We recently showed that the Vitamin B12 binding proteins typified by transcobalamin, required for B12 uptake in animals, has been derived through lateral transfer from the Gram-positive bacteria prior to the divergence of the extant animal lineages. These proteins contain a novel version of the b-grasp (ubiquitin-like) fold that has been adapted for binding small molecules like B12. In bacteria and archaea is shows a rich diversity of architectures including fusions to Helix-turn-helix domains in one-component transcription factors
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