Glycosyltransferase that can glycosylate a wide range of substrates, including various flavonoids (flavones, flavonols, flavanones, flavanols, chalcones), isoflavonoids and stilbenes, to produce multiple glycosylated products (PubMed:23542617, PubMed:23974133, PubMed:24170092, PubMed:24893262, PubMed:25239890, PubMed:24949266, PubMed:27444326, PubMed:32238768). It can accept diverse nucleotide diphosphate-D/L-sugars as donors, including ADP-, GDP-, CDP-, TDP- or UDP-alpha-D-glucose, and catalyzes O-, N-, or S-glycosylation (PubMed:23542617, PubMed:23974133, PubMed:24170092, PubMed:24893262, PubMed:25239890, PubMed:24949266, PubMed:27444326, PubMed:32238768). In vitro, catalyzes the glycosylation of, among others, apigenin, 3-hydroxyflavone, phloretin or resveratrol, resulting in multiple glucosylated products, along with mono-, di-, tri- and tetraglucosides (PubMed:23542617, PubMed:23974133, PubMed:24170092, PubMed:24893262, PubMed:25239890, PubMed:27444326). Can also catalyze the glycosylation of the macrolide epothilone A with diverse NDP-D/L-sugars, forming different epothilone A glycoside derivatives (PubMed:24949266). an NDP-glycose + an acceptor = a glycosylated acceptor + NDP. Such glycosyltransferases with substrate flexibility and less regioselectivity can be utilized for glucosylation of a broad range of pharmacologically and industrially important compounds (PubMed:24170092). Glycosylation is an efficient tool for generating biologically potent and diverse novel natural and unnatural product glycoside compounds with enhanced drug efficacy. For instance, generation of novel resveratrol glycosides could facilitate the development of drugs to treat oxidative- stress-induced diseases and to provide antiaging functions (PubMed:25239890). Glycosylation of epothilones, a class of potential cancer drugs, may improve their efficacy as therapeutic drugs (PubMed:24949266). YjiC is a promiscuous enzyme for conjugating diverse sugars at amine and thiol functional groups of small molecules applicable for generating glycofunctionalized chemical diversity libraries (PubMed:32238768). Belongs to the UDP-glycosyltransferase family.