KEGG   ENZYME: 2.7.1.181
Entry
EC 2.7.1.181                Enzyme                                 

Name
polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase;
WbdD;
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-phosphotransferase
Class
Transferases;
Transferring phosphorus-containing groups;
Phosphotransferases with an alcohol group as acceptor
Sysname
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 3-phosphotransferase
Reaction(IUBMB)
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 [RN:R10657]
Reaction(KEGG)
R10657
Substrate
ATP [CPD:C00002];
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:C20761]
Product
ADP [CPD:C00008];
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]
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 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, 3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase).
History
EC 2.7.1.181 created 2014, modified 2017
Orthology
K18827  O-antigen chain-terminating bifunctional methyltransferase/kinase
Genes
ECX: EcHS_A2169
SBG: SBG_0615(wbdD)
SBZ: A464_688
SBV: N643_03100
KPJ: N559_1771
KVA: Kvar_1569
KPE: KPK_1679
KVD: KR75_26285
KVQ: SP68_06430
KQU: AVR78_21675
 » 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: 2.7.1.181
IUBMB Enzyme Nomenclature: 2.7.1.181
ExPASy - ENZYME nomenclature database: 2.7.1.181
BRENDA, the Enzyme Database: 2.7.1.181

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