Catalyzes the reversible conversion of sucrose and a nucleotide disphosphate (NDP) into fructose and NDP-glucose; although the reaction is freely reversible in vitro, the physiological reaction seems to be sucrose cleavage. Unlike characterized plant enzymes prefers ADP as a cosubstrate, whereas plants prefer UDP (PubMed:23196182). Its preference for ADP over UDP suggests it may directly link sucrose and glycogen metabolism (Probable). an NDP-alpha-D-glucose + D-fructose = a ribonucleoside 5'-diphosphate + H(+) + sucrose ADP-alpha-D-glucose + D-fructose = ADP + H(+) + sucrose kcat/KM for sucrose synthesis is 70094 for ADP-gluce and 2673 for UDP-glucose. Optimum pH is 7-9 for sucrose cleavage with ADP as substrate. Optimum temperature is 60 degrees Celsius for sucrose degradation with UDP and 70 degrees Celsius with ADP. The enzyme remains stable for 10 minutes at 50 degrees Celsius, while addition of ADP, UDP or sucrose enhances thermal stability by 5 degrees Celsius. Probably a homotetramer (PubMed:23196182). Belongs to the glycosyltransferase 1 family.