sugar transferase.

Escherichia coli WbuB and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.

phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.

glycosyltransferases MtfB, WbpX, and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.

GlycosyltransferaseC from Streptococcus agalactiae [Streptococcus agalactiae COH1],4W6Q_B Glycosyltransferase C from Streptococcus agalactiae [Streptococcus agalactiae COH1],4W6Q_C Glycosyltransferase C from Streptococcus agalactiae [Streptococcus agalactiae COH1],4W6Q_D Glycosyltransferase C from Streptococcus agalactiae [Streptococcus agalactiae COH1]

Beta-1,6-galactofuranosyltransferase WbbI OS=Escherichia coli (strain K12) OX=83333 GN=wbbI PE=1 SV=1

Glucosyltransferase 3 OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=gtf3 PE=1 SV=1

Glucosyltransferase 3 OS=Streptococcus gordonii OX=1302 GN=gtf3 PE=3 SV=1

Glucosyltransferase 3 OS=Limosilactobacillus reuteri (strain DSM 17509 / CIP 109821 / 100-23) OX=349123 GN=gtf3 PE=3 SV=1

N-acetylglucosaminyltransferase OS=Limosilactobacillus reuteri (strain ATCC 53608) OX=927703 GN=gtf3 PE=1 SV=1