Phylogenetic analysis of the putative phosphorylation domain in the pyruvate kinase of Bacillus stearothermophilus

Res Microbiol. Nov-Dec 1995;146(9):713-9. doi: 10.1016/0923-2508(96)81067-9.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Geobacillus stearothermophilus / chemistry
  • Geobacillus stearothermophilus / enzymology*
  • In Vitro Techniques
  • Molecular Sequence Data
  • Phosphoenolpyruvate Sugar Phosphotransferase System / chemistry*
  • Phosphoenolpyruvate Sugar Phosphotransferase System / classification
  • Phosphorylation
  • Pyruvate Kinase / chemistry*
  • Pyruvate Kinase / classification

Substances

  • Phosphoenolpyruvate Sugar Phosphotransferase System
  • Pyruvate Kinase