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3-hydroxyacyl-CoA dehydrogenase NAD-binding domain-containing protein
The term 3-hydroxyacyl-CoA dehydrogenase, corresponding to EC 1.1.1.35, covers a range of specificities, as the acyl group is not specified. Beta-hydroxyacyl dehydrogenase is a synonym. There may be mulitple members of the family in a single genome, e.g. FadB, FabJ, and PaaH from Escherichia coli K-12.
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)
thiazole biosynthesis adenylyltransferase ThiF
thiazole biosynthesis adenylyltransferase ThiF catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein ThiS
Members of the HesA/MoeB/ThiF family of proteins (PF00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with the Escherichia. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the more widely distributed clade of ThiF proteins such found in E. coli.
MoeB/ThiF family adenylyltransferase
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