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Shikimate / quinate 5-dehydrogenase
This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyses the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyses the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate. Discusses the pentafunctional AROM multi-domain protein, which possesses a shikimate 5-dehydrogenase enzyme. The AROM protein catalyses steps two to six in the shikimate pathway in many microbial eukaryotes. [1]. 7556173. The molecular biology of multidomain proteins. Selected examples. Hawkins AR, Lamb HK;. Eur J Biochem 1995;232:7-18. (from Pfam)
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
molybdopterin-synthase adenylyltransferase MoeB catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein MoaD
MoeB/ThiF family adenylyltransferase
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