[ $^{31}PNMR$ ] spectroscopy revealed the adenylate kinase-like activity and the phosphotransferase activity from $F_1-ATPase$ of Escherichia coli. Incubation of $F_1-ATPase$ with ADP in the presence of $Mg^{2+}$ shows the appearance of $^{31}P$ resonances from AMP and Pi, suggesting the generation of AMP and ATP by adenylate kinase-like activity and the subsequent hydrolysis to Pi. Incubation of $F_1-ATPase$ with ADP in the presence of methanol shows additional peak from methyl phosphate, suggesting phosphotransferase activity of $F_1-ATPase$. Both adenylate kinase-like activity and the phosphotransferase activity has not been reported from $F_1-ATPase$ from Escherichia coli. $^{31}P$ NMR proved that it could be a valuable tool for the investigation of phosphorous related enzyme.