Braconidae Alysiinae Asobara Asobara tabida (Parasitic wasp) |
| Enzyme Sequence | RIIEPIAGGPFIVMTWNYPGTIGIIAVDANGHIAVGTSTN |
| Enzyme Length | 40 |
| Uniprot Accession Number | P83451 |
| Absorption | |
| Active Site | ACT_SITE 21; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P20933 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine = H(+) + L-aspartate + N-acetyl-beta-D-glucosaminylamine; Xref=Rhea:RHEA:11544, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15947, ChEBI:CHEBI:29991, ChEBI:CHEBI:58080; EC=3.5.1.26; |
| DNA Binding | |
| EC Number | 3.5.1.26 |
| Enzyme Function | FUNCTION: Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins. {ECO:0000250|UniProtKB:P20933}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Non-adjacent residues (1); Non-terminal residue (1) |
| Keywords | Autocatalytic cleavage;Direct protein sequencing;Glycoprotein;Hydrolase;Protease;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15110870}. |
| Modified Residue | |
| Post Translational Modification | PTM: May be N-glycosylated. {ECO:0000269|PubMed:15110870}.; 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 | 4,138 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:11544 |
| Cross Reference Brenda |