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Conserved domains on  [gi|446606104|ref|WP_000683450|]
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MULTISPECIES: NAD(P)H-dependent oxidoreductase [Bacillus]

Protein Classification

NAD(P)H-dependent oxidoreductase( domain architecture ID 10006206)

NAD(P)H-dependent oxidoreductase which catalyzes the reduction or oxidation of a substrate coupled to the oxidation or reduction, respectively, of a nicotinamide adenine dinucleotide cofactor NAD(P)H or NAD(P)+

CATH:  3.40.50.360
EC:  1.-.-.-
Gene Ontology:  GO:0009055|GO:0050136|GO:0008753|GO:0010181
PubMed:  25372605|7568029
SCOP:  3001217

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 2-193 1.03e-75

Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction only];


:

Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 225.49  E-value: 1.03e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446606104   2 KHVIVYAHPNTESFNHAILETVKSELEGNGHEVRVRDLYELNFNPVLGASDFisFSQGNTPEDIKEEQEHISWADSITFI 81
Cdd:COG2249    1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAADF--YRDGPLPIDVAAEQELLLWADHLVFQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446606104  82 YPVWWAGLPAILKGYVDRVFSHGFAYAYGENGIEKLLSGKKGLLLSTMGNSKEAYTAGGMFDAMKKTVDVGIFEFTGIET 161
Cdd:COG2249   79 FPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGPIEELLFRGTLGYCGMKV 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 446606104 162 IEHTFYTSVPSVDDSVRKQYLEEVKDVVNRAF 193
Cdd:COG2249  159 LPPFVLYGVDRSSDEERAAWLERVRELLAALA 190
 
Name Accession Description Interval E-value
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 2-193 1.03e-75

Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction only];


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 225.49  E-value: 1.03e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446606104   2 KHVIVYAHPNTESFNHAILETVKSELEGNGHEVRVRDLYELNFNPVLGASDFisFSQGNTPEDIKEEQEHISWADSITFI 81
Cdd:COG2249    1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAADF--YRDGPLPIDVAAEQELLLWADHLVFQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446606104  82 YPVWWAGLPAILKGYVDRVFSHGFAYAYGENGIEKLLSGKKGLLLSTMGNSKEAYTAGGMFDAMKKTVDVGIFEFTGIET 161
Cdd:COG2249   79 FPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGPIEELLFRGTLGYCGMKV 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 446606104 162 IEHTFYTSVPSVDDSVRKQYLEEVKDVVNRAF 193
Cdd:COG2249  159 LPPFVLYGVDRSSDEERAAWLERVRELLAALA 190
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 1-189 3.09e-48

Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family includes bacterial and eukaryotic NAD(P)H dehydrogenase (quinone) EC:1.6.99.2. These enzymes catalyze the NAD(P)H-dependent two-electron reductions of quinones and protect cells against damage by free radicals and reactive oxygen species. This enzyme uses a FAD co-factor. The equation for this reaction is:- NAD(P)H + acceptor <=> NAD(P)(+) + reduced acceptor. This enzyme is also involved in the bioactivation of prodrugs used in chemotherapy. The family also includes acyl carrier protein phosphodiesterase EC:3.1.4.14. This enzyme converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine residue from ACP. This family is related to pfam03358 and pfam00258.


Pssm-ID: 426816 [Multi-domain]  Cd Length: 193  Bit Score: 155.57  E-value: 3.09e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446606104    1 MKHVIVYAHPNTESFNHAILETVKSELEGNGHEVRVRDLYELnFNPVLGASDFISFSQGNTPEDIKEEQEHISWADSITF 80
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYAL-FLPVLDAEDLADLTYPQGAADVESEQEELLAADVIVF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446606104   81 IYPVWWAGLPAILKGYVDRVFSHGFAYAYGENGIEKLLSGK-KGLLLSTMGNSKEAYTAGGM----FDAMKKTVDvGIFE 155
Cdd:pfam02525  80 QFPLYWFSVPALLKGWIDRVLRAGFAFKYEEGGPGGGGLLGkKVLVIVTTGGPEYAYGKGGYngfsLDELLPYLR-GILG 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 446606104  156 FTGIETIEHTFYTSVPSVDDS-VRKQYLEEVKDVV 189
Cdd:pfam02525 159 FCGITDLPPFAVEGTAGPEDEaALAEALERYEERL 193
PRK09739 PRK09739
NAD(P)H oxidoreductase;
1-183 8.72e-29

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 105.94  E-value: 8.72e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446606104   1 MKHVIVYAHPNTESFNHAILETVKSELEGNGHEVRVRDLYELNFNPVLGASDFISFSQGNTP--EDIKEEQEHISWADSI 78
Cdd:PRK09739   4 MRIYLVWAHPRHDSLTAKVAEAIHQRAQERGHQVEELDLYRSGFDPVLTPEDEPDWKNPDKRysPEVHQLYSELLEHDAL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446606104  79 TFIYPVWWAGLPAILKGYVDRVFSHGFAYaygenGIEKLLSGKKGLLLSTMGNSKEAYTAGGMFDAMKKTVDVGIFEFTG 158
Cdd:PRK09739  84 VFVFPLWWYSFPAMLKGYIDRVWNNGLAY-----GDGHKLPFNKVRWVALVGGSKESFVKRGWEKNMSDYLNVGMASYLG 158

                        170       180
                 ....*....|....*....|....*.
gi 446606104 159 IETIEHTF-YTSVPSVDDSVRKQYLE 183
Cdd:PRK09739 159 IEDSDVTFlYNTLVFDGEELHASHYQ 184
 
Name Accession Description Interval E-value
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 2-193 1.03e-75

Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction only];


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 225.49  E-value: 1.03e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446606104   2 KHVIVYAHPNTESFNHAILETVKSELEGNGHEVRVRDLYELNFNPVLGASDFisFSQGNTPEDIKEEQEHISWADSITFI 81
Cdd:COG2249    1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAADF--YRDGPLPIDVAAEQELLLWADHLVFQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446606104  82 YPVWWAGLPAILKGYVDRVFSHGFAYAYGENGIEKLLSGKKGLLLSTMGNSKEAYTAGGMFDAMKKTVDVGIFEFTGIET 161
Cdd:COG2249   79 FPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGPIEELLFRGTLGYCGMKV 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 446606104 162 IEHTFYTSVPSVDDSVRKQYLEEVKDVVNRAF 193
Cdd:COG2249  159 LPPFVLYGVDRSSDEERAAWLERVRELLAALA 190
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 1-189 3.09e-48

Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family includes bacterial and eukaryotic NAD(P)H dehydrogenase (quinone) EC:1.6.99.2. These enzymes catalyze the NAD(P)H-dependent two-electron reductions of quinones and protect cells against damage by free radicals and reactive oxygen species. This enzyme uses a FAD co-factor. The equation for this reaction is:- NAD(P)H + acceptor <=> NAD(P)(+) + reduced acceptor. This enzyme is also involved in the bioactivation of prodrugs used in chemotherapy. The family also includes acyl carrier protein phosphodiesterase EC:3.1.4.14. This enzyme converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine residue from ACP. This family is related to pfam03358 and pfam00258.


Pssm-ID: 426816 [Multi-domain]  Cd Length: 193  Bit Score: 155.57  E-value: 3.09e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446606104    1 MKHVIVYAHPNTESFNHAILETVKSELEGNGHEVRVRDLYELnFNPVLGASDFISFSQGNTPEDIKEEQEHISWADSITF 80
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYAL-FLPVLDAEDLADLTYPQGAADVESEQEELLAADVIVF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446606104   81 IYPVWWAGLPAILKGYVDRVFSHGFAYAYGENGIEKLLSGK-KGLLLSTMGNSKEAYTAGGM----FDAMKKTVDvGIFE 155
Cdd:pfam02525  80 QFPLYWFSVPALLKGWIDRVLRAGFAFKYEEGGPGGGGLLGkKVLVIVTTGGPEYAYGKGGYngfsLDELLPYLR-GILG 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 446606104  156 FTGIETIEHTFYTSVPSVDDS-VRKQYLEEVKDVV 189
Cdd:pfam02525 159 FCGITDLPPFAVEGTAGPEDEaALAEALERYEERL 193
PRK09739 PRK09739
NAD(P)H oxidoreductase;
1-183 8.72e-29

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 105.94  E-value: 8.72e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446606104   1 MKHVIVYAHPNTESFNHAILETVKSELEGNGHEVRVRDLYELNFNPVLGASDFISFSQGNTP--EDIKEEQEHISWADSI 78
Cdd:PRK09739   4 MRIYLVWAHPRHDSLTAKVAEAIHQRAQERGHQVEELDLYRSGFDPVLTPEDEPDWKNPDKRysPEVHQLYSELLEHDAL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446606104  79 TFIYPVWWAGLPAILKGYVDRVFSHGFAYaygenGIEKLLSGKKGLLLSTMGNSKEAYTAGGMFDAMKKTVDVGIFEFTG 158
Cdd:PRK09739  84 VFVFPLWWYSFPAMLKGYIDRVWNNGLAY-----GDGHKLPFNKVRWVALVGGSKESFVKRGWEKNMSDYLNVGMASYLG 158

                        170       180
                 ....*....|....*....|....*.
gi 446606104 159 IETIEHTF-YTSVPSVDDSVRKQYLE 183
Cdd:PRK09739 159 IEDSDVTFlYNTLVFDGEELHASHYQ 184
PRK00871 PRK00871
glutathione-regulated potassium-efflux system oxidoreductase KefF;
4-110 4.23e-13

glutathione-regulated potassium-efflux system oxidoreductase KefF;


Pssm-ID: 234852  Cd Length: 176  Bit Score: 64.42  E-value: 4.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446606104   4 VIVYAHPNTE--SFNHAILETVKSeLEgnghEVRVRDLYEL--NFNPvlgasdfisfsqgntpeDIKEEQEHISWADSIT 79
Cdd:PRK00871   3 LIIYAHPYPHhsHANKRMLEQART-LE----GVEIRSLYQLypDFNI-----------------DIAAEQEALSRADLIV 60

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446606104  80 FIYPVWWAGLPAILKGYVDRVFSHGFAYAYG 110
Cdd:PRK00871  61 WQHPMQWYSIPPLLKLWIDKVLSHGWAYGHG 91
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 2-102 1.09e-09

Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and conversion];


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 54.94  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446606104   2 KHVIVYAHPNTESFNHAILETVKSELEGNGHEVRVRDLYELNFNPVLGASDFISFSQGntpEDIKEEQEHISWADSITFI 81
Cdd:COG0655    1 KILVINGSPRKNGNTAALAEAVAEGAEEAGAEVELIRLADLDIKPCIGCGGTGKCVIK---DDMNAIYEKLLEADGIIFG 77

                         90       100
                 ....*....|....*....|.
gi 446606104  82 YPVWWAGLPAILKGYVDRVFS 102
Cdd:COG0655   78 SPTYFGNMSAQLKAFIDRLYA 98
FMN_red pfam03358
NADPH-dependent FMN reductase;
1-101 1.49e-08

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 51.47  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446606104    1 MKHVIVYAHPNTESFNHAILETVKSELEgNGHEVRVRDLYELNFnPVLGASDFisfSQGNTPEDIKEEQEHISWADSITF 80
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLE-EGAEVELIDLADLIL-PLCDEDLE---EEQGDPDDVQELREKIAAADAIII 75

                          90       100
                  ....*....|....*....|.
gi 446606104   81 IYPVWWAGLPAILKGYVDRVF 101
Cdd:pfam03358  76 VTPEYNGSVSGLLKNAIDWLS 96
PRK04930 PRK04930
glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional
 2-140 1.54e-08

glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional


Pssm-ID: 179895 [Multi-domain]  Cd Length: 184  Bit Score: 51.93  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446606104   2 KHVIVYAHPNTES--FNHAILETVKSeLEgnghEVRVRDLYEL--NFnpvlgasdFIsfsqgntpeDIKEEQEHISWADS 77
Cdd:PRK04930   7 KVLLLYAHPESQDsvANRVLLKPAQQ-LE----HVTVHDLYAHypDF--------FI---------DIPHEQALLREHDV 64

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446606104  78 ITFIYPVWWAGLPAILKGYVDRVFSHGFAYAYGENGIEkllsGKKGLLLSTMGNSKEAYTAGG 140
Cdd:PRK04930  65 IVFQHPLYTYSCPALLKEWLDRVLSRGFASGPGGNALA----GKYWRSVITTGEPESAYRYDG 123
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
1-107 7.18e-07

NAD(P)H-dependent FMN reductase [Energy production and conversion];


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 47.07  E-value: 7.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446606104   1 MKHVIVYAHPNTESFNHAILETVKSELEGNGHEVRVRDLYELN---FNPVLGAsdfisfsqGNTPEDIKEEQEHISWADS 77
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPAAGAEVELIDLRDLDlplYDEDLEA--------DGAPPAVKALREAIAAADG 72

                         90       100       110
                 ....*....|....*....|....*....|
gi 446606104  78 ITFIYPVWWAGLPAILKGYVDRVFSHGFAY 107
Cdd:COG0431   73 VVIVTPEYNGSYPGVLKNALDWLSRSELAG 102
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
31-113 1.15e-03

FMN-dependent NADH-azoreductase [Energy production and conversion];


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 38.19  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446606104  31 GHEVRVRDLYELNFnPVLGASDFISFS---QGNTPEDIKEEQ------EHISWADSITFIYPVWWAGLPAILKGYVDRVF 101
Cdd:COG1182   35 DDEVTYRDLAAEPL-PHLDGAWLAAFFtpaEGRTPEQQAALAlsdeliDELLAADVIVIGAPMYNFGIPSQLKAWIDHIA 113

                         90
                 ....*....|..
gi 446606104 102 SHGFAYAYGENG 113
Cdd:COG1182  114 RAGRTFRYTENG 125
PRK00170 PRK00170
azoreductase; Reviewed
 31-115 2.01e-03

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 37.57  E-value: 2.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446606104  31 GHEVRVRDLYElNFNPVLGASDFISFSQGNTPEDIKEEQ---------EHISWADSITFIYPVWWAGLPAILKGYVDRVF 101
Cdd:PRK00170  35 DDEVTVRDLAA-EPIPVLDGEVVGALGKSAETLTPRQQEavalsdellEEFLAADKIVIAAPMYNFSIPTQLKAYIDLIA 113

                         90
                 ....*....|....
gi 446606104 102 SHGFAYAYGENGIE 115
Cdd:PRK00170 114 RAGKTFRYTENGPV 127
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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