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

• Published in: Molecular biology and evolution Vol. 7; no. 1; pp. 74 - 81
• Main Authors: ROSS, C. M, KAPLAN, J. B, WINKLER, M. E, NICHOLS, B. P
• Format: Journal Article
• Language: English
• Published: Oxford Oxford University Press 1990
• Subjects: Acinetobacter - enzymology; Acinetobacter - genetics; Aldose-Ketose Isomerases; Amino Acid Sequence; Bacteria - enzymology; Bacteria - genetics; Base Sequence; Biological and medical sciences; Biological Evolution; Carbohydrate Epimerases - genetics; DNA, Bacterial - genetics; DNA, Fungal - genetics; Fundamental and applied biological sciences. Psychology; Fungi - enzymology; Fungi - genetics; Genes, Bacterial; Genes, Fungal; Genes. Genome; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Sequence Homology, Nucleic Acid; Tryptophan - biosynthesis; Nucleotide sequence; Enzyme; Interspecific comparison; Neisseriaceae; Homology; Molecular evolution; Acinetobacter calcoaceticus; DNA; Deletion; Bacteria; Micrococcales; Molecular cloning; Aminoacid sequence
• ISSN: 0737-4038; 1537-1719; 1537-1719
• DOI: 10.1093/oxfordjournals.molbev.a040587

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.