Involved in cell wall synthesis (Probable). Preferentially catalyzes the addition of fucose in alpha 1-3 linkage to the first GlcNAc residue next to the peptide chains in N-glycans (PubMed:11420147, PubMed:11696361, PubMed:21515584). GDP-beta-L-fucose + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] = GDP + H(+) + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[(1->4)-alpha-L-Fuc]-beta-D-GlcNAc}-L-asparaginyl-[protein] Can also use Co(2+), Ca(2+) or Ni(2+) in vitro. Inhibited by Cu(2+) and Zn(2+). Protein modification; protein glycosylation. Membrane-bound form in trans cisternae of Golgi. The C-terminus (388-501) is important for catalytic activity or for enzyme stability. The N-terminus (1-89) appears to be dispensable for enzymatic activity. Glycosylation may be important for enzymatic activity. Belongs to the glycosyltransferase 10 family.