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Conserved domains on  [gi|2532857375|ref|WP_290273663|]
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NADPH-dependent FMN reductase [Halomonas sabkhae]

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];
4-174 4.73e-59

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


:

Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 181.89  E-value: 4.73e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532857375   4 PRILVFAGSAREASYNKQLARLAAQRIEALGGTPTFVDLRDYPVPLYDGDLEEhQGLPDNVVALRQLLAEHQGLLIASPE 83
Cdd:COG0431     1 MKILVISGSLRPGSFNRKLARAAAELAPAAGAEVELIDLRDLDLPLYDEDLEA-DGAPPAVKALREAIAAADGVVIVTPE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532857375  84 YNGFVTPLLVNTIDWLTRPHqgesglalFQDRQAALVGASPGGLGGLRALNPLRQLLTNIGVTVLPNQLAVGGAGDAFDA 163
Cdd:COG0431    80 YNGSYPGVLKNALDWLSRSE--------LAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLPPQVSIPKAGEAFDE 151
                         170
                  ....*....|.
gi 2532857375 164 QGQLTNDKQRD 174
Cdd:COG0431   152 DGELTDEELAE 162
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
4-174 4.73e-59

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 181.89  E-value: 4.73e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532857375   4 PRILVFAGSAREASYNKQLARLAAQRIEALGGTPTFVDLRDYPVPLYDGDLEEhQGLPDNVVALRQLLAEHQGLLIASPE 83
Cdd:COG0431     1 MKILVISGSLRPGSFNRKLARAAAELAPAAGAEVELIDLRDLDLPLYDEDLEA-DGAPPAVKALREAIAAADGVVIVTPE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532857375  84 YNGFVTPLLVNTIDWLTRPHqgesglalFQDRQAALVGASPGGLGGLRALNPLRQLLTNIGVTVLPNQLAVGGAGDAFDA 163
Cdd:COG0431    80 YNGSYPGVLKNALDWLSRSE--------LAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLPPQVSIPKAGEAFDE 151
                         170
                  ....*....|.
gi 2532857375 164 QGQLTNDKQRD 174
Cdd:COG0431   152 DGELTDEELAE 162
FMN_red pfam03358
NADPH-dependent FMN reductase;
4-159 2.79e-46

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 149.31  E-value: 2.79e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532857375   4 PRILVFAGSAREASYNKQLARLAAQRIEAlGGTPTFVDLRDYPVPLYDGDLEEHQGLPDNVVALRQLLAEHQGLLIASPE 83
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEE-GAEVELIDLADLILPLCDEDLEEEQGDPDDVQELREKIAAADAIIIVTPE 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2532857375  84 YNGFVTPLLVNTIDWLTRPHQGESglalFQDRQAALVGASPGGLGGLRALNPLRQLLTNIGVTVLP-NQLAVGGAGD 159
Cdd:pfam03358  80 YNGSVSGLLKNAIDWLSRLRGGKE----LRGKPVAIVSTGGGRSGGLRAVEQLRQVLAELGAIVVPsGQVAVGNATD 152
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
4-174 4.73e-59

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 181.89  E-value: 4.73e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532857375   4 PRILVFAGSAREASYNKQLARLAAQRIEALGGTPTFVDLRDYPVPLYDGDLEEhQGLPDNVVALRQLLAEHQGLLIASPE 83
Cdd:COG0431     1 MKILVISGSLRPGSFNRKLARAAAELAPAAGAEVELIDLRDLDLPLYDEDLEA-DGAPPAVKALREAIAAADGVVIVTPE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532857375  84 YNGFVTPLLVNTIDWLTRPHqgesglalFQDRQAALVGASPGGLGGLRALNPLRQLLTNIGVTVLPNQLAVGGAGDAFDA 163
Cdd:COG0431    80 YNGSYPGVLKNALDWLSRSE--------LAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLPPQVSIPKAGEAFDE 151
                         170
                  ....*....|.
gi 2532857375 164 QGQLTNDKQRD 174
Cdd:COG0431   152 DGELTDEELAE 162
FMN_red pfam03358
NADPH-dependent FMN reductase;
4-159 2.79e-46

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 149.31  E-value: 2.79e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532857375   4 PRILVFAGSAREASYNKQLARLAAQRIEAlGGTPTFVDLRDYPVPLYDGDLEEHQGLPDNVVALRQLLAEHQGLLIASPE 83
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEE-GAEVELIDLADLILPLCDEDLEEEQGDPDDVQELREKIAAADAIIIVTPE 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2532857375  84 YNGFVTPLLVNTIDWLTRPHQGESglalFQDRQAALVGASPGGLGGLRALNPLRQLLTNIGVTVLP-NQLAVGGAGD 159
Cdd:pfam03358  80 YNGSVSGLLKNAIDWLSRLRGGKE----LRGKPVAIVSTGGGRSGGLRAVEQLRQVLAELGAIVVPsGQVAVGNATD 152
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
5-164 5.77e-12

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: 61.58  E-value: 5.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532857375   5 RILVFAGSAREASYNKQLARLAAQRIEALGGTPTFVDLRDYPVPLYDGDLEEHQGLPD---NVVALRQLLAEHQGLLIAS 81
Cdd:pfam02525   2 KILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYALFLPVLDAEDLADLTYPQgaaDVESEQEELLAADVIVFQF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532857375  82 PEYNGFVTPLL------VNTIDWLTRPHQGESGLALFQDRQAALVGASPG-----GLGGLRA------LNPLRQLLTNIG 144
Cdd:pfam02525  82 PLYWFSVPALLkgwidrVLRAGFAFKYEEGGPGGGGLLGKKVLVIVTTGGpeyayGKGGYNGfsldelLPYLRGILGFCG 161
                         170       180
                  ....*....|....*....|
gi 2532857375 145 VTVLPNQLAVGGAGDAFDAQ 164
Cdd:pfam02525 162 ITDLPPFAVEGTAGPEDEAA 181
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
5-165 9.14e-12

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 60.71  E-value: 9.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532857375   5 RILVFAGSAREASYNKQLARLAAQRIEALGGTPTFVDLRDYPVPLYDGDLEEHQ-GLPDNVVALRQLLAEHQGLLIASPE 83
Cdd:COG0655     1 KILVINGSPRKNGNTAALAEAVAEGAEEAGAEVELIRLADLDIKPCIGCGGTGKcVIKDDMNAIYEKLLEADGIIFGSPT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532857375  84 YNGFVTPLLVNTIDWLTRPHqgeSGLALFQDRQAALVGASpGGLGGLRALNPLRQLLTNIGVTVLP----NQLAVGGAGD 159
Cdd:COG0655    81 YFGNMSAQLKAFIDRLYALW---AKGKLLKGKVGAVFTTG-GHGGAEATLLSLNTFLLHHGMIVVGlppyGAVGGGGPGD 156

                  ....*.
gi 2532857375 160 AFDAQG 165
Cdd:COG0655   157 VLDEEG 162
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
5-190 4.23e-08

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 50.99  E-value: 4.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532857375   5 RILVFAGSAREASYNKQLARLAAQRIEALGGTPTFVDL--RDYPVPLYDGDLEEHQGLPDNVVALRQLLAEHQGLLIASP 82
Cdd:COG2249     1 KILIIYAHPDPSSFNAALAEAAAEGLEAAGHEVTVHDLyaEGFDPVLSAADFYRDGPLPIDVAAEQELLLWADHLVFQFP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532857375  83 EYNGFVTPLL------VNTIDWLTRPHQGESGlALFQDRQAALV---GA-----SPGGLGGlralnPLRQLLTN-----I 143
Cdd:COG2249    81 LWWYSMPALLkgwidrVLTPGFAYGYGGGYPG-GLLKGKKALLVvttGGpeeaySRLGYGG-----PIEELLFRgtlgyC 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2532857375 144 GVTVLPNqLAVGGAGDAFDAQgqltndkqrdsLDAICQRLITTLDRL 190
Cdd:COG2249   155 GMKVLPP-FVLYGVDRSSDEE-----------RAAWLERVRELLAAL 189
 
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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