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Conserved domains on  [gi|15232856|ref|NP_189427|]
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NADPH:quinone oxidoreductase [Arabidopsis thaliana]

Protein Classification

NADPH-dependent FMN reductase( domain architecture ID 10001414)

NAD(P)H-dependent FMN reductase may carry out reductase activities that are NAD(P)H-dependent and involve FMN as a cofactor, such as catalyzing the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
11-177 6.96e-48

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


:

Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 153.77  E-value: 6.96e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232856  11 IRVAALSGSLRKTSFHTGLLRAAIDLTKEsvPGLQIEYIDIS--PLPLINTDLEVNGTyPPVVEAFRQKILEADSILFAS 88
Cdd:COG0431   1 MKILVISGSLRPGSFNRKLARAAAELAPA--AGAEVELIDLRdlDLPLYDEDLEADGA-PPAVKALREAIAAADGVVIVT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232856  89 PEYNFSVSAPLKNALDWASRppNVWADKPAAIIST-GGGFGGGRSQYHLRQIGVFLDLHFINkPEFTLNAFQppQKFDAE 167
Cdd:COG0431  78 PEYNGSYPGVLKNALDWLSR--SELAGKPVALVSTsGGARGGLRALEHLRPVLSELGAVVLP-PQVSIPKAG--EAFDED 152
                       170
                ....*....|
gi 15232856 168 GNLVDEVTKE 177
Cdd:COG0431 153 GELTDEELAE 162
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
11-177 6.96e-48

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 153.77  E-value: 6.96e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232856  11 IRVAALSGSLRKTSFHTGLLRAAIDLTKEsvPGLQIEYIDIS--PLPLINTDLEVNGTyPPVVEAFRQKILEADSILFAS 88
Cdd:COG0431   1 MKILVISGSLRPGSFNRKLARAAAELAPA--AGAEVELIDLRdlDLPLYDEDLEADGA-PPAVKALREAIAAADGVVIVT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232856  89 PEYNFSVSAPLKNALDWASRppNVWADKPAAIIST-GGGFGGGRSQYHLRQIGVFLDLHFINkPEFTLNAFQppQKFDAE 167
Cdd:COG0431  78 PEYNGSYPGVLKNALDWLSR--SELAGKPVALVSTsGGARGGLRALEHLRPVLSELGAVVLP-PQVSIPKAG--EAFDED 152
                       170
                ....*....|
gi 15232856 168 GNLVDEVTKE 177
Cdd:COG0431 153 GELTDEELAE 162
FMN_red pfam03358
NADPH-dependent FMN reductase;
11-158 9.63e-42

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 137.75  E-value: 9.63e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232856    11 IRVAALSGSLRKTSFHTGLLRAAIDLTKEsvpGLQIEYIDIS--PLPLINTDLEVNGTYPPVVEAFRQKILEADSILFAS 88
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEE---GAEVELIDLAdlILPLCDEDLEEEQGDPDDVQELREKIAAADAIIIVT 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232856    89 PEYNFSVSAPLKNALDWASRPPN--VWADKPAAIISTGGGFG-GGRSQYHLRQIGVFLDLHFINKPEFTLNAF 158
Cdd:pfam03358  78 PEYNGSVSGLLKNAIDWLSRLRGgkELRGKPVAIVSTGGGRSgGLRAVEQLRQVLAELGAIVVPSGQVAVGNA 150
PRK00170 PRK00170
azoreductase; Reviewed
23-123 6.45e-07

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 47.58  E-value: 6.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232856   23 TSFHTGLLRAAIDLTKESVPGLQIEYIDI--SPLPLINTDLeVNGTYPPVVE-AFRQK------------ILEADSILFA 87
Cdd:PRK00170  15 YSQSMQLGDAFIEAYKEAHPDDEVTVRDLaaEPIPVLDGEV-VGALGKSAETlTPRQQeavalsdelleeFLAADKIVIA 93
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 15232856   88 SPEYNFSVSAPLKNALDWASR-----------PPNVWADKPAAIIST 123
Cdd:PRK00170  94 APMYNFSIPTQLKAYIDLIARagktfrytengPVGLVTGKKALLITS 140
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
11-177 6.96e-48

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 153.77  E-value: 6.96e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232856  11 IRVAALSGSLRKTSFHTGLLRAAIDLTKEsvPGLQIEYIDIS--PLPLINTDLEVNGTyPPVVEAFRQKILEADSILFAS 88
Cdd:COG0431   1 MKILVISGSLRPGSFNRKLARAAAELAPA--AGAEVELIDLRdlDLPLYDEDLEADGA-PPAVKALREAIAAADGVVIVT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232856  89 PEYNFSVSAPLKNALDWASRppNVWADKPAAIIST-GGGFGGGRSQYHLRQIGVFLDLHFINkPEFTLNAFQppQKFDAE 167
Cdd:COG0431  78 PEYNGSYPGVLKNALDWLSR--SELAGKPVALVSTsGGARGGLRALEHLRPVLSELGAVVLP-PQVSIPKAG--EAFDED 152
                       170
                ....*....|
gi 15232856 168 GNLVDEVTKE 177
Cdd:COG0431 153 GELTDEELAE 162
FMN_red pfam03358
NADPH-dependent FMN reductase;
11-158 9.63e-42

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 137.75  E-value: 9.63e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232856    11 IRVAALSGSLRKTSFHTGLLRAAIDLTKEsvpGLQIEYIDIS--PLPLINTDLEVNGTYPPVVEAFRQKILEADSILFAS 88
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEE---GAEVELIDLAdlILPLCDEDLEEEQGDPDDVQELREKIAAADAIIIVT 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232856    89 PEYNFSVSAPLKNALDWASRPPN--VWADKPAAIISTGGGFG-GGRSQYHLRQIGVFLDLHFINKPEFTLNAF 158
Cdd:pfam03358  78 PEYNGSVSGLLKNAIDWLSRLRGgkELRGKPVAIVSTGGGRSgGLRAVEQLRQVLAELGAIVVPSGQVAVGNA 150
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
12-123 1.06e-15

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 71.50  E-value: 1.06e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232856  12 RVAALSGSLRKTSfHTG-LLRAAIDLTKEsvPGLQIEYIDISPLPlINTDLEVNGTYPPV----VEAFRQKILEADSILF 86
Cdd:COG0655   1 KILVINGSPRKNG-NTAaLAEAVAEGAEE--AGAEVELIRLADLD-IKPCIGCGGTGKCVikddMNAIYEKLLEADGIIF 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15232856  87 ASPEYNFSVSAPLKNALD-----WASRppNVWADKPAAIIST 123
Cdd:COG0655  77 GSPTYFGNMSAQLKAFIDrlyalWAKG--KLLKGKVGAVFTT 116
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
12-123 2.21e-11

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: 60.04  E-value: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232856    12 RVAALSGSLRKTSFHTGLLRAAIDLTKESvpGLQIEYIDI--SPLPLINTDLEVNGTYP---PVVEAFRQKILEADSILF 86
Cdd:pfam02525   2 KILIINAHPRPGSFSSRLADALVEALKAA--GHEVTVRDLyaLFLPVLDAEDLADLTYPqgaADVESEQEELLAADVIVF 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 15232856    87 ASPEYNFSVSAPLKNALD------WASRPPN------VWADKPAAIIST 123
Cdd:pfam02525  80 QFPLYWFSVPALLKGWIDrvlragFAFKYEEggpgggGLLGKKVLVIVT 128
PRK00170 PRK00170
azoreductase; Reviewed
23-123 6.45e-07

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 47.58  E-value: 6.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232856   23 TSFHTGLLRAAIDLTKESVPGLQIEYIDI--SPLPLINTDLeVNGTYPPVVE-AFRQK------------ILEADSILFA 87
Cdd:PRK00170  15 YSQSMQLGDAFIEAYKEAHPDDEVTVRDLaaEPIPVLDGEV-VGALGKSAETlTPRQQeavalsdelleeFLAADKIVIA 93
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 15232856   88 SPEYNFSVSAPLKNALDWASR-----------PPNVWADKPAAIIST 123
Cdd:PRK00170  94 APMYNFSIPTQLKAYIDLIARagktfrytengPVGLVTGKKALLITS 140
PRK01355 PRK01355
azoreductase; Reviewed
12-104 1.72e-03

azoreductase; Reviewed


Pssm-ID: 234946 [Multi-domain]  Cd Length: 199  Bit Score: 37.76  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232856   12 RVAALSGSL--RKTSFHTGLLRAAIDLTKESVPGLQIEYIDISPLPLINTDLeVNGTYPP-----VVEAFRQKILEADSI 84
Cdd:PRK01355   3 KVLVIKGSMvaKEKSFSSALTDKFVEEYKKVNPNDEIIILDLNETKVGSVTL-TSENFKTffkeeVSDKYINQLKSVDKV 81
                         90       100
                 ....*....|....*....|
gi 15232856   85 LFASPEYNFSVSAPLKNALD 104
Cdd:PRK01355  82 VISCPMTNFNVPATLKNYLD 101
PRK13556 PRK13556
FMN-dependent NADH-azoreductase;
38-108 2.46e-03

FMN-dependent NADH-azoreductase;


Pssm-ID: 184140 [Multi-domain]  Cd Length: 208  Bit Score: 37.43  E-value: 2.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232856   38 KESVPGLQIEYIDI--SPLPLINTDLeVNGTYPP---------------VVEAFRQKILEADSILFASPEYNFSVSAPLK 100
Cdd:PRK13556  31 KEAHPNDTVVELDLykEELPYVGVDM-INGTFKAgkgfelteeeakavaVADKYLNQFLEADKVVFAFPLWNFTIPAVLH 109

                 ....*...
gi 15232856  101 NALDWASR 108
Cdd:PRK13556 110 TYIDYLNR 117
 
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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