| IED ID | IndEnz0002014357 |
| Enzyme Type ID | protease014357 |
| 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; Glycosylasparaginase beta chain Fragment |
| Gene Name | |
| Organism | Spodoptera frugiperda (Fall armyworm) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Amphiesmenoptera Lepidoptera (butterflies and moths) Glossata Neolepidoptera Heteroneura Ditrysia Obtectomera Noctuoidea Noctuidae (owlet moths) Amphipyrinae Spodoptera Spodoptera frugiperda (Fall armyworm) |
| Enzyme Sequence | EKNMPIVITTWSFTNASQKAWEVLKDEGKALDAVEQGGIVCENEQCDRTVGYGGSPDEDGETTLDAFIMDGSTMNVGAVAALRRIKSAISVARHVMEYTTHSFLAGELATKFAVEMGFKEESLSTDESRELWSKWRFEKQCQPNFRKNVKPDPRKHCGPYHKKRNFVDYIHPEVFVVDQYNHDTIGMVAVDSKGDVAAGTSTNGAKFKIPGRVGDSPIPGAGAYADNTVGGAAATGNGDTMMRFLPSFLAVEEMRRGASPANAAKTAIKRISAHHPDFMGAVIALSKNGQYGAACNGIETFPFVVQDKTRKTFEVVTIKC |
| Enzyme Length | 320 |
| Uniprot Accession Number | O02467 |
| Absorption | |
| Active Site | ACT_SITE 184; /note=Nucleophile; /evidence=ECO:0000250 |
| 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. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Disulfide bond (3); Glycosylation (1); Non-terminal residue (1); Region (2) |
| Keywords | Autocatalytic cleavage;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome. |
| 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 (Probable). {ECO:0000305}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 34,841 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:11544 |
| Cross Reference Brenda |