2.3.1.209: dTDP-4-amino-4,6-dideoxy-D-glucose acyltransferase
This is an abbreviated version!
For detailed information about dTDP-4-amino-4,6-dideoxy-D-glucose acyltransferase, go to the full flat file.
Reaction
Synonyms
dTDP-viosamine acetyltransferase, VioB
ECTree
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General Information
General Information on EC 2.3.1.209 - dTDP-4-amino-4,6-dideoxy-D-glucose acyltransferase
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metabolism
physiological function
additional information
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dTDP-D-Qui4N is synthesized from alpha-D-glucose-1-phosphate in three reaction steps catalyzed by glucose-1-phosphate thymidyltransferase (RmlA), dTDP-D-glucose 4,6-dehydratase (RmlB), and dTDP-4-keto-6-deoxy-D-glucose aminotransferase (VioA). An additional acetyltransferase (VioB) catalyzes the conversion of dTDP-D-Qui4N into dTDP-D-Qui4NAc, biosynthetic pathway, overview
metabolism
dTDP-D-Qui4N is synthesized from alpha-D-glucose-1-phosphate in three reaction steps catalyzed by glucose-1-phosphate thymidyltransferase (RmlA), dTDP-D-glucose 4,6-dehydratase (RmlB), and dTDP-4-keto-6-deoxy-D-glucose aminotransferase (VioA). An additional acetyltransferase (VioB) catalyzes the conversion of dTDP-D-Qui4N into dTDP-D-Qui4NAc, biosynthetic pathway, overview
metabolism
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dTDP-D-Qui4N is synthesized from alpha-D-glucose-1-phosphate in three reaction steps catalyzed by glucose-1-phosphate thymidyltransferase (RmlA), dTDP-D-glucose 4,6-dehydratase (RmlB), and dTDP-4-keto-6-deoxy-D-glucose aminotransferase (VioA). An additional acetyltransferase (VioB) catalyzes the conversion of dTDP-D-Qui4N into dTDP-D-Qui4NAc, biosynthetic pathway, overview
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glycosylation of Xagellin contributes to swimming and swarming motilities, adhesion ability, and consequently virulence with glycan structure at position Ser 201 harboring two L-rhamnoses and one modified 4-amino-4,6-dideoxyglucose, i.e. viosamine. Genes vioA, vioB, and vioT are essential for glycosylation of flagellin, and accordingly are required for bacterial virulence, e.g. on Nicotiana tabacum
physiological function
the O antigens of Escherichia coli O7 contains 4-acetamido-4,6-dideoxy-D-glucose, i.e. D-Qui4NAc
physiological function
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the O antigens of Shigella dysenteriae type 7 contains 4-(N-acetylglycyl)amino-4,6-dideoxy-D-glucose, i.e. D-Qui4NGlyAc
physiological function
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glycosylation of Xagellin contributes to swimming and swarming motilities, adhesion ability, and consequently virulence with glycan structure at position Ser 201 harboring two L-rhamnoses and one modified 4-amino-4,6-dideoxyglucose, i.e. viosamine. Genes vioA, vioB, and vioT are essential for glycosylation of flagellin, and accordingly are required for bacterial virulence, e.g. on Nicotiana tabacum
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physiological function
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the O antigens of Escherichia coli O7 contains 4-acetamido-4,6-dideoxy-D-glucose, i.e. D-Qui4NAc
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a vioB deletion mutant shows affected swimming and swarming motilities, adhesion ability, and virulence, phenotype, overview. Flagellins from DELTAvioA, DELTAvioB, and DELTAvioT mutants contain no viosamine residues but rhamnose chains of mixed lengths
additional information
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a vioB deletion mutant shows affected swimming and swarming motilities, adhesion ability, and virulence, phenotype, overview. Flagellins from DELTAvioA, DELTAvioB, and DELTAvioT mutants contain no viosamine residues but rhamnose chains of mixed lengths
additional information
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a vioB deletion mutant shows affected swimming and swarming motilities, adhesion ability, and virulence, phenotype, overview. Flagellins from DELTAvioA, DELTAvioB, and DELTAvioT mutants contain no viosamine residues but rhamnose chains of mixed lengths
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