KEGG   ENZYME: 2.4.1.52Help
Entry
EC 2.4.1.52                 Enzyme                                 

Name
poly(glycerol-phosphate) alpha-glucosyltransferase;
UDP glucose-poly(glycerol-phosphate) alpha-glucosyltransferase;
uridine diphosphoglucose-poly(glycerol-phosphate) alpha-glucosyltransferase;
tagE (gene name);
UDP-glucose:poly(glycerol-phosphate) alpha-D-glucosyltransferase
Class
Transferases;
Glycosyltransferases;
Hexosyltransferases
BRITE hierarchy
Sysname
UDP-alpha-D-glucose:4-O-{poly[(2R)-glycerophospho]-(2R)-glycerophospho}-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol alpha-D-glucosyltransferase (configuration-retaining)
Reaction(IUBMB)
n UDP-alpha-D-glucose + 4-O-{poly[(2R)-glycerophospho]-(2R)-glycerophospho}-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n UDP + 4-O-{poly[(2R)-2-alpha-D-glucosyl-1-glycerophospho]-(2R)-glycerophospho}-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol [RN:R04041]
Reaction(KEGG)
Substrate
UDP-alpha-D-glucose [CPD:C00029];
4-O-{poly[(2R)-glycerophospho]-(2R)-glycerophospho}-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Product
UDP [CPD:C00015];
4-O-{poly[(2R)-2-alpha-D-glucosyl-1-glycerophospho]-(2R)-glycerophospho}-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Comment
Involved in the biosynthesis of poly glycerol phosphate teichoic acids in bacterial cell walls. This enzyme, isolated from Bacillus subtilis 168, adds an alpha-D-glucose to the free OH groups of the glycerol units. The enzyme has a strong preference for UDP-alpha-glucose as the sugar donor. It has no activity with poly(ribitol phosphate).
History
EC 2.4.1.52 created 1972, modified 2017
Orthology
K00712  poly(glycerol-phosphate) alpha-glucosyltransferase
Genes
ETE: ETEE_3362
EDW: QY76_13070
EDL: AAZ33_07150
APJ: APJL_1608
PGB: H744_2c2867
ABM: ABSDF2312
ACC: BDGL_000003(tagE)
ALC: OTEC02_15270
ACV: AMD27_04695
VBO: CKY39_08845
BSU: BSU35730(tagE)
BSR: I33_3702
BSH: BSU6051_35730(tagE)
BSUT: BSUB_03806(tagE)
BSUL: BSUA_03806(tagE)
BSQ: B657_35730(tagE)
BAMP: B938_16875
BAMT: AJ82_18555
BAO: BAMF_3412(tagE)
BAZ: BAMTA208_18080(tagE)
BQL: LL3_03707(tagE)
BXH: BAXH7_03696(tagE)
BPU: BPUM_3229
BPUS: UP12_16725
BACW: QR42_16230
BACL: BS34A_38860(tagE)
BALM: BsLM_3589
SER: SERP0208
SEPP: SEB_00254
SCA: SCA_2110(tagE)
SDT: SPSE_0282
SCAP: AYP1020_2024(gtf1_2) AYP1020_2025(tagE_1) AYP1020_2194(tagE_2) AYP1020_2313(tagE_3)
SSCH: LH95_08400
SSCZ: RN70_02040
EAN: Eab7_2556
LLA: L76469(yohH) L78550(yohJ)
LLK: LLKF_1561(yohH) LLKF_1562(yohJ)
LLT: CVCAS_1364(yohH)
LLS: lilo_1372(yohH) lilo_1373(yohJ)
LLJ: LG36_0924(yohJ) LG36_0925(yohH)
SPN: SP_1758
SGO: SGO_0975(gtaA)
LPL: lp_1299(tagE1) lp_1311(tagE2) lp_1312(tagE3) lp_2498(tagE4) lp_2843(tagE5) lp_2844(tagE6)
LPJ: JDM1_1099(tagE1) JDM1_1106(tagE2) JDM1_1107(tagE3) JDM1_2011(tagE4) JDM1_2280(tagE5) JDM1_2282(tagE6)
LPT: zj316_1318(tagE1) zj316_1319(tagE1) zj316_1327(tagE2) zj316_1328(tagE3) zj316_2429(tagE4) zj316_2714(tagE5) zj316_2715(tagE6)
LPS: LPST_C1052(tagE1) LPST_C1058(tagE2) LPST_C1059(tagE3) LPST_C2058(tagE4) LPST_C2332(tagE5) LPST_C2333(tagE6)
LCB: LCABL_10040(tagE2) LCABL_10050(tagE3)
LRH: LGG_00348(yohJ) LGG_00349(yohH) LGG_01586(yohH) LGG_01587(yohJ) LGG_02285(yohH)
LRL: LC705_00333(yohJ) LC705_00334(yohH) LC705_01567(yohH) LC705_01568(yohJ) LC705_02276(yohH)
LBH: Lbuc_2160
LCI: LCK_01447(yohH)
LKI: LKI_07900
MTS: MTES_0867
ARM: ART_1251
IDO: I598_3340(tagE_2)
SERJ: SGUI_1312
RBA: RB2471
 » show all
Taxonomy
Reference
1  [PMID:14245359]
  Authors
GLASER L, BURGER MM.
  Title
THE SYNTHESIS OF TEICHOIC ACIDS. 3. GLUCOSYLATION OF POLYGLYCEROPHOSPHATE.
  Journal
J Biol Chem 239:3187-91 (1964)
Reference
2  [PMID:21558268]
  Authors
Allison SE, D'Elia MA, Arar S, Monteiro MA, Brown ED
  Title
Studies of the genetics, function, and kinetic mechanism of TagE, the wall teichoic acid glycosyltransferase in Bacillus subtilis 168.
  Journal
J Biol Chem 286:23708-16 (2011)
DOI:10.1074/jbc.M111.241265
  Sequence
[bsu:BSU35730]
Other DBs
ExplorEnz - The Enzyme Database: 2.4.1.52
IUBMB Enzyme Nomenclature: 2.4.1.52
ExPASy - ENZYME nomenclature database: 2.4.1.52
BRENDA, the Enzyme Database: 2.4.1.52
CAS: 37277-60-4

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