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Conserved domains on  [gi|504706677|ref|WP_014893779|]
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MULTISPECIES: NADPH-dependent FMN reductase [Bacillus]

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];
1-150 7.40e-48

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


:

Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 153.00  E-value: 7.40e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706677   1 MKLVVINGTPRKFGRTRVVAKYIADQFEG-----ELFDLAVEELPLYNG-EESQRELEAVKKLKALVKNADGVVLCTPEY 74
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPAagaevELIDLRDLDLPLYDEdLEADGAPPAVKALREAIAAADGVVIVTPEY 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504706677  75 HNAMSGALKNSLDYLSSSEFVHKPVALLAVAGGGKGGINALNSMRTVARGVYANAIPKQVVLDGLHVQ---DGELGEDA 150
Cdd:COG0431   81 NGSYPGVLKNALDWLSRSELAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLPPQVSIPKAGEAfdeDGELTDEE 159
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
1-150 7.40e-48

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 153.00  E-value: 7.40e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706677   1 MKLVVINGTPRKFGRTRVVAKYIADQFEG-----ELFDLAVEELPLYNG-EESQRELEAVKKLKALVKNADGVVLCTPEY 74
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPAagaevELIDLRDLDLPLYDEdLEADGAPPAVKALREAIAAADGVVIVTPEY 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504706677  75 HNAMSGALKNSLDYLSSSEFVHKPVALLAVAGGGKGGINALNSMRTVARGVYANAIPKQVVLDGLHVQ---DGELGEDA 150
Cdd:COG0431   81 NGSYPGVLKNALDWLSRSELAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLPPQVSIPKAGEAfdeDGELTDEE 159
FMN_red pfam03358
NADPH-dependent FMN reductase;
1-135 1.40e-39

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 131.59  E-value: 1.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706677    1 MKLVVINGTPRKFGRTRVVAKYIADQ----FEGELFDLAVEELPLYNG--EESQRELEAVKKLKALVKNADGVVLCTPEY 74
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELleegAEVELIDLADLILPLCDEdlEEEQGDPDDVQELREKIAAADAIIIVTPEY 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504706677   75 HNAMSGALKNSLDYLS----SSEFVHKPVALLAVAGGGKGGINALNSMRTVARGVYANAIPKQVV 135
Cdd:pfam03358  81 NGSVSGLLKNAIDWLSrlrgGKELRGKPVAIVSTGGGRSGGLRAVEQLRQVLAELGAIVVPSGQV 145
PRK10569 PRK10569
NAD(P)H-dependent FMN reductase; Provisional
1-152 2.77e-09

NAD(P)H-dependent FMN reductase; Provisional


Pssm-ID: 182557  Cd Length: 191  Bit Score: 53.84  E-value: 2.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706677   1 MKLVVINGTPRKFGRTRVVAKYIADQFEG--------ELFDLAVEELpLYNGEESqrelEAVKKLKALVKNADGVVLCTP 72
Cdd:PRK10569   1 MRVITLAGSPRFPSRSSALLEYAREWLNGlgvevyhwNLQNFAPEDL-LYARFDS----PALKTFTEQLAQADGLIVATP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706677  73 EYHNAMSGALKNSLDYLSSSEFVHKPVALLAvAGGGKGGINALNsmrtvargvYA-----NAIPKQVVLDGLHVQDGELG 147
Cdd:PRK10569  76 VYKASFSGALKTLLDLLPERALEHKVVLPLA-TGGSVAHMLAVD---------YAlkpvlSALKAQEILHGVFADDSQVI 145

                 ....*
gi 504706677 148 EDAKP 152
Cdd:PRK10569 146 DYHHQ 150
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
1-150 7.40e-48

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 153.00  E-value: 7.40e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706677   1 MKLVVINGTPRKFGRTRVVAKYIADQFEG-----ELFDLAVEELPLYNG-EESQRELEAVKKLKALVKNADGVVLCTPEY 74
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPAagaevELIDLRDLDLPLYDEdLEADGAPPAVKALREAIAAADGVVIVTPEY 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504706677  75 HNAMSGALKNSLDYLSSSEFVHKPVALLAVAGGGKGGINALNSMRTVARGVYANAIPKQVVLDGLHVQ---DGELGEDA 150
Cdd:COG0431   81 NGSYPGVLKNALDWLSRSELAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLPPQVSIPKAGEAfdeDGELTDEE 159
FMN_red pfam03358
NADPH-dependent FMN reductase;
1-135 1.40e-39

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 131.59  E-value: 1.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706677    1 MKLVVINGTPRKFGRTRVVAKYIADQ----FEGELFDLAVEELPLYNG--EESQRELEAVKKLKALVKNADGVVLCTPEY 74
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELleegAEVELIDLADLILPLCDEdlEEEQGDPDDVQELREKIAAADAIIIVTPEY 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504706677   75 HNAMSGALKNSLDYLS----SSEFVHKPVALLAVAGGGKGGINALNSMRTVARGVYANAIPKQVV 135
Cdd:pfam03358  81 NGSVSGLLKNAIDWLSrlrgGKELRGKPVAIVSTGGGRSGGLRAVEQLRQVLAELGAIVVPSGQV 145
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
2-122 2.21e-14

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 67.26  E-value: 2.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706677   2 KLVVINGTPRKFGRTRVVAKYIADQF-----EGELFDLAVEELPLYNGEESQRELEA---VKKLKALVKNADGVVLCTPE 73
Cdd:COG0655    1 KILVINGSPRKNGNTAALAEAVAEGAeeagaEVELIRLADLDIKPCIGCGGTGKCVIkddMNAIYEKLLEADGIIFGSPT 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504706677  74 YHNAMSGALKNSLD-----YLSSSEFVHKPVALLAVAGGGkGGINALNSMRTVA 122
Cdd:COG0655   81 YFGNMSAQLKAFIDrlyalWAKGKLLKGKVGAVFTTGGHG-GAEATLLSLNTFL 133
PRK10569 PRK10569
NAD(P)H-dependent FMN reductase; Provisional
1-152 2.77e-09

NAD(P)H-dependent FMN reductase; Provisional


Pssm-ID: 182557  Cd Length: 191  Bit Score: 53.84  E-value: 2.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706677   1 MKLVVINGTPRKFGRTRVVAKYIADQFEG--------ELFDLAVEELpLYNGEESqrelEAVKKLKALVKNADGVVLCTP 72
Cdd:PRK10569   1 MRVITLAGSPRFPSRSSALLEYAREWLNGlgvevyhwNLQNFAPEDL-LYARFDS----PALKTFTEQLAQADGLIVATP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706677  73 EYHNAMSGALKNSLDYLSSSEFVHKPVALLAvAGGGKGGINALNsmrtvargvYA-----NAIPKQVVLDGLHVQDGELG 147
Cdd:PRK10569  76 VYKASFSGALKTLLDLLPERALEHKVVLPLA-TGGSVAHMLAVD---------YAlkpvlSALKAQEILHGVFADDSQVI 145

                 ....*
gi 504706677 148 EDAKP 152
Cdd:PRK10569 146 DYHHQ 150
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
1-129 4.93e-07

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: 47.71  E-value: 4.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706677    1 MKLVVINGTPRKFGRTRVVAKYIADQFEG-----ELFDLAVEELPLYNGEE-----SQRELEAVKKLKALVKNADGVVLC 70
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEALKAaghevTVRDLYALFLPVLDAEDladltYPQGAADVESEQEELLAADVIVFQ 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504706677   71 TPEYHNAMSGALKNSLDYLSSSEF--------------VHKPVALLAVAGG-----GKGGINAlNSMRTVARGVYANA 129
Cdd:pfam02525  81 FPLYWFSVPALLKGWIDRVLRAGFafkyeeggpgggglLGKKVLVIVTTGGpeyayGKGGYNG-FSLDELLPYLRGIL 157
FldA COG0716
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ...
14-161 2.24e-03

Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440480 [Multi-domain]  Cd Length: 135  Bit Score: 36.42  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706677  14 GRTRVVAKYIADQFEGELFDLaveelplyngeesqreLEAVKKLKALVKNADGVVLCTP----EYHNAMSGALKNSLDYL 89
Cdd:COG0716   10 GNTEKVAEAIAEALGAAGVDL----------------FEIEDADLDDLEDYDLLILGTPtwagELPDDWEDFLEELKEDL 73
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504706677  90 SssefvHKPVALLAVaGGGKGGINALNSMRTVARGVYANaipkqvVLDGLHVQDGELGEDAKPL--IHDLVKEL 161
Cdd:COG0716   74 S-----GKKVALFGT-GDSSGYGDALGELKELLEEKGAK------VVGGYDFEGSKAPDAEDTEerAEEWLKQL 135
 
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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