In this study, the full-length cDNA sequence of HK gene was cloned from Haematococcus pluvialis by the combined homologous cloning and rapid-amplification of cDNA ends (RACE) methods. The physical and chemical properties, structure, and evolution were analyzed by bioinformatics methods. The full-length cDNA of HaeHK was 2 047 bp, it contained an open reading frame of 1 716 bp and encoded a protein of 571 amino acids. The deduced protein had a calculated molecular mass of 60.61 kD with an estimated isoelectric point (pI) of 6.49. Homologous alignment analysis revealed that HaeHK had similarity with other HKs from different organisms, Volvox carteri (50%) and Chlamydomonas reinhardtii (46%). Conserved domains analysis showed that the typical domain of the HKs was highly conserved in the protein sequences of HaeHK, including a remarkable characteristic with a“butterfly” tertiary structure. Phylogenetic analysis of the HKs showed that HaeHK is highly similar to the HKs of high plants and Chlorophyta, which indicated that they were from a common origin. In this study, the gene sequence encoding HK in Haematococcus pluvialis was obtained for the first time, the above results laid the foundation for further study on gene expression and functional identification, which may provide clues for revealing utilization and metabolism molecular mechanism of hexose in Haematococcus pluvialis.