Amino acid sequence similarities between the vacuolar proton-pumping inorganic pyrophosphatase and the c-subunit of F0F1-ATPases.
Comparison of the Arabidopsis thaliana vacuolar proton-pumping inorganic pyrophosphatase with three F0F1-ATPase c-subunits revealed a strong similarity between a stretch containing amino acids 227-245 of the H(+)-PPase and a transmembrane alpha-helix of the c-subunits which contains the glutamate which binds N,N'-dicyclohexylcarbodiimide.
Nyrén
P
P
Institutionen för Biokemi och Biokemisk teknologi, Kungliga Tekniska Högskolan, Stockholm, Sweden.
Sakai-Nore
Y
Y
Strid
A
A
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000201:enzymology*; D001665:Binding Sites; D004024:Dicyclohexylcarbodiimide / Q000378:metabolism; D043564:Inorganic Pyrophosphatase; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D006180:Proton-Translocating ATPases / Q000737:chemistry*; D011755:Pyrophosphatases / Q000737:chemistry*; D012247:Rhodospirillum rubrum / Q000201:enzymology; D017386:Sequence Homology, Amino Acid; D014617:Vacuoles / Q000201:enzymology
D046911:Macromolecular Substances; D004024:Dicyclohexylcarbodiimide; D011755:Pyrophosphatases; D043564:Inorganic Pyrophosphatase; D006180:Proton-Translocating ATPases