Specifically catalyzes the transfer of a galactosyl residue to the hydroxyproline-linked saccharide on Skp1 protein (fpaA/fpaB). Catalyzes the formation of a Gal-alpha-1,3-Fuc linkage, leading to Gal-Fuc-Gal-GlcNAc-HyPro143-Skp1. an alpha-L-fucosyl-(1->2)-beta-D-galactosyl derivative + UDP-alpha-D-galactose = an alpha-D-galactosyl-(1->3)-[alpha-L-fucosyl-(1->2)]-beta-D-galactosyl derivative + H(+) + UDP Divalent metal cations. Mn(2+) is 4-fold better than Mg(2+). Stimulated by dithiothreitol (DTT) in vitro. Totally inhibited by EDTA. The catalytic efficiency with the presumed natural substrate Fuc-alpha-1,2-Gal-beta-1,3-GlcNAc-alpha-1-Skp1 is 21-fold and 21000-fold higher than that of the synthetic substrates Fuc-alpha-1,2-Gal-beta-1-pNP and Fuc-alpha-1-Bn, respectively. Optimum pH is 6.4-7.4. Optimum temperature is 37 degrees Celsius. Protein modification; protein glycosylation. Consists of two domains: an N-terminal catalytic domain and a C-terminal domain, not required for activity, that is predicted to form a beta-propeller-like protein-protein interaction domain. Cells show an accumulation of the non-galactosylated isoform of Skp1 in cells. Not required for growth. Belongs to the glycosyltransferase 77 family.