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Information on EC 2.7.1.181 - polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase
for references in articles please use BRENDA:EC2.7.1.181
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.1 Phosphotransferases with an alcohol group as acceptor
2.7.1.181 polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase
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 methylation of 3-phospho-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 2.1.1.294, 3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase).
The expected taxonomic range for this enzyme is: Escherichia coli
Reaction Schemes
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Synonyms
wbdd kinase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
WbdD
WbdDO9a
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + 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 = ADP + 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
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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
ATP: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-phosphotransferase
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 methylation of 3-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 (cf. EC 2.1.1.294, 3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase).
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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
ATP + 8-azidooctyl alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man
ADP + 8-azidooctyl 3-O-phospho-alpha-D-mannopyranosyl-(1->2)-alpha-D-mannopyranosyl-(1->3)-alpha-D-mannopyranosyl-(1->3)-alpha-D-mannopyranoside
ATP + 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
ADP + 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
ATP + 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
ADP + 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
ATP + 2-alpha-D-mannosyl-D-mannose
ADP + 3-O-phospho-2-alpha-D-mannosyl-D-mannose
Substrates: -
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ATP + 2-alpha-D-mannosyl-D-mannose
ADP + 3-O-phospho-2-alpha-D-mannosyl-D-mannose
Substrates: -
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?
ATP + 8-azidooctyl alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man
ADP + 8-azidooctyl 3-O-phospho-alpha-D-mannopyranosyl-(1->2)-alpha-D-mannopyranosyl-(1->3)-alpha-D-mannopyranosyl-(1->3)-alpha-D-mannopyranoside
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Substrates: the substrate is an an 8-azidooctyl glycoside derivatives of the Escherichia coli serotype O9a O-chain repeating unit. WbdD shows dual kinase and methyltransferase activity
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ATP + 8-azidooctyl alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man
ADP + 8-azidooctyl 3-O-phospho-alpha-D-mannopyranosyl-(1->2)-alpha-D-mannopyranosyl-(1->3)-alpha-D-mannopyranosyl-(1->3)-alpha-D-mannopyranoside
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Substrates: the substrate is an an 8-azidooctyl glycoside derivatives of the Escherichia coli serotype O9a O-chain repeating unit. WbdD shows dual kinase and methyltransferase activity
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ATP + 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
ADP + 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
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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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ATP + 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
ADP + 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
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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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ATP + 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
ADP + 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
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Substrates: the phosphorylation of the O9a O-polysaccharide is a prerequisite for methylation
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ATP + 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
ADP + 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
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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
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ATP + 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
ADP + 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
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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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ATP + 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
ADP + 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
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Substrates: the phosphorylation of the O9a O-polysaccharide is a prerequisite for methylation
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ATP + 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
ADP + 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
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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: -
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ATP + 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
ADP + 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
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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
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ATP + 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
ADP + 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
Substrates: -
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ATP + 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
ADP + 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
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Substrates: -
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ATP + D-mannose
ADP + 3-O-phospho-D-mannose
Substrates: -
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?
ATP + D-mannose
ADP + 3-O-phospho-D-mannose
Substrates: -
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additional information
?
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Substrates: enzyme WbdD is bifunctional and shows both kinase and methyltransferase activities
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additional information
?
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Substrates: enzyme WbdD is bifunctional and shows both kinase and methyltransferase activities
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
ATP + 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
ADP + 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
ATP + 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
ADP + 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
ATP + 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
ADP + 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
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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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ATP + 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
ADP + 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
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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: -
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ATP + 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
ADP + 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
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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: -
?
ATP + 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
ADP + 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
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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: -
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ATP + 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
ADP + 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
Substrates: -
Products: -
Products: -
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ATP + 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
ADP + 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
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Substrates: -
Products: -
Products: -
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
-
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
malfunction
physiological function
additional information
malfunction
-
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
-
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
-
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
-
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
-
physiological function
-
the glycan of the polymannose O-polysaccharide of Escherichia coli O9a is assembled on a 55-carbon lipid acceptor (undecaprenol 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
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-antigen polysaccharide (O-PS) is exported and incorporated into LPS. Enzyme WbdD is bifunctional and shows both kinase and methyltransferase activities. WbdD mutants reveal that although the kinase activity is solely responsible for chain-length regulation, both activities are essential for CBM recognition and export. Direct interaction between the CBM and the terminal methyl group. 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. Essential to this chain-length regulation strategy is a quality control mechanism on the ABC transporter protein complex, which ensures that only terminated (and chain-regulated) O-PS is exported for assembly on the cell surface. O-PS ABC transporters are composed of homodimers of the transmembrane domain protein (Wzm) and the nucleotide-binding domain protein (Wzt). Wzt possesses a C-terminal CBM, which is specific for its cognate O-PS. Binding of O-PS by the CBM is a prerequisite for transport, and removal or mutation of the CBM abrogates export. WbdD kinase activity is solely responsible for arresting O9a O-PS polymerization. Catalytic mechanism, overview
physiological function
-
the glycan of the polymannose O-polysaccharide of Escherichia coli O9a is assembled on a 55-carbon lipid acceptor (undecaprenol 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
-
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-antigen polysaccharide (O-PS) is exported and incorporated into LPS. Enzyme WbdD is bifunctional and shows both kinase and methyltransferase activities. WbdD mutants reveal that although the kinase activity is solely responsible for chain-length regulation, both activities are essential for CBM recognition and export. Direct interaction between the CBM and the terminal methyl group. 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. Essential to this chain-length regulation strategy is a quality control mechanism on the ABC transporter protein complex, which ensures that only terminated (and chain-regulated) O-PS is exported for assembly on the cell surface. O-PS ABC transporters are composed of homodimers of the transmembrane domain protein (Wzm) and the nucleotide-binding domain protein (Wzt). Wzt possesses a C-terminal CBM, which is specific for its cognate O-PS. Binding of O-PS by the CBM is a prerequisite for transport, and removal or mutation of the CBM abrogates export. WbdD kinase activity is solely responsible for arresting O9a O-PS polymerization. Catalytic mechanism, overview
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additional information
structural requirements for glycan recognition by the CBM, overview
additional information
-
structural requirements for glycan recognition by the CBM, overview
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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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
?
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x * 65500, soluble His6-tagged truncated derivative comprising amino acids 1 to 600 of WbdD
?
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x * 65500, soluble His6-tagged truncated derivative comprising amino acids 1 to 600 of WbdD
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2.2 A resolution structure reveals a bacterial methyltransferase domain joined to a eukaryotic kinase domain. The kinase domain is again fused to an extended C-terminal coiled-coil domain reminiscent of eukaryotic Myotonic Dystrophy Protein Kinase family kinases. Structures of co-complexes with two known eukaryotic protein kinase inhibitors which are potent inhibitors in vitro, but do not show any in vivo activity
crystallization and modeling by molecular-replacement to obtain high-resolution diffraction, and development of methods to control the hydration status
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D350A
88.8% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 95.2% with substrate D-mannose
D351A
0.9% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 1.1% with substrate D-mannose
D351E
4.5% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 1.5% with substrate D-mannose
DELTA398-418
6.7% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 4.7% with substrate D-mannose
E274A
45.4% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 66.6% with substrate D-mannose
R270A
72.8% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 85.7% with substrate D-mannose
W355F
72.4% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 1.9% with substrate D-mannose
W355H
48.7% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 50.7% with substrate D-mannose
Y230F
0.1% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 2.5% with substrate D-mannose
additional information
additional information
uncoupling of WbdD kinase and methyltransferase activities, revealing 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, revealing that although the kinase activity is solely responsible for chain-length regulation, both activities are essential for CBM recognition and export
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
soluble His6-tagged truncated derivative comprising amino acids 1 to 600 of WbdD
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
strategy for improving poor 3.5 A resolution initial phases by density modification and cross-crystal averaging with an additional data set to build a crude model
analysis
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strategy for improving poor 3.5 A resolution initial phases by density modification and cross-crystal averaging with an additional data set to build a crude model
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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
Hagelueken, G.; Huang, H.; Harlos, K.; Clarke, B.R.; Whitfield, C.; Naismith, J.H.
Crystallization, dehydration and experimental phasing of WbdD, a bifunctional kinase and methyltransferase from Escherichia coli O9a
Acta Crystallogr. Sect. D
68
1371-1379
2012
Escherichia coli (J7I4B7), Escherichia coli O9a (J7I4B7)
brenda
Hagelueken, G.; Huang, H.; Clarke, B.R.; Lebl, T.; Whitfield, C.; Naismith, J.H.
Structure of WbdD: a bifunctional kinase and methyltransferase that regulates the chain length of the O antigen in Escherichia coli O9a
Mol. Microbiol.
86
730-742
2012
Escherichia coli (J7I4B7), Escherichia coli O9a (J7I4B7)
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)
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brenda
EXTERNAL LINKS (specific for EC-Number 2.7.1.181)
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