KEGG ENZYME: 2.7.1.181

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

PGE:	LG71_13030

ASUB:

NLZ15_07780

TCI:	A7K98_13155

PPI:

YSA_02210

PTAI:

ICN73_13155

» 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

[ag:AFQ31610]

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

[ag:AFQ31610]

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

[ag:AFQ31610]

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