KEGG   ENZYME: 2.4.1.371
Entry
EC 2.4.1.371                Enzyme                                 
Name
polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 2,3-alpha-mannosylpolymerase;
WbdA
Class
Transferases;
Glycosyltransferases;
Hexosyltransferases
Sysname
GDP-alpha-D-mannose: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 2,3-alpha-mannosyltransferase (configuration-retaining)
Reaction(IUBMB)
(1) 2 GDP-alpha-D-mannose + [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 = 2 GDP + 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:R12525];
(2) 2 GDP-alpha-D-mannose + 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 = 2 GDP + [alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n+1-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol [RN:R12526]
Reaction(KEGG)
R12525 R12526
Substrate
GDP-alpha-D-mannose [CPD:C00096];
[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:C22229];
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
GDP [CPD:C00035];
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];
[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n+1-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Comment
The enzyme is involved in the biosynthesis of polymannose O-polysaccharide in the outer leaflet of the membrane of Escherichia coli serotype O9a. The enzymes consists of two domains that are responsible for the 1->2 and 1->3 linkages, respectively.
History
EC 2.4.1.371 created 2019
Orthology
K12993  O-antigen biosynthesis alpha-1,2-mannosyltransferase
K24658  O-antigen biosynthesis alpha-1,2-mannosyltransferase
Genes
ECX: EcHS_A2168
ECR: ECIAI1_2099(wbdA)
SBG: SBG_0616(wbdA)
SBZ: A464_689
SBV: N643_03105
KPJ: N559_1772
KVA: Kvar_1570
KPE: KPK_1680
KVD: KR75_26280
KVQ: SP68_06425
KQU: AVR78_21670
EAR: CCG29190
KLW: DA718_09850
PGE: LG71_13035
SNEM: NLX84_07970
RCB: O1V66_05895
TCI: A7K98_13150
AANT: HUK68_19155
 » show all
Reference
1  [PMID:22875852]
  Authors
Greenfield LK, Richards MR, Li J, Wakarchuk WW, Lowary TL, Whitfield C
  Title
Biosynthesis of the polymannose lipopolysaccharide O-antigens from Escherichia coli serotypes O8 and O9a requires a unique combination of single- and multiple-active site mannosyltransferases.
  Journal
J Biol Chem 287:35078-91 (2012)
DOI:10.1074/jbc.M112.401000
  Sequence
[ag:AGH30276]
Reference
2  [PMID:22989876]
  Authors
Greenfield LK, Richards MR, Vinogradov E, Wakarchuk WW, Lowary TL, Whitfield C
  Title
Domain organization of the polymerizing mannosyltransferases involved in synthesis of the Escherichia coli O8 and O9a lipopolysaccharide O-antigens.
  Journal
J Biol Chem 287:38135-49 (2012)
DOI:10.1074/jbc.M112.412577
  Sequence
[ag:AGH30276]
Reference
3  [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: 2.4.1.371
IUBMB Enzyme Nomenclature: 2.4.1.371
ExPASy - ENZYME nomenclature database: 2.4.1.371
BRENDA, the Enzyme Database: 2.4.1.371

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Chemical substance (4)   
   KEGG COMPOUND (4)   
Chemical reaction (2)   
   KEGG REACTION (2)   
Gene (22)   
   KEGG ORTHOLOGY (2)   
   KEGG GENES (20)   
Protein sequence (4)   
   UniProt (2)   
   SWISS-PROT (2)   
Protein domain (1)   
   InterPro (1)   
All databases (33)   

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