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Conserved domains on  [gi|1237882491|gb|PAJ76303|]
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NADPH-dependent FMN reductase [Pseudoalteromonas sp. NBT06-2]

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];
1-164 1.07e-45

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


:

Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 147.22  E-value: 1.07e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882491   1 MKVLAFAASNSKNSINKQLATYAANLVE--NAEVEILDINDYEMPIFSEDREKKlGQPEQAQAFYKKLGEADAIIISFAE 78
Cdd:COG0431     1 MKILVISGSLRPGSFNRKLARAAAELAPaaGAEVELIDLRDLDLPLYDEDLEAD-GAPPAVKALREAIAAADGVVIVTPE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882491  79 HNGSYTAAYKNLFDWTSRidmKVFQSKSMLMLATSPGPGGANSVLTTASGSAPYFAANVK-ASISIPSFYDNFDvETGKL 157
Cdd:COG0431    80 YNGSYPGVLKNALDWLSR---SELAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLpPQVSIPKAGEAFD-EDGEL 155

                  ....*..
gi 1237882491 158 TNPELID 164
Cdd:COG0431   156 TDEELAE 162
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
1-164 1.07e-45

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 147.22  E-value: 1.07e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882491   1 MKVLAFAASNSKNSINKQLATYAANLVE--NAEVEILDINDYEMPIFSEDREKKlGQPEQAQAFYKKLGEADAIIISFAE 78
Cdd:COG0431     1 MKILVISGSLRPGSFNRKLARAAAELAPaaGAEVELIDLRDLDLPLYDEDLEAD-GAPPAVKALREAIAAADGVVIVTPE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882491  79 HNGSYTAAYKNLFDWTSRidmKVFQSKSMLMLATSPGPGGANSVLTTASGSAPYFAANVK-ASISIPSFYDNFDvETGKL 157
Cdd:COG0431    80 YNGSYPGVLKNALDWLSR---SELAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLpPQVSIPKAGEAFD-EDGEL 155

                  ....*..
gi 1237882491 158 TNPELID 164
Cdd:COG0431   156 TDEELAE 162
FMN_red pfam03358
NADPH-dependent FMN reductase;
1-123 1.48e-39

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 131.21  E-value: 1.48e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882491   1 MKVLAFAASNSKNSINKQLATYAANLVE-NAEVEILDINDYEMPIFSEDREKKLGQPEQAQAFYKKLGEADAIIISFAEH 79
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEeGAEVELIDLADLILPLCDEDLEEEQGDPDDVQELREKIAAADAIIIVTPEY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1237882491  80 NGSYTAAYKNLFDWTSRI-DMKVFQSKSMLMLATSPGP-GGANSVL 123
Cdd:pfam03358  81 NGSVSGLLKNAIDWLSRLrGGKELRGKPVAIVSTGGGRsGGLRAVE 126
 
Name Accession Description Interval E-value
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
1-164 1.07e-45

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 147.22  E-value: 1.07e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882491   1 MKVLAFAASNSKNSINKQLATYAANLVE--NAEVEILDINDYEMPIFSEDREKKlGQPEQAQAFYKKLGEADAIIISFAE 78
Cdd:COG0431     1 MKILVISGSLRPGSFNRKLARAAAELAPaaGAEVELIDLRDLDLPLYDEDLEAD-GAPPAVKALREAIAAADGVVIVTPE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882491  79 HNGSYTAAYKNLFDWTSRidmKVFQSKSMLMLATSPGPGGANSVLTTASGSAPYFAANVK-ASISIPSFYDNFDvETGKL 157
Cdd:COG0431    80 YNGSYPGVLKNALDWLSR---SELAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLpPQVSIPKAGEAFD-EDGEL 155

                  ....*..
gi 1237882491 158 TNPELID 164
Cdd:COG0431   156 TDEELAE 162
FMN_red pfam03358
NADPH-dependent FMN reductase;
1-123 1.48e-39

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 131.21  E-value: 1.48e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882491   1 MKVLAFAASNSKNSINKQLATYAANLVE-NAEVEILDINDYEMPIFSEDREKKLGQPEQAQAFYKKLGEADAIIISFAEH 79
Cdd:pfam03358   1 MKILAISGSPRKGSNTRKLARWAAELLEeGAEVELIDLADLILPLCDEDLEEEQGDPDDVQELREKIAAADAIIIVTPEY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1237882491  80 NGSYTAAYKNLFDWTSRI-DMKVFQSKSMLMLATSPGP-GGANSVL 123
Cdd:pfam03358  81 NGSVSGLLKNAIDWLSRLrGGKELRGKPVAIVSTGGGRsGGLRAVE 126
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
2-125 1.03e-10

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 57.25  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882491   2 KVLAFAASNSKNSINKQLATYAANLVE--NAEVEILDINDYEM-PIFSEDREKKLGQPEQAQAFYKKLGEADAIIISFAE 78
Cdd:COG0655     1 KILVINGSPRKNGNTAALAEAVAEGAEeaGAEVELIRLADLDIkPCIGCGGTGKCVIKDDMNAIYEKLLEADGIIFGSPT 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1237882491  79 HNGSYTAAYKNLFDWTSRI--DMKVFQSKSMLMLATSpGPGGANSVLTT 125
Cdd:COG0655    81 YFGNMSAQLKAFIDRLYALwaKGKLLKGKVGAVFTTG-GHGGAEATLLS 128
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
1-117 7.43e-10

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: 55.42  E-value: 7.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882491   1 MKVLAFAASNSKNSINKQLA-TYAANLVE-NAEVEILDINDYEMPIFSEDREKKLGQPEQ---AQAFYKKLGEADAIIIS 75
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLAdALVEALKAaGHEVTVRDLYALFLPVLDAEDLADLTYPQGaadVESEQEELLAADVIVFQ 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1237882491  76 FAEHNGSYTAAYKNLFD-----------WTSRIDMKVFQSKSMLMLATSPGPG 117
Cdd:pfam02525  81 FPLYWFSVPALLKGWIDrvlragfafkyEEGGPGGGGLLGKKVLVIVTTGGPE 133
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
12-76 4.22e-04

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 39.05  E-value: 4.22e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237882491  12 KNSINKQLATYAANLVENA--EVEILDIndYEM---PIFS-EDREKKLGQPEQAQAFYKKLGEADAIIISF 76
Cdd:COG2249    11 PSSFNAALAEAAAEGLEAAghEVTVHDL--YAEgfdPVLSaADFYRDGPLPIDVAAEQELLLWADHLVFQF 79
 
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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