KEGG   ENZYME: 1.1.1.405Help
Entry
EC 1.1.1.405                Enzyme                                 

Name
ribitol-5-phosphate 2-dehydrogenase (NADP+);
acs1 (gene name);
bcs1 (gene name);
tarJ (gene name);
ribulose-5-phosphate reductase;
ribulose-5-P reductase;
D-ribulose 5-phosphate reductase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
D-ribitol-5-phosphate:NADP+ 2-oxidoreductase
Reaction(IUBMB)
D-ribitol 5-phosphate + NADP+ = D-ribulose 5-phosphate + NADPH + H+ [RN:R01525]
Reaction(KEGG)
Substrate
D-ribitol 5-phosphate [CPD:C01068];
NADP+ [CPD:C00006]
Product
D-ribulose 5-phosphate [CPD:C00199];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
Requires Zn2+. The enzyme, characterized in bacteria, is specific for NADP. It is part of the synthesis pathway of CDP-ribitol. In Haemophilus influenzae it is part of a multifunctional enzyme also catalysing EC 2.7.7.40, D-ribitol-5-phosphate cytidylyltransferase. cf. EC 1.1.1.137, ribitol-5-phosphate 2-dehydrogenase.
History
EC 1.1.1.405 created 2017
Pathway
ec00040  Pentose and glucuronate interconversions
ec01100  Metabolic pathways
Orthology
K05352  ribitol-5-phosphate 2-dehydrogenase (NADP+)
K21681  ribitol-5-phosphate 2-dehydrogenase (NADP+) / D-ribitol-5-phosphate cytidylyltransferase
Genes
ECOS: EC958_3340
EBR: ECB_02822
EBL: ECD_02822
KCO: BWI95_19355
HIU: HIB_11690(bcs1') HIB_11840(bcs1')
PAET: NCTC13378_01387
AEU: ACEE_10835
BTRA: F544_4610
PCQ: PcP3B5_16180(ispD1)
CKE: B5M06_15305
HPSE: HPF_20235(ispD2)
CCQ: N149_1385(ispD)
NAM: NAMH_1606
CPAF: C6V80_08920(ispD)
PPRF: DPRO_1984(bcs)
ZMO: ZMO0353
ZMN: Za10_0885
ZMM: Zmob_0895
ZMB: ZZ6_0893
ZMI: ZCP4_0917
ZMC: A265_00908(ispD2)
ZMR: A254_00908(ispD2)
BSL: A7A1_1142
BSUS: Q433_19600
BSS: BSUW23_17570(tarJ)
BST: GYO_3934(tarJ)
BSX: C663_3469(tarJ)
BJS: MY9_3631
BACY: QF06_16295
SUW: SATW20_02540(tarJ') SATW20_02580(tarJ)
SUF: SARLGA251_02160(tarJ') SARLGA251_02200(tarJ)
SAB: SAB0195
SAUR: SABB_01596(tarJ) SABB_01601
SEP: SE0320
SER: SERP0197
SEPP: SEB_00242
SEPS: DP17_1630
SPAS: STP1_1638
SSCH: LH95_01795
LMO: lmo1087
LMOE: BN418_1305
LMOB: BN419_1302
LMOD: LMON_1097
LMOW: AX10_14015
LMOQ: LM6179_1407(tarJ)
LMR: LMR479A_1115(tarJ)
LMOM: IJ09_04850
LMOG: BN389_11140(tarJ)
LMP: MUO_05675
LMOX: AX24_02825
LMQ: LMM7_1111
LMS: LMLG_2570
LMOK: CQ02_05635
LIN: lin1072
LWE: lwe1062
LSG: lse_0977
LIV: LIV_1028
ESI: Exig_0190
EAN: Eab7_0182(tarJ)
GMO: NCTC11323_00090(idnD)
SPN: SP_1270
SPD: SPD_1126
SPR: spr1148
SPW: SPCG_1234
SJJ: SPJ_1184
SPX: SPG_1164
SNT: SPT_0958
SND: MYY_0970
SPNN: T308_04435
SPV: SPH_1386
SPP: SPP_1308
SNP: SPAP_1295
SMB: smi_1227(tarJ)
SOR: SOR_1098(tarJ)
STRN: SNAG_1096(yjjN)
LSL: LSL_1953(tdh)
LSI: HN6_01675(tdh)
LCB: LCABL_29250(tdh)
LCS: LCBD_2953
LCE: LC2W_2927
LCW: BN194_28680(tarJ)
PCE: PECL_1839
WCE: WS08_0696
WCT: WS74_0698
CBN: CbC4_0710
CBT: CLH_2995
CBV: U729_1135
EHL: EHLA_2452
PMIC: NW74_04235
SGR: SGR_4956
SGB: WQO_10720
SFA: Sfla_4295
STRP: F750_2413
SFI: SFUL_2153
SPRI: SPRI_4927
SRW: TUE45_03196(ispD1)
SRN: A4G23_01658(ispD2)
SLAU: SLA_5894
SGE: DWG14_05586(bcs1)
MOO: BWL13_02200(bcs1)
JDE: Jden_1842
MPH: MLP_25850(ispD)
NOY: EXE57_09945(ispD)
PSIM: KR76_03415
NAL: B005_2753
STRR: EKD16_03260(ispD2)
SRO: Sros_1351
SAQ: Sare_1679
MIL: ML5_2188
TBI: Tbis_0719
SNG: SNE_A02450(ispD)
OTE: Oter_0455
BTH: BT_1651
BTHO: Btheta7330_01408(ispD2_2)
PDI: BDI_1841
BUY: D8S85_08665(ispD)
MBAS: ALGA_0189
FJO: Fjoh_2239
MSI: Msm_0376
MRU: mru_1057
MEB: Abm4_1002
MMIL: sm9_0634
MEYE: TL18_03055
MCUB: MCBB_1533(tarJ)
ABI: Aboo_0706
TSI: TSIB_2019
 » show all
Taxonomy
Reference
1  [PMID:11305920]
  Authors
Zolli M, Kobric DJ, Brown ED
  Title
Reduction precedes cytidylyl transfer without substrate channeling in distinct active sites of the bifunctional CDP-ribitol synthase from Haemophilus influenzae.
  Journal
Biochemistry 40:5041-8 (2001)
DOI:10.1021/bi002745n
  Sequence
[hiu:HIB_11840]
Reference
2  [PMID:15362865]
  Authors
Pereira MP, Brown ED
  Title
Bifunctional catalysis by CDP-ribitol synthase: convergent recruitment of reductase and cytidylyltransferase activities in Haemophilus influenzae and Staphylococcus aureus.
  Journal
Biochemistry 43:11802-12 (2004)
DOI:10.1021/bi048866v
Reference
3  [PMID:18556787]
  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
J Bacteriol 190:5642-9 (2008)
DOI:10.1128/JB.00526-08
Reference
4  [PMID:19074383]
  Authors
Baur S, Marles-Wright J, Buckenmaier S, Lewis RJ, Vollmer W
  Title
Synthesis of CDP-activated ribitol for teichoic acid precursors in Streptococcus  pneumoniae.
  Journal
J Bacteriol 191:1200-10 (2009)
DOI:10.1128/JB.01120-08
  Sequence
[spr:spr1148]
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.405
IUBMB Enzyme Nomenclature: 1.1.1.405
ExPASy - ENZYME nomenclature database: 1.1.1.405
BRENDA, the Enzyme Database: 1.1.1.405

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