A Curcuma longa L. lectin was purified by aqueous extraction, 80% ammonium sulfate precipitation and ConA Sepharose affinity chromatography. Its specific activity was of 64,566 HU/mg protein for a yield of 41.2% total protein. The molecular weight is of 17.3 kDa. It has hemagglutinating activity against human blood group B, rabbit, mouse, rat, guinea pig, geese, and sheep erythrocytes. The optimum pH is between 6-7, and stable up to $40^{circ}C$. Activity was stimulated by $Ca^{2+}$ and $Mn^{2+}$. The internal sequence indicated similarity with legume lectin family. Moreover, at concentration of 47 and 94 mg/0.3 $cm^2$ disc showed antifungal activity against Exserohilum turicicum, Fusarium oxysporum, and Colectrotrichum cassiicola. The minimal inhibitory concentration were 0.002, 0.005, 0.011, 0.09, and 0.046 mg/mL Pseudomonas aeruginosa, Staphylococcus aureus, Bacillus subtilis, Escheriehia coli, and Candida albicans, respectively. Additionally, it contains a high $alpha$-glucosidase inhibitory activity with an $IC_{50}$ of 8 mg/mL.