Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation. Required for elongation factor Tu receptor (EFR), but not flagellin-sensing 2 (FLS2) signaling. Protein modification; protein glycosylation. The N-terminal non-catalytic domain is assumed to mediate recognition of proteins with partial folding defects. No visible phenotype, but activation of the unfolded protein response. Loss of seedling growth inhibition in response to the pathogen-associated molecular pattern (PAMP) elf18. Belongs to the glycosyltransferase 8 family.