amylovoran biosynthesis glycosyltransferase AmsD and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.

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.

Glycosyl transferases group 1. Mutations in this domain of PIGA lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.

accessory Sec system glycosyltransferase GtfA and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general 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 in bacteria.

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.

Structureof a glycosyltransferase [Campylobacter jejuni],6EJI_B Structure of a glycosyltransferase [Campylobacter jejuni],6EJK_A Structure of a glycosyltransferase [Campylobacter jejuni],6EJK_B Structure of a glycosyltransferase [Campylobacter jejuni]

Structureof a glycosyltransferase / state 2 [Campylobacter jejuni],6EJJ_B Structure of a glycosyltransferase / state 2 [Campylobacter jejuni]

ChainA, Glycosyl transferase, group 1 family protein [Staphylococcus aureus subsp. aureus USA300],7EC2_B Chain B, Glycosyl transferase, group 1 family protein [Staphylococcus aureus subsp. aureus USA300]

ChainA, TarM [Staphylococcus aureus subsp. aureus 21178],4X7M_B Chain B, TarM [Staphylococcus aureus subsp. aureus 21178],4X7R_A Chain A, TarM [Staphylococcus aureus subsp. aureus 21178],4X7R_B Chain B, TarM [Staphylococcus aureus subsp. aureus 21178]

ChainA, TarM [Staphylococcus aureus subsp. aureus 21178],4X6L_B Chain B, TarM [Staphylococcus aureus subsp. aureus 21178],4X6L_C Chain C, TarM [Staphylococcus aureus subsp. aureus 21178],4X6L_D Chain D, TarM [Staphylococcus aureus subsp. aureus 21178],4X7P_A Chain A, TarM [Staphylococcus aureus subsp. aureus 21178],4X7P_B Chain B, TarM [Staphylococcus aureus subsp. aureus 21178]

Amylovoran biosynthesis glycosyltransferase AmsD OS=Erwinia amylovora OX=552 GN=amsD PE=3 SV=2

Exopolysaccharide phosphotransferase SCO2592 OS=Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) OX=100226 GN=SCO2592 PE=3 SV=1

Uncharacterized glycosyltransferase HI_1698 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_1698 PE=3 SV=1

Poly(glycerol-phosphate) alpha-glucosyltransferase OS=Bacillus subtilis (strain 168) OX=224308 GN=tagE PE=1 SV=1

Poly(ribitol-phosphate) alpha-N-acetylglucosaminyltransferase OS=Staphylococcus aureus (strain COL) OX=93062 GN=tarM PE=1 SV=1