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Information on EC 2.3.1.209 - dTDP-4-amino-4,6-dideoxy-D-glucose acyltransferase
for references in articles please use BRENDA:EC2.3.1.209
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.209 dTDP-4-amino-4,6-dideoxy-D-glucose acyltransferase
IUBMB Comments
The non-activated product, 4-acetamido-4,6-dideoxy-α-D-glucose, is part of the O antigens of Shigella dysenteriae type 7 and Escherichia coli O7.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
dtdp-viosamine acetyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dTDP-viosamine acetyltransferase
VioB
VioB
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose = CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
dTDP-N-acetylviosamine biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:dTDP-4-amino-4,6-dideoxy-alpha-D-glucose N-acetyltransferase
The non-activated product, 4-acetamido-4,6-dideoxy-alpha-D-glucose, is part of the O antigens of Shigella dysenteriae type 7 and Escherichia coli O7.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose
Substrates: -
Products: -
Products: -
?
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose
Substrates: -
Products: product identificatin by capillary electrophoresis, electrospray, ionization-mass spectrometry, and NMR spectroscopy, overview
Products: product identificatin by capillary electrophoresis, electrospray, ionization-mass spectrometry, and NMR spectroscopy, overview
?
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose
Substrates: -
Products: -
Products: -
?
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose
Substrates: -
Products: product identificatin by capillary electrophoresis, electrospray, ionization-mass spectrometry, and NMR spectroscopy, overview
Products: product identificatin by capillary electrophoresis, electrospray, ionization-mass spectrometry, and NMR spectroscopy, overview
?
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose
Substrates: -
Products: -
Products: -
?
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose
Substrates: i.e. dTDP-viosamine
Products: i.e. dTDP-N-acetylviosamine
Products: i.e. dTDP-N-acetylviosamine
?
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose
Substrates: -
Products: -
Products: -
?
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose
Substrates: i.e. dTDP-viosamine
Products: i.e. dTDP-N-acetylviosamine
Products: i.e. dTDP-N-acetylviosamine
?
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose
-
Substrates: -
Products: product identification by capillary electrophoresis, electrospray, ionization-mass spectrometry, and NMR spectroscopy, overview
Products: product identification by capillary electrophoresis, electrospray, ionization-mass spectrometry, and NMR spectroscopy, overview
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose
Substrates: -
Products: -
Products: -
?
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose
Substrates: -
Products: -
Products: -
?
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose
Substrates: -
Products: -
Products: -
?
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose
Substrates: -
Products: -
Products: -
?
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
no effect by presence of Mg2+, Ca2+, Mn2+, and Co2+or EDTA on enzyne activity, the enzyme is divalent cation-independent
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.142
dTDP-4-amino-4,6-dideoxy-alpha-D-glucose
pH 7.4, 37°C, recombinant His-tagged enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
155.3
dTDP-4-amino-4,6-dideoxy-alpha-D-glucose
pH 7.4, 37°C, recombinant His-tagged enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
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
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
-
physiological function
-
the O antigens of Shigella dysenteriae type 7 contains 4-(N-acetylglycyl)amino-4,6-dideoxy-D-glucose, i.e. D-Qui4NGlyAc
physiological function
the O antigens of Escherichia coli O7 contains 4-acetamido-4,6-dideoxy-D-glucose, i.e. D-Qui4NAc
physiological function
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
-
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
-
additional information
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
-
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
-
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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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). VIOB_ECOLX
192
0
20695
Swiss-Prot
other Location (Reliability: 4)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of a DELTAvioB deletion mutant strain
additional information
-
construction of a DELTAvioB deletion mutant strain
additional information
-
construction of a DELTAvioB deletion mutant strain
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
from strain G1112, DNA and amino acid sequence determination and analysis, overexpression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene vioB, DNA and amino acid sequence determination and analysis
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
drug development
-
the enzyme might be a valuable source for the production of dTDP-D-Qui4N and dTDP-D-Qui4NAc, which are potentially useful in the pharmaceutical industry for drug development
drug development
the enzyme might be a valuable source for the production of dTDP-D-Qui4N and dTDP-D-Qui4NAc, which are potentially useful in the pharmaceutical industry for drug development
drug development
-
the enzyme might be a valuable source for the production of dTDP-D-Qui4N and dTDP-D-Qui4NAc, which are potentially useful in the pharmaceutical industry for drug development
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, Y.; Xu, Y.; Perepelov, A.V.; Qi, Y.; Knirel, Y.A.; Wang, L.; Feng, L.
Biochemical characterization of dTDP-D-Qui4N and dTDP-D-Qui4NAc biosynthetic pathways in Shigella dysenteriae type 7 and Escherichia coli O7
J. Bacteriol.
189
8626-8635
2007
Escherichia coli (Q9XCW3), Escherichia coli O7 (Q9XCW3), Shigella dysenteriae
brenda
Nguyen, L.C.; Yamamoto, M.; Ohnishi-Kameyama, M.; Andi, S.; Taguchi, F.; Iwaki, M.; Yoshida, M.; Ishii, T.; Konishi, T.; Tsunemi, K.; Ichinose, Y.
Genetic analysis of genes involved in synthesis of modified 4-amino-4,6-dideoxyglucose in flagellin of Pseudomonas syringae pv. tabaci
Mol. Genet. Genomics
282
595-605
2009
Pseudomonas syringae (C4B8D3), Pseudomonas syringae, Pseudomonas syringae 6605 (C4B8D3)
brenda
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