KEGG   ENZYME: 2.1.1.294
Entry
EC 2.1.1.294                Enzyme                                 
Name
3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase;
WbdD;
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)-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 3-phospho-methyltransferase
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
Sysname
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 3-phospho-methyltransferase
Reaction(IUBMB)
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 [RN:R10658]
Reaction(KEGG)
R10658
Substrate
S-adenosyl-L-methionine [CPD:C00019];
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 [CPD:C20762]
Product
S-adenosyl-L-homocysteine [CPD:C00021];
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 [CPD:C20763]
Comment
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 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, polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase).
History
EC 2.1.1.294 created 2014, modified 2018
Orthology
K18827  O-antigen chain-terminating bifunctional methyltransferase/kinase
Genes
ECXEcHS_A2169
SBGSBG_0615(wbdD)
SBZA464_688
SBVN643_03100
KPJN559_1771
KVAKvar_1569
KPEKPK_1679
KVDKR75_26285
KVQSP68_06430
KQUAVR78_21675
PGELG71_13030
TCIA7K98_13155
ENWMJO57_09745
 » show all
Reference
1  [PMID:15184370]
  Authors
Clarke BR, Cuthbertson L, Whitfield C
  Title
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.
  Journal
J Biol Chem 279:35709-18 (2004)
DOI:10.1074/jbc.M404738200
  Sequence
Reference
2  [PMID:19734145]
  Authors
Clarke BR, Greenfield LK, Bouwman C, Whitfield C
  Title
Coordination of polymerization, chain termination, and export in assembly of the Escherichia coli lipopolysaccharide O9a antigen in an ATP-binding cassette transporter-dependent pathway.
  Journal
J Biol Chem 284:30662-72 (2009)
DOI:10.1074/jbc.M109.052878
  Sequence
Reference
3  [PMID:21990359]
  Authors
Clarke BR, Richards MR, Greenfield LK, Hou D, Lowary TL, Whitfield C
  Title
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.
  Journal
J Biol Chem 286:41391-401 (2011)
DOI:10.1074/jbc.M111.295857
  Sequence
Reference
4  [PMID:25422321]
  Authors
Liston SD, Clarke BR, Greenfield LK, Richards MR, Lowary TL, Whitfield C
  Title
Domain interactions control complex formation and polymerase specificity in the biosynthesis of the Escherichia coli O9a antigen.
  Journal
J Biol Chem 290:1075-85 (2015)
DOI:10.1074/jbc.M114.622480
Other DBs
ExplorEnz - The Enzyme Database: 2.1.1.294
IUBMB Enzyme Nomenclature: 2.1.1.294
ExPASy - ENZYME nomenclature database: 2.1.1.294
BRENDA, the Enzyme Database: 2.1.1.294

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