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Phosphoenolpyruvate carboxykinase (PCK) catalyzes the decarboxylation and phosphorylation of oxaloacetate to phosphoenolpyruvate in the gluconeogenic pathway in most organisms. A  pckA  gene encoding PCK was cloned and sequenced from strain  Rhizobium pusense  NRCPB100, a spontaneous rifampicin resistant mutant of  R. pusense  NRCPB10 T  (JCM16209 T ) of a recently described new species of a non-nodulating and non-tumorigenic bacterium. The mapping of the  pck  gene region following  Tn5  mutagenesis located the gene downstream of a transcriptional regulatory protein gene (c hvI ) and upstream of a conserved hypothetical protein gene. The  pck  of 1,611 bp was deduced to encode 536 amino acids and showed high homology to the genes of known ATP-dependent PCK enzymes. Phylogenetic analysis of the gene placed it in a cluster with  pck  of other known members of Rhizobiales. Amino acid sequences of the putative functional regions of the deduced enzyme were found to be conserved.

Characterization of a (pckA) mutant of the non-nodulating bacterium Rhizobium pusense NRCPB10 induced by transposon Tn5 mutagenesis