KEGG ENZYME: 2.4.1.70

ENZYME: 2.4.1.70

Entry

EC 2.4.1.70                 Enzyme

Name

poly(ribitol-phosphate) alpha-N-acetylglucosaminyltransferase;
TarM;
UDP acetylglucosamine-poly(ribitol phosphate) acetylglucosaminyltransferase (ambiguous);
uridine diphosphoacetylglucosamine-poly(ribitol phosphate) acetylglucosaminyltransferase (ambiguous);
UDP-N-acetyl-D-glucosamine:poly(ribitol-phosphate) N-acetyl-D-glucosaminyltransferase (ambiguous);
UDP-N-acetyl-alpha-D-glucosamine:poly(ribitol-phosphate) N-acetyl-alpha-D-glucosaminyltransferase (ambiguous);
poly(ribitol-phosphate) N-acetylglucosaminyltransferase (ambiguous)

Class

Transferases;
Glycosyltransferases;
Hexosyltransferases

Sysname

UDP-N-acetyl-alpha-D-glucosamine:4-O-(D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol alpha-N-acetyl-D-glucosaminyltransferase (configuration-retaining)

Reaction(IUBMB)

n UDP-N-acetyl-alpha-D-glucosamine + 4-O-(D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n UDP + 4-O-(2-N-acetyl-alpha-D-glucosaminyl-D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol [RN:R12037 R12870]

Reaction(KEGG)

R12037 R12870(G);
(other) R02717 R06182(G)

Substrate

UDP-N-acetyl-alpha-D-glucosamine [CPD:C00043];
4-O-(D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol [CPD:C21508]

Product

UDP [CPD:C00015];
4-O-(2-N-acetyl-alpha-D-glucosaminyl-D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol [CPD:C21870]

Comment

Involved in the biosynthesis of poly(ribitol phosphate) teichoic acids in the cell wall of the bacterium Staphylococcus aureus. This enzyme adds an N-acetyl-alpha-D-glucosamine to the hydroxyl group at the 2 position of the ribitol phosphate units. cf. EC 2.4.1.355 [poly(ribitol-phosphate) beta-N-acetylglucosaminyltransferase].

History

EC 2.4.1.70 created 1972, modified 2018

Pathway

ec00552

Teichoic acid biosynthesis

Orthology

K22710

poly(ribitol-phosphate) alpha-N-acetylglucosaminyltransferase

Genes

SAM:

MW0919

SAS:

SAS0971

SAC:

SACOL1043

SAX:	USA300HOU_0984

SAA:	SAUSA300_0939

SAE:

NWMN_0906

SUV:	SAVC_04345

SUJ:	SAA6159_00892

SUK:	SAA6008_00990

SUT:	SAT0131_01070

SUQ:	HMPREF0772_12199

SUZ:

MS7_0993

SUW:	SATW20_10320

SAUA:

SAAG_02146

SAUZ:

SAZ172_0976

SAUF:

X998_1035

SAB:

SAB0901

SAUM:

BN843_9420

SAUR:

SABB_01002

SAUI:

AZ30_04940

SUH:	SAMSHR1132_08830

SDP:	NCTC12225_00342(tagE_1)

SSCH:

LH95_01430

SKL:	C7J89_02280

SARL:

SAP2_11820

SSH:	NCTC13712_00981(tagE_3)

SSIM:

SAMEA4384339_0209(tagE_1)

SFF:	FOB90_06365

SSTE:

SAMEA4384403_0871(tagE_1)

MLEN:

H3V22_11340

MRN:	K8F61_06200

MOJ:	D7D94_12705

MAUG:

KV397_01200

MSUF:

KV394_03740

PFLU:

BWO91_07610

GPR:	JQN66_07680

GNC:	QQS42_07620

GEY:	QMQ05_07380

MQR:	AB3M34_19640

» show all

Reference

Authors

Nathenson SG, Ishimoto N, Strominger JL.

Title

UDP-N-acetylglucosamine:polyribitol phosphate N-acetylglucosaminyltransferases from Staphylococcus aureus.

Journal

Methods Enzymol 8:426-429 (1966)

Reference

2 [PMID:20185825]

Authors

Xia G, Maier L, Sanchez-Carballo P, Li M, Otto M, Holst O, Peschel A

Title

Glycosylation of wall teichoic acid in Staphylococcus aureus by TarM.

Journal

J Biol Chem 285:13405-15 (2010)
DOI:10.1074/jbc.M109.096172

Sequence

[sac:SACOL1043]

Reference

3 [PMID:25624472]

Authors

Sobhanifar S, Worrall LJ, Gruninger RJ, Wasney GA, Blaukopf M, Baumann L, Lameignere E, Solomonson M, Brown ED, Withers SG, Strynadka NC

Title

Structure and mechanism of Staphylococcus aureus TarM, the wall teichoic acid alpha-glycosyltransferase.

Journal

Proc Natl Acad Sci U S A 112:E576-85 (2015)
DOI:10.1073/pnas.1418084112

Sequence

[sac:SACOL1043]

Reference

4 [PMID:25697358]

Authors

Koc C, Gerlach D, Beck S, Peschel A, Xia G, Stehle T

Title

Structural and enzymatic analysis of TarM glycosyltransferase from Staphylococcus aureus reveals an oligomeric protein specific for the glycosylation of wall teichoic acid.

Journal

J Biol Chem 290:9874-85 (2015)
DOI:10.1074/jbc.M114.619924

Sequence

[sac:SACOL1043]

Other DBs

ExplorEnz - The Enzyme Database:

2.4.1.70

IUBMB Enzyme Nomenclature:

2.4.1.70

ExPASy - ENZYME nomenclature database:

2.4.1.70

BRENDA, the Enzyme Database:

2.4.1.70

CAS:	37277-71-7

All links

Protein sequence (4)   
   UniProt (3)   
   SWISS-PROT (1)   
DNA sequence (210)   
   GenBank (105)   
   EMBL (105)   
Protein domain (1)   
   InterPro (1)   
All databases (215)   

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