The phosphoserine aminotransferase activity (and the associated enzymes) are diffused in a great variety of organisms. The enzyme sequences are sufficiently similar to each other to be included in a single family, but the gene genealogies are rather confuse.
This family includes only two archaeal sequences, which are very similar to eubacterial (gram +) enzymes, possibly due to a recent horizontal gene transfer. In methanococcales a broad-specificity aminotransferase seems able to carry out the transamination of phosphoserine, as well as those of aspartate, glutamate, alanine, and cysteate (Helgadóttir et al., 2007, J Bacteriol 189(2):575-82). The sequences of these archaeal enzymes are most similar to those of alanine-glyoxylate aminotransferases (EC 2.6.1.51) and may be grouped in an independent family as soon as their substrate specificity becomes better defined.