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Conserved domains on  [gi|45387531|ref|NP_991105|]
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NAD(P)H dehydrogenase [quinone] 1 isoform 2 [Danio rerio]

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 ...
 6-212 2.81e-67

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


:

Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 207.00  E-value: 2.81e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45387531   6 ALIVYAHQSPASFNAAARDVAVQALTKKGYKVLVSDLYAMKFKASATAEDIkgdlqnpehfvynnemmvaWKEGRLSDDV 85
Cdd:COG2249   2 ILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAADF-------------------YRDGPLPIDV 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45387531  86 AEEQHKVEQADLIIFQYPLYWFTIPAIMKGWIDRVLTQGFAFSMQNMYDNGIFKNKRAMLSFTTGGMESMYKDDSLHGDI 165
Cdd:COG2249  63 AAEQELLLWADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGPI 142

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 45387531 166 NILlwpLQNGVLRFCGFQVLAPQIFWSPAYTPPEGRAAMLDGWRERL 212
Cdd:COG2249 143 EEL---LFRGTLGYCGMKVLPPFVLYGVDRSSDEERAAWLERVRELL 186
 
Name Accession Description Interval E-value
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 6-212 2.81e-67

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 207.00  E-value: 2.81e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45387531   6 ALIVYAHQSPASFNAAARDVAVQALTKKGYKVLVSDLYAMKFKASATAEDIkgdlqnpehfvynnemmvaWKEGRLSDDV 85
Cdd:COG2249   2 ILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAADF-------------------YRDGPLPIDV 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45387531  86 AEEQHKVEQADLIIFQYPLYWFTIPAIMKGWIDRVLTQGFAFSMQNMYDNGIFKNKRAMLSFTTGGMESMYKDDSLHGDI 165
Cdd:COG2249  63 AAEQELLLWADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGPI 142

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 45387531 166 NILlwpLQNGVLRFCGFQVLAPQIFWSPAYTPPEGRAAMLDGWRERL 212
Cdd:COG2249 143 EEL---LFRGTLGYCGMKVLPPFVLYGVDRSSDEERAAWLERVRELL 186
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 4-212 9.00e-52

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: 167.90  E-value: 9.00e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45387531     4 KTALIVYAHQSPASFNAAARDVAVQALTKKGYKVLVSDLYAMkFKASATAEDIKGdlQNPEHFVYnnemmvawkegrlsd 83
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYAL-FLPVLDAEDLAD--LTYPQGAA--------------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45387531    84 DVAEEQHKVEQADLIIFQYPLYWFTIPAIMKGWIDRVLTQGFAFSM-QNMYDNGIFKNKRAMLSFTTGGMESMYKDDSLH 162
Cdd:pfam02525  63 DVESEQEELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYeEGGPGGGGLLGKKVLVIVTTGGPEYAYGKGGYN 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 45387531   163 G-DINILLWPLQnGVLRFCGFQVLAPQIFWSPAY-TPPEGRAAMLDGWRERL 212
Cdd:pfam02525 143 GfSLDELLPYLR-GILGFCGITDLPPFAVEGTAGpEDEAALAEALERYEERL 193
PRK09739 PRK09739
NAD(P)H oxidoreductase;
1-127 2.02e-17

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 78.21  E-value: 2.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45387531    1 MAQKTALIVYAHQSPASFNAAARDVAVQALTKKGYKVLVSDLYAMKFKASATAEDiKGDLQNPEHfvynnemmvawkegR 80
Cdd:PRK09739   1 MQSMRIYLVWAHPRHDSLTAKVAEAIHQRAQERGHQVEELDLYRSGFDPVLTPED-EPDWKNPDK--------------R 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 45387531   81 LSDDVAEEQHKVEQADLIIFQYPLYWFTIPAIMKGWIDRVLTQGFAF 127
Cdd:PRK09739  66 YSPEVHQLYSELLEHDALVFVFPLWWYSFPAMLKGYIDRVWNNGLAY 112
 
Name Accession Description Interval E-value
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 6-212 2.81e-67

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 207.00  E-value: 2.81e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45387531   6 ALIVYAHQSPASFNAAARDVAVQALTKKGYKVLVSDLYAMKFKASATAEDIkgdlqnpehfvynnemmvaWKEGRLSDDV 85
Cdd:COG2249   2 ILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAADF-------------------YRDGPLPIDV 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45387531  86 AEEQHKVEQADLIIFQYPLYWFTIPAIMKGWIDRVLTQGFAFSMQNMYDNGIFKNKRAMLSFTTGGMESMYKDDSLHGDI 165
Cdd:COG2249  63 AAEQELLLWADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGPI 142

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 45387531 166 NILlwpLQNGVLRFCGFQVLAPQIFWSPAYTPPEGRAAMLDGWRERL 212
Cdd:COG2249 143 EEL---LFRGTLGYCGMKVLPPFVLYGVDRSSDEERAAWLERVRELL 186
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 4-212 9.00e-52

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: 167.90  E-value: 9.00e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45387531     4 KTALIVYAHQSPASFNAAARDVAVQALTKKGYKVLVSDLYAMkFKASATAEDIKGdlQNPEHFVYnnemmvawkegrlsd 83
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYAL-FLPVLDAEDLAD--LTYPQGAA--------------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45387531    84 DVAEEQHKVEQADLIIFQYPLYWFTIPAIMKGWIDRVLTQGFAFSM-QNMYDNGIFKNKRAMLSFTTGGMESMYKDDSLH 162
Cdd:pfam02525  63 DVESEQEELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYeEGGPGGGGLLGKKVLVIVTTGGPEYAYGKGGYN 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 45387531   163 G-DINILLWPLQnGVLRFCGFQVLAPQIFWSPAY-TPPEGRAAMLDGWRERL 212
Cdd:pfam02525 143 GfSLDELLPYLR-GILGFCGITDLPPFAVEGTAGpEDEAALAEALERYEERL 193
PRK09739 PRK09739
NAD(P)H oxidoreductase;
1-127 2.02e-17

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 78.21  E-value: 2.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45387531    1 MAQKTALIVYAHQSPASFNAAARDVAVQALTKKGYKVLVSDLYAMKFKASATAEDiKGDLQNPEHfvynnemmvawkegR 80
Cdd:PRK09739   1 MQSMRIYLVWAHPRHDSLTAKVAEAIHQRAQERGHQVEELDLYRSGFDPVLTPED-EPDWKNPDK--------------R 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 45387531   81 LSDDVAEEQHKVEQADLIIFQYPLYWFTIPAIMKGWIDRVLTQGFAF 127
Cdd:PRK09739  66 YSPEVHQLYSELLEHDALVFVFPLWWYSFPAMLKGYIDRVWNNGLAY 112
PRK00871 PRK00871
glutathione-regulated potassium-efflux system oxidoreductase KefF;
84-187 1.32e-16

glutathione-regulated potassium-efflux system oxidoreductase KefF;


Pssm-ID: 234852  Cd Length: 176  Bit Score: 75.59  E-value: 1.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45387531   84 DVAEEQHKVEQADLIIFQYPLYWFTIPAIMKGWIDRVLTQGFAFSMqnmydNGI-FKNKRAMLSFTTGGMESMYKDDSlH 162
Cdd:PRK00871  45 DIAAEQEALSRADLIVWQHPMQWYSIPPLLKLWIDKVLSHGWAYGH-----GGTaLHGKHLLWAVTTGGGESHFEIGA-H 118

                         90       100
                 ....*....|....*....|....*
gi 45387531  163 GDINILLWPLQNGVLrFCGFQVLAP 187
Cdd:PRK00871 119 PGFDVLSQPLQATAL-YCGLNWLPP 142
PRK04930 PRK04930
glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional
 7-212 2.86e-16

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


Pssm-ID: 179895 [Multi-domain]  Cd Length: 184  Bit Score: 74.65  E-value: 2.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45387531    7 LIVYAHqsPASFNAAARDVAVQALTKKGYkVLVSDLYAmkfkasataedikgdlQNPEHFVynnemmvawkegrlsdDVA 86
Cdd:PRK04930   9 LLLYAH--PESQDSVANRVLLKPAQQLEH-VTVHDLYA----------------HYPDFFI----------------DIP 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45387531   87 EEQHKVEQADLIIFQYPLYWFTIPAIMKGWIDRVLTQGFAFSMQNMYDNGifKNKRAMLsfTTGGMESMYKDDSLHgdin 166
Cdd:PRK04930  54 HEQALLREHDVIVFQHPLYTYSCPALLKEWLDRVLSRGFASGPGGNALAG--KYWRSVI--TTGEPESAYRYDGYN---- 125

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 45387531  167 ilLWPLQNgVLR-------FCGFQVLAPQIFWSPAYTPPEGRAAMLDGWRERL 212
Cdd:PRK04930 126 --RYPMSD-ILRpfeltaaMCRMHWLSPIIIYWARRQSPEELASHARAYGDWL 175
PRK00170 PRK00170
azoreductase; Reviewed
 67-159 3.06e-09

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 55.29  E-value: 3.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45387531   67 VYNNEMMVAWkegRLSDDV--AEEQHKVE----------QADLIIFQYPLYWFTIPAIMKGWIDRVLTQGFAFSMQNMYD 134
Cdd:PRK00170  50 VLDGEVVGAL---GKSAETltPRQQEAVAlsdelleeflAADKIVIAAPMYNFSIPTQLKAYIDLIARAGKTFRYTENGP 126

                         90       100
                 ....*....|....*....|....*
gi 45387531  135 NGIFKNKRAMLSFTTGGmesMYKDD 159
Cdd:PRK00170 127 VGLVTGKKALLITSRGG---IHKDG 148
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
80-152 1.67e-08

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 53.21  E-value: 1.67e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45387531  80 RLSDDVAEEqhkVEQADLIIFQYPLYWFTIPAIMKGWIDRVLTQGFAFSmqnmYDN----GIFKNKRAMLSFTTGGM 152
Cdd:COG1182  75 ALSDELIDE---LLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGRTFR----YTEngpvGLLTGKKAVVITARGGV 144
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 83-151 3.71e-07

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 49.16  E-value: 3.71e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45387531  83 DDVAEEQHKVEQADLIIFQYPLYWFTIPAIMKGWIDRvlTQGFAFSmqnmydNGIFKNKRAMLsFTTGG 151
Cdd:COG0655  59 DDMNAIYEKLLEADGIIFGSPTYFGNMSAQLKAFIDR--LYALWAK------GKLLKGKVGAV-FTTGG 118
FMN_red pfam03358
NADPH-dependent FMN reductase;
76-152 2.25e-05

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 43.38  E-value: 2.25e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45387531    76 WKEGRLSDDVAEEQHKVEQADLIIFQYPLYWFTIPAIMKGWIDRvltqgfaFSMQnmYDNGIFKNKRAMLSFTTGGM 152
Cdd:pfam03358  51 EEEQGDPDDVQELREKIAAADAIIIVTPEYNGSVSGLLKNAIDW-------LSRL--RGGKELRGKPVAIVSTGGGR 118
PRK13556 PRK13556
FMN-dependent NADH-azoreductase;
54-154 1.48e-03

FMN-dependent NADH-azoreductase;


Pssm-ID: 184140 [Multi-domain]  Cd Length: 208  Bit Score: 38.97  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45387531   54 EDIKGDLQNPEHFVYNNEMMVA-WKEGRLSDDVAEEQHKVE----------QADLIIFQYPLYWFTIPAIMKGWIDRVLT 122
Cdd:PRK13556  38 TVVELDLYKEELPYVGVDMINGtFKAGKGFELTEEEAKAVAvadkylnqflEADKVVFAFPLWNFTIPAVLHTYIDYLNR 117

                         90       100       110
                 ....*....|....*....|....*....|..
gi 45387531  123 QGFAFSMQNMYDNGIFKNKRAMLSFTTGGMES 154
Cdd:PRK13556 118 AGKTFKYTPEGPVGLIGDKKVALLNARGGVYS 149
 
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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