The analysis of the structure and function of long chain-producing polyprenyl diphosphate synthase, which syn-thesizes the side chain of ubiquinone, has largely focused on the prokaryotic enzymes, and little is known about the eukaryotic counterparts. Here we show that decaprenyl diphosphate synthase fromSchizosaccharomyces pombeis comprised of a novel protein named Dlp1 acting in part-nership with Dps1. Dps1 is highly homologous to other prenyl diphosphate synthases but Dlp1 shares only weak homologywithDps1
