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Information on EC 2.1.1.294 - 3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase
for references in articles please use BRENDA:EC2.1.1.294
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.294 3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase
IUBMB Comments
The enzyme is involved in the biosynthesis of the polymannose O-polysaccharide in the outer leaflet of the membrane of Escherichia coli serotype O9a. O-Polysaccharide structures vary extensively because of differences in the number and type of sugars in the repeat unit. The dual kinase/methylase WbdD also catalyses the preceding phosphorylation of α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol (cf. EC 2.7.1.181, polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase).
The enzyme appears in viruses and cellular organisms
- 2.1.1.294
- polymerases
-
klenow
-
azt-resistant
- transcriptases
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ddhctp
Reaction Schemes
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Synonyms
chain terminator, chain-terminating dual kinase/methyltransferase, chain-terminator enzyme, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bifunctional methyltransferase/kinase
chain terminator
chain-terminator enzyme
dual kinase methyltransferase
methyltransf_25 domain-containing protein
o-antigen chain terminator
WarA
WbdD
WbdD-like O antigen regulator
WbdDO9a
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol = S-adenosyl-L-homocysteine + 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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PATHWAY SOURCE
PATHWAYS
MetaCyc
Escherichia coli serotype O:9 O antigen biosynthesis, Escherichia coli serotype O:9a O antigen biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase
The enzyme is involved in the biosynthesis of the polymannose O-polysaccharide in the outer leaflet of the membrane of Escherichia coli serotype O9a. O-Polysaccharide structures vary extensively because of differences in the number and type of sugars in the repeat unit. The dual kinase/methylase WbdD also catalyses the preceding phosphorylation of alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol (cf. EC 2.7.1.181, polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase).
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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
S-adenosyl-L-methionine + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
S-adenosyl-L-homocysteine + 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
S-adenosyl-L-methionine + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
S-adenosyl-L-homocysteine + 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
S-adenosyl-L-methionine + 8-azidooctyl 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man
S-adenosyl-L-homocysteine + 8-azidooctyl 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man
S-adenosyl-L-methionine + O9a antigenic polysaccharide
S-adenosyl-L-homocysteine + methylated O9a antigenic polysaccharide
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Substrates: -
Products: -
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?
S-adenosyl-L-methionine + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
S-adenosyl-L-homocysteine + 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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Substrates: the phosphorylation of the O9a O-polysaccharide is a prerequisite for methylation. Terminal phosphorylation of the O9a repeating unit prevents polymer elongation by the mannosyltransferases and thus phosphorylation alone is sufficient for chain-length control of the O9a O-polysaccharide
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?
S-adenosyl-L-methionine + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
S-adenosyl-L-homocysteine + 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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Substrates: the chain length of bacterial lipopolysaccharide O antigens is determined in the ATP-binding cassette (ABC) transporter-dependent pathway. Escherichia coli O8 polymannan is synthesized in the cytoplasm, and an ABC transporter exports the nascent polymer across the inner membrane prior to completion of the lipopolysaccharide molecule. The polymannan O antigens has nonreducing terminal methyl groups. The 3-O-methyl group in serotype O8 is transferred from S-adenosylmethionine by the WbdDO8 enzyme, and this modification terminates polymerization. Methyl groups are added to the O9a polymannan in a reaction dependent on preceding phosphorylation. The bifunctional WbdDO9a catalyzes both reactions
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?
S-adenosyl-L-methionine + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
S-adenosyl-L-homocysteine + 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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Substrates: overexpression of WbdD decreases O-polysaccharide chain length. O-Polysaccharide chain length is not reduced by overexpressing the heterologous plasmid encoded WbdD proteins. The WbdD proteins are therefore specific for a given serotype
Products: -
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?
S-adenosyl-L-methionine + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
S-adenosyl-L-homocysteine + 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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Substrates: the phosphorylation of the O9a O-polysaccharide is a prerequisite for methylation. Terminal phosphorylation of the O9a repeating unit prevents polymer elongation by the mannosyltransferases and thus phosphorylation alone is sufficient for chain-length control of the O9a O-polysaccharide
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?
S-adenosyl-L-methionine + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
S-adenosyl-L-homocysteine + 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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Substrates: the chain length of bacterial lipopolysaccharide O antigens is determined in the ATP-binding cassette (ABC) transporter-dependent pathway. Escherichia coli O8 polymannan is synthesized in the cytoplasm, and an ABC transporter exports the nascent polymer across the inner membrane prior to completion of the lipopolysaccharide molecule. The polymannan O antigens has nonreducing terminal methyl groups. The 3-O-methyl group in serotype O8 is transferred from S-adenosylmethionine by the WbdDO8 enzyme, and this modification terminates polymerization. Methyl groups are added to the O9a polymannan in a reaction dependent on preceding phosphorylation. The bifunctional WbdDO9a catalyzes both reactions
Products: -
Products: -
?
S-adenosyl-L-methionine + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
S-adenosyl-L-homocysteine + 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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Substrates: overexpression of WbdD decreases O-polysaccharide chain length. O-Polysaccharide chain length is not reduced by overexpressing the heterologous plasmid encoded WbdD proteins. The WbdD proteins are therefore specific for a given serotype
Products: -
Products: -
?
S-adenosyl-L-methionine + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
S-adenosyl-L-homocysteine + 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Substrates: -
Products: -
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?
S-adenosyl-L-methionine + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
S-adenosyl-L-homocysteine + 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Substrates: -
Products: -
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?
S-adenosyl-L-methionine + 8-azidooctyl 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man
S-adenosyl-L-homocysteine + 8-azidooctyl 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man
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Substrates: artificial substrate. The phosphorylation of the O9a O-polysaccharide is a prerequisite for methylation. Terminal phosphorylation of the O9a repeating unit prevents polymer elongation by the mannosyltransferases and thus phosphorylation alone is sufficient for chain-length control of the O9a O-polysaccharide
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?
S-adenosyl-L-methionine + 8-azidooctyl 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man
S-adenosyl-L-homocysteine + 8-azidooctyl 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man
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Substrates: artificial substrate. The phosphorylation of the O9a O-polysaccharide is a prerequisite for methylation. Terminal phosphorylation of the O9a repeating unit prevents polymer elongation by the mannosyltransferases and thus phosphorylation alone is sufficient for chain-length control of the O9a O-polysaccharide
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?
additional information
?
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Substrates: enzyme WbdD is also active as polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase, EC 2.7.1.181
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?
additional information
?
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Substrates: each carbohydrate-binding module (CBM) can bind the O-antigen polysaccharide (O-PS) only with the native repeat unit, revealing that methylphosphate is essential but not sufficient for substrate recognition and export
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?
additional information
?
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Substrates: each carbohydrate-binding module (CBM) can bind the O-antigen polysaccharide (O-PS) only with the native repeat unit, revealing that methylphosphate is essential but not sufficient for substrate recognition and export
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?
additional information
?
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Substrates: each carbohydrate-binding module (CBM) can bind the O-antigen polysaccharide (O-PS) only with the native repeat unit, revealing that methylphosphate is essential but not sufficient for substrate recognition and export. The O7 O-PS has a tetrasaccharide repeat unit [->2-alpha-L-Rhap-(1->2)-beta-D-Ribf-(1->3)-alpha-L-Rhap-(1->3)-alpha-L-Rhap-(1->)]
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additional information
?
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Substrates: each carbohydrate-binding module (CBM) can bind the O-antigen polysaccharide (O-PS) only with the native repeat unit, revealing that methylphosphate is essential but not sufficient for substrate recognition and export. The O7 O-PS has a tetrasaccharide repeat unit [->2-alpha-L-Rhap-(1->2)-beta-D-Ribf-(1->3)-alpha-L-Rhap-(1->3)-alpha-L-Rhap-(1->)]
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additional information
?
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Substrates: SadC interacts with the methyltransferase WarA, identification of the protein-protein interaction network surrounding the central switch component SadC, overview. Bacterial two-hybrid assay
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additional information
?
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Substrates: SadC interacts with the methyltransferase WarA, identification of the protein-protein interaction network surrounding the central switch component SadC, overview. Bacterial two-hybrid assay
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additional information
?
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Substrates: SadC interacts with the methyltransferase WarA, identification of the protein-protein interaction network surrounding the central switch component SadC, overview. Bacterial two-hybrid assay
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Products: -
?
additional information
?
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Substrates: SadC interacts with the methyltransferase WarA, identification of the protein-protein interaction network surrounding the central switch component SadC, overview. Bacterial two-hybrid assay
Products: -
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?
additional information
?
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Substrates: SadC interacts with the methyltransferase WarA, identification of the protein-protein interaction network surrounding the central switch component SadC, overview. Bacterial two-hybrid assay
Products: -
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?
additional information
?
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Substrates: SadC interacts with the methyltransferase WarA, identification of the protein-protein interaction network surrounding the central switch component SadC, overview. Bacterial two-hybrid assay
Products: -
Products: -
?
additional information
?
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Substrates: SadC interacts with the methyltransferase WarA, identification of the protein-protein interaction network surrounding the central switch component SadC, overview. Bacterial two-hybrid assay
Products: -
Products: -
?
additional information
?
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Substrates: SadC interacts with the methyltransferase WarA, identification of the protein-protein interaction network surrounding the central switch component SadC, overview. Bacterial two-hybrid assay
Products: -
Products: -
?
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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
S-adenosyl-L-methionine + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
S-adenosyl-L-homocysteine + 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
S-adenosyl-L-methionine + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
S-adenosyl-L-homocysteine + 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
S-adenosyl-L-methionine + O9a antigenic polysaccharide
S-adenosyl-L-homocysteine + methylated O9a antigenic polysaccharide
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Substrates: -
Products: -
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?
S-adenosyl-L-methionine + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
S-adenosyl-L-homocysteine + 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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Substrates: the phosphorylation of the O9a O-polysaccharide is a prerequisite for methylation. Terminal phosphorylation of the O9a repeating unit prevents polymer elongation by the mannosyltransferases and thus phosphorylation alone is sufficient for chain-length control of the O9a O-polysaccharide
Products: -
Products: -
?
S-adenosyl-L-methionine + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
S-adenosyl-L-homocysteine + 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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Substrates: the chain length of bacterial lipopolysaccharide O antigens is determined in the ATP-binding cassette (ABC) transporter-dependent pathway. Escherichia coli O8 polymannan is synthesized in the cytoplasm, and an ABC transporter exports the nascent polymer across the inner membrane prior to completion of the lipopolysaccharide molecule. The polymannan O antigens has nonreducing terminal methyl groups. The 3-O-methyl group in serotype O8 is transferred from S-adenosylmethionine by the WbdDO8 enzyme, and this modification terminates polymerization. Methyl groups are added to the O9a polymannan in a reaction dependent on preceding phosphorylation. The bifunctional WbdDO9a catalyzes both reactions
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S-adenosyl-L-methionine + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
S-adenosyl-L-homocysteine + 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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Substrates: the phosphorylation of the O9a O-polysaccharide is a prerequisite for methylation. Terminal phosphorylation of the O9a repeating unit prevents polymer elongation by the mannosyltransferases and thus phosphorylation alone is sufficient for chain-length control of the O9a O-polysaccharide
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S-adenosyl-L-methionine + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
S-adenosyl-L-homocysteine + 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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Substrates: the chain length of bacterial lipopolysaccharide O antigens is determined in the ATP-binding cassette (ABC) transporter-dependent pathway. Escherichia coli O8 polymannan is synthesized in the cytoplasm, and an ABC transporter exports the nascent polymer across the inner membrane prior to completion of the lipopolysaccharide molecule. The polymannan O antigens has nonreducing terminal methyl groups. The 3-O-methyl group in serotype O8 is transferred from S-adenosylmethionine by the WbdDO8 enzyme, and this modification terminates polymerization. Methyl groups are added to the O9a polymannan in a reaction dependent on preceding phosphorylation. The bifunctional WbdDO9a catalyzes both reactions
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S-adenosyl-L-methionine + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
S-adenosyl-L-homocysteine + 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Substrates: -
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S-adenosyl-L-methionine + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
S-adenosyl-L-homocysteine + 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Substrates: -
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additional information
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Substrates: enzyme WbdD is also active as polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase, EC 2.7.1.181
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additional information
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Substrates: SadC interacts with the methyltransferase WarA, identification of the protein-protein interaction network surrounding the central switch component SadC, overview. Bacterial two-hybrid assay
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additional information
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Substrates: SadC interacts with the methyltransferase WarA, identification of the protein-protein interaction network surrounding the central switch component SadC, overview. Bacterial two-hybrid assay
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additional information
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Substrates: SadC interacts with the methyltransferase WarA, identification of the protein-protein interaction network surrounding the central switch component SadC, overview. Bacterial two-hybrid assay
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additional information
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Substrates: SadC interacts with the methyltransferase WarA, identification of the protein-protein interaction network surrounding the central switch component SadC, overview. Bacterial two-hybrid assay
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additional information
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Substrates: SadC interacts with the methyltransferase WarA, identification of the protein-protein interaction network surrounding the central switch component SadC, overview. Bacterial two-hybrid assay
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additional information
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Substrates: SadC interacts with the methyltransferase WarA, identification of the protein-protein interaction network surrounding the central switch component SadC, overview. Bacterial two-hybrid assay
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additional information
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Substrates: SadC interacts with the methyltransferase WarA, identification of the protein-protein interaction network surrounding the central switch component SadC, overview. Bacterial two-hybrid assay
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additional information
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Substrates: SadC interacts with the methyltransferase WarA, identification of the protein-protein interaction network surrounding the central switch component SadC, overview. Bacterial two-hybrid assay
Products: -
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cyclic-di-GMP
WarA binds to cyclic-di-GMP, which potentiates its methyltransferase activity
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Hepatitis C
Canonical 3'-deoxyribonucleotides as a chain terminator for HCV NS5B RNA-dependent RNA polymerase.
Infections
Understanding the molecular mechanism of sequence dependent tenofovir removal by HIV-1 reverse transcriptase: differences in primer binding site versus polypurine tract.
Influenza, Human
The mechanism of action of T-705 as a unique delayed chain terminator on influenza viral polymerase transcription.
Leukemia
Presence of the anti-leukemic nucleotide analog, 2-chloro-2'-deoxyadenosine-5'-monophosphate, in a promoter sequence alters DNA binding of TATA-binding protein (TBP).
Leukemia, Hairy Cell
Presence of the anti-leukemic nucleotide analog, 2-chloro-2'-deoxyadenosine-5'-monophosphate, in a promoter sequence alters DNA binding of TATA-binding protein (TBP).
Melanoma
Antitumor activity of 2',3'-dideoxycytidine nucleotide analog against tumors up-regulating DNA polymerase beta.
Muscular Diseases
Early features of zidovudine-associated myopathy: histopathological findings and clinical correlations.
Neoplasms
Antitumor activity of 2',3'-dideoxycytidine nucleotide analog against tumors up-regulating DNA polymerase beta.
Neoplasms
Mre11 exonuclease activity removes the chain-terminating nucleoside analog gemcitabine from the nascent strand during DNA replication.
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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the WbdD protein is tethered to the membrane via a C-terminal region containing amphipathic helices located between residues 601 and 669
brenda
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the WbdD protein is tethered to the membrane via a C-terminal region containing amphipathic helices located between residues 601 and 669
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brenda
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
evolution
malfunction
metabolism
physiological function
additional information
evolution
WarA and WarB have structural similarities with the bi-functional Escherichia coli LPS O antigen regulator WbdD. A predicted three-dimensional model is generated with a very high confidence on the Escherichia coli serotype O9a WbdD protein (19% sequence identity, 69% sequence coverage, 100% confidence)
evolution
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WarA and WarB have structural similarities with the bi-functional Escherichia coli LPS O antigen regulator WbdD. A predicted three-dimensional model is generated with a very high confidence on the Escherichia coli serotype O9a WbdD protein (19% sequence identity, 69% sequence coverage, 100% confidence)
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evolution
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WarA and WarB have structural similarities with the bi-functional Escherichia coli LPS O antigen regulator WbdD. A predicted three-dimensional model is generated with a very high confidence on the Escherichia coli serotype O9a WbdD protein (19% sequence identity, 69% sequence coverage, 100% confidence)
-
evolution
-
WarA and WarB have structural similarities with the bi-functional Escherichia coli LPS O antigen regulator WbdD. A predicted three-dimensional model is generated with a very high confidence on the Escherichia coli serotype O9a WbdD protein (19% sequence identity, 69% sequence coverage, 100% confidence)
-
evolution
-
WarA and WarB have structural similarities with the bi-functional Escherichia coli LPS O antigen regulator WbdD. A predicted three-dimensional model is generated with a very high confidence on the Escherichia coli serotype O9a WbdD protein (19% sequence identity, 69% sequence coverage, 100% confidence)
-
evolution
-
WarA and WarB have structural similarities with the bi-functional Escherichia coli LPS O antigen regulator WbdD. A predicted three-dimensional model is generated with a very high confidence on the Escherichia coli serotype O9a WbdD protein (19% sequence identity, 69% sequence coverage, 100% confidence)
-
evolution
-
WarA and WarB have structural similarities with the bi-functional Escherichia coli LPS O antigen regulator WbdD. A predicted three-dimensional model is generated with a very high confidence on the Escherichia coli serotype O9a WbdD protein (19% sequence identity, 69% sequence coverage, 100% confidence)
-
evolution
-
WarA and WarB have structural similarities with the bi-functional Escherichia coli LPS O antigen regulator WbdD. A predicted three-dimensional model is generated with a very high confidence on the Escherichia coli serotype O9a WbdD protein (19% sequence identity, 69% sequence coverage, 100% confidence)
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malfunction
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membrane preparations from a wbdD mutant have severely diminished mannosyltransferase activity in vitro, and no significant amounts of the WbdA protein are targeted to the membrane fraction. Expression of a polypeptide comprising the WbdD C-terminal region is sufficient to restore both proper localization of WbdA and mannosyltransferase activity
malfunction
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construction of a chromosomal wbdDO9a::aacC1 mutation by allelic exchange. Membranes of the mutant are still able to synthesize O9a polymannan in vitro, although the chain length is increased relative to that made by the parent
malfunction
The immune response to Pseudomonas aeruginosa in a Pseudomonas-zebrafish hindbrain infection model shows that deletion of warA or sadC does not reduce bacterial load. A phenotype of significantly increased neutrophil recruitment is observed for a warA deletion mutant. Infection with a warA mutant also induces TNF-alpha mRNA levels significantly higher than wild-type infected larvae
malfunction
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membrane preparations from a wbdD mutant have severely diminished mannosyltransferase activity in vitro, and no significant amounts of the WbdA protein are targeted to the membrane fraction. Expression of a polypeptide comprising the WbdD C-terminal region is sufficient to restore both proper localization of WbdA and mannosyltransferase activity
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malfunction
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construction of a chromosomal wbdDO9a::aacC1 mutation by allelic exchange. Membranes of the mutant are still able to synthesize O9a polymannan in vitro, although the chain length is increased relative to that made by the parent
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malfunction
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The immune response to Pseudomonas aeruginosa in a Pseudomonas-zebrafish hindbrain infection model shows that deletion of warA or sadC does not reduce bacterial load. A phenotype of significantly increased neutrophil recruitment is observed for a warA deletion mutant. Infection with a warA mutant also induces TNF-alpha mRNA levels significantly higher than wild-type infected larvae
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malfunction
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The immune response to Pseudomonas aeruginosa in a Pseudomonas-zebrafish hindbrain infection model shows that deletion of warA or sadC does not reduce bacterial load. A phenotype of significantly increased neutrophil recruitment is observed for a warA deletion mutant. Infection with a warA mutant also induces TNF-alpha mRNA levels significantly higher than wild-type infected larvae
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malfunction
-
The immune response to Pseudomonas aeruginosa in a Pseudomonas-zebrafish hindbrain infection model shows that deletion of warA or sadC does not reduce bacterial load. A phenotype of significantly increased neutrophil recruitment is observed for a warA deletion mutant. Infection with a warA mutant also induces TNF-alpha mRNA levels significantly higher than wild-type infected larvae
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malfunction
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The immune response to Pseudomonas aeruginosa in a Pseudomonas-zebrafish hindbrain infection model shows that deletion of warA or sadC does not reduce bacterial load. A phenotype of significantly increased neutrophil recruitment is observed for a warA deletion mutant. Infection with a warA mutant also induces TNF-alpha mRNA levels significantly higher than wild-type infected larvae
-
malfunction
-
The immune response to Pseudomonas aeruginosa in a Pseudomonas-zebrafish hindbrain infection model shows that deletion of warA or sadC does not reduce bacterial load. A phenotype of significantly increased neutrophil recruitment is observed for a warA deletion mutant. Infection with a warA mutant also induces TNF-alpha mRNA levels significantly higher than wild-type infected larvae
-
malfunction
-
The immune response to Pseudomonas aeruginosa in a Pseudomonas-zebrafish hindbrain infection model shows that deletion of warA or sadC does not reduce bacterial load. A phenotype of significantly increased neutrophil recruitment is observed for a warA deletion mutant. Infection with a warA mutant also induces TNF-alpha mRNA levels significantly higher than wild-type infected larvae
-
malfunction
-
The immune response to Pseudomonas aeruginosa in a Pseudomonas-zebrafish hindbrain infection model shows that deletion of warA or sadC does not reduce bacterial load. A phenotype of significantly increased neutrophil recruitment is observed for a warA deletion mutant. Infection with a warA mutant also induces TNF-alpha mRNA levels significantly higher than wild-type infected larvae
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metabolism
the enzyme WbdD takes part in the biosynthesis of lipopolysaccharide O-antigen in Escherichia coli strain O9a, genetic organization, LPS structure, and pathway, overview. Model for export of lipopolysaccharide (LPS) O-antigen polysaccharide (O-PS) via ABC transporters. In O9a biosynthesis, the chain-terminator enzyme WbdD caps the nonreducing end of the glycan with a methylphosphate moiety and thereby establishes chain-length distribution. A carbohydrate-binding module (CBM) in the ABC transporter recognizes terminated glycans, ensuring that only mature O-PS is exported and incorporated into LPS. Each CBM can bind the O-PS only with the native repeat unit, revealing that methylphosphate is essential but not sufficient for substrate recognition and export
metabolism
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the enzyme WbdD takes part in the biosynthesis of lipopolysaccharide O-antigen in Klebsiella pneumoniae strain O7, pathway overview
metabolism
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the enzyme WbdD takes part in the biosynthesis of lipopolysaccharide O-antigen in Escherichia coli strain O9a, genetic organization, LPS structure, and pathway, overview. Model for export of lipopolysaccharide (LPS) O-antigen polysaccharide (O-PS) via ABC transporters. In O9a biosynthesis, the chain-terminator enzyme WbdD caps the nonreducing end of the glycan with a methylphosphate moiety and thereby establishes chain-length distribution. A carbohydrate-binding module (CBM) in the ABC transporter recognizes terminated glycans, ensuring that only mature O-PS is exported and incorporated into LPS. Each CBM can bind the O-PS only with the native repeat unit, revealing that methylphosphate is essential but not sufficient for substrate recognition and export
-
metabolism
-
the enzyme WbdD takes part in the biosynthesis of lipopolysaccharide O-antigen in Klebsiella pneumoniae strain O7, pathway overview
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physiological function
-
the glycan of the polymannose O-polysaccharide of Escherichia coli O9a is assembled on a 55-carbon lipid acceptor (undecaprenyl phosphate) in the inner (cytoplasmic) membrane. Chain extension is mediated by three mannosyltransferases, designated WbdCBA, and occurs by the addition of mannose residues to the non-reducing terminus of the glycan. The chain length of the O9a O-polysaccharide is controlled by the activity of the WbdD protein by addition of methylphosphate to the non-reducing terminus
physiological function
-
WbdD controls polymerization reaction in biosynthesis of the O-polysaccharide by coordinating the correct membrane association required for activity of one of the critical mannosyltransferases, WbdA. Identification of regions in the C terminus of WbdD that contribute to the interaction
physiological function
-
the WbdD proteins control the chain length of the Escherichia coli O9a polymannan by modifying the nonreducing end of nascent undecaprenol diphosphate-linked polymer. Overexpression of WbdD decreases O-polysaccharide chain length. WbdD activity coordinates polymannan chain termination with export across the inner membrane
physiological function
-
In Escherichia coli O9a, the peripheral membrane protein WbdD terminates polymerization by adding a methyl phosphate to the non-reducing end of the nascent O9a polymer. The O9a system is a representative of the widespread ATP-binding cassette transporter-dependent assembly pathway. This terminal modification is required for recognition and export of the completed O-PS across the cytoplasmic membrane by its cognate ATP-binding cassette transporter. The recognition event is mediated by the nucleotide-binding domain polypeptide of the transporter, which possesses a serotype-specific carbohydrate-binding module that only binds terminated O-PS chains. The WbdD terminator plays an additional pivotal structural role in recruiting WbdA to the membrane. The stoichiometry of WbdA:WbdD in active complexes is a critical factor in establishing the chain length distribution of the resulting glycans. The size of the O9a polysaccharide is determined by the chain-terminating dual kinase/methyltransferase (WbdD) that is tethered to the membrane and recruits polymerase/glycosyltransferase WbdA into an active enzyme complex by protein-protein interactions. Identification via bacterial two-hybrid analysis of a surface-exposed alpha-helix in the C-terminal mannosyltransferase domain of WbdA as the site of interaction with WbdD, the C-terminal domain was unable to interact with WbdD in the absence of its N-terminal partner. The WbdD protein orchestrates critical localization and coordination of activities involved in chain extension and termination. Complex domain interactions are needed to position the polymerase components appropriately for assembly into a functional complex located at the cytoplasmic membrane. WbdD is therefore a central player in a sophisticated quality control system that dictates the distribution of chain lengths and marks those chains with a terminal export tag
physiological function
the more intricate Escherichia coli serotype O9a O-antigen polysaccharide (O-PS) assembly system incorporates an additional mechanism that imposes a stricter level of control over chain length. This requires the installation of a chain-terminating residue that creates an export signal recognized by a carbohydrate-binding module (CBM) attached to the ABC transporter. In this system, polymerization and export can be temporally uncoupled in vitro. In O9a biosynthesis, a chain-terminator enzyme, WbdD, caps the nonreducing end of the glycan with a methylphosphate moiety and thereby establishes chain-length distribution. A carbohydrate-binding module (CBM) in the ABC transporter recognizes terminated glycans, ensuring that only mature O-PS is exported and incorporated into LPS. Enzyme WbdD has both kinase and methyltransferase activities. Although the kinase activity is solely responsible for chain-length regulation, both activities are essential for CBM recognition and export. Each CBM can bind the O-PS only with the native repeat unit, revealing that methylphosphate is essential but not sufficient for substrate recognition and export
physiological function
-
the enzyme WbdD takes part in the biosynthesis of lipopolysaccharide O-antigen in Klebsiella pneumoniae strain O7, pathway overview. In the simpler process exhibited by Klebsiella pneumoniae serotype O2a, the O-PS is polymerized to completion within the cytosol by a biosynthetic enzyme complex. The chain-length distribution is controlled by the relative activities of a complex of glycosyltransferase (GT) enzymes and the ABC transporter. The O2a ABC transporter does not possess strict O-PS specificity, and it can export polymers with diverse repeat-unit structures, but polymerization and export are obligatorily coupled
physiological function
WarA influences Pseudomonas aeruginosa O antigen modal distribution and interacts with the LPS biogenesis machinery. LPS is known to modulate the immune response in the host, WarA is involved in the ability of Pseudomonas aeruginosa to evade detection by the host. Cyclic-di-GMP regulates lipopolysaccharide modification and contributes to Pseudomonas aeruginosa immune evasion. WarA might play a similar functional role as WbdD in regulating chain length and termination of LPS O antigen synthesis. The immune response to Pseudomonas aeruginosa in a Pseudomonas-zebrafish hindbrain infection model shows that deletion of warA or sadC does not reduce bacterial load. The regulation of LPS by SadC and WarA plays a critical role in immune cell evasion during infection
physiological function
-
the glycan of the polymannose O-polysaccharide of Escherichia coli O9a is assembled on a 55-carbon lipid acceptor (undecaprenyl phosphate) in the inner (cytoplasmic) membrane. Chain extension is mediated by three mannosyltransferases, designated WbdCBA, and occurs by the addition of mannose residues to the non-reducing terminus of the glycan. The chain length of the O9a O-polysaccharide is controlled by the activity of the WbdD protein by addition of methylphosphate to the non-reducing terminus
-
physiological function
-
WbdD controls polymerization reaction in biosynthesis of the O-polysaccharide by coordinating the correct membrane association required for activity of one of the critical mannosyltransferases, WbdA. Identification of regions in the C terminus of WbdD that contribute to the interaction
-
physiological function
-
the WbdD proteins control the chain length of the Escherichia coli O9a polymannan by modifying the nonreducing end of nascent undecaprenol diphosphate-linked polymer. Overexpression of WbdD decreases O-polysaccharide chain length. WbdD activity coordinates polymannan chain termination with export across the inner membrane
-
physiological function
-
the more intricate Escherichia coli serotype O9a O-antigen polysaccharide (O-PS) assembly system incorporates an additional mechanism that imposes a stricter level of control over chain length. This requires the installation of a chain-terminating residue that creates an export signal recognized by a carbohydrate-binding module (CBM) attached to the ABC transporter. In this system, polymerization and export can be temporally uncoupled in vitro. In O9a biosynthesis, a chain-terminator enzyme, WbdD, caps the nonreducing end of the glycan with a methylphosphate moiety and thereby establishes chain-length distribution. A carbohydrate-binding module (CBM) in the ABC transporter recognizes terminated glycans, ensuring that only mature O-PS is exported and incorporated into LPS. Enzyme WbdD has both kinase and methyltransferase activities. Although the kinase activity is solely responsible for chain-length regulation, both activities are essential for CBM recognition and export. Each CBM can bind the O-PS only with the native repeat unit, revealing that methylphosphate is essential but not sufficient for substrate recognition and export
-
physiological function
-
WarA influences Pseudomonas aeruginosa O antigen modal distribution and interacts with the LPS biogenesis machinery. LPS is known to modulate the immune response in the host, WarA is involved in the ability of Pseudomonas aeruginosa to evade detection by the host. Cyclic-di-GMP regulates lipopolysaccharide modification and contributes to Pseudomonas aeruginosa immune evasion. WarA might play a similar functional role as WbdD in regulating chain length and termination of LPS O antigen synthesis. The immune response to Pseudomonas aeruginosa in a Pseudomonas-zebrafish hindbrain infection model shows that deletion of warA or sadC does not reduce bacterial load. The regulation of LPS by SadC and WarA plays a critical role in immune cell evasion during infection
-
physiological function
-
WarA influences Pseudomonas aeruginosa O antigen modal distribution and interacts with the LPS biogenesis machinery. LPS is known to modulate the immune response in the host, WarA is involved in the ability of Pseudomonas aeruginosa to evade detection by the host. Cyclic-di-GMP regulates lipopolysaccharide modification and contributes to Pseudomonas aeruginosa immune evasion. WarA might play a similar functional role as WbdD in regulating chain length and termination of LPS O antigen synthesis. The immune response to Pseudomonas aeruginosa in a Pseudomonas-zebrafish hindbrain infection model shows that deletion of warA or sadC does not reduce bacterial load. The regulation of LPS by SadC and WarA plays a critical role in immune cell evasion during infection
-
physiological function
-
WarA influences Pseudomonas aeruginosa O antigen modal distribution and interacts with the LPS biogenesis machinery. LPS is known to modulate the immune response in the host, WarA is involved in the ability of Pseudomonas aeruginosa to evade detection by the host. Cyclic-di-GMP regulates lipopolysaccharide modification and contributes to Pseudomonas aeruginosa immune evasion. WarA might play a similar functional role as WbdD in regulating chain length and termination of LPS O antigen synthesis. The immune response to Pseudomonas aeruginosa in a Pseudomonas-zebrafish hindbrain infection model shows that deletion of warA or sadC does not reduce bacterial load. The regulation of LPS by SadC and WarA plays a critical role in immune cell evasion during infection
-
physiological function
-
WarA influences Pseudomonas aeruginosa O antigen modal distribution and interacts with the LPS biogenesis machinery. LPS is known to modulate the immune response in the host, WarA is involved in the ability of Pseudomonas aeruginosa to evade detection by the host. Cyclic-di-GMP regulates lipopolysaccharide modification and contributes to Pseudomonas aeruginosa immune evasion. WarA might play a similar functional role as WbdD in regulating chain length and termination of LPS O antigen synthesis. The immune response to Pseudomonas aeruginosa in a Pseudomonas-zebrafish hindbrain infection model shows that deletion of warA or sadC does not reduce bacterial load. The regulation of LPS by SadC and WarA plays a critical role in immune cell evasion during infection
-
physiological function
-
WarA influences Pseudomonas aeruginosa O antigen modal distribution and interacts with the LPS biogenesis machinery. LPS is known to modulate the immune response in the host, WarA is involved in the ability of Pseudomonas aeruginosa to evade detection by the host. Cyclic-di-GMP regulates lipopolysaccharide modification and contributes to Pseudomonas aeruginosa immune evasion. WarA might play a similar functional role as WbdD in regulating chain length and termination of LPS O antigen synthesis. The immune response to Pseudomonas aeruginosa in a Pseudomonas-zebrafish hindbrain infection model shows that deletion of warA or sadC does not reduce bacterial load. The regulation of LPS by SadC and WarA plays a critical role in immune cell evasion during infection
-
physiological function
-
WarA influences Pseudomonas aeruginosa O antigen modal distribution and interacts with the LPS biogenesis machinery. LPS is known to modulate the immune response in the host, WarA is involved in the ability of Pseudomonas aeruginosa to evade detection by the host. Cyclic-di-GMP regulates lipopolysaccharide modification and contributes to Pseudomonas aeruginosa immune evasion. WarA might play a similar functional role as WbdD in regulating chain length and termination of LPS O antigen synthesis. The immune response to Pseudomonas aeruginosa in a Pseudomonas-zebrafish hindbrain infection model shows that deletion of warA or sadC does not reduce bacterial load. The regulation of LPS by SadC and WarA plays a critical role in immune cell evasion during infection
-
physiological function
-
WarA influences Pseudomonas aeruginosa O antigen modal distribution and interacts with the LPS biogenesis machinery. LPS is known to modulate the immune response in the host, WarA is involved in the ability of Pseudomonas aeruginosa to evade detection by the host. Cyclic-di-GMP regulates lipopolysaccharide modification and contributes to Pseudomonas aeruginosa immune evasion. WarA might play a similar functional role as WbdD in regulating chain length and termination of LPS O antigen synthesis. The immune response to Pseudomonas aeruginosa in a Pseudomonas-zebrafish hindbrain infection model shows that deletion of warA or sadC does not reduce bacterial load. The regulation of LPS by SadC and WarA plays a critical role in immune cell evasion during infection
-
physiological function
-
the enzyme WbdD takes part in the biosynthesis of lipopolysaccharide O-antigen in Klebsiella pneumoniae strain O7, pathway overview. In the simpler process exhibited by Klebsiella pneumoniae serotype O2a, the O-PS is polymerized to completion within the cytosol by a biosynthetic enzyme complex. The chain-length distribution is controlled by the relative activities of a complex of glycosyltransferase (GT) enzymes and the ABC transporter. The O2a ABC transporter does not possess strict O-PS specificity, and it can export polymers with diverse repeat-unit structures, but polymerization and export are obligatorily coupled
-
additional information
direct interaction between the CBM and the terminal methyl group. The nonreducing terminal modification is the sole contributor to ABC transporter WztO9a-C O-PS recognition
additional information
WarA is a methyltransferase in complex with a putative kinase WarB. WarA binds to cyclic-di-GMP, which potentiates its methyltransferase activity. Bacterial two-hybrid assay
additional information
-
direct interaction between the CBM and the terminal methyl group. The nonreducing terminal modification is the sole contributor to ABC transporter WztO9a-C O-PS recognition
-
additional information
-
WarA is a methyltransferase in complex with a putative kinase WarB. WarA binds to cyclic-di-GMP, which potentiates its methyltransferase activity. Bacterial two-hybrid assay
-
additional information
-
WarA is a methyltransferase in complex with a putative kinase WarB. WarA binds to cyclic-di-GMP, which potentiates its methyltransferase activity. Bacterial two-hybrid assay
-
additional information
-
WarA is a methyltransferase in complex with a putative kinase WarB. WarA binds to cyclic-di-GMP, which potentiates its methyltransferase activity. Bacterial two-hybrid assay
-
additional information
-
WarA is a methyltransferase in complex with a putative kinase WarB. WarA binds to cyclic-di-GMP, which potentiates its methyltransferase activity. Bacterial two-hybrid assay
-
additional information
-
WarA is a methyltransferase in complex with a putative kinase WarB. WarA binds to cyclic-di-GMP, which potentiates its methyltransferase activity. Bacterial two-hybrid assay
-
additional information
-
WarA is a methyltransferase in complex with a putative kinase WarB. WarA binds to cyclic-di-GMP, which potentiates its methyltransferase activity. Bacterial two-hybrid assay
-
additional information
-
WarA is a methyltransferase in complex with a putative kinase WarB. WarA binds to cyclic-di-GMP, which potentiates its methyltransferase activity. Bacterial two-hybrid assay
-
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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). WBDD2_ECOLX
708
0
81571
Swiss-Prot
other Location (Reliability: 1)
Q9HW23_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
227
0
26228
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65500
-
x * 65500, soluble His6-tagged truncated derivative comprising amino acids 1 to 600 of WbdD
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 65500, soluble His6-tagged truncated derivative comprising amino acids 1 to 600 of WbdD
?
-
x * 65500, soluble His6-tagged truncated derivative comprising amino acids 1 to 600 of WbdD
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
uncoupling of WbdD kinase and methyltransferase activities. The WbdD mutants reveal that although the kinase activity is solely responsible for chain-length regulation, both activities are essential for CBM recognition and export
additional information
-
uncoupling of WbdD kinase and methyltransferase activities. The WbdD mutants reveal that although the kinase activity is solely responsible for chain-length regulation, both activities are essential for CBM recognition and export
-
additional information
generation of a gene replacement mutants, deletion of the PA4379 (warA) gene in the Pseudomonas aeruginosa PAK chromosome
additional information
-
generation of a gene replacement mutants, deletion of the PA4379 (warA) gene in the Pseudomonas aeruginosa PAK chromosome
-
additional information
-
generation of a gene replacement mutants, deletion of the PA4379 (warA) gene in the Pseudomonas aeruginosa PAK chromosome
-
additional information
-
generation of a gene replacement mutants, deletion of the PA4379 (warA) gene in the Pseudomonas aeruginosa PAK chromosome
-
additional information
-
generation of a gene replacement mutants, deletion of the PA4379 (warA) gene in the Pseudomonas aeruginosa PAK chromosome
-
additional information
-
generation of a gene replacement mutants, deletion of the PA4379 (warA) gene in the Pseudomonas aeruginosa PAK chromosome
-
additional information
-
generation of a gene replacement mutants, deletion of the PA4379 (warA) gene in the Pseudomonas aeruginosa PAK chromosome
-
additional information
-
generation of a gene replacement mutants, deletion of the PA4379 (warA) gene in the Pseudomonas aeruginosa PAK chromosome
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinat GST-His-tagged wild-type and mutant enzymes from Escherichia coli strain B834(DE3) by nickel affinity chromatography and gel filtration
soluble His6-tagged truncated derivative comprising amino acids 1 to 600 of WbdD
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene warA, quantitative RT-PCR expression analysis, recombinant expression of N-terminally His- or GFP-tagged enzyme, recombinat expression of GST-His-tagged wild-type and mutant enzymes in Escherichia coli strain B834(DE3)
overexpression of WbdD decreases O-polysaccharide chain length. O-polysaccharide chain length is not reduced by overexpressing the heterologous plasmid encoded WbdD proteins. The WbdD proteins are therefore specific for a given serotype
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Clarke, B.R.; Cuthbertson, L.; Whitfield, C.
Nonreducing terminal modifications determine the chain length of polymannose O antigens of Escherichia coli and couple chain termination to polymer export via an ATP-binding cassette transporter
J. Biol. Chem.
279
35709-35718
2004
Escherichia coli, Escherichia coli O9a
brenda
Clarke, B.R.; Greenfield, L.K.; Bouwman, C.; Whitfield, C.
Coordination of polymerization, chain termination, and export in assembly of the Escherichia coli lipopolysaccharide O9a antigen in an ATP-binding cassette transporter-dependent pathway
J. Biol. Chem.
284
30662-30672
2009
Escherichia coli, Escherichia coli O9a
brenda
Clarke, B.R.; Richards, M.R.; Greenfield, L.K.; Hou, D.; Lowary, T.L.; Whitfield, C.
In vitro reconstruction of the chain termination reaction in biosynthesis of the Escherichia coli O9a O-polysaccharide; the chain-length regulator, WbdD, catalyzes the addition of methyl phosphate to the non-reducing terminus of the growing glycan
J. Biol. Chem.
286
41391-41401
2011
Escherichia coli, Escherichia coli O9a
brenda
Liston, S.D.; Clarke, B.R.; Greenfield, L.K.; Richards, M.R.; Lowary, T.L.; Whitfield, C.
Domain interactions control complex formation and polymerase specificity in the biosynthesis of the Escherichia coli O9a antigen
J. Biol. Chem.
290
1075-1085
2015
Escherichia coli
brenda
Mann, E.; Kelly, S.; Al-Abdul-Wahid, M.; Clarke, B.; Ovchinnikova, O.; Liu, B.; Whitfield, C.
Substrate recognition by a carbohydrate-binding module in the prototypical ABC transporter for lipopolysaccharide O-antigen from Escherichia coli O9a
J. Biol. Chem.
294
14978-14990
2019
Escherichia coli (J7I4B7), Klebsiella pneumoniae, Escherichia coli O9a (J7I4B7), Klebsiella pneumoniae O7
-
brenda
McCarthy, R.; Mazon-Moya, M.; Moscoso, J.; Hao, Y.; Lam, J.; Bordi, C.; Mostowy, S.; Filloux, A.
Cyclic-di-GMP regulates lipopolysaccharide modification and contributes to Pseudomonas aeruginosa immune evasion
Nat. Microbiol.
2
17027
2017
Pseudomonas aeruginosa (Q9HW23), Pseudomonas aeruginosa ATCC 15692 (Q9HW23), Pseudomonas aeruginosa DSM 22644 (Q9HW23), Pseudomonas aeruginosa CIP 104116 (Q9HW23), Pseudomonas aeruginosa JCM 14847 (Q9HW23), Pseudomonas aeruginosa LMG 12228 (Q9HW23), Pseudomonas aeruginosa 1C (Q9HW23), Pseudomonas aeruginosa PRS 101 (Q9HW23)
brenda
EXTERNAL LINKS (specific for EC-Number 2.1.1.294)
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