Phylogenetic analysis of the putative phosphorylation domain in the pyruvate kinase of Bacillus stearothermophilus.
All sequenced phosphoenolpyruvate synthases (PPS), pyruvate:phosphate dikinases (PPDK) and enzymes I (EI) of the phosphoenolpyruvate:sugar phosphotransferase system comprise the PEP family. Linked to the C terminus of the sequenced pyruvate kinase from Bacillus stearothermophilus (PKBst) is a domain that is homologous to the putative phosphorylation domains of PEP family enzymes. We report sequence and phylogenetic analyses that lead to the following conclusions: (1) the phosphorylation domain of PKBst was derived from a PPS, late in the evolutionary process, after the divergence of PPSs from PPDKs and EIs; (2) this domain is probably functional in phosphoryl transfer; (3) the C-terminal phosphorylation domain in PKBst probably defines a compact domain in all PEP family proteins that is linked to other domains in these proteins via flexible linkers.
Nguyen
C C
CC
Department of Biology, University of California at San Diego, La Jolla 92093-0116, USA.
Saier
M H
MH
D000595:Amino Acid Sequence; D001411:Geobacillus stearothermophilus / Q000737:chemistry / Q000201:enzymology*; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000737:chemistry* / Q000145:classification; D010766:Phosphorylation; D011770:Pyruvate Kinase / Q000737:chemistry* / Q000145:classification
D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; D011770:Pyruvate Kinase