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Conserved domains on  [gi|504409251|ref|WP_014596353|]
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NAD(P)H-dependent oxidoreductase [Stutzerimonas stutzeri]

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 ...
 2-220 3.41e-88

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


:

Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 259.77  E-value: 3.41e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251   2 NVLIVYAHPEPRSLNGALKDFTVQRLRTAGHAVQLSDLYAMGWKAPVDARDsldhdlesrfdpsqdsrrAFASGRQSPDI 81
Cdd:COG2249    1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAAD------------------FYRDGPLPIDV 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251  82 AAEQDKLRWADALILQFPLWWFSMPAILKGWVDRVYAYGFAYGVgehsdarwGDRYGEGTMVGKRAMLIVTTGGWASHYS 161
Cdd:COG2249   63 AAEQELLLWADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGY--------GGGYPGGLLKGKKALLVVTTGGPEEAYS 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504409251 162 PRGINGPIDDLLFpiqHGILHYPGFDVLPPFVVYRTSRIDEARFADIREQLGERLDNLW 220
Cdd:COG2249  135 RLGYGGPIEELLF---RGTLGYCGMKVLPPFVLYGVDRSSDEERAAWLERVRELLAALA 190
 
Name Accession Description Interval E-value
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 2-220 3.41e-88

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 259.77  E-value: 3.41e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251   2 NVLIVYAHPEPRSLNGALKDFTVQRLRTAGHAVQLSDLYAMGWKAPVDARDsldhdlesrfdpsqdsrrAFASGRQSPDI 81
Cdd:COG2249    1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAAD------------------FYRDGPLPIDV 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251  82 AAEQDKLRWADALILQFPLWWFSMPAILKGWVDRVYAYGFAYGVgehsdarwGDRYGEGTMVGKRAMLIVTTGGWASHYS 161
Cdd:COG2249   63 AAEQELLLWADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGY--------GGGYPGGLLKGKKALLVVTTGGPEEAYS 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504409251 162 PRGINGPIDDLLFpiqHGILHYPGFDVLPPFVVYRTSRIDEARFADIREQLGERLDNLW 220
Cdd:COG2249  135 RLGYGGPIEELLF---RGTLGYCGMKVLPPFVLYGVDRSSDEERAAWLERVRELLAALA 190
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 1-216 9.41e-63

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: 195.24  E-value: 9.41e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251    1 MNVLIVYAHPEPRSLNGALKDFTVQRLRTAGHAVQLSDLYAMgwkapvdardsldhdlesrFDP--SQDSRRAFASGRQS 78
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYAL-------------------FLPvlDAEDLADLTYPQGA 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251   79 PDIAAEQDKLRWADALILQFPLWWFSMPAILKGWVDRVYAYGFAYGVGEhsdarwgDRYGEGTMVGKRAMLIVTTGGWAS 158
Cdd:pfam02525  62 ADVESEQEELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYEE-------GGPGGGGLLGKKVLVIVTTGGPEY 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251  159 HYSPRGING-PIDDLLFPIqHGILHYPGFDVLPPFVVYRTSRID-EARFADIREQLGERL 216
Cdd:pfam02525 135 AYGKGGYNGfSLDELLPYL-RGILGFCGITDLPPFAVEGTAGPEdEAALAEALERYEERL 193
PRK09739 PRK09739
NAD(P)H oxidoreductase;
1-133 1.76e-30

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 112.49  E-value: 1.76e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251   1 MNVLIVYAHPEPRSLNGALKDFTVQRLRTAGHAVQLSDLYAMGWKAPVDARDSLDHDlesrfDPSQdsrrafasgRQSPD 80
Cdd:PRK09739   4 MRIYLVWAHPRHDSLTAKVAEAIHQRAQERGHQVEELDLYRSGFDPVLTPEDEPDWK-----NPDK---------RYSPE 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504409251  81 IAAEQDKLRWADALILQFPLWWFSMPAILKGWVDRVYAYGFAYGVGE---HSDARW 133
Cdd:PRK09739  70 VHQLYSELLEHDALVFVFPLWWYSFPAMLKGYIDRVWNNGLAYGDGHklpFNKVRW 125
 
Name Accession Description Interval E-value
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 2-220 3.41e-88

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 259.77  E-value: 3.41e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251   2 NVLIVYAHPEPRSLNGALKDFTVQRLRTAGHAVQLSDLYAMGWKAPVDARDsldhdlesrfdpsqdsrrAFASGRQSPDI 81
Cdd:COG2249    1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAAD------------------FYRDGPLPIDV 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251  82 AAEQDKLRWADALILQFPLWWFSMPAILKGWVDRVYAYGFAYGVgehsdarwGDRYGEGTMVGKRAMLIVTTGGWASHYS 161
Cdd:COG2249   63 AAEQELLLWADHLVFQFPLWWYSMPALLKGWIDRVLTPGFAYGY--------GGGYPGGLLKGKKALLVVTTGGPEEAYS 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504409251 162 PRGINGPIDDLLFpiqHGILHYPGFDVLPPFVVYRTSRIDEARFADIREQLGERLDNLW 220
Cdd:COG2249  135 RLGYGGPIEELLF---RGTLGYCGMKVLPPFVLYGVDRSSDEERAAWLERVRELLAALA 190
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 1-216 9.41e-63

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: 195.24  E-value: 9.41e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251    1 MNVLIVYAHPEPRSLNGALKDFTVQRLRTAGHAVQLSDLYAMgwkapvdardsldhdlesrFDP--SQDSRRAFASGRQS 78
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYAL-------------------FLPvlDAEDLADLTYPQGA 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251   79 PDIAAEQDKLRWADALILQFPLWWFSMPAILKGWVDRVYAYGFAYGVGEhsdarwgDRYGEGTMVGKRAMLIVTTGGWAS 158
Cdd:pfam02525  62 ADVESEQEELLAADVIVFQFPLYWFSVPALLKGWIDRVLRAGFAFKYEE-------GGPGGGGLLGKKVLVIVTTGGPEY 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251  159 HYSPRGING-PIDDLLFPIqHGILHYPGFDVLPPFVVYRTSRID-EARFADIREQLGERL 216
Cdd:pfam02525 135 AYGKGGYNGfSLDELLPYL-RGILGFCGITDLPPFAVEGTAGPEdEAALAEALERYEERL 193
PRK09739 PRK09739
NAD(P)H oxidoreductase;
1-133 1.76e-30

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 112.49  E-value: 1.76e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251   1 MNVLIVYAHPEPRSLNGALKDFTVQRLRTAGHAVQLSDLYAMGWKAPVDARDSLDHDlesrfDPSQdsrrafasgRQSPD 80
Cdd:PRK09739   4 MRIYLVWAHPRHDSLTAKVAEAIHQRAQERGHQVEELDLYRSGFDPVLTPEDEPDWK-----NPDK---------RYSPE 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504409251  81 IAAEQDKLRWADALILQFPLWWFSMPAILKGWVDRVYAYGFAYGVGE---HSDARW 133
Cdd:PRK09739  70 VHQLYSELLEHDALVFVFPLWWYSFPAMLKGYIDRVWNNGLAYGDGHklpFNKVRW 125
PRK04930 PRK04930
glutathione-regulated potassium-efflux system ancillary protein KefG; Provisional
 2-218 3.02e-20

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


Pssm-ID: 179895 [Multi-domain]  Cd Length: 184  Bit Score: 85.05  E-value: 3.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251   2 NVLIVYAHPEPRS--LNGALkdftVQRLRTAGHaVQLSDLYAmgwkapvdardsldhdlesrfdpsqdsrrafasgrQSP 79
Cdd:PRK04930   7 KVLLLYAHPESQDsvANRVL----LKPAQQLEH-VTVHDLYA-----------------------------------HYP 46

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251  80 ----DIAAEQDKLRWADALILQFPLWWFSMPAILKGWVDRVYAYGFAYGVGEHSdarwgdrygegtMVGKRAMLIVTTGG 155
Cdd:PRK04930  47 dffiDIPHEQALLREHDVIVFQHPLYTYSCPALLKEWLDRVLSRGFASGPGGNA------------LAGKYWRSVITTGE 114

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251 156 WASHYSPRGING-PIDDLLFPIQ------HgiLHYpgfdvLPPFVVYRTSRIDEARFADIREQLGERLDN 218
Cdd:PRK04930 115 PESAYRYDGYNRyPMSDILRPFEltaamcR--MHW-----LSPIIIYWARRQSPEELASHARAYGDWLAN 177
PRK00871 PRK00871
glutathione-regulated potassium-efflux system oxidoreductase KefF;
80-216 8.15e-19

glutathione-regulated potassium-efflux system oxidoreductase KefF;


Pssm-ID: 234852  Cd Length: 176  Bit Score: 81.37  E-value: 8.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251  80 DIAAEQDKLRWADALILQFPLWWFSMPAILKGWVDRVYAYGFAYGVGEHSdarwgdrygegtMVGKRAMLIVTTGGWASH 159
Cdd:PRK00871  45 DIAAEQEALSRADLIVWQHPMQWYSIPPLLKLWIDKVLSHGWAYGHGGTA------------LHGKHLLWAVTTGGGESH 112

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504409251 160 YSPRGINGpIDDLLFPIQHGILhYPGFDVLPPFVVYRTSRIDEARFADIREQLGERL 216
Cdd:PRK00871 113 FEIGAHPG-FDVLSQPLQATAL-YCGLNWLPPFAMHCTFICDDETLEGQARHYKQRL 167
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
1-170 1.57e-09

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 56.29  E-value: 1.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251   1 MNVLIVYAHP-EPRSLNGALKDFTVQRLRTAGHAVQLS--DLYAM-----------GWKAPVDARDsldhdlesrfdPSQ 66
Cdd:COG1182    2 MKLLHIDSSPrGEGSVSRRLADAFVAALRAAHPDDEVTyrDLAAEplphldgawlaAFFTPAEGRT-----------PEQ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251  67 dsRRAFAsgrQSPDIAAEqdkLRWADALILQFPLWWFSMPAILKGWVDRVYAYG--FAYgvgehsdarwgDRYG-EGTMV 143
Cdd:COG1182   71 --QAALA---LSDELIDE---LLAADVIVIGAPMYNFGIPSQLKAWIDHIARAGrtFRY-----------TENGpVGLLT 131

                        170       180
                 ....*....|....*....|....*..
gi 504409251 144 GKRAMLIVTTGGWashYSPrGINGPID 170
Cdd:COG1182  132 GKKAVVITARGGV---YSG-GPAAGMD 154
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 80-155 3.44e-08

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 51.85  E-value: 3.44e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504409251  80 DIAAEQDKLRWADALILQFPLWWFSMPAILKGWVDRVYAYGFAYGVgehsdarwgdrygegtMVGKRAMLIVTTGG 155
Cdd:COG0655   60 DMNAIYEKLLEADGIIFGSPTYFGNMSAQLKAFIDRLYALWAKGKL----------------LKGKVGAVFTTGGH 119
PRK00170 PRK00170
azoreductase; Reviewed
 1-155 1.23e-06

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 47.97  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251   1 MNVLIVYAHP-EPRSLNGALKDFTVQRLRTA--GHAVQLSDLYAMgwKAPVdardsLDHDLESRFDPSQDSRrafaSGRQ 77
Cdd:PRK00170   2 SKVLVIKSSIlGDYSQSMQLGDAFIEAYKEAhpDDEVTVRDLAAE--PIPV-----LDGEVVGALGKSAETL----TPRQ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251  78 SP--DIAAE-QDKLRWADALILQFPLWWFSMPAILKGWVDRVyaygfaygvgehsdARWGD--RYGE----GTMVGKRAM 148
Cdd:PRK00170  71 QEavALSDElLEEFLAADKIVIAAPMYNFSIPTQLKAYIDLI--------------ARAGKtfRYTEngpvGLVTGKKAL 136


                 ....*..
gi 504409251 149 LIVTTGG 155
Cdd:PRK00170 137 LITSRGG 143
FMN_red pfam03358
NADPH-dependent FMN reductase;
1-159 5.30e-06

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 45.31  E-value: 5.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251    1 MNVLIVYAHPEPRSLNGALKDFTVQRLRtAGHAVQLSDLYAMgwkapvdARDSLDHDLESRfdpsqdsrrafasGRQSPD 80
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLE-EGAEVELIDLADL-------ILPLCDEDLEEE-------------QGDPDD 59

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504409251   81 IAAEQDKLRWADALILQFPLWWFSMPAILKGWVDRVyaygfaygvgehsdarwGDRYGEGTMVGKRAMlIVTTGGWASH 159
Cdd:pfam03358  60 VQELREKIAAADAIIIVTPEYNGSVSGLLKNAIDWL-----------------SRLRGGKELRGKPVA-IVSTGGGRSG 120
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
1-123 6.37e-05

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 42.06  E-value: 6.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504409251   1 MNVLIVYAHPEPRSLNGALKDFTVQRLRTAGHAVQLSDL--YAMgwkaPVdardsLDHDLESRFDPsqdsrrafasgrqs 78
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPAAGAEVELIDLrdLDL----PL-----YDEDLEADGAP-------------- 57

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 504409251  79 PDIAAEQDKLRWADALILQFPLWWFSMPAILKGWVDRVYAYGFAY 123
Cdd:COG0431   58 PAVKALREAIAAADGVVIVTPEYNGSYPGVLKNALDWLSRSELAG 102
 
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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