| IED ID | IndEnz0002014347 |
| Enzyme Type ID | protease014347 |
| 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 | |
| Organism | Elizabethkingia miricola (Chryseobacterium miricola) |
| Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Flavobacteriia Flavobacteriales Weeksellaceae Elizabethkingia Elizabethkingia miricola (Chryseobacterium miricola) |
| Enzyme Sequence | MRIIYKQQTMNNNRRDFIKKLGIATAAIAINPLEAKNLLDTSEPKTTNKPIVLSTWNFGLHANVEAWKVLSKGGKALDAVEKGVRLVEDDPTERSVGYGGRPDRDGRVTLDACIMDENYNIGSVACMEHIKNPISVARAVMEKTPHVMLVGDGALEFALSQGFKKENLLTAESEKEWKEWLKTSQYKPIVNIENHDTIGMIALDAQGNLSGACTTSGMAYKMHGRVGDSPIIGAGLFVDNEIGAATATGHGEEVIRTVGTHLVVELMNQGRTPQQACKEAVERIVKIVNRRGKNLKDIQVGFIALNKKGEYGAYCIQDGFNFAVHDQKGNRLETPGFALK |
| Enzyme Length | 340 |
| Uniprot Accession Number | Q47898 |
| Absorption | |
| Active Site | ACT_SITE 197; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:10490104, ECO:0000269|PubMed:17157318, ECO:0000269|PubMed:20800597, ECO:0000269|PubMed:9685368" |
| 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. Requires that the glycosylated asparagine moiety is not substituted on its N-(R1) and C- (R2) terminus. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (14); Chain (2); Helix (11); Mutagenesis (2); Region (2); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Autocatalytic cleavage;Direct protein sequencing;Hydrolase;Periplasm;Protease;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm. |
| 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. |
| Signal Peptide | SIGNAL 1..45; /evidence=ECO:0000269|PubMed:8250923 |
| Structure 3D | X-ray crystallography (12) |
| Cross Reference PDB | 1AYY; 1P4K; 1P4V; 2GAC; 2GAW; 2GL9; 3LJQ; 4R4Y; 5V2I; 9GAA; 9GAC; 9GAF; |
| Mapped Pubmed ID | 12906830; 25456816; 28457719; |
| Motif | |
| Gene Encoded By | |
| Mass | 37,263 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:11544 |
| Cross Reference Brenda | 3.5.1.26; |