glycosyltransferase, SP_1767 family; Members of this protein family are putative ...
550-812
1.23e-147
glycosyltransferase, SP_1767 family; Members of this protein family are putative glycosyltransferases. Some members are found close to genes for the accessory secretory (SecA2) system, and are suggested by Partial Phylogenetic Profiling to correlate with SecA2 systems. Glycosylation, therefore, may occur in the cytosol prior to secretion.
:
Pssm-ID: 163440 Cd Length: 265 Bit Score: 433.64 E-value: 1.23e-147
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
3-234
1.55e-71
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.
:
Pssm-ID: 133037 [Multi-domain] Cd Length: 248 Bit Score: 234.80 E-value: 1.55e-71
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
415-524
2.71e-14
glycosyltransferase family 1 and related proteins with GTB topology; 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. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common 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 actual alignment was detected with superfamily member TIGR02919:
Pssm-ID: 471961 Cd Length: 438 Bit Score: 75.82 E-value: 2.71e-14
glycosyltransferase, SP_1767 family; Members of this protein family are putative ...
550-812
1.23e-147
glycosyltransferase, SP_1767 family; Members of this protein family are putative glycosyltransferases. Some members are found close to genes for the accessory secretory (SecA2) system, and are suggested by Partial Phylogenetic Profiling to correlate with SecA2 systems. Glycosylation, therefore, may occur in the cytosol prior to secretion.
Pssm-ID: 163440 Cd Length: 265 Bit Score: 433.64 E-value: 1.23e-147
Glycosyltransferase GT-D fold; This domain is found at the C terminus of proteins such as the ...
568-790
9.30e-100
Glycosyltransferase GT-D fold; This domain is found at the C terminus of proteins such as the probable glycosyltransferase Gly that also contain the glycosyl transferase domain at the N terminus. It is also found N-terminal in numerous putative glycosyltransferases such as GalT1. GalT1 has been shown to catalyze the third step of Fap1 glycosylation. This domain is structurally distinct from all known GT folds of glycosyltransferases and contains a metal binding site. This new glycosyltransferase fold has been named GT-D.
Pssm-ID: 430197 Cd Length: 223 Bit Score: 308.37 E-value: 9.30e-100
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
3-234
1.55e-71
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.
Pssm-ID: 133037 [Multi-domain] Cd Length: 248 Bit Score: 234.80 E-value: 1.55e-71
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
5-234
2.35e-38
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.
Pssm-ID: 279798 [Multi-domain] Cd Length: 252 Bit Score: 143.23 E-value: 2.35e-38
accessory Sec system glycosyltransferase GtfB; Members of this protein family are found only ...
415-524
2.71e-14
accessory Sec system glycosyltransferase GtfB; Members of this protein family are found only in Gram-positive bacteria of the Firmicutes lineage, including several species of Staphylococcus, Streptococcus, and Lactobacillus. [Protein fate, Protein modification and repair]
Pssm-ID: 274351 Cd Length: 438 Bit Score: 75.82 E-value: 2.71e-14
glycosyltransferase, SP_1767 family; Members of this protein family are putative ...
550-812
1.23e-147
glycosyltransferase, SP_1767 family; Members of this protein family are putative glycosyltransferases. Some members are found close to genes for the accessory secretory (SecA2) system, and are suggested by Partial Phylogenetic Profiling to correlate with SecA2 systems. Glycosylation, therefore, may occur in the cytosol prior to secretion.
Pssm-ID: 163440 Cd Length: 265 Bit Score: 433.64 E-value: 1.23e-147
Glycosyltransferase GT-D fold; This domain is found at the C terminus of proteins such as the ...
568-790
9.30e-100
Glycosyltransferase GT-D fold; This domain is found at the C terminus of proteins such as the probable glycosyltransferase Gly that also contain the glycosyl transferase domain at the N terminus. It is also found N-terminal in numerous putative glycosyltransferases such as GalT1. GalT1 has been shown to catalyze the third step of Fap1 glycosylation. This domain is structurally distinct from all known GT folds of glycosyltransferases and contains a metal binding site. This new glycosyltransferase fold has been named GT-D.
Pssm-ID: 430197 Cd Length: 223 Bit Score: 308.37 E-value: 9.30e-100
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
3-234
1.55e-71
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.
Pssm-ID: 133037 [Multi-domain] Cd Length: 248 Bit Score: 234.80 E-value: 1.55e-71
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
5-234
2.35e-38
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.
Pssm-ID: 279798 [Multi-domain] Cd Length: 252 Bit Score: 143.23 E-value: 2.35e-38
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
5-234
2.59e-20
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis and glycogen synthesis; Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. GT-8 comprises enzymes with a number of known activities: lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase, and N-acetylglucosaminyltransferase. GT-8 enzymes contains a conserved DXD motif which is essential in the coordination of a catalytic divalent cation, most commonly Mn2+.
Pssm-ID: 132996 [Multi-domain] Cd Length: 246 Bit Score: 90.96 E-value: 2.59e-20
accessory Sec system glycosyltransferase GtfB; Members of this protein family are found only ...
415-524
2.71e-14
accessory Sec system glycosyltransferase GtfB; Members of this protein family are found only in Gram-positive bacteria of the Firmicutes lineage, including several species of Staphylococcus, Streptococcus, and Lactobacillus. [Protein fate, Protein modification and repair]
Pssm-ID: 274351 Cd Length: 438 Bit Score: 75.82 E-value: 2.71e-14
GT8_like_1 represents a subfamily of GT8 with unknown function; A subfamily of ...
19-250
4.45e-13
GT8_like_1 represents a subfamily of GT8 with unknown function; A subfamily of glycosyltransferase family 8 with unknown function: Glycosyltransferase family 8 comprises enzymes with a number of known activities; lipopolysaccharide galactosyltransferase lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase and inositol 1-alpha-galactosyltransferase. It is classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed.
Pssm-ID: 133051 [Multi-domain] Cd Length: 257 Bit Score: 70.11 E-value: 4.45e-13
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
49-251
1.04e-08
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.
Pssm-ID: 133018 [Multi-domain] Cd Length: 240 Bit Score: 56.89 E-value: 1.04e-08
LARGE catalytic domain has closest homology to GT8 glycosyltransferase involved in ...
5-232
2.78e-03
LARGE catalytic domain has closest homology to GT8 glycosyltransferase involved in lipooligosaccharide synthesis; The catalytic domain of LARGE is a putative glycosyltransferase. Mutations of LARGE in mouse and human cause dystroglycanopathies, a disease associated with hypoglycosylation of the membrane protein alpha-dystroglycan (alpha-DG) and consequent loss of extracellular ligand binding. LARGE needs to both physically interact with alpha-dystroglycan and function as a glycosyltransferase in order to stimulate alpha-dystroglycan hyperglycosylation. LARGE localizes to the Golgi apparatus and contains three conserved DxD motifs. While two of the motifs are indispensible for glycosylation function, one is important for localization of th eenzyme. LARGE was originally named because it covers approximately large trunck of genomic DNA, more than 600bp long. The predicted protein structure contains an N-terminal cytoplasmic domain, a transmembrane region, a coiled-coil motif, and two putative catalytic domains. This catalytic domain has closest homology to GT8 glycosyltransferase involved in lipooligosaccharide synthesis.
Pssm-ID: 133053 Cd Length: 280 Bit Score: 40.54 E-value: 2.78e-03
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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