Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632938   6 PGGDQGILNTFFSSWAttdIRKHLPFIYNLSSISIYSYLPAfKVFGASAKVVHFLGRVKPWNYTYDPKTKSVKseahdpn 85
Cdd:cd02537   156 DGGDQGLLNSYFSDRG---IWKRLPFTYNALKPLRYLHPEA-LWFGDEIKVVHFIGGDKPWSWWRDPETKEKD------- 224

                          90
                  ....*....|....*
gi 1034632938  86 mTHPEFLILWWNIFT 100
Cdd:cd02537   225 -DYNELHQWWWDIYD 238

Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin initiates the biosynthesis of glycogen by incorporating glucose residues through a self-glucosylation reaction at a Tyr residue, and then acts as substrate for chain elongation by glycogen synthase and branching enzyme. It contains a conserved DxD motif and an N-terminal beta-alpha-beta Rossmann-like fold that are common to the nucleotide-binding domains of most glycosyltransferases. The DxD motif is essential for coordination of the catalytic divalent cation, most commonly Mn2+. Glycogenin can be classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. It is placed in glycosyltransferase family 8 which includes lipopolysaccharide glucose and galactose transferases and galactinol synthases.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632938   6 PGGDQGILNTFFSSWAttdIRKHLPFIYNLSSISIYSYLPAfKVFGASAKVVHFLGRVKPWNYTYDPKTKSVKseahdpn 85
Cdd:cd02537   156 DGGDQGLLNSYFSDRG---IWKRLPFTYNALKPLRYLHPEA-LWFGDEIKVVHFIGGDKPWSWWRDPETKEKD------- 224

                          90
                  ....*....|....*
gi 1034632938  86 mTHPEFLILWWNIFT 100
Cdd:cd02537   225 -DYNELHQWWWDIYD 238

Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis];

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034632938   9 DQGILNTFFSSWAttdirKHLPFIYN-----LSSISIYSYLPAFKVFGASAKVVHFLGRVKPWNYTY 70
Cdd:COG1442   194 DQDILNIVLGGKV-----KFLPPRYNyqyslYYELKDKSNKKELLEARKNPVIIHYTGPTKPWHKWC 255

Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin initiates the biosynthesis of glycogen by incorporating glucose residues through a self-glucosylation reaction at a Tyr residue, and then acts as substrate for chain elongation by glycogen synthase and branching enzyme. It contains a conserved DxD motif and an N-terminal beta-alpha-beta Rossmann-like fold that are common to the nucleotide-binding domains of most glycosyltransferases. The DxD motif is essential for coordination of the catalytic divalent cation, most commonly Mn2+. Glycogenin can be classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. It is placed in glycosyltransferase family 8 which includes lipopolysaccharide glucose and galactose transferases and galactinol synthases.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632938   6 PGGDQGILNTFFSSWAttdIRKHLPFIYNLSSISIYSYLPAfKVFGASAKVVHFLGRVKPWNYTYDPKTKSVKseahdpn 85
Cdd:cd02537   156 DGGDQGLLNSYFSDRG---IWKRLPFTYNALKPLRYLHPEA-LWFGDEIKVVHFIGGDKPWSWWRDPETKEKD------- 224

                          90
                  ....*....|....*
gi 1034632938  86 mTHPEFLILWWNIFT 100
Cdd:cd02537   225 -DYNELHQWWWDIYD 238

Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to donor molecules. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. This family includes Lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, and glycogenin glucosyltransferase.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034632938   8 GDQGILN-TFFSSWATTDIRKHlpFIYNLSSISIYSYLPAFKvfgaSAKVVHFLGRVKPWNYT 69
Cdd:pfam01501 195 GDQDPLNiVFYGKVKPLDPRWN--VLGLGYYNKKKSLNEITE----NAAVIHYNGPTKPWLDI 251

A4GalT_like proteins catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface; The members of this family of glycosyltransferases catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The enzymes exhibit broad substrate specificities. The known functions found in this family include: Alpha-1,4-galactosyltransferase, LOS-alpha-1,3-D-galactosyltransferase, UDP-glucose:(galactosyl) LPS alpha1,2-glucosyltransferase, UDP-galactose: (glucosyl) LPS alpha1,2-galactosyltransferase, and UDP-glucose:(glucosyl) LPS alpha1,2-glucosyltransferase. Alpha-1,4-galactosyltransferase from N. meningitidis adds an alpha-galactose from UDP-Gal (the donor) to a terminal lactose (the acceptor) of the LOS structure of outer membrane. LOSs are virulence factors that enable the organism to evade the immune system of host cells. In E. coli, the three alpha-1,2-glycosyltransferases, that are involved in the synthesis of the outer core region of the LPS, are all members of this family. The three enzymes share 40 % of sequence identity, but have different sugar donor or acceptor specificities, representing the structural diversity of LPS.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034632938   8 GDQGILN-TFFSSWattdirKHLPFIYNLSsISIYSYLPAFKVF-------GASAKVVHFLGRVKPWNY 68
Cdd:cd04194   187 PDQDILNaVLKDKI------LYLPPRYNFQ-TGFYYLLKKKSKEeqeleeaRKNPVIIHYTGSDKPWNK 248