NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|759909278|ref|WP_043595342|]
View 

NADPH-dependent FMN reductase [Chromobacterium violaceum]

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];
4-163 3.01e-44

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


:

Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 144.14  E-value: 3.01e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759909278   4 IKVLGICGSLRRASANMGLLRHAASCLPA-GMELQIADLSEV--PFYNADLASK--PAPVARLLEQIGEADALLLACPEY 78
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPAaGAEVELIDLRDLdlPLYDEDLEADgaPPAVKALREAIAAADGVVIVTPEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759909278  79 NYSMAPALKNALDWASREPenklLAGKPVAIMGA-GGGMGTSRAQYHLRQTCVFLDLLPLNkPEVFANAFAGGFDGDGNL 157
Cdd:COG0431   81 NGSYPGVLKNALDWLSRSE----LAGKPVALVSTsGGARGGLRALEHLRPVLSELGAVVLP-PQVSIPKAGEAFDEDGEL 155

                 ....*.
gi 759909278 158 TDERLQ 163
Cdd:COG0431  156 TDEELA 161
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
4-163 3.01e-44

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 144.14  E-value: 3.01e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759909278   4 IKVLGICGSLRRASANMGLLRHAASCLPA-GMELQIADLSEV--PFYNADLASK--PAPVARLLEQIGEADALLLACPEY 78
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPAaGAEVELIDLRDLdlPLYDEDLEADgaPPAVKALREAIAAADGVVIVTPEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759909278  79 NYSMAPALKNALDWASREPenklLAGKPVAIMGA-GGGMGTSRAQYHLRQTCVFLDLLPLNkPEVFANAFAGGFDGDGNL 157
Cdd:COG0431   81 NGSYPGVLKNALDWLSRSE----LAGKPVALVSTsGGARGGLRALEHLRPVLSELGAVVLP-PQVSIPKAGEAFDEDGEL 155

                 ....*.
gi 759909278 158 TDERLQ 163
Cdd:COG0431  156 TDEELA 161
FMN_red pfam03358
NADPH-dependent FMN reductase;
4-149 5.30e-37

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 125.04  E-value: 5.30e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759909278    4 IKVLGICGSLRRASANMGLLRHAASCLPAGMELQIADLSEV--PFYNADLASK---PAPVARLLEQIGEADALLLACPEY 78
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEEGAEVELIDLADLilPLCDEDLEEEqgdPDDVQELREKIAAADAIIIVTPEY 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759909278   79 NYSMAPALKNALDWASREPENKLLAGKPVAIMGAGGGMG-TSRAQYHLRQTCVFLDLLPLNKPEVFANAFAG 149
Cdd:pfam03358  81 NGSVSGLLKNAIDWLSRLRGGKELRGKPVAIVSTGGGRSgGLRAVEQLRQVLAELGAIVVPSGQVAVGNATD 152
PRK10569 PRK10569
NAD(P)H-dependent FMN reductase; Provisional
6-91 6.00e-03

NAD(P)H-dependent FMN reductase; Provisional


Pssm-ID: 182557  Cd Length: 191  Bit Score: 36.12  E-value: 6.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759909278   6 VLGICGSLRRASANMGLLRHAASCLPA-GME---LQIADLSEVPFYNADLASkPApVARLLEQIGEADALLLACPEYNYS 81
Cdd:PRK10569   3 VITLAGSPRFPSRSSALLEYAREWLNGlGVEvyhWNLQNFAPEDLLYARFDS-PA-LKTFTEQLAQADGLIVATPVYKAS 80
                         90
                 ....*....|
gi 759909278  82 MAPALKNALD 91
Cdd:PRK10569  81 FSGALKTLLD 90
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
4-163 3.01e-44

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 144.14  E-value: 3.01e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759909278   4 IKVLGICGSLRRASANMGLLRHAASCLPA-GMELQIADLSEV--PFYNADLASK--PAPVARLLEQIGEADALLLACPEY 78
Cdd:COG0431    1 MKILVISGSLRPGSFNRKLARAAAELAPAaGAEVELIDLRDLdlPLYDEDLEADgaPPAVKALREAIAAADGVVIVTPEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759909278  79 NYSMAPALKNALDWASREPenklLAGKPVAIMGA-GGGMGTSRAQYHLRQTCVFLDLLPLNkPEVFANAFAGGFDGDGNL 157
Cdd:COG0431   81 NGSYPGVLKNALDWLSRSE----LAGKPVALVSTsGGARGGLRALEHLRPVLSELGAVVLP-PQVSIPKAGEAFDEDGEL 155

                 ....*.
gi 759909278 158 TDERLQ 163
Cdd:COG0431  156 TDEELA 161
FMN_red pfam03358
NADPH-dependent FMN reductase;
4-149 5.30e-37

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 125.04  E-value: 5.30e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759909278    4 IKVLGICGSLRRASANMGLLRHAASCLPAGMELQIADLSEV--PFYNADLASK---PAPVARLLEQIGEADALLLACPEY 78
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEEGAEVELIDLADLilPLCDEDLEEEqgdPDDVQELREKIAAADAIIIVTPEY 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759909278   79 NYSMAPALKNALDWASREPENKLLAGKPVAIMGAGGGMG-TSRAQYHLRQTCVFLDLLPLNKPEVFANAFAG 149
Cdd:pfam03358  81 NGSVSGLLKNAIDWLSRLRGGKELRGKPVAIVSTGGGRSgGLRAVEQLRQVLAELGAIVVPSGQVAVGNATD 152
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
5-107 8.87e-11

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 57.63  E-value: 8.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759909278   5 KVLGICGSLRRASANMGLLRHAASCLP-AGMELQIADLSEVPFYNADLASKPAP------VARLLEQIGEADALLLACPE 77
Cdd:COG0655    1 KILVINGSPRKNGNTAALAEAVAEGAEeAGAEVELIRLADLDIKPCIGCGGTGKcvikddMNAIYEKLLEADGIIFGSPT 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 759909278  78 YNYSMAPALKNALD-WASREPENKLLAGKPV 107
Cdd:COG0655   81 YFGNMSAQLKAFIDrLYALWAKGKLLKGKVG 111
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
5-107 9.25e-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: 46.94  E-value: 9.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759909278    5 KVLGICGSLRRASANMGLLRHAASCLPA-GMELQIADLSE--VPFYNADLAS------KPAPVARLLEQIGEADALLLAC 75
Cdd:pfam02525   2 KILIINAHPRPGSFSSRLADALVEALKAaGHEVTVRDLYAlfLPVLDAEDLAdltypqGAADVESEQEELLAADVIVFQF 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 759909278   76 PEYNYSMAPALKNALD----------WASREPENKLLAGKPV 107
Cdd:pfam02525  82 PLYWFSVPALLKGWIDrvlragfafkYEEGGPGGGGLLGKKV 123
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
14-107 3.70e-05

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 42.13  E-value: 3.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759909278  14 RRASANMGLLRHAASCLP-AGMELQIADLSEVPF----YNADLASK---PAPVARLLEQIGEADALLLACPEYNYSMaPA 85
Cdd:COG2249   10 DPSSFNAALAEAAAEGLEaAGHEVTVHDLYAEGFdpvlSAADFYRDgplPIDVAAEQELLLWADHLVFQFPLWWYSM-PA 88
                         90       100       110
                 ....*....|....*....|....*....|..
gi 759909278  86 -LKNALD------WA---SREPENKLLAGKPV 107
Cdd:COG2249   89 lLKGWIDrvltpgFAygyGGGYPGGLLKGKKA 120
PRK10569 PRK10569
NAD(P)H-dependent FMN reductase; Provisional
6-91 6.00e-03

NAD(P)H-dependent FMN reductase; Provisional


Pssm-ID: 182557  Cd Length: 191  Bit Score: 36.12  E-value: 6.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759909278   6 VLGICGSLRRASANMGLLRHAASCLPA-GME---LQIADLSEVPFYNADLASkPApVARLLEQIGEADALLLACPEYNYS 81
Cdd:PRK10569   3 VITLAGSPRFPSRSSALLEYAREWLNGlGVEvyhWNLQNFAPEDLLYARFDS-PA-LKTFTEQLAQADGLIVATPVYKAS 80
                         90
                 ....*....|
gi 759909278  82 MAPALKNALD 91
Cdd:PRK10569  81 FSGALKTLLD 90
 
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