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Conserved domains on  [gi|554790420|ref|NP_001273066|]
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NAD(P)H dehydrogenase [quinone] 1 isoform d [Homo sapiens]

Protein Classification

NAD(P)H-dependent oxidoreductase( domain architecture ID 1904052)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MdaB super family cl43659
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 5-144 9.37e-20

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


The actual alignment was detected with superfamily member COG2249:

Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 82.58  E-value: 9.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790420   5 RALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESDLYAMNFNPIISRKDItgklkdpanfqypaesvlaYKEGHLSPD 84
Cdd:COG2249    1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAADF-------------------YRDGPLPID 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790420  85 IVAEQKKLEAADLVIFQS-------------------------------------------------------------- 102
Cdd:COG2249   62 VAAEQELLLWADHLVFQFplwwysmpallkgwidrvltpgfaygygggypggllkgkkallvvttggpeeaysrlgyggp 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 554790420 103 -------GILHFCGFQVLEPQLTYSIGHTPADARIQILEGWKKRLENIW 144
Cdd:COG2249  142 ieellfrGTLGYCGMKVLPPFVLYGVDRSSDEERAAWLERVRELLAALA 190
 
Name Accession Description Interval E-value
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 5-144 9.37e-20

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 82.58  E-value: 9.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790420   5 RALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESDLYAMNFNPIISRKDItgklkdpanfqypaesvlaYKEGHLSPD 84
Cdd:COG2249    1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAADF-------------------YRDGPLPID 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790420  85 IVAEQKKLEAADLVIFQS-------------------------------------------------------------- 102
Cdd:COG2249   62 VAAEQELLLWADHLVFQFplwwysmpallkgwidrvltpgfaygygggypggllkgkkallvvttggpeeaysrlgyggp 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 554790420 103 -------GILHFCGFQVLEPQLTYSIGHTPADARIQILEGWKKRLENIW 144
Cdd:COG2249  142 ieellfrGTLGYCGMKVLPPFVLYGVDRSSDEERAAWLERVRELLAALA 190
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 5-101 3.10e-09

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: 54.26  E-value: 3.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790420    5 RALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESDLYAMnFNPIISRKDITGklkdpanfqypaesvLAYKEGhlSPD 84
Cdd:pfam02525   2 KILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYAL-FLPVLDAEDLAD---------------LTYPQG--AAD 63

                          90
                  ....*....|....*..
gi 554790420   85 IVAEQKKLEAADLVIFQ 101
Cdd:pfam02525  64 VESEQEELLAADVIVFQ 80
 
Name Accession Description Interval E-value
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 5-144 9.37e-20

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 82.58  E-value: 9.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790420   5 RALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESDLYAMNFNPIISRKDItgklkdpanfqypaesvlaYKEGHLSPD 84
Cdd:COG2249    1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLYAEGFDPVLSAADF-------------------YRDGPLPID 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790420  85 IVAEQKKLEAADLVIFQS-------------------------------------------------------------- 102
Cdd:COG2249   62 VAAEQELLLWADHLVFQFplwwysmpallkgwidrvltpgfaygygggypggllkgkkallvvttggpeeaysrlgyggp 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 554790420 103 -------GILHFCGFQVLEPQLTYSIGHTPADARIQILEGWKKRLENIW 144
Cdd:COG2249  142 ieellfrGTLGYCGMKVLPPFVLYGVDRSSDEERAAWLERVRELLAALA 190
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 5-101 3.10e-09

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: 54.26  E-value: 3.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790420    5 RALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESDLYAMnFNPIISRKDITGklkdpanfqypaesvLAYKEGhlSPD 84
Cdd:pfam02525   2 KILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYAL-FLPVLDAEDLAD---------------LTYPQG--AAD 63

                          90
                  ....*....|....*..
gi 554790420   85 IVAEQKKLEAADLVIFQ 101
Cdd:pfam02525  64 VESEQEELLAADVIVFQ 80
 
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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