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ThiF family adenylyltransferase
This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1 [1-3]. [1]. 11713534. Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex. Lake MW, Wuebbens MM, Rajagopalan KV, Schindelin H;. Nature. 2001;414:325-329. [2]. 15660128. Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1. Lois LM, Lima CD;. EMBO J. 2005;24:439-451. [3]. 18662542. Structural insights into E1-catalyzed ubiquitin activation and transfer to conjugating enzymes. Lee I, Schindelin H;. Cell. 2008;134:268-278. (from Pfam)
molybdopterin-synthase adenylyltransferase MoeB
ATP-dependent adenylate transferase, transfers adenyl moiety to the MoeD subunit of molybdopterin synthase
HesA/MoeB/ThiF family protein
HesA/MoeB/ThiF family protein is an E1-like enzyme containing an NAD/FAD-binding fold that is involved in molybdopterin and thiamine biosynthesis
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