Natural history of the E1-like superfamily: implication for adenylation, sulfur transfer, and ubiquitin conjugation.

ABSTRACT: The E1-like superfamily is central to ubiquitin (Ub) conjugation, biosynthesis of cysteine, thiamine, and MoCo, and several secondary metabolites. Yet, its functional diversity and evolutionary history is not well understood. We develop a natural classification of this superfamily and use it to decipher the major adaptive trends occurring in the evolution of the E1-like superfamily. Within the Rossmann fold, E1-like proteins are closest to NAD(P)/FAD-dependent dehydrogenases and S-AdoMet-dependent methyltransferases. Hence, their phosphotransfer activity is an independent catalytic "invention" with respect to such activities seen in other Rossmannoid folds. Sequence and structure analysis reveals a striking diversity of residues and structures involved in adenylation, sulfotransfer, and su

SUBMITTER: Burroughs AM 

PROVIDER: S-EPMC2732565 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature