Entry
Name
CDP-ribitol ribitolphosphotransferase;
teichoic-acid synthase (ambiguous);
polyribitol phosphate synthetase (ambiguous);
teichoate synthetase (ambiguous);
poly(ribitol phosphate) synthetase (ambiguous);
polyribitol phosphate polymerase (ambiguous);
teichoate synthase (ambiguous);
CDP-ribitol:poly(ribitol phosphate) ribitolphosphotransferase
Class
Transferases;
Transferring phosphorus-containing groups;
Transferases for other substituted phosphate groups
BRITE hierarchy
Sysname
CDP-ribitol:4-O-di[(2R)-1-glycerophospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol ribitolphosphotransferase
Reaction(IUBMB)
n CDP-ribitol + 4-O-di[(2R)-1-glycerophospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n CMP + 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 [RN:
R11621 R12869 ]
Reaction(KEGG)
Substrate
CDP-ribitol [CPD:
C00789 ];
4-O-di[(2R)-1-glycerophospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol [CPD:
C21502 ]
Product
CMP [CPD:
C00055 ];
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 ]
Comment
Involved in the biosynthesis of poly ribitol phosphate teichoic acids in the cell wall of the bacterium Staphylococcus aureus. This enzyme adds around 40 ribitol units to the linker molecule.
History
EC 2.7.8.14 created 1972 as EC 2.4.1.55, transferred 1982 to EC 2.7.8.14, modified 2017
Pathway
Orthology
K18704 CDP-ribitol ribitolphosphotransferase / teichoic acid ribitol-phosphate polymerase
Genes
CCOO : ATE51_00688(epsJ_1)
BTEQ : G4P54_18355 G4P54_18385
VIG : BKP57_07895 BKP57_07900
PRD : F7984_17505 F7984_17510
GAJ : MY490_02505 MY490_02510
SAH : SaurJH1_0244 SaurJH1_0248
SAJ : SaurJH9_0238 SaurJH9_0242
SAX : USA300HOU_0264(tagB1) USA300HOU_0268(tagB2)
SAA : SAUSA300_0247 SAUSA300_0251
SAO : SAOUHSC_00222 SAOUHSC_00227
SUU : M013TW_0234 M013TW_0238
SUV : SAVC_01005 SAVC_01025
SUJ : SAA6159_00230 SAA6159_00234
SUK : SAA6008_00226 SAA6008_00231
SUT : SAT0131_00245 SAT0131_00250
SUQ : HMPREF0772_10245 HMPREF0772_10250
SUD : ST398NM01_0265 ST398NM01_0270
SUX : SAEMRSA15_02120 SAEMRSA15_02160
SUW : SATW20_02550(tarK) SATW20_02590(tarL)
SUF : SARLGA251_02170(tarK) SARLGA251_02210(tarL)
SAUA : SAAG_00734 SAAG_00738
SAUE : RSAU_000197 RSAU_000201
SAUN : SAKOR_00230 SAKOR_00236
SAUS : SA40_0211 SA40_0215
SAUU : SA957_0226 SA957_0230
SAUG : SA268_0223 SA268_0227
SAUZ : SAZ172_0255 SAZ172_0260
SAUT : SAI1T1_2001940 SAI1T1_2001980
SAUJ : SAI2T2_1001940 SAI2T2_1001980
SAUK : SAI3T3_1001940 SAI3T3_1001980
SAUQ : SAI4T8_1001940 SAI4T8_1001980
SAUV : SAI7S6_1001940 SAI7S6_1001980
SAUW : SAI5S5_1001930 SAI5S5_1001970
SAUX : SAI6T6_1001940 SAI6T6_1001980
SAUY : SAI8T7_1001940 SAI8T7_1001980
SAUF : X998_0229 X998_0233
SUY : SA2981_0253 SA2981_0257
SAUB : C248_0240 C248_0245
SAUM : BN843_2520 BN843_2560
SAUC : CA347_260 CA347_264
SAUR : SABB_01595 SABB_01600
SAUI : AZ30_01270 AZ30_01290
SAUD : CH52_04440 CH52_04460
SAMS : NI36_01165 NI36_01185
SUH : SAMSHR1132_02210 SAMSHR1132_02250
SCV : A4G25_08200 A4G25_08205 A4G25_09305
SPET : CEP67_06495 CEP67_08275
SSH : NCTC13712_00199(tagF_1) NCTC13712_00203(tagF_3)
SSIM : SAMEA4384339_0090(tagF_1)
SPSD : JMB28_02430 JMB28_13565
SROT : ML435_01080 ML435_01100
LMN : LM5578_1160 LM5578_1168
LMY : LM5923_1114 LM5923_1122
LMT : LMRG_00539 LMRG_00547
LMOC : LMOSLCC5850_1083 LMOSLCC5850_1091
LMOE : BN418_1295 BN418_1303
LMOB : BN419_1292 BN419_1300
LMOD : LMON_1087 LMON_1095
LMOW : AX10_13965 AX10_14005
LMOQ : LM6179_01397 LM6179_01405
LMR : LMR479A_1105 LMR479A_1113
LMOM : IJ09_04860 IJ09_04900
LMG : LMKG_01835 LMKG_01843
LMJ : LMOG_00633 LMOG_03302
LMW : LMOSLCC2755_1075 LMOSLCC2755_1083
LMX : LMOSLCC2372_1091 LMOSLCC2372_1099
LMZ : LMOSLCC2482_1120 LMOSLCC2482_1129
LMOS : LMOSLCC7179_1058 LMOSLCC7179_1066
LMOY : LMOSLCC2479_1090 LMOSLCC2479_1099
LMOT : LMOSLCC2540_1073 LMOSLCC2540_1082
LGZ : NCTC10812_01040(tagF_3) NCTC10812_01812(tagF_6) NCTC10812_01814(tagF_7) NCTC10812_02004(kfoC_3)
ALIC : GI364_00580 GI364_00650
RUS : RBI_I00537 RBI_I01994
EHL : EHLA_1018 EHLA_2957 EHLA_2962 EHLA_3127 EHLA_3144
LBX : lbkm_2929 lbkm_2930 lbkm_2931
AARG : Aargi30884_26940(tagB)
ABSI : A9CBEGH2_00110(tagB)
EBM : SG0102_21250 SG0102_21290
SHI : Shel_14500 Shel_14640
MHOT : PU630_11635 PU630_11655
BBP : BBPR_0698 BBPR_0699(tagB)
BBF : BBB_0690(tarK) BBB_0691
» show all
Taxonomy
Reference
Authors
Ishimoto N, Strominger JL.
Title
Polyribitol phosphate synthetase of Staphylococcus aureus.
Journal
J Biol Chem 241:639-50 (1966)
Reference
Authors
Brown S, Zhang YH, Walker S
Title
A revised pathway proposed for Staphylococcus aureus wall teichoic acid biosynthesis based on in vitro reconstitution of the intracellular steps.
Journal
Sequence
Reference
Authors
Pereira MP, D'Elia MA, Troczynska J, Brown ED
Title
Duplication of teichoic acid biosynthetic genes in Staphylococcus aureus leads to functionally redundant poly(ribitol phosphate) polymerases.
Journal
Reference
Authors
Brown S, Meredith T, Swoboda J, Walker S
Title
Staphylococcus aureus and Bacillus subtilis W23 make polyribitol wall teichoic acids using different enzymatic pathways.
Journal
Other DBs
ExplorEnz - The Enzyme Database: 2.7.8.14
ExPASy - ENZYME nomenclature database: 2.7.8.14
LinkDB
All DBs