glycosyltransferase family protein may 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
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
7-241
8.43e-56
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.
The actual alignment was detected with superfamily member cd02526:
Pssm-ID: 472172 [Multi-domain] Cd Length: 237 Bit Score: 180.17 E-value: 8.43e-56
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
7-241
8.43e-56
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.
Pssm-ID: 133017 [Multi-domain] Cd Length: 237 Bit Score: 180.17 E-value: 8.43e-56
L-rhamnosyltransferase; This model subfamily is comprised of gamma proteobacteria whose ...
10-286
8.88e-33
L-rhamnosyltransferase; This model subfamily is comprised of gamma proteobacteria whose proteins function as L-rhamnosyltransferases in the synthesis of their respective surface polysaccharides. Rhamnolipids are glycolipids containing mono- or di- L-rhamnose molecules. Rhamnolipid synthesis occurs by sequential glycosyltransferase reactions involving two distinct rhamnosyltransferase enzymes. In P.aeruginosa, the synthesis of mono-rhamnolipids is catalyzed by rhamnosyltransferase 1, and proceeds by a glycosyltransfer reaction catalyzed by rhamnosyltransferase 2 to yield di-rhamnolipids. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 130619 [Multi-domain] Cd Length: 281 Bit Score: 121.82 E-value: 8.88e-33
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
85-269
3.18e-05
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.
Pssm-ID: 433365 [Multi-domain] Cd Length: 192 Bit Score: 43.86 E-value: 3.18e-05
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
7-241
8.43e-56
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.
Pssm-ID: 133017 [Multi-domain] Cd Length: 237 Bit Score: 180.17 E-value: 8.43e-56
L-rhamnosyltransferase; This model subfamily is comprised of gamma proteobacteria whose ...
10-286
8.88e-33
L-rhamnosyltransferase; This model subfamily is comprised of gamma proteobacteria whose proteins function as L-rhamnosyltransferases in the synthesis of their respective surface polysaccharides. Rhamnolipids are glycolipids containing mono- or di- L-rhamnose molecules. Rhamnolipid synthesis occurs by sequential glycosyltransferase reactions involving two distinct rhamnosyltransferase enzymes. In P.aeruginosa, the synthesis of mono-rhamnolipids is catalyzed by rhamnosyltransferase 1, and proceeds by a glycosyltransfer reaction catalyzed by rhamnosyltransferase 2 to yield di-rhamnolipids. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 130619 [Multi-domain] Cd Length: 281 Bit Score: 121.82 E-value: 8.88e-33
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
8-209
2.06e-12
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 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. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
Pssm-ID: 133029 [Multi-domain] Cd Length: 166 Bit Score: 64.12 E-value: 2.06e-12
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
167-238
2.05e-06
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 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. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
Pssm-ID: 133028 [Multi-domain] Cd Length: 202 Bit Score: 47.63 E-value: 2.05e-06
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
85-269
3.18e-05
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.
Pssm-ID: 433365 [Multi-domain] Cd Length: 192 Bit Score: 43.86 E-value: 3.18e-05
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
8-212
5.50e-04
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have 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. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
Pssm-ID: 133055 [Multi-domain] Cd Length: 202 Bit Score: 40.22 E-value: 5.50e-04
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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