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UniProt functional annotation for Q47898 | ||
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| UniProt code: Q47898. |
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| Organism: | |
Elizabethkingia miricola (Chryseobacterium miricola). |
| Taxonomy: | |
Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; Weeksellaceae; Elizabethkingia. |
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| 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. |
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| 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; |
| Subunit: | |
Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers. {ECO:0000269|PubMed:10490104, ECO:0000269|PubMed:17157318, ECO:0000269|PubMed:20800597, ECO:0000269|PubMed:9685368}. |
| Subcellular location: | |
Periplasm. |
| 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. |
| Similarity: | |
Belongs to the Ntn-hydrolase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.