Abstract: In order to study the properties and structure function of DXS enzyme of medicinal plants, the amino acid sequences of 1-deoxy-D-xylulose 5-phosphate synthase (DXS) from Artemisia annua, Amomum villosum, Dendrobium officinale and so on, which were registered in GenBank, were analyzed and predicted by the tools of bioinformatics in the following aspects: physical and chemical characteristics of amino acid sequences, molecular phylogenetic evolution, hyophobicity or hydrophilicity, subcellular localization, phosphorylation site, signal peptide, secondary structure of protein, transmembrane topological structures, function domain, and so on. The results showed that DXS did not have signal peptide, transmembrane topological structures; the most abundant amino acids include Gly, Ala, Leu, Ser, Val. The dominant was the serine phosphorylation sites; mainly located in the chloroplast, the minor part located in mitochondria. The main was a hydrophilic protein, α-helix and random coil were the major motifs of predicted secondary structure of DXS; with three function domains for TPP_superfamily, Transket_pyr_ superfamily and Transketolase_C superfamily. The result provided theoretical reference for studies on both the enzymatic characteristics of DXS and the biosynthesis pathway of terpenoid.