Cloning of an ORF With Homology toMycobacterium echAl, Encoding the Enoyl-CoA Hydratase, inRhodococcus fascians

Abstract

An open reading frame encoding a polypeptide of significant homology (55.7% identity) with the enoyl-CoA hydratase encoded by the gene echA1 from Mycobacterium tuberculosis has been found in the genome of the plant-pathogen bacteria Rhodococcus fascians strain NRRL-B-15096. Sequence alignments showed that it possesses several conserved blocks common to E. coli, M. tuberculosis and human mitochondria. One of such blocks includes a glutamate residue located at position 149, corresponding to the glutamate 139 of Escherichia coli. This glutamate was previously shown to be the catalytic residue of enoyl-CoA hydratase in the multienzyme complex of fatty acid oxidation from E. coli. Our results provide additional information on the conserved domains of this enzyme. Significant homologies in other genome regions between R. fascians and M. tuberculosis confirm their phylogenetic relationship.

Can whole genome analysis refine the taxonomy of the genusRhodococcus?

“…This group includes enzymes that share protein sequence homology with each other, but have different enzyme functions. Included are those proteins that are part of large families and superfamilies (Table Table 6 Gene clusters from members of the genus Rhodococcus encoding proteins with sequence homology to single products in unrelated species [369][370][371][372][373][374][375][376][377][378] The green pink and yellow shading represents the presence of genes in species within the Rhodococcus, Gordonia and Nocardia clades that have been shaded the same colors as those in Fig. 1.…”