[1][2] This enzyme belongs to the family of transferases, to be specific, those transferring phosphorus-containing groups (phosphotransferases) with paired acceptors (dikinases).
According to the BRENDA database, pyruvate, water dikinase has been studied in nine unique bacterial and archaea species under a wide range of names.
Many of the studied organisms are thermophilic or hyperthermophilic, meaning they live and function in very high temperatures in their natural environments, and have been found in hot springs, volcanos, and deep sea hydrothermal vents.
Pyrococcus furiosus is a deep sea hyperthermophilic archaea that is commonly found living in extremely hot waters around hydrothermal vents.
[1] This reaction is thought to be important because it converts AMP into usable ATP energy during this sugar M-EMP metabolism.
Two sugar kinase enzymes (glucokinase and phosphofructokinase) were found in the M-EMP pathway in Pyrococcus furiosus that catalyze the reaction that used ADP and produces AMP.
[1] The hyperthermostable pyruvate, water dikinase enzyme in Pyrococcus furiosus is encoded by the mlrA gene, which was found to be regulated by at least in part by maltose at a transcription level.
[2][4] Pyruvate, water dikinase in Pyrococcus furiosus is sensitive to oxygen, with no enzyme activity measured in aerobic conditions.