Abstract:

In order to study the resistant mechanism of choline monooxygenase (CMO), bioinformatics analysis of CMO from GenBank, including Beta vulgaris, Spinacia oleracea, Atriplex prostrate, Atriplex hortensis, Amaranthus tricolor, etc. were employed by NCBI, Expasy, Psort, NetPhosK, TMHMM, NPSA web and MEGA5, DNAman software. The results were listed as follows. CMO, which has abundant Ala, Ser and Leu, belonged to a type of stable protein. The amino acid sequence of CMO in different plants showed an identity of 81.52%, containing transit peptide, Rieske type Fe-S cluster motif and non-heme Fe binding motif. Phylogenetic tree analysis indicated that CMO had highly structural conservation, and could be used for the plants genetic differentiation and molecular evolution research. There was no transmembrane domain, which was consistent with the prediction of hydrophobic domain. The protein could be phosphorylated by protein kinase C, with the potential phosphorylated site Ser326. Random coil was the major structural element of polypeptide chain. CMO contained two functional domains which belonged to Rieske-type super family and SRPBCC-type super family respectively. The result provided theoretical reference for studies on both the enzymatic characteristics of CMO and the biosynthesis pathway of glycine betaine.