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 1733480420   2 EKPEGLNIEFIKNECNVGLVSQFNK-LKEMFNDtLIVVQAGDDMSKPQRLEKQYQAWKEQRDVKLILSQFDKIDEHGNFV 80
Cdd:cd04195    50 EFKRKLPLKVVPLEKNRGLGKALNEgLKHCTYD-WVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSDGNDI 128

                          90
                  ....*....|....
gi 1733480420  81 SGRDEGEVFDDSYQ 94
Cdd:cd04195   129 GKRRLPTSHDDILK 142

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733480420   2 EKPEGLNIEFIKNECNVGLVSQFNK-LKEMFNDtLIVVQAGDDMSKPQRLEKQYQAWKEQRDVKLILSQFDKIDEHGNFV 80
Cdd:cd04195    50 EFKRKLPLKVVPLEKNRGLGKALNEgLKHCTYD-WVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSDGNDI 128

                          90
                  ....*....|....
gi 1733480420  81 SGRDEGEVFDDSYQ 94
Cdd:cd04195   129 GKRRLPTSHDDILK 142

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733480420   2 EKPEGLNIEFIKNECNVGLVSQFNK-LKEMFNDtLIVVQAGDDMSKPQRLEKQYQAWKEQRDVKLILSQFDKIDEHGNFV 80
Cdd:cd04195    50 EFKRKLPLKVVPLEKNRGLGKALNEgLKHCTYD-WVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSDGNDI 128

                          90
                  ....*....|....
gi 1733480420  81 SGRDEGEVFDDSYQ 94
Cdd:cd04195   129 GKRRLPTSHDDILK 142