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Conserved domains on  [gi|1772516659|gb|QGA24449|]
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FMN reductase [Alistipes sp. dk3624]

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];
2-115 6.82e-32

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


:

Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 112.56  E-value: 6.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516659   2 KRIAILSSSVRTGRLSHRVALYLQHYLTANElAETEILDLKAYDFPLFEERFAFlPNPSGKVIDFTERLVAADALIIVTP 81
Cdd:COG0431     1 MKILVISGSLRPGSFNRKLARAAAELAPAAG-AEVELIDLRDLDLPLYDEDLEA-DGAPPAVKALREAIAAADGVVIVTP 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1772516659  82 VYNASFSAALKNVID-LYLQEWRRQPVAVVSVTSG 115
Cdd:COG0431    79 EYNGSYPGVLKNALDwLSRSELAGKPVALVSTSGG 113
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
2-115 6.82e-32

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 112.56  E-value: 6.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516659   2 KRIAILSSSVRTGRLSHRVALYLQHYLTANElAETEILDLKAYDFPLFEERFAFlPNPSGKVIDFTERLVAADALIIVTP 81
Cdd:COG0431     1 MKILVISGSLRPGSFNRKLARAAAELAPAAG-AEVELIDLRDLDLPLYDEDLEA-DGAPPAVKALREAIAAADGVVIVTP 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1772516659  82 VYNASFSAALKNVID-LYLQEWRRQPVAVVSVTSG 115
Cdd:COG0431    79 EYNGSYPGVLKNALDwLSRSELAGKPVALVSTSGG 113
FMN_red pfam03358
NADPH-dependent FMN reductase;
3-122 1.61e-28

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 103.47  E-value: 1.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516659   3 RIAILSSSVRTGRLSHRVALYLQHYLTANelAETEILDLKAYDFPLFEERFAFLPNPSGKVIDFTERLVAADALIIVTPV 82
Cdd:pfam03358   2 KILAISGSPRKGSNTRKLARWAAELLEEG--AEVELIDLADLILPLCDEDLEEEQGDPDDVQELREKIAAADAIIIVTPE 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1772516659  83 YNASFSAALKNVIDL-----YLQEWRRQPVAVVSVTSGKVPGIAT 122
Cdd:pfam03358  80 YNGSVSGLLKNAIDWlsrlrGGKELRGKPVAIVSTGGGRSGGLRA 124
PRK10569 PRK10569
NAD(P)H-dependent FMN reductase; Provisional
3-97 9.18e-11

NAD(P)H-dependent FMN reductase; Provisional


Pssm-ID: 182557  Cd Length: 191  Bit Score: 58.08  E-value: 9.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516659   3 RIAILSSSVRTGRLSHRVALYLQHYLTANELaetEILDLKAYDFP---LFEERFaflpnPSGKVIDFTERLVAADALIIV 79
Cdd:PRK10569    2 RVITLAGSPRFPSRSSALLEYAREWLNGLGV---EVYHWNLQNFApedLLYARF-----DSPALKTFTEQLAQADGLIVA 73
                          90
                  ....*....|....*...
gi 1772516659  80 TPVYNASFSAALKNVIDL 97
Cdd:PRK10569   74 TPVYKASFSGALKTLLDL 91
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
2-115 6.82e-32

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 112.56  E-value: 6.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516659   2 KRIAILSSSVRTGRLSHRVALYLQHYLTANElAETEILDLKAYDFPLFEERFAFlPNPSGKVIDFTERLVAADALIIVTP 81
Cdd:COG0431     1 MKILVISGSLRPGSFNRKLARAAAELAPAAG-AEVELIDLRDLDLPLYDEDLEA-DGAPPAVKALREAIAAADGVVIVTP 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1772516659  82 VYNASFSAALKNVID-LYLQEWRRQPVAVVSVTSG 115
Cdd:COG0431    79 EYNGSYPGVLKNALDwLSRSELAGKPVALVSTSGG 113
FMN_red pfam03358
NADPH-dependent FMN reductase;
3-122 1.61e-28

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 103.47  E-value: 1.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516659   3 RIAILSSSVRTGRLSHRVALYLQHYLTANelAETEILDLKAYDFPLFEERFAFLPNPSGKVIDFTERLVAADALIIVTPV 82
Cdd:pfam03358   2 KILAISGSPRKGSNTRKLARWAAELLEEG--AEVELIDLADLILPLCDEDLEEEQGDPDDVQELREKIAAADAIIIVTPE 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1772516659  83 YNASFSAALKNVIDL-----YLQEWRRQPVAVVSVTSGKVPGIAT 122
Cdd:pfam03358  80 YNGSVSGLLKNAIDWlsrlrGGKELRGKPVAIVSTGGGRSGGLRA 124
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
2-96 5.12e-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: 5.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516659   2 KRIAILSSSVRTGRLSHRVALYLQHYLTANElAETEILDLKAYDFPLFEERFAFLPNPSGKVID---FTERLVAADALII 78
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEALKAAG-HEVTVRDLYALFLPVLDAEDLADLTYPQGAADvesEQEELLAADVIVF 79
                          90
                  ....*....|....*...
gi 1772516659  79 VTPVYNASFSAALKNVID 96
Cdd:pfam02525  80 QFPLYWFSVPALLKGWID 97
PRK10569 PRK10569
NAD(P)H-dependent FMN reductase; Provisional
3-97 9.18e-11

NAD(P)H-dependent FMN reductase; Provisional


Pssm-ID: 182557  Cd Length: 191  Bit Score: 58.08  E-value: 9.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516659   3 RIAILSSSVRTGRLSHRVALYLQHYLTANELaetEILDLKAYDFP---LFEERFaflpnPSGKVIDFTERLVAADALIIV 79
Cdd:PRK10569    2 RVITLAGSPRFPSRSSALLEYAREWLNGLGV---EVYHWNLQNFApedLLYARF-----DSPALKTFTEQLAQADGLIVA 73
                          90
                  ....*....|....*...
gi 1772516659  80 TPVYNASFSAALKNVIDL 97
Cdd:PRK10569   74 TPVYKASFSGALKTLLDL 91
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
3-115 3.63e-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: 3.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516659   3 RIAILSSSVR----TGRLSHRVALYLQhyltaNELAETEILDLKAYDFPLFEERFAFLPNP-SGKVIDFTERLVAADALI 77
Cdd:COG0655     1 KILVINGSPRkngnTAALAEAVAEGAE-----EAGAEVELIRLADLDIKPCIGCGGTGKCViKDDMNAIYEKLLEADGII 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1772516659  78 IVTPVYNASFSAALKNVID----LYLQE--WRRQPVAVVSVTSG 115
Cdd:COG0655    76 FGSPTYFGNMSAQLKAFIDrlyaLWAKGklLKGKVGAVFTTGGH 119
AzoR COG1182
FMN-dependent NADH-azoreductase [Energy production and conversion];
1-97 3.07e-08

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


Pssm-ID: 440795 [Multi-domain]  Cd Length: 205  Bit Score: 51.28  E-value: 3.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516659   1 MKRIAILSSSVRTGR-LSHRVA-LYLQHYLTANELAETEILDLKAYDFPLF-EERFAFLPNP--------------SGKV 63
Cdd:COG1182     1 MMKLLHIDSSPRGEGsVSRRLAdAFVAALRAAHPDDEVTYRDLAAEPLPHLdGAWLAAFFTPaegrtpeqqaalalSDEL 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1772516659  64 IDfteRLVAADALIIVTPVYNASFSAALKNVIDL 97
Cdd:COG1182    81 ID---ELLAADVIVIGAPMYNFGIPSQLKAWIDH 111
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
3-96 3.73e-06

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 45.22  E-value: 3.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516659   3 RIAILSSSVRTGRLSHRVALYLQHYLTANElAETEILDLKAYDFPL---FEERFAFLPNPSGkVIDFTERLVAADALIIV 79
Cdd:COG2249     1 KILIIYAHPDPSSFNAALAEAAAEGLEAAG-HEVTVHDLYAEGFDPvlsAADFYRDGPLPID-VAAEQELLLWADHLVFQ 78
                          90
                  ....*....|....*..
gi 1772516659  80 TPVYNASFSAALKNVID 96
Cdd:COG2249    79 FPLWWYSMPALLKGWID 95
PRK00170 PRK00170
azoreductase; Reviewed
1-113 3.43e-05

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 42.57  E-value: 3.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516659   1 MKRIAILSSSVRtGRLSHRVALY---LQHYLTANELAETEILDLKAYDFPLFE-ERFAFLpNPSGKVID----------- 65
Cdd:PRK00170    1 MSKVLVIKSSIL-GDYSQSMQLGdafIEAYKEAHPDDEVTVRDLAAEPIPVLDgEVVGAL-GKSAETLTprqqeavalsd 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1772516659  66 -FTERLVAADALIIVTPVYNASFSAALKNVIDLylqewrrqpVAVVSVT 113
Cdd:PRK00170   79 eLLEEFLAADKIVIAAPMYNFSIPTQLKAYIDL---------IARAGKT 118
PRK09739 PRK09739
NAD(P)H oxidoreductase;
1-96 5.48e-03

NAD(P)H oxidoreductase;


Pssm-ID: 236620 [Multi-domain]  Cd Length: 199  Bit Score: 36.22  E-value: 5.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772516659   1 MKRIAILSSSVRTGRLSHRVALYLQHYLtANELAETEILDL--KAYDFPLFEERFAFLPNP----SGKVIDFTERLVAAD 74
Cdd:PRK09739    3 SMRIYLVWAHPRHDSLTAKVAEAIHQRA-QERGHQVEELDLyrSGFDPVLTPEDEPDWKNPdkrySPEVHQLYSELLEHD 81
                          90       100
                  ....*....|....*....|..
gi 1772516659  75 ALIIVTPVYNASFSAALKNVID 96
Cdd:PRK09739   82 ALVFVFPLWWYSFPAMLKGYID 103
 
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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