A pyrophosphate synthase gene: molecular cloning and sequencing of the cDNA encoding the inorganic pyrophosphate synthase from Rhodospirillum rubrum.
The integrally membrane-bound, proton-pumping inorganic pyrophosphate (PPi) synthase in phototrophic bacteria is hitherto the only described alternative to the ATP synthase in biological electron transport phosphorylation. We have identified and sequenced the first gene coding for a pyrophosphate synthase. The deduced protein contains 660 amino acid residues and 15 putative membrane-spanning segments. It is homologous to the vacuolar pyrophosphatases from plants.
Baltscheffsky
M
M
Department of Biochemistry, Arrhenius Laboratories, Stockholm University, S-106 91 Stockholm, Sweden. meg@biokemi.su.se
Nadanaciva
S
S
Schultz
A
A
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics*; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000737:chemistry*; D011756:Diphosphates / Q000378:metabolism*; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D017494:Proton Pumps; D012247:Rhodospirillum rubrum / Q000201:enzymology*
D001426:Bacterial Proteins; D018076:DNA, Complementary; D011756:Diphosphates; D017494:Proton Pumps