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Molecular Biology and Evolution, Vol 7, 74-81, Copyright © 1990 by Society for Molecular Biology and Evolution

ORIGINAL ARTICLE

An evolutionary comparison of Acinetobacter calcoaceticus trpF with trpF genes of several organisms

CM Ross, JB Kaplan, ME Winkler and BP Nichols
Department of Molecular Biology, Northwestern University Medical School, Chicago, Illinois 60611.

The deduced amino acid sequence of Acinetobacter calcoaceticus N-(5'- phosphoribosyl) anthranilate isomerase (PRAI), which is coded by trpF, was compared with TrpF of Caulobacter crescentus, Escherichia coli, Bacillus subtilis, Saccharomyces cerevisiae, Neurospora crassa, and Aspergillus nidulans. Sixty percent of identical or similar amino acids were located in alpha/beta TIM (triose-phosphate isomerase) barrels and in residues important in substrate binding and catalysis. In addition, the analysis of trpF genes presented here supports a model by which fusion between separate trpC and trpF genes arose in some cases by in- frame deletions.
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