In order to acquired the cytochrome P450 protein gene (Cyp450) in wheat and physicochemical properties, structural characteristics and relevant information of the corresponding protein, the ectroniccloning technology and bioinformatics methods were utilized for its cDNA and the corresponding amid acid sequence as well as physical and chemical properties, subcellular localization, senior structural and its functional domains of the protein. The results showed that the length of cDNA sequence was 2155 bp, encoding 511 amino acids. In N-terminal of the protein seuence there was a significant signal peptide, it belonged to CypX surperfamily. The protein located in the cytoplasm was signal peptide protein in secretory pathway; it contained multiple different phosphorylation sites. The α-helix (accounted for 48.14%) and random coil (accounted for 33.68%) was main secondary structure, it had five disorder region and a potential globulin area in 85-511 amid acid of the protein sequence. The protein had higher sequece indentities with that from other gramineae plants including Hordeum vulgare, brachypodium distachyon, oryza sativa and zea may, the evolution distance among them was near. A new Cyp450 gene in wheat was cloned, and some sequence characters of the corresponding protein were studied, these results provided theory basis for the gene cloning by PCR technique and functional analysis.