lipid-A-disaccharide synthase catalyzes the condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell
lipid-A-disaccharide synthase; Lipid-A precursor biosynthesis producing lipid A disaccharide ...
1-383
0e+00
lipid-A-disaccharide synthase; Lipid-A precursor biosynthesis producing lipid A disaccharide in a condensation reaction. transcribed as part of an operon including lpxA [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
:
Pssm-ID: 129319 [Multi-domain] Cd Length: 385 Bit Score: 630.39 E-value: 0e+00
lipid-A-disaccharide synthase; Lipid-A precursor biosynthesis producing lipid A disaccharide ...
1-383
0e+00
lipid-A-disaccharide synthase; Lipid-A precursor biosynthesis producing lipid A disaccharide in a condensation reaction. transcribed as part of an operon including lpxA [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 129319 [Multi-domain] Cd Length: 385 Bit Score: 630.39 E-value: 0e+00
Lipid A disaccharide synthetase [Cell wall/membrane/envelope biogenesis]; Lipid A disaccharide ...
6-387
0e+00
Lipid A disaccharide synthetase [Cell wall/membrane/envelope biogenesis]; Lipid A disaccharide synthetase is part of the Pathway/BioSystem: Lipid A biosynthesis
Pssm-ID: 440526 Cd Length: 378 Bit Score: 561.22 E-value: 0e+00
Lipid-A-disaccharide synthetase; This is a family of lipid-A-disaccharide synthetases, EC:2.4. ...
8-380
0e+00
Lipid-A-disaccharide synthetase; This is a family of lipid-A-disaccharide synthetases, EC:2.4.2.128. These enzymes catalyze the reaction: UDP-2,3-bis(3-hydroxytetradecanoyl) glucosamine + 2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate <=> UDP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6 -beta-D-2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate. These enzymes catalyze the fist disaccharide step in the synthesis of lipid-A-disaccharide.
Pssm-ID: 397004 Cd Length: 374 Bit Score: 560.52 E-value: 0e+00
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
8-362
9.38e-04
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). 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. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the 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 members of this family are found mainly in certain bacteria and archaea.
Pssm-ID: 340831 [Multi-domain] Cd Length: 366 Bit Score: 40.98 E-value: 9.38e-04
lipid-A-disaccharide synthase; Lipid-A precursor biosynthesis producing lipid A disaccharide ...
1-383
0e+00
lipid-A-disaccharide synthase; Lipid-A precursor biosynthesis producing lipid A disaccharide in a condensation reaction. transcribed as part of an operon including lpxA [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 129319 [Multi-domain] Cd Length: 385 Bit Score: 630.39 E-value: 0e+00
Lipid A disaccharide synthetase [Cell wall/membrane/envelope biogenesis]; Lipid A disaccharide ...
6-387
0e+00
Lipid A disaccharide synthetase [Cell wall/membrane/envelope biogenesis]; Lipid A disaccharide synthetase is part of the Pathway/BioSystem: Lipid A biosynthesis
Pssm-ID: 440526 Cd Length: 378 Bit Score: 561.22 E-value: 0e+00
Lipid-A-disaccharide synthetase; This is a family of lipid-A-disaccharide synthetases, EC:2.4. ...
8-380
0e+00
Lipid-A-disaccharide synthetase; This is a family of lipid-A-disaccharide synthetases, EC:2.4.2.128. These enzymes catalyze the reaction: UDP-2,3-bis(3-hydroxytetradecanoyl) glucosamine + 2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate <=> UDP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6 -beta-D-2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate. These enzymes catalyze the fist disaccharide step in the synthesis of lipid-A-disaccharide.
Pssm-ID: 397004 Cd Length: 374 Bit Score: 560.52 E-value: 0e+00
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
8-362
9.38e-04
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). 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. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the 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 members of this family are found mainly in certain bacteria and archaea.
Pssm-ID: 340831 [Multi-domain] Cd Length: 366 Bit Score: 40.98 E-value: 9.38e-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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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(labeled illustration) Four types of hits can be shown, as available,
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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the domain superfamily to which the specific and non-specific hits belong
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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