glycosyltransferase family 25 protein may be involved in lipopolysaccharide (LPS) biosynthesis, facilitating the transfer of one of a variety of sugars onto a growing LPS chain
Glycosyltransferase family 25 [lipooligosaccharide (LOS) biosynthesis protein] is a family of ...
221-406
1.69e-42
Glycosyltransferase family 25 [lipooligosaccharide (LOS) biosynthesis protein] is a family of glycosyltransferases involved in LOS biosynthesis. The members include the beta(1,4) galactosyltransferases: Lgt2 of Moraxella catarrhalis, LgtB and LgtE of Neisseria gonorrhoeae and Lic2A of Haemophilus influenzae. M. catarrhalis Lgt2 catalyzes the addition of galactose (Gal) to the growing chain of LOS on the cell surface. N. gonorrhoeae LgtB and LgtE link Gal-beta(1,4) to GlcNAc (N-acetylglucosamine) and Glc (glucose), respectively. The genes encoding LgtB and LgtE are two genes of a five gene locus involved in the synthesis of gonococcal LOS. LgtE is believed to perform the first step in LOS biosynthesis.
The actual alignment was detected with superfamily member pfam01755:
Pssm-ID: 470150 Cd Length: 200 Bit Score: 149.90 E-value: 1.69e-42
Glycosyltransferase family 25 (LPS biosynthesis protein); Members of this family belong to ...
221-406
1.69e-42
Glycosyltransferase family 25 (LPS biosynthesis protein); Members of this family belong to Glycosyltransferase family 25 This is a family of glycosyltransferases involved in lipopolysaccharide (LPS) biosynthesis. These enzymes catalyze the transfer of various sugars onto the growing LPS chain during its biosynthesis.
Pssm-ID: 366794 Cd Length: 200 Bit Score: 149.90 E-value: 1.69e-42
Glycosyltransferase family 25 [lipooligosaccharide (LOS) biosynthesis protein] is a family of ...
242-406
2.13e-27
Glycosyltransferase family 25 [lipooligosaccharide (LOS) biosynthesis protein] is a family of glycosyltransferases involved in LOS biosynthesis. The members include the beta(1,4) galactosyltransferases: Lgt2 of Moraxella catarrhalis, LgtB and LgtE of Neisseria gonorrhoeae and Lic2A of Haemophilus influenzae. M. catarrhalis Lgt2 catalyzes the addition of galactose (Gal) to the growing chain of LOS on the cell surface. N. gonorrhoeae LgtB and LgtE link Gal-beta(1,4) to GlcNAc (N-acetylglucosamine) and Glc (glucose), respectively. The genes encoding LgtB and LgtE are two genes of a five gene locus involved in the synthesis of gonococcal LOS. LgtE is believed to perform the first step in LOS biosynthesis.
Pssm-ID: 133474 Cd Length: 128 Bit Score: 106.53 E-value: 2.13e-27
Glycosyltransferase family 25 (LPS biosynthesis protein); Members of this family belong to ...
221-406
1.69e-42
Glycosyltransferase family 25 (LPS biosynthesis protein); Members of this family belong to Glycosyltransferase family 25 This is a family of glycosyltransferases involved in lipopolysaccharide (LPS) biosynthesis. These enzymes catalyze the transfer of various sugars onto the growing LPS chain during its biosynthesis.
Pssm-ID: 366794 Cd Length: 200 Bit Score: 149.90 E-value: 1.69e-42
Glycosyltransferase family 25 [lipooligosaccharide (LOS) biosynthesis protein] is a family of ...
242-406
2.13e-27
Glycosyltransferase family 25 [lipooligosaccharide (LOS) biosynthesis protein] is a family of glycosyltransferases involved in LOS biosynthesis. The members include the beta(1,4) galactosyltransferases: Lgt2 of Moraxella catarrhalis, LgtB and LgtE of Neisseria gonorrhoeae and Lic2A of Haemophilus influenzae. M. catarrhalis Lgt2 catalyzes the addition of galactose (Gal) to the growing chain of LOS on the cell surface. N. gonorrhoeae LgtB and LgtE link Gal-beta(1,4) to GlcNAc (N-acetylglucosamine) and Glc (glucose), respectively. The genes encoding LgtB and LgtE are two genes of a five gene locus involved in the synthesis of gonococcal LOS. LgtE is believed to perform the first step in LOS biosynthesis.
Pssm-ID: 133474 Cd Length: 128 Bit Score: 106.53 E-value: 2.13e-27
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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