NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|447074181|ref|WP_001151437|]
View 

MULTISPECIES: NAD(P)H:quinone oxidoreductase [Enterobacteriaceae]

Protein Classification

NAD(P)H:quinone oxidoreductase( domain architecture ID 10012077)

NAD(P)H:quinone oxidoreductase catalyzes the transfer of electrons from NADH to ubiquinone

CATH:  3.40.50.360
EC:  1.6.5.2
Gene Ontology:  GO:0010181|GO:0050660|GO:0030554|GO:0003955
SCOP:  3001217

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK03767 PRK03767
NAD(P)H:quinone oxidoreductase; Provisional
 1-198 1.38e-133

NAD(P)H:quinone oxidoreductase; Provisional


:

Pssm-ID: 179647  Cd Length: 200  Bit Score: 372.33  E-value: 1.38e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181   1 MAKVLVLYYSMYGHIETMARAVAEGASKVDGAEVVVKRVPETMPPQLFEKAGGKT-QTAPVATPQELADYDAIIFGTPTR 79
Cdd:PRK03767   1 MAKVLVLYYSMYGHIETMAEAVAEGAREVAGAEVTIKRVPETVPEEVAKKAGGKTdQAAPVATPDELADYDAIIFGTPTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181  80 FGNMSGQMRTFLDQTGGLWASGALYGKLASVFSSTGTG-GGQEQTITSTWTTLAHHGMVIVPIGYAAQELFDVSQVRGGT 158
Cdd:PRK03767  81 FGNMAGQMRNFLDQTGGLWAKGALVGKVGSVFTSTGTQhGGQETTITSTHTTLLHHGMVIVGLPYAFQGQMDVDEVTGGS 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 447074181 159 PYGATTIAGGDGSRQPSQEELSIARYQGEYVAGLAVKLNG 198
Cdd:PRK03767 161 PYGATTIAGGDGSRQPSENELAGARYQGRHVAEIAAKLAG 200
 
Name Accession Description Interval E-value
PRK03767 PRK03767
NAD(P)H:quinone oxidoreductase; Provisional
 1-198 1.38e-133

NAD(P)H:quinone oxidoreductase; Provisional


Pssm-ID: 179647  Cd Length: 200  Bit Score: 372.33  E-value: 1.38e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181   1 MAKVLVLYYSMYGHIETMARAVAEGASKVDGAEVVVKRVPETMPPQLFEKAGGKT-QTAPVATPQELADYDAIIFGTPTR 79
Cdd:PRK03767   1 MAKVLVLYYSMYGHIETMAEAVAEGAREVAGAEVTIKRVPETVPEEVAKKAGGKTdQAAPVATPDELADYDAIIFGTPTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181  80 FGNMSGQMRTFLDQTGGLWASGALYGKLASVFSSTGTG-GGQEQTITSTWTTLAHHGMVIVPIGYAAQELFDVSQVRGGT 158
Cdd:PRK03767  81 FGNMAGQMRNFLDQTGGLWAKGALVGKVGSVFTSTGTQhGGQETTITSTHTTLLHHGMVIVGLPYAFQGQMDVDEVTGGS 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 447074181 159 PYGATTIAGGDGSRQPSQEELSIARYQGEYVAGLAVKLNG 198
Cdd:PRK03767 161 PYGATTIAGGDGSRQPSENELAGARYQGRHVAEIAAKLAG 200
flav_wrbA TIGR01755
NAD(P)H:quinone oxidoreductase, type IV; This model represents a protein, WrbA, related to and ...
 2-196 8.18e-121

NAD(P)H:quinone oxidoreductase, type IV; This model represents a protein, WrbA, related to and slightly larger than flavodoxin. It was just shown, in E. coli and Archaeoglobus fulgidus (and previously for some eukaryotic homologs) to act as fourth type of NAD(P)H:quinone oxidoreductase. In E. coli, this protein was earlier reported to be produced during stationary phase, bind to the trp repressor, and make trp operon repression more efficient. WrbA does not interact with the trp operator by itself. Members are found in species in which homologs of the E. coli trp operon repressor TrpR (SP:P03032) are not detected. [Energy metabolism, Electron transport]


Pssm-ID: 130816 [Multi-domain]  Cd Length: 197  Bit Score: 339.95  E-value: 8.18e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181    2 AKVLVLYYSMYGHIETMARAVAEGASKVDGAEVVVKRVPETMPPQLFEKAGGKT-QTAPVATPQELADYDAIIFGTPTRF 80
Cdd:TIGR01755   1 VKVLVLYYSMYGHIETMARAVAEGAREVDGAEVVVKRVPETVPEEVAEKSHGKTdQTAPVATPQELADYDAIIFGTPTRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181   81 GNMSGQMRTFLDQTGGLWASGALYGKLASVFSSTGTG-GGQEQTITSTWTTLAHHGMVIVPIGYAAQELFDVSQVRGGTP 159
Cdd:TIGR01755  81 GNMASQMRNFLDQTGGLWASGALVGKVGSVFTSTGTQhGGQESTILSTWTTLLHHGMIIVPLPYAAQEQMGVDEVRGGSP 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 447074181  160 YGATTIAGGDGSRQPSQEELSIARYQGEYVAGLAVKL 196
Cdd:TIGR01755 161 YGATTIAGGDGSRQPSAEELDIARYQGRHVAGLAAKL 197
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 3-196 9.83e-50

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 159.32  E-value: 9.83e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181   3 KVLVLYYS--MYGHIETMARAVAEGASKvDGAEVVVKRVPETM--PPQLFEKAGGKTQTAPV-ATPQELADYDAIIFGTP 77
Cdd:COG0655    1 KILVINGSprKNGNTAALAEAVAEGAEE-AGAEVELIRLADLDikPCIGCGGTGKCVIKDDMnAIYEKLLEADGIIFGSP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181  78 TRFGNMSGQMRTFLDQTGGLWASGA-LYGKLASVFSSTGtGGGQEQTITSTWTTLAHHGMVIVPIGyaaqelfdvsqvrg 156
Cdd:COG0655   80 TYFGNMSAQLKAFIDRLYALWAKGKlLKGKVGAVFTTGG-HGGAEATLLSLNTFLLHHGMIVVGLP-------------- 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 447074181 157 gtPYGAttIAGGDGSRQPSQEELSIARYQGEYVAGLAVKL 196
Cdd:COG0655  145 --PYGA--VGGGGPGDVLDEEGLATARELGKRLAELAKKL 180
FMN_red pfam03358
NADPH-dependent FMN reductase;
3-145 9.30e-17

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 73.43  E-value: 9.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181    3 KVLVLYYSMY--GHIETMARAVAEGASKvdGAEVVVKRVPETMPPQLFEKAGGKTQTAPVATP--QELADYDAIIFGTPT 78
Cdd:pfam03358   2 KILAISGSPRkgSNTRKLARWAAELLEE--GAEVELIDLADLILPLCDEDLEEEQGDPDDVQElrEKIAAADAIIIVTPE 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447074181   79 RFGNMSGQMRTFLDQTGGLWASGALYGKLASVFSSTGTGGG----QEQTITStwttLAHHGMVIVPIGYAA 145
Cdd:pfam03358  80 YNGSVSGLLKNAIDWLSRLRGGKELRGKPVAIVSTGGGRSGglraVEQLRQV----LAELGAIVVPSGQVA 146
 
Name Accession Description Interval E-value
PRK03767 PRK03767
NAD(P)H:quinone oxidoreductase; Provisional
 1-198 1.38e-133

NAD(P)H:quinone oxidoreductase; Provisional


Pssm-ID: 179647  Cd Length: 200  Bit Score: 372.33  E-value: 1.38e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181   1 MAKVLVLYYSMYGHIETMARAVAEGASKVDGAEVVVKRVPETMPPQLFEKAGGKT-QTAPVATPQELADYDAIIFGTPTR 79
Cdd:PRK03767   1 MAKVLVLYYSMYGHIETMAEAVAEGAREVAGAEVTIKRVPETVPEEVAKKAGGKTdQAAPVATPDELADYDAIIFGTPTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181  80 FGNMSGQMRTFLDQTGGLWASGALYGKLASVFSSTGTG-GGQEQTITSTWTTLAHHGMVIVPIGYAAQELFDVSQVRGGT 158
Cdd:PRK03767  81 FGNMAGQMRNFLDQTGGLWAKGALVGKVGSVFTSTGTQhGGQETTITSTHTTLLHHGMVIVGLPYAFQGQMDVDEVTGGS 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 447074181 159 PYGATTIAGGDGSRQPSQEELSIARYQGEYVAGLAVKLNG 198
Cdd:PRK03767 161 PYGATTIAGGDGSRQPSENELAGARYQGRHVAEIAAKLAG 200
flav_wrbA TIGR01755
NAD(P)H:quinone oxidoreductase, type IV; This model represents a protein, WrbA, related to and ...
 2-196 8.18e-121

NAD(P)H:quinone oxidoreductase, type IV; This model represents a protein, WrbA, related to and slightly larger than flavodoxin. It was just shown, in E. coli and Archaeoglobus fulgidus (and previously for some eukaryotic homologs) to act as fourth type of NAD(P)H:quinone oxidoreductase. In E. coli, this protein was earlier reported to be produced during stationary phase, bind to the trp repressor, and make trp operon repression more efficient. WrbA does not interact with the trp operator by itself. Members are found in species in which homologs of the E. coli trp operon repressor TrpR (SP:P03032) are not detected. [Energy metabolism, Electron transport]


Pssm-ID: 130816 [Multi-domain]  Cd Length: 197  Bit Score: 339.95  E-value: 8.18e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181    2 AKVLVLYYSMYGHIETMARAVAEGASKVDGAEVVVKRVPETMPPQLFEKAGGKT-QTAPVATPQELADYDAIIFGTPTRF 80
Cdd:TIGR01755   1 VKVLVLYYSMYGHIETMARAVAEGAREVDGAEVVVKRVPETVPEEVAEKSHGKTdQTAPVATPQELADYDAIIFGTPTRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181   81 GNMSGQMRTFLDQTGGLWASGALYGKLASVFSSTGTG-GGQEQTITSTWTTLAHHGMVIVPIGYAAQELFDVSQVRGGTP 159
Cdd:TIGR01755  81 GNMASQMRNFLDQTGGLWASGALVGKVGSVFTSTGTQhGGQESTILSTWTTLLHHGMIIVPLPYAAQEQMGVDEVRGGSP 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 447074181  160 YGATTIAGGDGSRQPSQEELSIARYQGEYVAGLAVKL 196
Cdd:TIGR01755 161 YGATTIAGGDGSRQPSAEELDIARYQGRHVAGLAAKL 197
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 3-196 9.83e-50

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 159.32  E-value: 9.83e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181   3 KVLVLYYS--MYGHIETMARAVAEGASKvDGAEVVVKRVPETM--PPQLFEKAGGKTQTAPV-ATPQELADYDAIIFGTP 77
Cdd:COG0655    1 KILVINGSprKNGNTAALAEAVAEGAEE-AGAEVELIRLADLDikPCIGCGGTGKCVIKDDMnAIYEKLLEADGIIFGSP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181  78 TRFGNMSGQMRTFLDQTGGLWASGA-LYGKLASVFSSTGtGGGQEQTITSTWTTLAHHGMVIVPIGyaaqelfdvsqvrg 156
Cdd:COG0655   80 TYFGNMSAQLKAFIDRLYALWAKGKlLKGKVGAVFTTGG-HGGAEATLLSLNTFLLHHGMIVVGLP-------------- 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 447074181 157 gtPYGAttIAGGDGSRQPSQEELSIARYQGEYVAGLAVKL 196
Cdd:COG0655  145 --PYGA--VGGGGPGDVLDEEGLATARELGKRLAELAKKL 180
FMN_red pfam03358
NADPH-dependent FMN reductase;
3-145 9.30e-17

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 73.43  E-value: 9.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181    3 KVLVLYYSMY--GHIETMARAVAEGASKvdGAEVVVKRVPETMPPQLFEKAGGKTQTAPVATP--QELADYDAIIFGTPT 78
Cdd:pfam03358   2 KILAISGSPRkgSNTRKLARWAAELLEE--GAEVELIDLADLILPLCDEDLEEEQGDPDDVQElrEKIAAADAIIIVTPE 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447074181   79 RFGNMSGQMRTFLDQTGGLWASGALYGKLASVFSSTGTGGG----QEQTITStwttLAHHGMVIVPIGYAA 145
Cdd:pfam03358  80 YNGSVSGLLKNAIDWLSRLRGGKELRGKPVAIVSTGGGRSGglraVEQLRQV----LAELGAIVVPSGQVA 146
NorV COG0426
Flavorubredoxin [Energy production and conversion];
3-119 6.15e-15

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 71.79  E-value: 6.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181   3 KVLVLYYSMYGHIETMARAVAEGASKVdGAEVVVKRVPETMPPQLFEkaggktqtapvatpqELADYDAIIFGTPTRFGN 82
Cdd:COG0426  248 KVVIVYASMYGNTEKMAEAIAEGLTEE-GVKVKLYDLEKTDPSEIIT---------------EIFDAKGIVIGSPTYNGG 311

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 447074181  83 MSGQMRTFLDQTGGLwasgALYGKLASVFSSTGTGGG 119
Cdd:COG0426  312 AFPPIADLLGYLKGL----APKNKLAGAFGSYGWSGE 344
FldA COG0716
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ...
 4-120 3.12e-13

Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440480 [Multi-domain]  Cd Length: 135  Bit Score: 63.77  E-value: 3.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181   4 VLVLYYSMYGHIETMARAVAEgasKVDGAEVVVKRVPEtmppqlfekaggktqtapvATPQELADYDAIIFGTPTRFGNM 83
Cdd:COG0716    1 ILIVYGSTTGNTEKVAEAIAE---ALGAAGVDLFEIED-------------------ADLDDLEDYDLLILGTPTWAGEL 58

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 447074181  84 SGQMRTFLDQTGGLWAsgalyGKLASVFsstGTGGGQ 120
Cdd:COG0716   59 PDDWEDFLEELKEDLS-----GKKVALF---GTGDSS 87
PRK05569 PRK05569
flavodoxin; Provisional
 1-93 1.62e-08

flavodoxin; Provisional


Pssm-ID: 135442 [Multi-domain]  Cd Length: 141  Bit Score: 51.37  E-value: 1.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181   1 MAKVLVLYYSMYGHIETMARAVAEGAsKVDGAEVVVKRVPEtmppqlfekaggktqtapvATPQELADYDAIIFGTPTRF 80
Cdd:PRK05569   1 MKKVSIIYWSCGGNVEVLANTIADGA-KEAGAEVTIKHVAD-------------------AKVEDVLEADAVAFGSPSMD 60

                         90
                 ....*....|....*
gi 447074181  81 GNMSGQ--MRTFLDQ 93
Cdd:PRK05569  61 NNNIEQeeMAPFLDQ 75
flav_short TIGR01753
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin ...
 4-118 2.46e-08

flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin mononucleotide (FMN) prosthetic group. They can act in nitrogen fixation by nitrogenase, in sulfite reduction, and light-dependent NADP+ reduction in during photosynthesis, among other roles. This model describes the short chain type. Many of these are involved in sulfite reduction. [Energy metabolism, Electron transport]


Pssm-ID: 273789 [Multi-domain]  Cd Length: 140  Bit Score: 50.80  E-value: 2.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181    4 VLVLYYSMYGHIETMARAVAEGAsKVDGAEVVVKRVPEtmppqlfekaggktqtapvATPQELADYDAIIFGTPTrFGN- 82
Cdd:TIGR01753   1 ILIVYASMTGNTEEMANIIAEGL-KEAGAEVDLLEVAD-------------------ADAEDLLSYDAVLLGCST-WGDe 59

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 447074181   83 --MSGQMRTFLDQTGGLWASgalyGKLASVFSSTGTGG 118
Cdd:TIGR01753  60 dlEQDDFEPFFEELEDIDLG----GKKVALFGSGDWGY 93
Flavodoxin_1 pfam00258
Flavodoxin;
6-135 2.93e-08

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 50.45  E-value: 2.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181    6 VLYYSMYGHIETMARAVAEGASKVDGAEVVVKRVPETMPPQLFEKAGG---KTQTAPVATPQ---ELADYDAIIFGTP-- 77
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVVDLDDVDETLSEIEEEDLllvVVSTWGEGEPPdnaKPFVDWLLLFGTLed 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447074181   78 TRFGNMSGQMRTFLDQTGGL--WASGALYGKLASVFSST--GTGGGQEQTITSTWTTLAHHG 135
Cdd:pfam00258  81 GDLSGLKYAVFGLGDSGYEGfcGAAKKLDEKLSELGASRvgPLGEGDEDPQEDGLEEAFEAW 142
PRK05568 PRK05568
flavodoxin; Provisional
 1-120 1.12e-07

flavodoxin; Provisional


Pssm-ID: 235508 [Multi-domain]  Cd Length: 142  Bit Score: 49.04  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181   1 MAKVLVLYYSMYGHIETMARAVAEGAsKVDGAEVVVKRVPEtmppqlfekaggktqtapvATPQELADYDAIIFGTPTRF 80
Cdd:PRK05568   1 MKKINIIYWSGTGNTEAMANLIAEGA-KENGAEVKLLNVSE-------------------ASVDDVKGADVVALGSPAMG 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 447074181  81 GNM--SGQMRTFLDQTgglwaSGALYGKLASVFSSTGTGGGQ 120
Cdd:PRK05568  61 DEVleEGEMEPFVESI-----SSLVKGKKLVLFGSYGWGDGE 97
HemG COG4635
Protoporphyrinogen IX oxidase, menaquinone-dependent (flavodoxin domain) [Coenzyme transport ...
 2-93 1.48e-05

Protoporphyrinogen IX oxidase, menaquinone-dependent (flavodoxin domain) [Coenzyme transport and metabolism];


Pssm-ID: 443673  Cd Length: 179  Bit Score: 43.73  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181   2 AKVLVLYYSMYGHIETMARAVAEGaskvdgaevvvkrvpetmppqlFEKAGGKTQTAPVATPQE--LADYDAIIFGTPTR 79
Cdd:COG4635    1 MKVLILYASRDGQTRKIAERIAEV----------------------LREAGHDVDLVDLEDAPDldLAGYDAVVIGASIR 58

                         90
                 ....*....|....
gi 447074181  80 FGNMSGQMRTFLDQ 93
Cdd:COG4635   59 YGKWLPEAVRFVRR 72
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 3-134 3.29e-04

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: 40.01  E-value: 3.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181    3 KVLVLYysmyGHIET------MARAVAEGASKvDGAEVVVKRVPEtMPPQLFEKAGGKTQTAPVATP------QELADYD 70
Cdd:pfam02525   2 KILIIN----AHPRPgsfssrLADALVEALKA-AGHEVTVRDLYA-LFLPVLDAEDLADLTYPQGAAdveseqEELLAAD 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447074181   71 AIIFGTPTRFGNMSGQMRTFLDQ----------TGGLWASGALYGKLASVFSSTGTGGGQEQTITSTWTTLAHH 134
Cdd:pfam02525  76 VIVFQFPLYWFSVPALLKGWIDRvlragfafkyEEGGPGGGGLLGKKVLVIVTTGGPEYAYGKGGYNGFSLDEL 149
PRK06756 PRK06756
flavodoxin; Provisional
 1-113 3.35e-04

flavodoxin; Provisional


Pssm-ID: 168663 [Multi-domain]  Cd Length: 148  Bit Score: 39.48  E-value: 3.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181   1 MAKVLVLYYSMYGHIETMARAVAEGASKVdGAEVVVKRVpetmppqlfekaggktQTAPVATpqELADYDAIIFGTPTRF 80
Cdd:PRK06756   1 MSKLVMIFASMSGNTEEMADHIAGVIRET-ENEIEVIDI----------------MDSPEAS--ILEQYDGIILGAYTWG 61

                         90       100       110
                 ....*....|....*....|....*....|....
gi 447074181  81 -GNMSGQMRTFLDQTGGLwasgALYGKLASVFSS 113
Cdd:PRK06756  62 dGDLPDDFLDFYDAMDSI----DLTGKKAAVFGS 91
Flavodoxin_5 pfam12724
Flavodoxin domain; This is a family of flavodoxins. Flavodoxins are electron transfer proteins ...
 5-121 4.49e-04

Flavodoxin domain; This is a family of flavodoxins. Flavodoxins are electron transfer proteins that carry a molecule of non-covalently bound FMN.


Pssm-ID: 463681 [Multi-domain]  Cd Length: 144  Bit Score: 38.78  E-value: 4.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181    5 LVLYYSMYGHIETMARAVAEgASKVDGAEVVVKRVPETMppqlfekaggktqtapvatpqELADYDAIIFGTPTRFGNMS 84
Cdd:pfam12724   1 LILYSSRDGQTKKIAERIAE-ELREEGELVDVEDVEAGE---------------------DLSSYDAVVIGASIYYGKHL 58

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 447074181   85 GQMRTFLDQTGglwasGALYGKLASVFSSTGTGGGQE 121
Cdd:pfam12724  59 PELRQFVTKHR-----DELSSKPVAFFSVNLTARKPE 90
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
16-150 5.18e-04

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 38.98  E-value: 5.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181  16 ETMARAVAEGASKvDGAEVVVKRVPETMPPQLFEKAGGKTQTAPVATPQE-LADYDAIIFGTPTRFGNMSGQMRTFLDqt 94
Cdd:COG0431   17 RKLARAAAELAPA-AGAEVELIDLRDLDLPLYDEDLEADGAPPAVKALREaIAAADGVVIVTPEYNGSYPGVLKNALD-- 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181  95 gglWAS-GALYGKLASVFSSTGTGGGQEQTITSTWTTLAHHGMVIVPIGYA---AQELFD 150
Cdd:COG0431   94 ---WLSrSELAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLPPQVSipkAGEAFD 150
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 3-116 9.97e-03

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 35.59  E-value: 9.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447074181   3 KVLVLYysmyGHIE------TMARAVAEGASKvDGAEVVV-----KRVPETMPPQLFEKAGgkTQTAPVATPQE-LADYD 70
Cdd:COG2249    1 KILIIY----AHPDpssfnaALAEAAAEGLEA-AGHEVTVhdlyaEGFDPVLSAADFYRDG--PLPIDVAAEQElLLWAD 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 447074181  71 AIIFGTPTRFGNMSGQMRTFLDQ---------TGGLWASGALYGKLASVFSSTGT 116
Cdd:COG2249   74 HLVFQFPLWWYSMPALLKGWIDRvltpgfaygYGGGYPGGLLKGKKALLVVTTGG 128
 
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