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Conserved domains on  [gi|2545445856|ref|WP_301059749|]
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NADPH-dependent FMN reductase [Ponticaulis sp.]

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];
7-166 2.90e-55

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


:

Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 172.26  E-value: 2.90e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545445856   7 IAVLVGSLRKESLNRKLAEAMTALAP-DGLSFEFVTIGD--LPLYNEDLEAD-VPDAWTRFRDTIKTKQGVLFFTPEYNR 82
Cdd:COG0431     3 ILVISGSLRPGSFNRKLARAAAELAPaAGAEVELIDLRDldLPLYDEDLEADgAPPAVKALREAIAAADGVVIVTPEYNG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545445856  83 SVPGALKNALDVGSRpygqSVWDKKPAAIVTASPGALAAFGANHHLRQSLVFLNMPTLqQPEAYIGQVNKLLSEDGEIVS 162
Cdd:COG0431    83 SYPGVLKNALDWLSR----SELAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVL-PPQVSIPKAGEAFDEDGELTD 157

                  ....
gi 2545445856 163 DDTK 166
Cdd:COG0431   158 EELA 161
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
7-166 2.90e-55

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 172.26  E-value: 2.90e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545445856   7 IAVLVGSLRKESLNRKLAEAMTALAP-DGLSFEFVTIGD--LPLYNEDLEAD-VPDAWTRFRDTIKTKQGVLFFTPEYNR 82
Cdd:COG0431     3 ILVISGSLRPGSFNRKLARAAAELAPaAGAEVELIDLRDldLPLYDEDLEADgAPPAVKALREAIAAADGVVIVTPEYNG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545445856  83 SVPGALKNALDVGSRpygqSVWDKKPAAIVTASPGALAAFGANHHLRQSLVFLNMPTLqQPEAYIGQVNKLLSEDGEIVS 162
Cdd:COG0431    83 SYPGVLKNALDWLSR----SELAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVL-PPQVSIPKAGEAFDEDGELTD 157

                  ....
gi 2545445856 163 DDTK 166
Cdd:COG0431   158 EELA 161
FMN_red pfam03358
NADPH-dependent FMN reductase;
7-152 3.94e-44

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 143.53  E-value: 3.94e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545445856   7 IAVLVGSLRKESLNRKLAEAMTALAPDGLSFEFVTIGD--LPLYNEDLEAD--VPDAWTRFRDTIKTKQGVLFFTPEYNR 82
Cdd:pfam03358   3 ILAISGSPRKGSNTRKLARWAAELLEEGAEVELIDLADliLPLCDEDLEEEqgDPDDVQELREKIAAADAIIIVTPEYNG 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545445856  83 SVPGALKNALDVGSRPYGQSVWDKKPAAIVTASPGALAAFGANHHLRQSLVFLNMPTLQQPEAYIGQVNK 152
Cdd:pfam03358  83 SVSGLLKNAIDWLSRLRGGKELRGKPVAIVSTGGGRSGGLRAVEQLRQVLAELGAIVVPSGQVAVGNATD 152
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
7-166 2.90e-55

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 172.26  E-value: 2.90e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545445856   7 IAVLVGSLRKESLNRKLAEAMTALAP-DGLSFEFVTIGD--LPLYNEDLEAD-VPDAWTRFRDTIKTKQGVLFFTPEYNR 82
Cdd:COG0431     3 ILVISGSLRPGSFNRKLARAAAELAPaAGAEVELIDLRDldLPLYDEDLEADgAPPAVKALREAIAAADGVVIVTPEYNG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545445856  83 SVPGALKNALDVGSRpygqSVWDKKPAAIVTASPGALAAFGANHHLRQSLVFLNMPTLqQPEAYIGQVNKLLSEDGEIVS 162
Cdd:COG0431    83 SYPGVLKNALDWLSR----SELAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVL-PPQVSIPKAGEAFDEDGELTD 157

                  ....
gi 2545445856 163 DDTK 166
Cdd:COG0431   158 EELA 161
FMN_red pfam03358
NADPH-dependent FMN reductase;
7-152 3.94e-44

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 143.53  E-value: 3.94e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545445856   7 IAVLVGSLRKESLNRKLAEAMTALAPDGLSFEFVTIGD--LPLYNEDLEAD--VPDAWTRFRDTIKTKQGVLFFTPEYNR 82
Cdd:pfam03358   3 ILAISGSPRKGSNTRKLARWAAELLEEGAEVELIDLADliLPLCDEDLEEEqgDPDDVQELREKIAAADAIIIVTPEYNG 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545445856  83 SVPGALKNALDVGSRPYGQSVWDKKPAAIVTASPGALAAFGANHHLRQSLVFLNMPTLQQPEAYIGQVNK 152
Cdd:pfam03358  83 SVSGLLKNAIDWLSRLRGGKELRGKPVAIVSTGGGRSGGLRAVEQLRQVLAELGAIVVPSGQVAVGNATD 152
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
7-137 3.95e-09

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 53.39  E-value: 3.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545445856   7 IAVLVGSLRKESLNRKLAEAMTALAPD-GLSFEFVTIGDLPLY-----NEDLEADVPDAWTRFRDTIKTKQGVLFFTPEY 80
Cdd:COG0655     2 ILVINGSPRKNGNTAALAEAVAEGAEEaGAEVELIRLADLDIKpcigcGGTGKCVIKDDMNAIYEKLLEADGIIFGSPTY 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545445856  81 NRSVPGALKNALD-VGSRPYGQSVWDKKPAAIVT--ASPGALAAFganHHLRQSLVFLNM 137
Cdd:COG0655    82 FGNMSAQLKAFIDrLYALWAKGKLLKGKVGAVFTtgGHGGAEATL---LSLNTFLLHHGM 138
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
9-148 8.16e-05

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: 41.55  E-value: 8.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545445856   9 VLVGSLRKESLNRKLAEA-MTALAPDGLSFEFVTIGDLPLYNEDLEADVPDAWTRFRDTIKTKQG-------VLFFTPEY 80
Cdd:pfam02525   5 IINAHPRPGSFSSRLADAlVEALKAAGHEVTVRDLYALFLPVLDAEDLADLTYPQGAADVESEQEellaadvIVFQFPLY 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545445856  81 NRSVPGALKNALDVGSRP-----YGQSVWDK-----KPAAIVTASPGALAAFGANHHLRQSLVFLnMPTLQQPEAYIG 148
Cdd:pfam02525  85 WFSVPALLKGWIDRVLRAgfafkYEEGGPGGggllgKKVLVIVTTGGPEYAYGKGGYNGFSLDEL-LPYLRGILGFCG 161
 
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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