NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|498343558|ref|WP_010657714|]
View 

MULTISPECIES: NADPH-dependent FMN reductase [Brucella/Ochrobactrum group]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
4-171 2.42e-52

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


:

Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 164.94  E-value: 2.42e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498343558   4 RILVFAGSVRIGAFSGHMADAAEKELRAQGAQVTRITLADYPLPIMDQNLEnEHGVPENAMRLGRLFAEQDGLMICSPEY 83
Cdd:COG0431    2 KILVISGSLRPGSFNRKLARAAAELAPAAGAEVELIDLRDLDLPLYDEDLE-ADGAPPAVKALREAIAAADGVVIVTPEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498343558  84 NASIPPLLKNTIDWVSRisrdgdrpfRPYAGLTVGLCSSSDGMFAGMRGLYHLRAVLMNVGVQIVTEQCSVGHASVAFND 163
Cdd:COG0431   81 NGSYPGVLKNALDWLSR---------SELAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLPPQVSIPKAGEAFDE 151

                 ....*...
gi 498343558 164 DGTLKEER 171
Cdd:COG0431  152 DGELTDEE 159
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
4-171 2.42e-52

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 164.94  E-value: 2.42e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498343558   4 RILVFAGSVRIGAFSGHMADAAEKELRAQGAQVTRITLADYPLPIMDQNLEnEHGVPENAMRLGRLFAEQDGLMICSPEY 83
Cdd:COG0431    2 KILVISGSLRPGSFNRKLARAAAELAPAAGAEVELIDLRDLDLPLYDEDLE-ADGAPPAVKALREAIAAADGVVIVTPEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498343558  84 NASIPPLLKNTIDWVSRisrdgdrpfRPYAGLTVGLCSSSDGMFAGMRGLYHLRAVLMNVGVQIVTEQCSVGHASVAFND 163
Cdd:COG0431   81 NGSYPGVLKNALDWLSR---------SELAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLPPQVSIPKAGEAFDE 151

                 ....*...
gi 498343558 164 DGTLKEER 171
Cdd:COG0431  152 DGELTDEE 159
FMN_red pfam03358
NADPH-dependent FMN reductase;
4-148 1.35e-36

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 124.66  E-value: 1.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498343558    4 RILVFAGSVRIGAFSGHMADAAEKELRAqGAQVTRITLADYPLPIMDQNLENEHGVPENAMRLGRLFAEQDGLMICSPEY 83
Cdd:pfam03358   2 KILAISGSPRKGSNTRKLARWAAELLEE-GAEVELIDLADLILPLCDEDLEEEQGDPDDVQELREKIAAADAIIIVTPEY 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498343558   84 NASIPPLLKNTIDWVSRIsrdgdRPFRPYAGLTVGLCSSSDGMFAGMRGLYHLRAVLMNVGVQIV 148
Cdd:pfam03358  81 NGSVSGLLKNAIDWLSRL-----RGGKELRGKPVAIVSTGGGRSGGLRAVEQLRQVLAELGAIVV 140
PRK00170 PRK00170
azoreductase; Reviewed
17-145 1.89e-05

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 43.34  E-value: 1.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498343558  17 FSGHMADAAEKELRAQ--GAQVTRITLADYPLPIMDQNLENEHGVPENAM---------RLGRLFAE---QDGLMICSPE 82
Cdd:PRK00170  17 QSMQLGDAFIEAYKEAhpDDEVTVRDLAAEPIPVLDGEVVGALGKSAETLtprqqeavaLSDELLEEflaADKIVIAAPM 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498343558  83 YNASIPPLLKNTIDwvsRISRDGdRPFRPYAGLTVGLC--------SSSDGMFAG----MrGLYHLRAVLMNVGV 145
Cdd:PRK00170  97 YNFSIPTQLKAYID---LIARAG-KTFRYTENGPVGLVtgkkalliTSRGGIHKDgptdM-GVPYLKTFLGFIGI 166
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
4-171 2.42e-52

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 164.94  E-value: 2.42e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498343558   4 RILVFAGSVRIGAFSGHMADAAEKELRAQGAQVTRITLADYPLPIMDQNLEnEHGVPENAMRLGRLFAEQDGLMICSPEY 83
Cdd:COG0431    2 KILVISGSLRPGSFNRKLARAAAELAPAAGAEVELIDLRDLDLPLYDEDLE-ADGAPPAVKALREAIAAADGVVIVTPEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498343558  84 NASIPPLLKNTIDWVSRisrdgdrpfRPYAGLTVGLCSSSDGMFAGMRGLYHLRAVLMNVGVQIVTEQCSVGHASVAFND 163
Cdd:COG0431   81 NGSYPGVLKNALDWLSR---------SELAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLPPQVSIPKAGEAFDE 151

                 ....*...
gi 498343558 164 DGTLKEER 171
Cdd:COG0431  152 DGELTDEE 159
FMN_red pfam03358
NADPH-dependent FMN reductase;
4-148 1.35e-36

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 124.66  E-value: 1.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498343558    4 RILVFAGSVRIGAFSGHMADAAEKELRAqGAQVTRITLADYPLPIMDQNLENEHGVPENAMRLGRLFAEQDGLMICSPEY 83
Cdd:pfam03358   2 KILAISGSPRKGSNTRKLARWAAELLEE-GAEVELIDLADLILPLCDEDLEEEQGDPDDVQELREKIAAADAIIIVTPEY 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498343558   84 NASIPPLLKNTIDWVSRIsrdgdRPFRPYAGLTVGLCSSSDGMFAGMRGLYHLRAVLMNVGVQIV 148
Cdd:pfam03358  81 NGSVSGLLKNAIDWLSRL-----RGGKELRGKPVAIVSTGGGRSGGLRAVEQLRQVLAELGAIVV 140
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
4-126 3.08e-14

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: 67.74  E-value: 3.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498343558    4 RILVFAGSVRIGAFSGHMADAAEKELRAQGAQVTRITLADYPLPIMDQNLENEHGVPE---NAMRLGRLFAEQDGLMICS 80
Cdd:pfam02525   2 KILIINAHPRPGSFSSRLADALVEALKAAGHEVTVRDLYALFLPVLDAEDLADLTYPQgaaDVESEQEELLAADVIVFQF 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 498343558   81 PEYNASIPPLLKNTIDWVSRI-----SRDGDRPFRPYAGLTVGLCSSSDGM 126
Cdd:pfam02525  82 PLYWFSVPALLKGWIDRVLRAgfafkYEEGGPGGGGLLGKKVLVIVTTGGP 132
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
4-148 1.62e-09

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 54.55  E-value: 1.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498343558   4 RILVFAGSVRIgafSGH---MADAAEKELRAQGAQVTRITLADYPL-PIMDQNLENEHGVPENAMRLGRLFAEQDGLMIC 79
Cdd:COG0655    1 KILVINGSPRK---NGNtaaLAEAVAEGAEEAGAEVELIRLADLDIkPCIGCGGTGKCVIKDDMNAIYEKLLEADGIIFG 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498343558  80 SPEYNASIPPLLKNTIDWVSRISRDGDR-PFRPYAGLTVGlcsSSDGmfaGMRGLYHLRAVLMNVGVQIV 148
Cdd:COG0655   78 SPTYFGNMSAQLKAFIDRLYALWAKGKLlKGKVGAVFTTG---GHGG---AEATLLSLNTFLLHHGMIVV 141
PRK00170 PRK00170
azoreductase; Reviewed
17-145 1.89e-05

azoreductase; Reviewed


Pssm-ID: 234675 [Multi-domain]  Cd Length: 201  Bit Score: 43.34  E-value: 1.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498343558  17 FSGHMADAAEKELRAQ--GAQVTRITLADYPLPIMDQNLENEHGVPENAM---------RLGRLFAE---QDGLMICSPE 82
Cdd:PRK00170  17 QSMQLGDAFIEAYKEAhpDDEVTVRDLAAEPIPVLDGEVVGALGKSAETLtprqqeavaLSDELLEEflaADKIVIAAPM 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498343558  83 YNASIPPLLKNTIDwvsRISRDGdRPFRPYAGLTVGLC--------SSSDGMFAG----MrGLYHLRAVLMNVGV 145
Cdd:PRK00170  97 YNFSIPTQLKAYID---LIARAG-KTFRYTENGPVGLVtgkkalliTSRGGIHKDgptdM-GVPYLKTFLGFIGI 166
FldA COG0716
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ...
5-148 4.22e-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: 36.03  E-value: 4.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498343558   5 ILVFAGSVrigafSGH---MADAAEKELRAQGAQVTRITLADYPlpimdqnlenehgvpenamrlgrLFAEQDGLMICSP 81
Cdd:COG0716    1 ILIVYGST-----TGNtekVAEAIAEALGAAGVDLFEIEDADLD-----------------------DLEDYDLLILGTP 52
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498343558  82 EYNASIPPLLKntiDWVSRISRDgdrpfrpYAGLTVGLCSSSDGMFAGmRGLYHLRAVLMNVGVQIV 148
Cdd:COG0716   53 TWAGELPDDWE---DFLEELKED-------LSGKKVALFGTGDSSGYG-DALGELKELLEEKGAKVV 108
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH