Information on EC 2.7.1.181 - polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase

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The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY hide
2.7.1.181
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RECOMMENDED NAME
GeneOntology No.
polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
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)-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
show the reaction diagram
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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)-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 3-ph
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)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-alpha-diphospho-ditrans,octacis-undecaprenol (cf. EC 2.1.1.294, 3-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase)
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 2-alpha-D-mannosyl-D-mannose
ADP + 3-O-phospho-2-alpha-D-mannosyl-D-mannose
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
ATP + D-mannose
ADP + 3-O-phospho-D-mannose
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
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
show the reaction diagram
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65500
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x * 65500, soluble His6-tagged truncated derivative comprising amino acids 1 to 600 of WbdD
81731
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x * 81731, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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crystallization and modeling by molecular-replacement to obtain high-resolution diffraction, and development of methods to control the hydration status
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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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D350A
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88.8% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 95.2% with substrate D-mannose
D351A
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0.9% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 1.1% with substrate D-mannose
D351E
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4.5% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 1.5% with substrate D-mannose
DELTA398-418
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6.7% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 4.7% with substrate D-mannose
E274A
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45.4% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 66.6% with substrate D-mannose
H132A
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complete loss of activity
H133A
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complete loss of activity
N34D/Q35E/H197E
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complete loss of activity
R203A
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complete loss of activity
R270A
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72.8% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 85.7% with substrate D-mannose
W355F
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72.4% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 1.9% with substrate D-mannose
W355H
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48.7% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 50.7% with substrate D-mannose
Y16F
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complete loss of activity
Y230F
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0.1% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 2.5% with substrate D-mannose
D350A
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88.8% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 95.2% with substrate D-mannose
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E274A
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45.4% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 66.6% with substrate D-mannose
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H132A
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complete loss of activity
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R203A
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complete loss of activity
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Y16F
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complete loss of activity
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis