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Conserved domains on  [gi|564391223|ref|XP_006253930|]
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ribosyldihydronicotinamide dehydrogenase [quinone] isoform X2 [Rattus norvegicus]

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

 Zoom to residue level

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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 ...
 1-195 2.38e-63

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


:

Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 194.67  E-value: 2.38e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391223   1 MKQVAVEELSKQGCTVTVSDLYTMNFEPRATRNDvtgalsnpevfkygieayeAYKKKALTSDILEEQRKVQEADLVIFQ 80
Cdd:COG2249   18 LAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAAD-------------------FYRDGPLPIDVAAEQELLLWADHLVFQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391223  81 FPLYWFSVPAILKGWMDRVLCQGFAFDVPGFYDSGFLKDKLALLSFTTGGTAEMYTKAGVNGDFRYFlwpLQHGTLHFCG 160
Cdd:COG2249   79 FPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGPIEEL---LFRGTLGYCG 155

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 564391223 161 FKVLAPQISFGPEVSSEEQRKVMLASWVQRLKSIW 195
Cdd:COG2249  156 MKVLPPFVLYGVDRSSDEERAAWLERVRELLAALA 190
 
Name Accession Description Interval E-value
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 1-195 2.38e-63

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 194.67  E-value: 2.38e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391223   1 MKQVAVEELSKQGCTVTVSDLYTMNFEPRATRNDvtgalsnpevfkygieayeAYKKKALTSDILEEQRKVQEADLVIFQ 80
Cdd:COG2249   18 LAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAAD-------------------FYRDGPLPIDVAAEQELLLWADHLVFQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391223  81 FPLYWFSVPAILKGWMDRVLCQGFAFDVPGFYDSGFLKDKLALLSFTTGGTAEMYTKAGVNGDFRYFlwpLQHGTLHFCG 160
Cdd:COG2249   79 FPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGPIEEL---LFRGTLGYCG 155

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 564391223 161 FKVLAPQISFGPEVSSEEQRKVMLASWVQRLKSIW 195
Cdd:COG2249  156 MKVLPPFVLYGVDRSSDEERAAWLERVRELLAALA 190
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 3-191 4.24e-50

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: 160.96  E-value: 4.24e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391223    3 QVAVEELSKQGCTVTVSDLYTMnFEPRATRNDVTgALSNPEVFKygieayeaykkkaltsDILEEQRKVQEADLVIFQFP 82
Cdd:pfam02525  21 DALVEALKAAGHEVTVRDLYAL-FLPVLDAEDLA-DLTYPQGAA----------------DVESEQEELLAADVIVFQFP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391223   83 LYWFSVPAILKGWMDRVLCQGFAFDVP-GFYDSGFLKDKLALLSFTTGGTAEMYTKAGVNG-DFRYFLWPLqHGTLHFCG 160
Cdd:pfam02525  83 LYWFSVPALLKGWIDRVLRAGFAFKYEeGGPGGGGLLGKKVLVIVTTGGPEYAYGKGGYNGfSLDELLPYL-RGILGFCG 161

                         170       180       190
                  ....*....|....*....|....*....|..
gi 564391223  161 FKVLAPQISFG-PEVSSEEQRKVMLASWVQRL 191
Cdd:pfam02525 162 ITDLPPFAVEGtAGPEDEAALAEALERYEERL 193
PRK04930 PRK04930
glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional
 63-146 1.85e-17

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


Pssm-ID: 179895 [Multi-domain]  Cd Length: 184  Bit Score: 76.58  E-value: 1.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391223  63 DILEEQRKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDVPGfydsGFLKDKLALLSFTTGGTAEMYTKAGVNg 142
Cdd:PRK04930  51 DIPHEQALLREHDVIVFQHPLYTYSCPALLKEWLDRVLSRGFASGPGG----NALAGKYWRSVITTGEPESAYRYDGYN- 125


                 ....
gi 564391223 143 dfRY 146
Cdd:PRK04930 126 --RY 127
 
Name Accession Description Interval E-value
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 1-195 2.38e-63

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 194.67  E-value: 2.38e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391223   1 MKQVAVEELSKQGCTVTVSDLYTMNFEPRATRNDvtgalsnpevfkygieayeAYKKKALTSDILEEQRKVQEADLVIFQ 80
Cdd:COG2249   18 LAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAAD-------------------FYRDGPLPIDVAAEQELLLWADHLVFQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391223  81 FPLYWFSVPAILKGWMDRVLCQGFAFDVPGFYDSGFLKDKLALLSFTTGGTAEMYTKAGVNGDFRYFlwpLQHGTLHFCG 160
Cdd:COG2249   79 FPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGPIEEL---LFRGTLGYCG 155

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 564391223 161 FKVLAPQISFGPEVSSEEQRKVMLASWVQRLKSIW 195
Cdd:COG2249  156 MKVLPPFVLYGVDRSSDEERAAWLERVRELLAALA 190
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 3-191 4.24e-50

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: 160.96  E-value: 4.24e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391223    3 QVAVEELSKQGCTVTVSDLYTMnFEPRATRNDVTgALSNPEVFKygieayeaykkkaltsDILEEQRKVQEADLVIFQFP 82
Cdd:pfam02525  21 DALVEALKAAGHEVTVRDLYAL-FLPVLDAEDLA-DLTYPQGAA----------------DVESEQEELLAADVIVFQFP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391223   83 LYWFSVPAILKGWMDRVLCQGFAFDVP-GFYDSGFLKDKLALLSFTTGGTAEMYTKAGVNG-DFRYFLWPLqHGTLHFCG 160
Cdd:pfam02525  83 LYWFSVPALLKGWIDRVLRAGFAFKYEeGGPGGGGLLGKKVLVIVTTGGPEYAYGKGGYNGfSLDELLPYL-RGILGFCG 161

                         170       180       190
                  ....*....|....*....|....*....|..
gi 564391223  161 FKVLAPQISFG-PEVSSEEQRKVMLASWVQRL 191
Cdd:pfam02525 162 ITDLPPFAVEGtAGPEDEAALAEALERYEERL 193
PRK04930 PRK04930
glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional
 63-146 1.85e-17

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


Pssm-ID: 179895 [Multi-domain]  Cd Length: 184  Bit Score: 76.58  E-value: 1.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391223  63 DILEEQRKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDVPGfydsGFLKDKLALLSFTTGGTAEMYTKAGVNg 142
Cdd:PRK04930  51 DIPHEQALLREHDVIVFQHPLYTYSCPALLKEWLDRVLSRGFASGPGG----NALAGKYWRSVITTGEPESAYRYDGYN- 125


                 ....
gi 564391223 143 dfRY 146
Cdd:PRK04930 126 --RY 127
PRK00871 PRK00871
glutathione-regulated potassium-efflux system oxidoreductase KefF;
63-197 1.24e-15

glutathione-regulated potassium-efflux system oxidoreductase KefF;


Pssm-ID: 234852  Cd Length: 176  Bit Score: 71.35  E-value: 1.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391223  63 DILEEQRKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDVPGFYdsgfLKDKLALLSFTTGGtAEMYTKAGVNG 142
Cdd:PRK00871  45 DIAAEQEALSRADLIVWQHPMQWYSIPPLLKLWIDKVLSHGWAYGHGGTA----LHGKHLLWAVTTGG-GESHFEIGAHP 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564391223 143 DFRYFLWPLQhGTLHFCGFKVLAPQISFGPEVSSEEQRKVMLASWVQRLKSiWKE 197
Cdd:PRK00871 120 GFDVLSQPLQ-ATALYCGLNWLPPFAMHCTFICDDETLEGQARHYKQRLLE-WQE 172
PRK09739 PRK09739
NAD(P)H oxidoreductase;
6-139 2.50e-14

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 68.58  E-value: 2.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391223   6 VEELSKQGCTVTVSDLYTMNFEPRATRNDvTGALSNPEvfkygieayeaykkKALTSDILEEQRKVQEADLVIFQFPLYW 85
Cdd:PRK09739  27 HQRAQERGHQVEELDLYRSGFDPVLTPED-EPDWKNPD--------------KRYSPEVHQLYSELLEHDALVFVFPLWW 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564391223  86 FSVPAILKGWMDRVLCQGFAFDvpgfyDSGFLKDKLALLSFTTGGTAEMYTKAG 139
Cdd:PRK09739  92 YSFPAMLKGYIDRVWNNGLAYG-----DGHKLPFNKVRWVALVGGSKESFVKRG 140
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
6-181 3.91e-09

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 54.37  E-value: 3.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391223   6 VEELSKQ--GCTVTVSDLYTMNFePRATrNDVTGALSNPEvfkygiEAYEAYKKKALT-SDILEEQrkVQEADLVIFQFP 82
Cdd:COG1182   26 VAALRAAhpDDEVTYRDLAAEPL-PHLD-GAWLAAFFTPA------EGRTPEQQAALAlSDELIDE--LLAADVIVIGAP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391223  83 LYWFSVPAILKGWMDRVLCQG--FAFDVPGFydSGFLKDKLALLSFTTGGTaemYTKAGVNG-DF--RYflwpLQHgTLH 157
Cdd:COG1182   96 MYNFGIPSQLKAWIDHIARAGrtFRYTENGP--VGLLTGKKAVVITARGGV---YSGGPAAGmDFqtPY----LRT-VLG 165

                        170       180
                 ....*....|....*....|....*...
gi 564391223 158 FCGFK----VLAPQISFGPEVSSEEQRK 181
Cdd:COG1182  166 FIGITdvefVRAEGTAAGPEAAEAALAA 193
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 1-131 2.49e-07

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 48.77  E-value: 2.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391223   1 MKQVAVEELSKQGCTVTVSDLYTMNFEPratrndvtgalsnpevfkygIEAYEAYKKKALTSDILEEQRKVQEADLVIFQ 80
Cdd:COG0655   18 LAEAVAEGAEEAGAEVELIRLADLDIKP--------------------CIGCGGTGKCVIKDDMNAIYEKLLEADGIIFG 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564391223  81 FPLYWFSVPAILKGWMDRvlCQGFAFDVpgfydsGFLKDKLALLsFTTGGT 131
Cdd:COG0655   78 SPTYFGNMSAQLKAFIDR--LYALWAKG------KLLKGKVGAV-FTTGGH 119
PRK00170 PRK00170
azoreductase; Reviewed
 59-130 7.91e-07

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 47.58  E-value: 7.91e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564391223  59 ALTSDILEEqrkVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDvpgfYDS----GFLKDKLALLSFTTGG 130
Cdd:PRK00170  75 ALSDELLEE---FLAADKIVIAAPMYNFSIPTQLKAYIDLIARAGKTFR----YTEngpvGLVTGKKALLITSRGG 143
FMN_red pfam03358
NADPH-dependent FMN reductase;
69-132 3.37e-04

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 39.53  E-value: 3.37e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564391223   69 RKVQEADLVIFQFPLYWFSVPAILKGWMDRvlcqgfafdVPGFYDSGFLKDKLALLsFTTGGTA 132
Cdd:pfam03358  65 EKIAAADAIIIVTPEYNGSVSGLLKNAIDW---------LSRLRGGKELRGKPVAI-VSTGGGR 118
PRK13556 PRK13556
FMN-dependent NADH-azoreductase;
15-125 3.85e-04

FMN-dependent NADH-azoreductase;


Pssm-ID: 184140 [Multi-domain]  Cd Length: 208  Bit Score: 40.13  E-value: 3.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391223  15 TVTVSDLYTMNFePRATRNDVTGalsnpeVFK--YGIEAYEAYKKKALTSDILEEQrkVQEADLVIFQFPLYWFSVPAIL 92
Cdd:PRK13556  38 TVVELDLYKEEL-PYVGVDMING------TFKagKGFELTEEEAKAVAVADKYLNQ--FLEADKVVFAFPLWNFTIPAVL 108

                         90       100       110
                 ....*....|....*....|....*....|....
gi 564391223  93 KGWMDRVLCQGFAFDVPGFYDSGFLKD-KLALLS 125
Cdd:PRK13556 109 HTYIDYLNRAGKTFKYTPEGPVGLIGDkKVALLN 142
 
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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