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Literature summary for 2.7.1.181 extracted from

  • 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 (2019), J. Biol. Chem., 294, 14978-14990 .
No PubMed abstract available
Search for more literature for 2.7.1.181

Cloned(Commentary)

Cloned (Comment) Organism
gene wbdD, genetic organization Escherichia coli

Protein Variants

Protein Variants Comment Organism
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 Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 Escherichia coli
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 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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 ?
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 Escherichia coli O9a
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 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
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli J7I4B7 serotype O9a
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
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 Escherichia coli 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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 ?
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
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 Escherichia coli O9a 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
-
 ?
additional information enzyme WbdD is bifunctional and shows both kinase and methyltransferase activities Escherichia coli ?
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additional information enzyme WbdD is bifunctional and shows both kinase and methyltransferase activities Escherichia coli O9a ?
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Synonyms

Synonyms Comment Organism
WbdD
-
 Escherichia coli
WbdD kinase
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli

General Information

General Information Comment Organism
additional information structural requirements for glycan recognition by the CBM, overview Escherichia coli
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 Escherichia coli