Abstract: The objectives of the present study were to provide a molecular mechanism basis in the studying of quality changes in postharvest and storage from Castanea mollissima blume, and further exploring the function of CAT1 gene. Full-length CAT1 c DNA was cloned from Castanea mollissima blume using rapid amplication of c DNA ends ( RACE) method, and were analyzed by bioinformatics technology.The results of sequence analysis indicated that CAT1 had a length of 1485 bp containing a 1479 bp open reading frame which encoded 492 amino acid residues. Amino acid sequence analysis indicated that, CAT1 was high identity with the catalases of Ziziphus jujuba, Nicotiana tabacum, Gossypium hirsutum and many other plants. The predicted molecular weight of the protein was 56947.31 Da with the p I of 6.65.Characteristic analysis of protein results revealed that CAT1 protein is a stable, non-transmenbrane and hydrophilic protein, located in microbody ( peroxisome) .It has no signal peptide and contains 30 phosphorylation sites. The conserved domains service analysis indicated that CAT1 belonged to catalase-like superfamily.The secondary structure prediction showed that Castanea mollissima blume CAT1 protein mainly contains α-helix and random coil.Castanea mollissima blume CAT1 gene were cloned in this study, which laid the foundation for further studying biological of the gene.