| IED ID | IndEnz0002014346 |
| Enzyme Type ID | protease014346 |
| Protein Name |
Putative 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 |
| Gene Name | R04B3.2 |
| Organism | Caenorhabditis elegans |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
| Enzyme Sequence | MRRFYIFLLLIPYINGTINDDSLPMVITTWGSDGFKKATKNAVDATLLGGRMFGLVEGLSTCEALQCDTTVGYGGSPDENGETCLDSLVIDADGMRVGAVANLHRIRDAARVAWGVMNFTKHTLLVGESATQFAKTLGFKEEDLSTEETKSWISKWKTEKCQPNFWKNVSPDPSSSCGPYKTNPLTKSMRYYSLVNQSDEAGYLVEKTNHDTIGMVVRDTENIFSAGTSSNGARFKIPGRVGDSPIPGAGAYANKFGGAAATGDGDVMMRFLPSFFAVTQMELGTKPSKAAYKAITRILKVFPKFSGAVVAMNVKGRIGASCANINKFGYNVAFQNGTVVTYSISCLKEVNSLKYLKEGIEFA |
| Enzyme Length | 363 |
| Uniprot Accession Number | Q21697 |
| Absorption | |
| Active Site | ACT_SITE 212; /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. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Disulfide bond (2); Glycosylation (4); Region (2); Signal peptide (1) |
| Keywords | Autocatalytic cleavage;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Protease;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. |
| 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..17; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10778742; 19123269; 21177967; 22267497; 22560298; 23800452; 24884423; 25487147; 6593563; |
| Motif | |
| Gene Encoded By | |
| Mass | 39,359 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:11544 |
| Cross Reference Brenda |