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Conserved domains on  [gi|537194877|gb|ERE77940|]
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ribosyldihydronicotinamide dehydrogenase [quinone]-like protein [Cricetulus griseus]

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)+; similar to Escherichia coli NADPH:quinone oxidoreductase MdaB

CATH:  3.40.50.360
EC:  1.6.99.-|1.-.-.-
Gene Ontology:  GO:0008753|GO:0009055|GO:0010181
PubMed:  25372605|24699637|16630630|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 ...
 11-222 8.42e-65

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


:

Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 199.30  E-value: 8.42e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537194877  11 KVLIVYAHQEPMSFNGSLKKVAVEELSKQGCTVTVSDLYAMNFEPRATRNDItgslsnpevfrygieayeaYKKTALTSD 90
Cdd:COG2249    1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAADF-------------------YRDGPLPID 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537194877  91 ILEEQKKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDIPGFYDSGLLKGKLALLSLTTGGTAEMYTKTGVSGD 170
Cdd:COG2249   62 VAAEQELLLWADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGP 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 537194877 171 FRYFlwpLQHGTLHFCGFKVLAPQISFGIDVSSEEERKVMVASWAKRLKSIW 222
Cdd:COG2249  142 IEEL---LFRGTLGYCGMKVLPPFVLYGVDRSSDEERAAWLERVRELLAALA 190
 
Name Accession Description Interval E-value
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 11-222 8.42e-65

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 199.30  E-value: 8.42e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537194877  11 KVLIVYAHQEPMSFNGSLKKVAVEELSKQGCTVTVSDLYAMNFEPRATRNDItgslsnpevfrygieayeaYKKTALTSD 90
Cdd:COG2249    1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAADF-------------------YRDGPLPID 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537194877  91 ILEEQKKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDIPGFYDSGLLKGKLALLSLTTGGTAEMYTKTGVSGD 170
Cdd:COG2249   62 VAAEQELLLWADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGP 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 537194877 171 FRYFlwpLQHGTLHFCGFKVLAPQISFGIDVSSEEERKVMVASWAKRLKSIW 222
Cdd:COG2249  142 IEEL---LFRGTLGYCGMKVLPPFVLYGVDRSSDEERAAWLERVRELLAALA 190
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 10-218 4.49e-53

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: 169.82  E-value: 4.49e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537194877   10 KKVLIVYAHQEPMSFNGSLKKVAVEELSKQGCTVTVSDLYAMnFEPRATRNDITGsLSNPEVFrygieayeaykktaltS 89
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYAL-FLPVLDAEDLAD-LTYPQGA----------------A 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537194877   90 DILEEQKKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDIP-GFYDSGLLKGKLALLSLTTGGTAEMYTKTGVS 168
Cdd:pfam02525  63 DVESEQEELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYEeGGPGGGGLLGKKVLVIVTTGGPEYAYGKGGYN 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 537194877  169 G-DFRYFLWPLqHGTLHFCGFKVLAPQISFGIDV-SSEEERKVMVASWAKRL 218
Cdd:pfam02525 143 GfSLDELLPYL-RGILGFCGITDLPPFAVEGTAGpEDEAALAEALERYEERL 193
PRK04930 PRK04930
glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional
 1-166 2.76e-18

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


Pssm-ID: 179895 [Multi-domain]  Cd Length: 184  Bit Score: 79.28  E-value: 2.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537194877   1 MHTPPsiyckKVLIVYAHQEPMS--FNGSLKKvAVEELSKqgctVTVSDLYAmnfepratrnditgslSNPEVFrygIea 78
Cdd:PRK04930   2 MSQPP-----KVLLLYAHPESQDsvANRVLLK-PAQQLEH----VTVHDLYA----------------HYPDFF---I-- 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537194877  79 yeaykktaltsDILEEQKKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDIPG------FYDSgllkgklallS 152
Cdd:PRK04930  51 -----------DIPHEQALLREHDVIVFQHPLYTYSCPALLKEWLDRVLSRGFASGPGGnalagkYWRS----------V 109

                        170
                 ....*....|....
gi 537194877 153 LTTGGTAEMYTKTG 166
Cdd:PRK04930 110 ITTGEPESAYRYDG 123
 
Name Accession Description Interval E-value
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 11-222 8.42e-65

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 199.30  E-value: 8.42e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537194877  11 KVLIVYAHQEPMSFNGSLKKVAVEELSKQGCTVTVSDLYAMNFEPRATRNDItgslsnpevfrygieayeaYKKTALTSD 90
Cdd:COG2249    1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAADF-------------------YRDGPLPID 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537194877  91 ILEEQKKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDIPGFYDSGLLKGKLALLSLTTGGTAEMYTKTGVSGD 170
Cdd:COG2249   62 VAAEQELLLWADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGYGGGYPGGLLKGKKALLVVTTGGPEEAYSRLGYGGP 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 537194877 171 FRYFlwpLQHGTLHFCGFKVLAPQISFGIDVSSEEERKVMVASWAKRLKSIW 222
Cdd:COG2249  142 IEEL---LFRGTLGYCGMKVLPPFVLYGVDRSSDEERAAWLERVRELLAALA 190
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 10-218 4.49e-53

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: 169.82  E-value: 4.49e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537194877   10 KKVLIVYAHQEPMSFNGSLKKVAVEELSKQGCTVTVSDLYAMnFEPRATRNDITGsLSNPEVFrygieayeaykktaltS 89
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYAL-FLPVLDAEDLAD-LTYPQGA----------------A 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537194877   90 DILEEQKKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDIP-GFYDSGLLKGKLALLSLTTGGTAEMYTKTGVS 168
Cdd:pfam02525  63 DVESEQEELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYEeGGPGGGGLLGKKVLVIVTTGGPEYAYGKGGYN 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 537194877  169 G-DFRYFLWPLqHGTLHFCGFKVLAPQISFGIDV-SSEEERKVMVASWAKRL 218
Cdd:pfam02525 143 GfSLDELLPYL-RGILGFCGITDLPPFAVEGTAGpEDEAALAEALERYEERL 193
PRK04930 PRK04930
glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional
 1-166 2.76e-18

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


Pssm-ID: 179895 [Multi-domain]  Cd Length: 184  Bit Score: 79.28  E-value: 2.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537194877   1 MHTPPsiyckKVLIVYAHQEPMS--FNGSLKKvAVEELSKqgctVTVSDLYAmnfepratrnditgslSNPEVFrygIea 78
Cdd:PRK04930   2 MSQPP-----KVLLLYAHPESQDsvANRVLLK-PAQQLEH----VTVHDLYA----------------HYPDFF---I-- 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537194877  79 yeaykktaltsDILEEQKKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDIPG------FYDSgllkgklallS 152
Cdd:PRK04930  51 -----------DIPHEQALLREHDVIVFQHPLYTYSCPALLKEWLDRVLSRGFASGPGGnalagkYWRS----------V 109

                        170
                 ....*....|....
gi 537194877 153 LTTGGTAEMYTKTG 166
Cdd:PRK04930 110 ITTGEPESAYRYDG 123
PRK09739 PRK09739
NAD(P)H oxidoreductase;
10-133 6.42e-17

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 75.89  E-value: 6.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537194877  10 KKVLIVYAHQEPMSFNGSLKKVAVEELSKQGCTVTVSDLYAMNFEPRATRNDiTGSLSNPEVfRYgieayeaykktalTS 89
Cdd:PRK09739   4 MRIYLVWAHPRHDSLTAKVAEAIHQRAQERGHQVEELDLYRSGFDPVLTPED-EPDWKNPDK-RY-------------SP 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 537194877  90 DILEEQKKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAF 133
Cdd:PRK09739  69 EVHQLYSELLEHDALVFVFPLWWYSFPAMLKGYIDRVWNNGLAY 112
PRK00871 PRK00871
glutathione-regulated potassium-efflux system oxidoreductase KefF;
90-224 5.73e-12

glutathione-regulated potassium-efflux system oxidoreductase KefF;


Pssm-ID: 234852  Cd Length: 176  Bit Score: 62.11  E-value: 5.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537194877  90 DILEEQKKVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDIPGfydsGLLKGKLALLSLTTGGtAEMYTKTGVSG 169
Cdd:PRK00871  45 DIAAEQEALSRADLIVWQHPMQWYSIPPLLKLWIDKVLSHGWAYGHGG----TALHGKHLLWAVTTGG-GESHFEIGAHP 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 537194877 170 DFRYFLWPLQhGTLHFCGFKVLAPQISFGIDVSSEEERKVMVASWAKRLKSiWKE 224
Cdd:PRK00871 120 GFDVLSQPLQ-ATALYCGLNWLPPFAMHCTFICDDETLEGQARHYKQRLLE-WQE 172
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 11-140 1.80e-06

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 46.85  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537194877  11 KVLIVYahqepmsfnGSLKK---------VAVEELSKQGCTVTVSDLYAMNFEPratrnditgslsnpevfrygIEAYEA 81
Cdd:COG0655    1 KILVIN---------GSPRKngntaalaeAVAEGAEEAGAEVELIRLADLDIKP--------------------CIGCGG 51

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 537194877  82 YKKTALTSDILEEQKKVQEADLVIFQFPLYWFSVPAILKGWMDRvlCQGFAFDIPGFYD 140
Cdd:COG0655   52 TGKCVIKDDMNAIYEKLLEADGIIFGSPTYFGNMSAQLKAFIDR--LYALWAKGKLLKG 108
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
10-127 3.19e-06

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 46.28  E-value: 3.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537194877  10 KKVLIVYAH-QEPMSFNGSLKKVAVEELSKQ--GCTVTVSDLYAMNFePRATRNDITGSLSNPEvfryGIEAYEAyKKTA 86
Cdd:COG1182    2 MKLLHIDSSpRGEGSVSRRLADAFVAALRAAhpDDEVTYRDLAAEPL-PHLDGAWLAAFFTPAE----GRTPEQQ-AALA 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 537194877  87 LTSDILEEqkkVQEADLVIFQFPLYWFSVPAILKGWMDRVL 127
Cdd:COG1182   76 LSDELIDE---LLAADVIVIGAPMYNFGIPSQLKAWIDHIA 113
PRK00170 PRK00170
azoreductase; Reviewed
 84-133 3.07e-05

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 43.34  E-value: 3.07e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 537194877  84 KTALTSDILEEqkkVQEADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAF 133
Cdd:PRK00170  73 AVALSDELLEE---FLAADKIVIAAPMYNFSIPTQLKAYIDLIARAGKTF 119
PRK13556 PRK13556
FMN-dependent NADH-azoreductase;
42-124 1.41e-04

FMN-dependent NADH-azoreductase;


Pssm-ID: 184140 [Multi-domain]  Cd Length: 208  Bit Score: 41.67  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537194877  42 TVTVSDLYAMNFePRATRNDITGSLSNPEvfryGIEAYEAYKKTALTSDILEEQkkVQEADLVIFQFPLYWFSVPAILKG 121
Cdd:PRK13556  38 TVVELDLYKEEL-PYVGVDMINGTFKAGK----GFELTEEEAKAVAVADKYLNQ--FLEADKVVFAFPLWNFTIPAVLHT 110


                 ...
gi 537194877 122 WMD 124
Cdd:PRK13556 111 YID 113
FMN_red pfam03358
NADPH-dependent FMN reductase;
11-126 1.57e-04

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 40.68  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537194877   11 KVLIVYAHQEPMSFNGSLKKVAVEELsKQGCTVTVSDLYAMNFePRATRnDITGSLSNPEVFRygiEAYEaykktaltsd 90
Cdd:pfam03358   2 KILAISGSPRKGSNTRKLARWAAELL-EEGAEVELIDLADLIL-PLCDE-DLEEEQGDPDDVQ---ELRE---------- 65

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 537194877   91 ileeqkKVQEADLVIFQFPLYWFSVPAILKGWMDRV 126
Cdd:pfam03358  66 ------KIAAADAIIIVTPEYNGSVSGLLKNAIDWL 95
 
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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