This enzyme is an integral-membrane protein that carries out the second prenyltransfer reaction involved in the formation of polar membrane lipids in Archaea. Requires a divalent metal cation, such as Mg2+ or Mn2+, for activity . 4-Hydroxybenzoate, 1,4-dihydroxy 2-naphthoate, homogentisate and alpha-glycerophosphate cannot act as prenyl-acceptor substrates . The other enzymes involved in the biosynthesis of polar lipids in Archaea are EC 188.8.131.521 (sn-glycerol-1-phosphate dehydrogenase), EC 184.108.40.206 (phosphoglycerol geranylgeranyltransferase), which, together with this enzyme, alkylates the hydroxy groups of glycerol 1-phosphate to yield unsaturated archaetidic acid, which is acted upon by EC 220.127.116.11 (CDP-archaeol synthase) to form CDP-unsaturated archaeol. The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine . Belongs in the UbiA prenyltransferase family .
Hemmi, H.; Shibuya, K.; Takahashi, Y.; Nakayama, T.; Nishino, T.
(S)-2,3-Di-O-geranylgeranylglyceryl phosphate synthase from the thermoacidophilic archaeon Sulfolobus solfataricus. Molecular cloning and characterization of a membrane-intrinsic prenyltransferase involved in the biosynthesis of archaeal ether-linked membrane lipids