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Literature summary for 2.1.1.294 extracted from
- Substrate recognition by a carbohydrate-binding module in the prototypical ABC transporter for lipopolysaccharide O-antigen from Escherichia coli O9a (2019), J. Biol. Chem., 294, 14978-14990 .
No PubMed abstract available
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| 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 | Escherichia coli |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Klebsiella pneumoniae | 5829 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | Escherichia coli | - |
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 + 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 | Escherichia coli O9a | - |
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 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | J7I4B7 | - |
- |
| Escherichia coli O9a | J7I4B7 | - |
- |
| Klebsiella pneumoniae | - |
- |
- |
| Klebsiella pneumoniae O7 | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | 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 | Escherichia coli | ? | - |
- |
|
| additional information | 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->)] | Klebsiella pneumoniae | ? | - |
- |
|
| additional information | 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 | Escherichia coli O9a | ? | - |
- |
|
| additional information | 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->)] | Klebsiella pneumoniae O7 | ? | - |
- |
|
| 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 | - |
Escherichia coli | 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 + 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 | - |
Escherichia coli O9a | 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 | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| bifunctional methyltransferase/kinase | - |
Klebsiella pneumoniae |
| chain terminator | - |
Escherichia coli |
| chain-terminator enzyme | - |
Escherichia coli |
| dual kinase methyltransferase | - |
Escherichia coli |
| o-antigen chain terminator | - |
Klebsiella pneumoniae |
| o-antigen chain terminator | - |
Escherichia coli |
| WbdD | - |
Klebsiella pneumoniae |
| WbdD | - |
Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| S-adenosyl-L-methionine | - |
Klebsiella pneumoniae | |
| S-adenosyl-L-methionine | - |
Escherichia coli | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Escherichia coli |
| metabolism | the enzyme WbdD takes part in the biosynthesis of lipopolysaccharide O-antigen in Klebsiella pneumoniae strain O7, pathway overview | Klebsiella pneumoniae |
| 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 | Escherichia coli |
| 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 | Klebsiella pneumoniae |
| 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 | Escherichia coli |
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