The trpFB operon from Acinetobacter calcoaceticus encoding the phosphoribosyl anthranilate isomerase and the ,I-subunit of tryptophan synthase has been cloned by complementation of a trpB mutation in A. calcoaceticus, identffied by deletion analysis, and sequenced. It encodes potential polypeptides of 214 amino acids with a calculated molecular weight of 23,008 (TrpF) and 403 amino acids with' a molecular weight of 44,296 (TrpB) this organism (10). Three clones in which the trpBJ8 mutation was complemented were obtained, and the respective plasmids carried insertions of about 22, 16, and 9.3 kilobases, respectively. None of these plasmids yielded complementation of the trpA mutation in A. calcoaceticus BD413 trpA23 (22), whereas two of them complemented the trpF mutation in E. coli trpC9830 (F-) (26). A partial restriction map was made of the plasmid with the smaller insert, and the plasmid was subjected to deletion analysis (Fig. 1). In pWH1754, roughly 3.3 kilobases of the DNA from A. calcoaceticus BD4 complemented both trp mutations, whereas further deletions i'n that DNA resulted in loss of complementation. Therefore, this DNA was partially sequenced, and the resulting reading frames were searched for homology to known trpFB genes. This led to the identification of the trp operon on that DNA (Fig. 1)