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Conserved domains on  [gi|496082229|ref|WP_008806736|]
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MULTISPECIES: NADPH-dependent FMN reductase [Klebsiella]

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];
5-170 1.17e-54

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


:

Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 170.72  E-value: 1.17e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082229   5 LKVVTLLGSLRKGSFNGMVARTLPGIAPA-GMDISAL-PSIGDIPLYDADMqEEEGFPQRVQDIAQQIREADGVVIVTPE 82
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPAaGAEVELIdLRDLDLPLYDEDL-EADGAPPAVKALREAIAAADGVVIVTPE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082229  83 YNYSVPGGLKNAIDWLSRlpeQPLSGKPVLIQTSSMGAIGGARCQYHLRQILVFLDAMVMNkPEFMGGVIQNKVDPQsGE 162
Cdd:COG0431   80 YNGSYPGVLKNALDWLSR---SELAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLP-PQVSIPKAGEAFDED-GE 154

                 ....*...
gi 496082229 163 VVDQSTLD 170
Cdd:COG0431  155 LTDEELAE 162
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
5-170 1.17e-54

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 170.72  E-value: 1.17e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082229   5 LKVVTLLGSLRKGSFNGMVARTLPGIAPA-GMDISAL-PSIGDIPLYDADMqEEEGFPQRVQDIAQQIREADGVVIVTPE 82
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPAaGAEVELIdLRDLDLPLYDEDL-EADGAPPAVKALREAIAAADGVVIVTPE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082229  83 YNYSVPGGLKNAIDWLSRlpeQPLSGKPVLIQTSSMGAIGGARCQYHLRQILVFLDAMVMNkPEFMGGVIQNKVDPQsGE 162
Cdd:COG0431   80 YNGSYPGVLKNALDWLSR---SELAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLP-PQVSIPKAGEAFDED-GE 154

                 ....*...
gi 496082229 163 VVDQSTLD 170
Cdd:COG0431  155 LTDEELAE 162
FMN_red pfam03358
NADPH-dependent FMN reductase;
5-148 1.80e-51

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 162.41  E-value: 1.80e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082229    5 LKVVTLLGSLRKGSFNGMVARTLPGIAPAGMDISALpSIGD--IPLYDADMQEEEGFPQRVQDIAQQIREADGVVIVTPE 82
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEEGAEVELI-DLADliLPLCDEDLEEEQGDPDDVQELREKIAAADAIIIVTPE 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082229   83 YNYSVPGGLKNAIDWLSRL-PEQPLSGKPVLIQTSSMGAIGGARCQYHLRQILVFLDAMVMNKPEFM 148
Cdd:pfam03358  80 YNGSVSGLLKNAIDWLSRLrGGKELRGKPVAIVSTGGGRSGGLRAVEQLRQVLAELGAIVVPSGQVA 146
PRK10569 PRK10569
NAD(P)H-dependent FMN reductase; Provisional
63-112 2.58e-08

NAD(P)H-dependent FMN reductase; Provisional


Pssm-ID: 182557  Cd Length: 191  Bit Score: 51.53  E-value: 2.58e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 496082229  63 VQDIAQQIREADGVVIVTPEYNYSVPGGLKNAIDWlsrLPEQPLSGKPVL 112
Cdd:PRK10569  57 LKTFTEQLAQADGLIVATPVYKASFSGALKTLLDL---LPERALEHKVVL 103
LLM_duo_CE1759 TIGR04037
LLM-partnered FMN reductase, CE1759 family; This family represents a distinct clade within ...
58-142 3.79e-05

LLM-partnered FMN reductase, CE1759 family; This family represents a distinct clade within pfam03358. That family includes enzymes such as the NADH-dependent FMN reductase MsuE. Members of the present family regularly co-occur in genomes, typically as gene pairs, with members of TIGR04036, a probable FMN-dependent member of the bacterial luciferase-like monooxygenase (LLM) family. At least one member, RF|YP_001509627.1 from Frankia sp. EAN1pec, is fused to the LLM protein. The function of these gene pairs is unknown.


Pssm-ID: 274935  Cd Length: 198  Bit Score: 42.65  E-value: 3.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082229   58 GFP-QRVQDIAQQIREADGVVIVTPEYNYSVPGGLKNAIDwlsRLPEQPLSGKPVLIqtssmGAIGG-AR----CQYHLR 131
Cdd:TIGR04037  57 GFPsPALRAALDAVAGADGLIAVTPVFSASYSGLFKSFFD---VLDPDALTGKPVLI-----AATGGtPRhslvLDHAMR 128
                          90
                  ....*....|.
gi 496082229  132 QILVFLDAMVM 142
Cdd:TIGR04037 129 PLFSYLRAVVV 139
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
5-170 1.17e-54

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 170.72  E-value: 1.17e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082229   5 LKVVTLLGSLRKGSFNGMVARTLPGIAPA-GMDISAL-PSIGDIPLYDADMqEEEGFPQRVQDIAQQIREADGVVIVTPE 82
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPAaGAEVELIdLRDLDLPLYDEDL-EADGAPPAVKALREAIAAADGVVIVTPE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082229  83 YNYSVPGGLKNAIDWLSRlpeQPLSGKPVLIQTSSMGAIGGARCQYHLRQILVFLDAMVMNkPEFMGGVIQNKVDPQsGE 162
Cdd:COG0431   80 YNGSYPGVLKNALDWLSR---SELAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLP-PQVSIPKAGEAFDED-GE 154

                 ....*...
gi 496082229 163 VVDQSTLD 170
Cdd:COG0431  155 LTDEELAE 162
FMN_red pfam03358
NADPH-dependent FMN reductase;
5-148 1.80e-51

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 162.41  E-value: 1.80e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082229    5 LKVVTLLGSLRKGSFNGMVARTLPGIAPAGMDISALpSIGD--IPLYDADMQEEEGFPQRVQDIAQQIREADGVVIVTPE 82
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEEGAEVELI-DLADliLPLCDEDLEEEQGDPDDVQELREKIAAADAIIIVTPE 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082229   83 YNYSVPGGLKNAIDWLSRL-PEQPLSGKPVLIQTSSMGAIGGARCQYHLRQILVFLDAMVMNKPEFM 148
Cdd:pfam03358  80 YNGSVSGLLKNAIDWLSRLrGGKELRGKPVAIVSTGGGRSGGLRAVEQLRQVLAELGAIVVPSGQVA 146
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
6-122 6.78e-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: 61.20  E-value: 6.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082229    6 KVVTLLGSLRKGSFNGMVARTL-PGIAPAGM-----DISALPsigdIPLYDADMQEEEGFPQRVQDIA---QQIREADGV 76
Cdd:pfam02525   2 KILIINAHPRPGSFSSRLADALvEALKAAGHevtvrDLYALF----LPVLDAEDLADLTYPQGAADVEseqEELLAADVI 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 496082229   77 VIVTPEYNYSVPGGLKNAIDWL-----------SRLPEQPLSGKPVLIqTSSMGAIG 122
Cdd:pfam02525  78 VFQFPLYWFSVPALLKGWIDRVlragfafkyeeGGPGGGGLLGKKVLV-IVTTGGPE 133
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
50-137 2.11e-09

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 54.37  E-value: 2.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082229  50 DADMQEEEgfpQRVQDIAQQIREADGVVIVTPEYNYSVPGGLKNAIDWLSRL----------PEQPLSGKPVLIQTSSMG 119
Cdd:COG1182   67 TPEQQAAL---ALSDELIDELLAADVIVIGAPMYNFGIPSQLKAWIDHIARAgrtfrytengPVGLLTGKKAVVITARGG 143
                         90       100
                 ....*....|....*....|....
gi 496082229 120 AI-GGARCQY-----HLRQILVFL 137
Cdd:COG1182  144 VYsGGPAAGMdfqtpYLRTVLGFI 167
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
6-173 2.88e-09

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 53.78  E-value: 2.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082229   6 KVVTLLGSLRKGSfN-----GMVARTL--PG-----IAPAGMDIS---ALPSIGDIPLYDaDMQEeegfpqrvqdIAQQI 70
Cdd:COG0655    1 KILVINGSPRKNG-NtaalaEAVAEGAeeAGaevelIRLADLDIKpciGCGGTGKCVIKD-DMNA----------IYEKL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082229  71 READGVVIVTPEYNYSVPGGLKNAIDWLSRL--PEQPLSGKPVLIQTSSmGAIGGARCqyhLRQILVFLDAMVMNkpeFM 148
Cdd:COG0655   69 LEADGIIFGSPTYFGNMSAQLKAFIDRLYALwaKGKLLKGKVGAVFTTG-GHGGAEAT---LLSLNTFLLHHGMI---VV 141
                        170       180
                 ....*....|....*....|....*.
gi 496082229 149 GGVIQNKVDPQS-GEVVDQSTLDHLR 173
Cdd:COG0655  142 GLPPYGAVGGGGpGDVLDEEGLATAR 167
PRK10569 PRK10569
NAD(P)H-dependent FMN reductase; Provisional
63-112 2.58e-08

NAD(P)H-dependent FMN reductase; Provisional


Pssm-ID: 182557  Cd Length: 191  Bit Score: 51.53  E-value: 2.58e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 496082229  63 VQDIAQQIREADGVVIVTPEYNYSVPGGLKNAIDWlsrLPEQPLSGKPVL 112
Cdd:PRK10569  57 LKTFTEQLAQADGLIVATPVYKASFSGALKTLLDL---LPERALEHKVVL 103
PRK00170 PRK00170
azoreductase; Reviewed
45-119 1.47e-06

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 46.43  E-value: 1.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082229  45 DIPLYDADM------------QEEEGFPQRVQDIAQQIREADGVVIVTPEYNYSVPGGLKNAIDWLSRL----------P 102
Cdd:PRK00170  47 PIPVLDGEVvgalgksaetltPRQQEAVALSDELLEEFLAADKIVIAAPMYNFSIPTQLKAYIDLIARAgktfrytengP 126
                         90
                 ....*....|....*..
gi 496082229 103 EQPLSGKPVLIQTSSMG 119
Cdd:PRK00170 127 VGLVTGKKALLITSRGG 143
LLM_duo_CE1759 TIGR04037
LLM-partnered FMN reductase, CE1759 family; This family represents a distinct clade within ...
58-142 3.79e-05

LLM-partnered FMN reductase, CE1759 family; This family represents a distinct clade within pfam03358. That family includes enzymes such as the NADH-dependent FMN reductase MsuE. Members of the present family regularly co-occur in genomes, typically as gene pairs, with members of TIGR04036, a probable FMN-dependent member of the bacterial luciferase-like monooxygenase (LLM) family. At least one member, RF|YP_001509627.1 from Frankia sp. EAN1pec, is fused to the LLM protein. The function of these gene pairs is unknown.


Pssm-ID: 274935  Cd Length: 198  Bit Score: 42.65  E-value: 3.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082229   58 GFP-QRVQDIAQQIREADGVVIVTPEYNYSVPGGLKNAIDwlsRLPEQPLSGKPVLIqtssmGAIGG-AR----CQYHLR 131
Cdd:TIGR04037  57 GFPsPALRAALDAVAGADGLIAVTPVFSASYSGLFKSFFD---VLDPDALTGKPVLI-----AATGGtPRhslvLDHAMR 128
                          90
                  ....*....|.
gi 496082229  132 QILVFLDAMVM 142
Cdd:TIGR04037 129 PLFSYLRAVVV 139
 
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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