NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2021284036|ref|WP_208885831|]
View 

MULTISPECIES: NAD(P)H-dependent oxidoreductase [Streptomyces]

Protein Classification

NAD(P)H-dependent oxidoreductase( domain architecture ID 10505769)

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:0016491|GO:0010181
SCOP:  3001217

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
FMN_red pfam03358
NADPH-dependent FMN reductase;
3-149 1.94e-47

NADPH-dependent FMN reductase;


:

Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 152.01  E-value: 1.94e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021284036   3 VRILALVGSLRAGSHNRQLAEAAVKLAPEGAEVELFEgLADV--PFYNEDIDVEGSVPAAAVKLREAAQAADAFLFFSPE 80
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEEGAEVELID-LADLilPLCDEDLEEEQGDPDDVQELREKIAAADAIIIVTPE 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2021284036  81 YNGTIPAVLKNAIDWLSRPYGAGAFGGKPVAVIGTAFGQYGGVWAQDDTRKAVGIAGGKVIEDIKLSIP 149
Cdd:pfam03358  80 YNGSVSGLLKNAIDWLSRLRGGKELRGKPVAIVSTGGGRSGGLRAVEQLRQVLAELGAIVVPSGQVAVG 148
 
Name Accession Description Interval E-value
FMN_red pfam03358
NADPH-dependent FMN reductase;
3-149 1.94e-47

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 152.01  E-value: 1.94e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021284036   3 VRILALVGSLRAGSHNRQLAEAAVKLAPEGAEVELFEgLADV--PFYNEDIDVEGSVPAAAVKLREAAQAADAFLFFSPE 80
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEEGAEVELID-LADLilPLCDEDLEEEQGDPDDVQELREKIAAADAIIIVTPE 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2021284036  81 YNGTIPAVLKNAIDWLSRPYGAGAFGGKPVAVIGTAFGQYGGVWAQDDTRKAVGIAGGKVIEDIKLSIP 149
Cdd:pfam03358  80 YNGSVSGLLKNAIDWLSRLRGGKELRGKPVAIVSTGGGRSGGLRAVEQLRQVLAELGAIVVPSGQVAVG 148
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
4-168 6.18e-47

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 151.08  E-value: 6.18e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021284036   4 RILALVGSLRAGSHNRQLAEAAVKLAPE-GAEVELFE-GLADVPFYNEDIDVEGsVPAAAVKLREAAQAADAFLFFSPEY 81
Cdd:COG0431     2 KILVISGSLRPGSFNRKLARAAAELAPAaGAEVELIDlRDLDLPLYDEDLEADG-APPAVKALREAIAAADGVVIVTPEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021284036  82 NGTIPAVLKNAIDWLSRPygagAFGGKPVAVIGTAFGQYGGVWAQDDTRKAVGIAGGKVIEDiKLSIPGSVTRFAETHPA 161
Cdd:COG0431    81 NGSYPGVLKNALDWLSRS----ELAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLPP-QVSIPKAGEAFDEDGEL 155

                  ....*..
gi 2021284036 162 DDAEVAA 168
Cdd:COG0431   156 TDEELAE 162
PRK00170 PRK00170
azoreductase; Reviewed
1-129 7.40e-05

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 41.42  E-value: 7.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021284036   1 MSvRILALVGSLRAG-SHNRQLAEA---AVKLAPEGAEV---ELFEglADVPFYNEDIDVEGSVPAAAVKLREAA----- 68
Cdd:PRK00170    1 MS-KVLVIKSSILGDySQSMQLGDAfieAYKEAHPDDEVtvrDLAA--EPIPVLDGEVVGALGKSAETLTPRQQEavals 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2021284036  69 -------QAADAFLFFSPEYNGTIPAVLKNAIDWLSRP-----YGA----GAFGGKPVAVIGTAfgqyGGVWAQDDT 129
Cdd:PRK00170   78 delleefLAADKIVIAAPMYNFSIPTQLKAYIDLIARAgktfrYTEngpvGLVTGKKALLITSR----GGIHKDGPT 150
 
Name Accession Description Interval E-value
FMN_red pfam03358
NADPH-dependent FMN reductase;
3-149 1.94e-47

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 152.01  E-value: 1.94e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021284036   3 VRILALVGSLRAGSHNRQLAEAAVKLAPEGAEVELFEgLADV--PFYNEDIDVEGSVPAAAVKLREAAQAADAFLFFSPE 80
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEEGAEVELID-LADLilPLCDEDLEEEQGDPDDVQELREKIAAADAIIIVTPE 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2021284036  81 YNGTIPAVLKNAIDWLSRPYGAGAFGGKPVAVIGTAFGQYGGVWAQDDTRKAVGIAGGKVIEDIKLSIP 149
Cdd:pfam03358  80 YNGSVSGLLKNAIDWLSRLRGGKELRGKPVAIVSTGGGRSGGLRAVEQLRQVLAELGAIVVPSGQVAVG 148
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
4-168 6.18e-47

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 151.08  E-value: 6.18e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021284036   4 RILALVGSLRAGSHNRQLAEAAVKLAPE-GAEVELFE-GLADVPFYNEDIDVEGsVPAAAVKLREAAQAADAFLFFSPEY 81
Cdd:COG0431     2 KILVISGSLRPGSFNRKLARAAAELAPAaGAEVELIDlRDLDLPLYDEDLEADG-APPAVKALREAIAAADGVVIVTPEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021284036  82 NGTIPAVLKNAIDWLSRPygagAFGGKPVAVIGTAFGQYGGVWAQDDTRKAVGIAGGKVIEDiKLSIPGSVTRFAETHPA 161
Cdd:COG0431    81 NGSYPGVLKNALDWLSRS----ELAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLPP-QVSIPKAGEAFDEDGEL 155

                  ....*..
gi 2021284036 162 DDAEVAA 168
Cdd:COG0431   156 TDEELAE 162
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
4-116 2.12e-15

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 70.34  E-value: 2.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021284036   4 RILALVGSLRAGSHNRQLAEAAVKLAPE-GAEVELFEgLADVPF-YNEDIDVEGSVPAA--AVKLREAAQAADAFLFFSP 79
Cdd:COG0655     1 KILVINGSPRKNGNTAALAEAVAEGAEEaGAEVELIR-LADLDIkPCIGCGGTGKCVIKddMNAIYEKLLEADGIIFGSP 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2021284036  80 EYNGTIPAVLKNAIDWLSRPYGAGA-FGGKPVAVIGTA 116
Cdd:COG0655    80 TYFGNMSAQLKAFIDRLYALWAKGKlLKGKVGAVFTTG 117
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
4-116 4.61e-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: 58.88  E-value: 4.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021284036   4 RILALVGSLRAGSHNRQLAEAAV-KLAPEGAEVELFEgLADVP---FYNEDIDVEGSVPAAAVKLREAAQ--AADAFLFF 77
Cdd:pfam02525   2 KILIINAHPRPGSFSSRLADALVeALKAAGHEVTVRD-LYALFlpvLDAEDLADLTYPQGAADVESEQEEllAADVIVFQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2021284036  78 SPEYNGTIPAVLKNAIDWLSRP----------YGAGAFGGKPVAVIGTA 116
Cdd:pfam02525  81 FPLYWFSVPALLKGWIDRVLRAgfafkyeeggPGGGGLLGKKVLVIVTT 129
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
1-122 1.11e-06

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 46.66  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021284036   1 MSvRILALVGSLR-AGSHNRQLAEAAV---KLAPEGAEVELFE-GLADVPFYNEDI------DVEGSVPA--AAVKLREA 67
Cdd:COG1182     1 MM-KLLHIDSSPRgEGSVSRRLADAFVaalRAAHPDDEVTYRDlAAEPLPHLDGAWlaafftPAEGRTPEqqAALALSDE 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2021284036  68 A----QAADAFLFFSPEYNGTIPAVLKNAIDWLSRP-----YGA----GAFGGKPVAVIGTAFGQYGG 122
Cdd:COG1182    80 LidelLAADVIVIGAPMYNFGIPSQLKAWIDHIARAgrtfrYTEngpvGLLTGKKAVVITARGGVYSG 147
PRK00170 PRK00170
azoreductase; Reviewed
1-129 7.40e-05

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 41.42  E-value: 7.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021284036   1 MSvRILALVGSLRAG-SHNRQLAEA---AVKLAPEGAEV---ELFEglADVPFYNEDIDVEGSVPAAAVKLREAA----- 68
Cdd:PRK00170    1 MS-KVLVIKSSILGDySQSMQLGDAfieAYKEAHPDDEVtvrDLAA--EPIPVLDGEVVGALGKSAETLTPRQQEavals 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2021284036  69 -------QAADAFLFFSPEYNGTIPAVLKNAIDWLSRP-----YGA----GAFGGKPVAVIGTAfgqyGGVWAQDDT 129
Cdd:PRK00170   78 delleefLAADKIVIAAPMYNFSIPTQLKAYIDLIARAgktfrYTEngpvGLVTGKKALLITSR----GGIHKDGPT 150
PRK13556 PRK13556
FMN-dependent NADH-azoreductase;
70-120 5.66e-03

FMN-dependent NADH-azoreductase;


Pssm-ID: 184140 [Multi-domain]  Cd Length: 208  Bit Score: 36.28  E-value: 5.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021284036  70 AADAFLFFSPEYNGTIPAVLKNAIDWLSR--------PYG-AGAFGGKPVAVIGTAFGQY 120
Cdd:PRK13556   89 EADKVVFAFPLWNFTIPAVLHTYIDYLNRagktfkytPEGpVGLIGDKKVALLNARGGVY 148
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH