| IED ID | IndEnz0002014338 |
| Enzyme Type ID | protease014338 |
| Protein Name |
Putative N 4 - beta-N-acetylglucosaminyl -L-asparaginase GM21137 EC 3.5.1.26 Aspartylglucosaminidase AGA Glycosylasparaginase N4- N-acetyl-beta-glucosaminyl -L-asparagine amidase Cleaved into: Glycosylasparaginase alpha chain; Glycosylasparaginase beta chain |
| Gene Name | GM21137 |
| Organism | Drosophila sechellia (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 melanogaster group melanogaster subgroup Drosophila sechellia (Fruit fly) |
| Enzyme Sequence | MRTHLRASLWVLCLASTAFSILAAVNTSPKPTLASAFSGKAGTTAVKANKTTDELLPMVINTWNFTAANVLAWRILKQSKGGLRQTRNAVVEGCSKCEKLQCDRTVGYGGSPDELGETTLDAMVMDGATMDVGAVAGLRRIKDAIKVARHVLEHTQHTMLVGDAASAFANAMGFESESLVTPESKDMWLQWTAENCQPNFWKNVHPDPKVSCGPYKPRPTPLTRWKEDRARNEYEIGRKNHDTIGMIAIDVENNIHAGTSTNGANHKIPGRVGDSPIPGAGAYADNEVGAAVATGDGDVMMRFLPSLLAVEAMRAGKPPAEAAQKGLRRILKHQKDFMGALIAVDRLGNYGAACYGLAEFPFMVSSPAGADRPTRLETVKCIAGQDKVNIVAL |
| Enzyme Length | 393 |
| Uniprot Accession Number | B4HT15 |
| Absorption | |
| Active Site | ACT_SITE 243; /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; Evidence={ECO:0000250|UniProtKB:P20933}; |
| 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); Disulfide bond (3); Region (2); Signal peptide (1) |
| Keywords | Autocatalytic cleavage;Disulfide bond;Hydrolase;Protease;Reference proteome;Signal |
| 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 | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 42,213 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:11544 |
| Cross Reference Brenda |