KEGG   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
SAMMW0919
SASSAS0971
SACSACOL1043
SAXUSA300HOU_0984
SAASAUSA300_0939
SAENWMN_0906
SUVSAVC_04345
SUJSAA6159_00892
SUKSAA6008_00990
SUTSAT0131_01070
SUQHMPREF0772_12199
SUZMS7_0993
SUWSATW20_10320
SAUASAAG_02146
SAUZSAZ172_0976
SAUFX998_1035
SABSAB0901
SAUMBN843_9420
SAURSABB_01002
SAUIAZ30_04940
SUHSAMSHR1132_08830
SDPNCTC12225_00342(tagE_1)
SSCHLH95_01430
SKLC7J89_02280
SARLSAP2_11820
SSHNCTC13712_00981(tagE_3)
SSIMSAMEA4384339_0209(tagE_1)
SFFFOB90_06365
SSTESAMEA4384403_0871(tagE_1)
MLENH3V22_11340
MRNK8F61_06200
GPRJQN66_07680
PAEYKUF55_10590
 » show all
Reference
1
  Authors
Nathenson, S.G., Ishimoto, N. and Strominger, J.L.
  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

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