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Enzyme Nomenclature
Information on EC 2.3.1.210 - dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase
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The expected taxonomic range for this enzyme is: Escherichia coli
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EC NUMBER 
COMMENTARY 
2.3.1.210
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RECOMMENDED NAME
GeneOntology No.
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose = CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-galactose
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:dTDP-4-amino-4,6-dideoxy-alpha-D-galactose N-acetyltransferase
The product, TDP-4-acetamido-4,6-dideoxy-D-galactose, is utilized in the biosynthesis of enterobacterial common antigen (ECA).
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
WecD is a GNAT family member. The GNAT N-acetyltransferase fold is common to a number of enzymes involved in acetylation of histones, aminoglycoside antibiotics, serotonin, and sugars
evolution
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WecD is a GNAT family member. The GNAT N-acetyltransferase fold is common to a number of enzymes involved in acetylation of histones, aminoglycoside antibiotics, serotonin, and sugars
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physiological function
the enzyme is involved in biosynthesis of enterobacterial common antigen, ECA, a polysaccharide found on the outer membrane of virtually all Gram-negative enteric bacteria, that consists of three sugars, N-acetyl-D-glucosamine, N-acetyl-D-mannosaminuronic acid, and 4-acetamido-4,6-dideoxy-D-galactose, organized into trisaccharide repeating units having the sequence ->3)-alpha-D-Fuc4NAc-(1->4)-beta-D-ManNAcA-(1->4)-alpha-D-GlcNAc-(1->
physiological function
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the enzyme is involved in biosynthesis of enterobacterial common antigen, ECA, a polysaccharide found on the outer membrane of virtually all Gram-negative enteric bacteria, that consists of three sugars, N-acetyl-D-glucosamine, N-acetyl-D-mannosaminuronic acid, and 4-acetamido-4,6-dideoxy-D-galactose, organized into trisaccharide repeating units having the sequence ->3)-alpha-D-Fuc4NAc-(1->4)-beta-D-ManNAcA-(1->4)-alpha-D-GlcNAc-(1->
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additional information
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usage of flexible docking to generate a WecD-bound model of the acetyl-CoATDP-fucosamine tetrahedral intermediate, representing the structure during acetyl transfer. that WecD does not possess a residue that directly functions as a catalytic base, although Tyr208 is well positioned to function as a general acid by protonating the thiolate anion of CoA, modeling of TDP-D-Fuc4N:acetyl-CoA transition state bound to WecD, overview. The WecD tetrahedral intermediate results from nucleophilic attack of the 4-amino group of TDP-fucosamine at the acetyl-CoA thioester carbon atom
additional information
usage of flexible docking to generate a WecD-bound model of the acetyl-CoATDP-fucosamine tetrahedral intermediate, representing the structure during acetyl transfer. that WecD does not possess a residue that directly functions as a catalytic base, although Tyr208 is well positioned to function as a general acid by protonating the thiolate anion of CoA, modeling of TDP-D-Fuc4N:acetyl-CoA transition state bound to WecD, overview. The WecD tetrahedral intermediate results from nucleophilic attack of the 4-amino group of TDP-fucosamine at the acetyl-CoA thioester carbon atom
additional information
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usage of flexible docking to generate a WecD-bound model of the acetyl-CoATDP-fucosamine tetrahedral intermediate, representing the structure during acetyl transfer. that WecD does not possess a residue that directly functions as a catalytic base, although Tyr208 is well positioned to function as a general acid by protonating the thiolate anion of CoA, modeling of TDP-D-Fuc4N:acetyl-CoA transition state bound to WecD, overview. The WecD tetrahedral intermediate results from nucleophilic attack of the 4-amino group of TDP-fucosamine at the acetyl-CoA thioester carbon atom
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-galactose
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-galactose
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?
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-galactose
acetyl-CoA binding site structure, overview
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?
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-galactose
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?
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-galactose
acetyl-CoA binding site structure, overview
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?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-galactose
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-galactose
Q8FBQ3
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?
acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose
CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-galactose
Q8FBQ3
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
WecD is a dimeric enzyme, with each monomer adopting the GNAT N-acetyltransferase fold, gel filtration and dynamic light scattering, three-dimensional structure comparison, overview
dimer
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WecD is a dimeric enzyme, with each monomer adopting the GNAT N-acetyltransferase fold, gel filtration and dynamic light scattering, three-dimensional structure comparison, overview
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant N-terminally His6-tagged WecD free and in complex with acetyl-CoA, hanging drop vapour diffusion method, mixing of 0.001 ml of 7.1 mg/ml protein in a 20 mM Tris-Cl, pH 8.0, 450 mM NaCl, and 5 mM DTT, with 0.001 ml reservoir solution aontaining 100 mM Na-acetate, pH 4.5, 10 mM ZnSO4, 20�C, 1 day, X-ray diffraction structure determination and analysis at 1.66-1.95 A resolution
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged WecD from Escherichia coli strain BL21(DE3)
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene wecD, expression of N-terminal fusion protein with a noncleavable His6-tag in Escherichia coli strain BL21(DE3)
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LINKS TO OTHER DATABASES (specific for EC-Number 2.3.1.210)
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