Entry
Name
rubredoxin---NAD+ reductase;
rubredoxin reductase;
rubredoxin-nicotinamide adenine dinucleotide reductase;
dihydronicotinamide adenine dinucleotide-rubredoxin reductase;
reduced nicotinamide adenine dinucleotide-rubredoxin reductase;
NADH-rubredoxin reductase;
rubredoxin-NAD reductase;
NADH: rubredoxin oxidoreductase;
DPNH-rubredoxin reductase;
NADH-rubredoxin oxidoreductase
Class
Oxidoreductases;
Acting on iron-sulfur proteins as donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
rubredoxin:NAD+ oxidoreductase
Reaction(IUBMB)
2 reduced rubredoxin + NAD+ + H+ = 2 oxidized rubredoxin + NADH [RN:
R02000 ]
Reaction(KEGG)
Substrate
Product
Comment
Requires FAD. The enzyme from Clostridium acetobutylicum reduces rubredoxin, ferricyanide and dichlorophenolindophenol, but not ferredoxin or flavodoxin. The reaction does not occur when NADPH is substituted for NADH. Contains iron at the redox centre.
History
EC 1.18.1.1 created 1972 as EC 1.6.7.2, transferred 1978 to EC 1.18.1.1, modified 2001
Pathway
Orthology
K05297 rubredoxin---NAD+ reductase
K21738 rubredoxin---NAD+ reductase
K22567 rubredoxin---NAD+ reductase
Genes
SKS : FCN78_06135 FCN78_12245
PRE : PCA10_34400 PCA10_55500(rubB)
PFUW : KF707C_29950 KF707C_55940
PAEB : NCGM1900_6194(rubB)
PNT : G5B91_04770 G5B91_31530
PPU : PP_5314(alkT) PP_5371
PPX : T1E_3940(rubB) T1E_3999
PALD : LU682_029160 LU682_029445
PVD : CFBP1590__5340(alkT)
PPRC : PFLCHA0_c60620(alkT)
PMUD : NCTC8068_05313(alkT)
PFW : PF1751_v1c54440(rubB)
PRH : LT40_07120 LT40_07165
PKE : DLD99_12320 DLD99_28440
PUM : HGP31_00235 HGP31_12865
PSEJ : HNQ25_02610 HNQ25_11295
PMAO : PMYSY11_2129 PMYSY11_4365(alkT)
PFAK : KSS94_23085 KSS94_26660
PWZ : J7655_00040 J7655_09485 J7655_20695
PTW : TUM18999_01360(alkT)
PTAE : NCTC10697_00117(alkT_1) NCTC10697_02146(alkT_2)
PIZ : LAB08_R20720 LAB08_R59490
PSJY : AA098_00125 AA098_00405
PSLP : BHQ29_08855 BHQ29_23545
PLAU : I0D68_02995 I0D68_08710
PSKP : KU43P_25560(alkT) KU43P_27940 KU43P_51940(rubB)
PBEZ : SBP02_00695 SBP02_06025
PALL : UYA_14270 UYA_23590
PTY : JWV26_09015 JWV26_11725
HPEG : EAO82_00380 EAO82_02465
MHC : MARHY2849(alkT) MARHY3494(rubB)
MSR : AU15_01845 AU15_22050
MARI : ACP86_07285 ACP86_20395
MLQ : ASQ50_08875 ASQ50_10975 ASQ50_12490
MARA : D0851_01590 D0851_10745
MARJ : MARI_17880(alkT_1) MARI_30590(alkT_2)
MALL : PBN92_01975 PBN92_18175
MSHE : MAALD49_20300 MAALD49_35730 MAALD49_40670(norW)
MANP : EHN06_18440 EHN06_20790
MMEE : NLK58_02235 NLK58_11340
PALI : A3K91_0387 A3K91_2007
PSYC : DABAL43B_0397(rubB)
PSYP : E5677_03375 E5677_11510
ABY : ABAYE1067 ABAYE2799(rubB)
ABC : ACICU_00955 ACICU_02608
ABZ : ABZJ_01098 ABZJ_02802
ABR : ABTJ_01105 ABTJ_02817
ABD : ABTW07_1084 ABTW07_2856
ABJ : BJAB07104_01092 BJAB07104_02766
ABAJ : BJAB0868_01106 BJAB0868_02648
ABW : BL01_04850 BL01_11680
ATN : FM020_04025 FM020_10750
AGYL : FPL18_12830 FPL18_15235
AVIV : LF296_04970 LF296_13025(rubB)
ACOT : QLH32_00370 QLH32_04520(rubB)
MCAT : MC25239_00086(norW)
MCUN : NCTC10297_00560(norW)
ALKM : NKI27_00235 NKI27_16700
ASEM : NNL22_13175 NNL22_18310
MICC : AUP74_00095(rubB_1) AUP74_02936(rubB_2)
MAGA : Mag101_09900 Mag101_11295 Mag101_12995
MHYD : GTQ55_10320 GTQ55_12815
MPAF : R5R33_01810 R5R33_14665
MBRG : PVT68_00635 PVT68_04670
HTR : EPV75_00365 EPV75_09705
TIB : THMIRHAM_01620(norW)
TSE : THMIRHAS_04100(rubB)
TZO : THMIRHAT_15060(norW)
NAX : HC341_07615 HC341_16180
HSI : BOX17_06760 BOX17_07650
HAAH : HALA3H3_360135(alkT)
HAAZ : HaloA020_10940(alkT)
ALCA : ASALC70_02480(rubB_1)
ADI : B5T_02839 B5T_04348(rubB)
OME : OLMES_3725 OLMES_4764
BUM : AXG89_24015 AXG89_28675
PLG : NCTC10937_05175(alkT)
RLH : MIZ03_0156 MIZ03_4593
JAG : GJA_3183(alkT) GJA_559(rubB)
EBA : ebA2965(norW) ebA6036
ABRE : pbN1_18290 pbN1_36310(rubB)
APET : ToN1_01030(rubB) ToN1_24900
AZA : AZKH_0051(norW) AZKH_2404(rubB)
AZD : CDA09_00240 CDA09_07180
ACOM : CEW83_06500 CEW83_14970
SPSE : SULPSESMR1_04189(alkT)
SPAG : sphantq_03864(rubB)
ECOG : FIV45_05045 FIV45_16800
» show all
Taxonomy
Reference
Authors
Peterson JA, Kusunose M, Kusunose E, Coon MJ.
Title
Enzymatic omega-oxidation. II. Function of rubredoxin as the electron carrier in omega-hydroxylation.
Journal
J Biol Chem 242:4334-40 (1967)
Reference
Authors
Enzymatic -oxidation. VI. Isolation of homogeneous reduced diphosphopyridine nucleotide-rubredoxin reductase.
Title
J Biol Chem 247:2109-16 (1972)
Reference
Authors
Ueda T, Coon MJ.
Title
Enzymatic oxidation. VII. Reduced diphosphopyridine nucleotide-rubredoxin reductase: properties and function as an electron carrier in hydroxylation.
Journal
J Biol Chem 247:5010-6 (1972)
Reference
Authors
Petitdemange H, Marczak R, Blusson H, Gay R.
Title
Isolation and properties of reduced nicotinamide adenine dinucleotiderubredoxin oxidoreductase of Clostridium acetobutylicum.
Journal
Other DBs
ExplorEnz - The Enzyme Database: 1.18.1.1
ExPASy - ENZYME nomenclature database: 1.18.1.1