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CATH Classification

Domain Context

CATH Clusters

Superfamily Phosphorylase Kinase; domain 1
Functional Family

Enzyme Information

2.1.1.294
3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase.
based on mapping to UniProt J7I4B7
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.
-!- 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 catalyzes 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).
2.7.1.181
Polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase.
based on mapping to UniProt J7I4B7
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.
-!- 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 catalyzes 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).

UniProtKB Entries (1)

J7I4B7
WBDD_ECOLX
Escherichia coli
O-antigen chain terminator bifunctional methyltransferase/kinase WbdD

PDB Structure

PDB 4AX8
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystallization, Dehydration and Experimental Phasing of Wbdd, a Bifunctional Kinase and Methyltransferase from Escherichia Coli O9A.
Hagelueken, G., Huang, H., Harlos, K., Clarke, B.R., Whitfield, C., Naismith, J.H.
Acta Crystallogr.,Sect.D
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