Characterisation of genes encoding two novel members of the aldo-keto reductase superfamily.

Abstract

The predicted amino acid sequence of the protein encoded by a cDNA clone isolated from the protozoan haemoparasite Babesia bovis has approximately 22% amino acid identity with the Pichia stipitis xylose reductase. There are similar levels of amino acid identity with other members of the aldo-keto reductase superfamily. The identities include many residues highly conserved in the superfamily. However, the amino acid sequence of the B. bovis protein (AKR1) clearly lies outside the cluster of the previously characterized members of the superfamily. A putative protein encoded by a previously undescribed partially characterized open reading frame at the igrA (increased glyphosate resistance) locus of Pseudomonas sp. strain PG2982 also exhibits similarity to AKR1 and the aldo-keto reductases.