| IED ID | IndEnz0002014356 |
| Enzyme Type ID | protease014356 |
| 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 |
| Gene Name | Aga |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MARKWNLPFLLLPLVLGIPLVRGSNPLPLVVNTWPFKNATEAAWWTLVSGGSALDAVEKGCAMCEKEQCGGTVGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRALHSDWLSRNCQPNYWRNVIPDPSKYCGPYKPPDFLEQNNRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGDGDTLLRFLPSYQAVEYMRGGDDPARACQKVISRIQKYYPKFFGAVICANVTGSYGAACNRLPTFTQFSFMVYNSLHNQAIEEKVDCM |
| Enzyme Length | 345 |
| Uniprot Accession Number | P30919 |
| Absorption | |
| Active Site | ACT_SITE 205; /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:0000269|PubMed:1554372, ECO:0000269|PubMed:2775174}; |
| 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:0000269|PubMed:1554372, ECO:0000269|PubMed:2775174}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Disulfide bond (4); Glycosylation (3); Region (2); Signal peptide (1) |
| Keywords | Autocatalytic cleavage;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Protease;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:2775174}.; PTM: Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme (PubMed:2775174). The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity (By similarity). {ECO:0000250|UniProtKB:P20933, ECO:0000269|PubMed:2775174}. |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000269|PubMed:2775174 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 7673341; |
| Motif | |
| Gene Encoded By | |
| Mass | 37,167 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:11544 |
| Cross Reference Brenda |