TCDB is operated by the Saier Lab Bioinformatics Group

4.D.2 The Glycosyl Transferase 2 (GT2) Family

The GT2 (COG0392) family has been implicated in several distinct functions including drug resistance and various enzymatic activities. Most members have about 8 - 10 TMSs plus a ~340aa C-terminal hydrophilic domain that may have catalytic activity. These proteins are implicated in glycosyl transfer with concomitant export across the membrane. They show very significant similarity to extra N-terminal domains in 3.A.3.4.3 and 4 as well as the C-terminal domain in 2.A.1.3.43 (unpublished results).

 

References associated with 4.D.2 family:

Ardiccioni, C., O.B. Clarke, D. Tomasek, H.A. Issa, D.C. von Alpen, H.L. Pond, S. Banerjee, K.R. Rajashankar, Q. Liu, Z. Guan, C. Li, B. Kloss, R. Bruni, E. Kloppmann, B. Rost, M.C. Manzini, L. Shapiro, and F. Mancia. (2016). Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis. Nat Commun 7: 10175. 26729507
Breazeale, S.D., A.A. Ribeiro, and C.R. Raetz. (2002). Oxidative decarboxylation of UDP-glucuronic acid in extracts of polymyxin-resistant Escherichia coli. Origin of lipid a species modified with 4-amino-4-deoxy-L-arabinose. J. Biol. Chem. 277: 2886-2896. 11706007
Tullius, M.V., C.A. Harmston, C.P. Owens, N. Chim, R.P. Morse, L.M. McMath, A. Iniguez, J.M. Kimmey, M.R. Sawaya, J.P. Whitelegge, M.A. Horwitz, and C.W. Goulding. (2011). Discovery and characterization of a unique mycobacterial heme acquisition system. Proc. Natl. Acad. Sci. USA 108: 5051-5056. 21383189