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.

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.

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].

Glycosyl transferases group 1.

Sucrose-phosphatesynthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_B Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_C Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_D Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_E Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_F Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_G Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_H Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_I Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_J Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_K Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_L Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus]

CrystalStructure of the Putative Mannosyl Transferase (wbaZ-1)from Archaeoglobus fulgidus, Northeast Structural Genomics Target GR29A. [Archaeoglobus fulgidus DSM 4304]

Thecrystal structure of sucrose synthase-1 in complex with a breakdown product of the UDP-glucose [Arabidopsis thaliana],3S28_B The crystal structure of sucrose synthase-1 in complex with a breakdown product of the UDP-glucose [Arabidopsis thaliana],3S28_C The crystal structure of sucrose synthase-1 in complex with a breakdown product of the UDP-glucose [Arabidopsis thaliana],3S28_D The crystal structure of sucrose synthase-1 in complex with a breakdown product of the UDP-glucose [Arabidopsis thaliana],3S28_E The crystal structure of sucrose synthase-1 in complex with a breakdown product of the UDP-glucose [Arabidopsis thaliana],3S28_F The crystal structure of sucrose synthase-1 in complex with a breakdown product of the UDP-glucose [Arabidopsis thaliana],3S28_G The crystal structure of sucrose synthase-1 in complex with a breakdown product of the UDP-glucose [Arabidopsis thaliana],3S28_H The crystal structure of sucrose synthase-1 in complex with a breakdown product of the UDP-glucose [Arabidopsis thaliana],3S29_A The crystal structure of sucrose synthase-1 from Arabidopsis thaliana and its functional implications. [Arabidopsis thaliana],3S29_B The crystal structure of sucrose synthase-1 from Arabidopsis thaliana and its functional implications. [Arabidopsis thaliana],3S29_C The crystal structure of sucrose synthase-1 from Arabidopsis thaliana and its functional implications. [Arabidopsis thaliana],3S29_D The crystal structure of sucrose synthase-1 from Arabidopsis thaliana and its functional implications. [Arabidopsis thaliana],3S29_E The crystal structure of sucrose synthase-1 from Arabidopsis thaliana and its functional implications. [Arabidopsis thaliana],3S29_F The crystal structure of sucrose synthase-1 from Arabidopsis thaliana and its functional implications. [Arabidopsis thaliana],3S29_G The crystal structure of sucrose synthase-1 from Arabidopsis thaliana and its functional implications. [Arabidopsis thaliana],3S29_H The crystal structure of sucrose synthase-1 from Arabidopsis thaliana and its functional implications. [Arabidopsis thaliana]

1.35Angstrom Crystal Structure of C-terminal Domain of Glycosyl Transferase Group 1 Family Protein (LpcC) from Francisella tularensis. [Francisella tularensis subsp. tularensis SCHU S4]

Structureof Mycobacterium smegmatis alpha-maltose-1-phosphate synthase GlgM [Mycolicibacterium smegmatis MC2 155],6TVP_B Structure of Mycobacterium smegmatis alpha-maltose-1-phosphate synthase GlgM [Mycolicibacterium smegmatis MC2 155]

Uncharacterized glycosyltransferase MJ1607 OS=Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) OX=243232 GN=MJ1607 PE=3 SV=1

Protein RfbU OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=rfbU PE=3 SV=1

Probable sucrose-phosphate synthase OS=Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429) OX=391009 GN=Tmel_0533 PE=3 SV=1

Mannosylfructose-phosphate synthase OS=Agrobacterium fabrum (strain C58 / ATCC 33970) OX=176299 GN=mfpsA PE=1 SV=1

Sulfoquinovosyl transferase SQD2 OS=Arabidopsis thaliana OX=3702 GN=SQD2 PE=1 SV=1