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Conserved domains on  [gi|493862570|ref|WP_006809323|]
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MULTISPECIES: NAD(P)H:quinone oxidoreductase [Enterobacter]

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

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List of domain hits

 Name Accession Description Interval E-value
PRK03767 PRK03767
NAD(P)H:quinone oxidoreductase; Provisional
 1-198 7.46e-133

NAD(P)H:quinone oxidoreductase; Provisional


:

Pssm-ID: 179647  Cd Length: 200  Bit Score: 370.41  E-value: 7.46e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570   1 MAKVLVLYYSMYGHIETMAHAVAEGANRVDGVEVVVKRVPETMQAEAFAKAGGKT-QNAPVATPQELADYDAIIFGTPTR 79
Cdd:PRK03767   1 MAKVLVLYYSMYGHIETMAEAVAEGAREVAGAEVTIKRVPETVPEEVAKKAGGKTdQAAPVATPDELADYDAIIFGTPTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570  80 FGNMSGQMRTFLDQTGGLWASGALYGKLASVFSSTGTG-GGQEQTITSTWTTLAHHGMVIVPIGYGAQELFDVSQVRGGT 158
Cdd:PRK03767  81 FGNMAGQMRNFLDQTGGLWAKGALVGKVGSVFTSTGTQhGGQETTITSTHTTLLHHGMVIVGLPYAFQGQMDVDEVTGGS 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 493862570 159 PYGATTIAGGDGSRQPSNEELSIARYQGEYVAGLAKKLNG 198
Cdd:PRK03767 161 PYGATTIAGGDGSRQPSENELAGARYQGRHVAEIAAKLAG 200
 
Name Accession Description Interval E-value
PRK03767 PRK03767
NAD(P)H:quinone oxidoreductase; Provisional
 1-198 7.46e-133

NAD(P)H:quinone oxidoreductase; Provisional


Pssm-ID: 179647  Cd Length: 200  Bit Score: 370.41  E-value: 7.46e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570   1 MAKVLVLYYSMYGHIETMAHAVAEGANRVDGVEVVVKRVPETMQAEAFAKAGGKT-QNAPVATPQELADYDAIIFGTPTR 79
Cdd:PRK03767   1 MAKVLVLYYSMYGHIETMAEAVAEGAREVAGAEVTIKRVPETVPEEVAKKAGGKTdQAAPVATPDELADYDAIIFGTPTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570  80 FGNMSGQMRTFLDQTGGLWASGALYGKLASVFSSTGTG-GGQEQTITSTWTTLAHHGMVIVPIGYGAQELFDVSQVRGGT 158
Cdd:PRK03767  81 FGNMAGQMRNFLDQTGGLWAKGALVGKVGSVFTSTGTQhGGQETTITSTHTTLLHHGMVIVGLPYAFQGQMDVDEVTGGS 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 493862570 159 PYGATTIAGGDGSRQPSNEELSIARYQGEYVAGLAKKLNG 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 3.80e-114

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: 323.00  E-value: 3.80e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570    2 AKVLVLYYSMYGHIETMAHAVAEGANRVDGVEVVVKRVPETMQAEAFAKAGGKT-QNAPVATPQELADYDAIIFGTPTRF 80
Cdd:TIGR01755   1 VKVLVLYYSMYGHIETMARAVAEGAREVDGAEVVVKRVPETVPEEVAEKSHGKTdQTAPVATPQELADYDAIIFGTPTRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570   81 GNMSGQMRTFLDQTGGLWASGALYGKLASVFSSTGTG-GGQEQTITSTWTTLAHHGMVIVPIGYGAQELFDVSQVRGGTP 159
Cdd:TIGR01755  81 GNMASQMRNFLDQTGGLWASGALVGKVGSVFTSTGTQhGGQESTILSTWTTLLHHGMIIVPLPYAAQEQMGVDEVRGGSP 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 493862570  160 YGATTIAGGDGSRQPSNEELSIARYQGEYVAGLAKKL 196
Cdd:TIGR01755 161 YGATTIAGGDGSRQPSAEELDIARYQGRHVAGLAAKL 197
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 3-196 1.30e-49

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 158.94  E-value: 1.30e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570   3 KVLVLYYS--MYGHIETMAHAVAEGANRvDGVEVVVKRVPETMQAEAFAKAGGK---TQNAPVATPQELADYDAIIFGTP 77
Cdd:COG0655    1 KILVINGSprKNGNTAALAEAVAEGAEE-AGAEVELIRLADLDIKPCIGCGGTGkcvIKDDMNAIYEKLLEADGIIFGSP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570  78 TRFGNMSGQMRTFLDQTGGLWASGA-LYGKLASVFSSTGtGGGQEQTITSTWTTLAHHGMVIVPIGygaqelfdvsqvrg 156
Cdd:COG0655   80 TYFGNMSAQLKAFIDRLYALWAKGKlLKGKVGAVFTTGG-HGGAEATLLSLNTFLLHHGMIVVGLP-------------- 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 493862570 157 gtPYGAttIAGGDGSRQPSNEELSIARYQGEYVAGLAKKL 196
Cdd:COG0655  145 --PYGA--VGGGGPGDVLDEEGLATARELGKRLAELAKKL 180
FMN_red pfam03358
NADPH-dependent FMN reductase;
3-143 4.30e-12

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 61.10  E-value: 4.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570    3 KVLVLYYSMY--GHIETMAHAVAEGANRVDGVEVV-VKRVPETMQAEAFAKAGGKTQNAPVATPQeLADYDAIIFGTPTR 79
Cdd:pfam03358   2 KILAISGSPRkgSNTRKLARWAAELLEEGAEVELIdLADLILPLCDEDLEEEQGDPDDVQELREK-IAAADAIIIVTPEY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493862570   80 FGNMSGQMRTFLDQTGGLWASGALYGKLASVFSSTGTGGG----QEQTITStwttLAHHGMVIVPIGY 143
Cdd:pfam03358  81 NGSVSGLLKNAIDWLSRLRGGKELRGKPVAIVSTGGGRSGglraVEQLRQV----LAELGAIVVPSGQ 144
 
Name Accession Description Interval E-value
PRK03767 PRK03767
NAD(P)H:quinone oxidoreductase; Provisional
 1-198 7.46e-133

NAD(P)H:quinone oxidoreductase; Provisional


Pssm-ID: 179647  Cd Length: 200  Bit Score: 370.41  E-value: 7.46e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570   1 MAKVLVLYYSMYGHIETMAHAVAEGANRVDGVEVVVKRVPETMQAEAFAKAGGKT-QNAPVATPQELADYDAIIFGTPTR 79
Cdd:PRK03767   1 MAKVLVLYYSMYGHIETMAEAVAEGAREVAGAEVTIKRVPETVPEEVAKKAGGKTdQAAPVATPDELADYDAIIFGTPTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570  80 FGNMSGQMRTFLDQTGGLWASGALYGKLASVFSSTGTG-GGQEQTITSTWTTLAHHGMVIVPIGYGAQELFDVSQVRGGT 158
Cdd:PRK03767  81 FGNMAGQMRNFLDQTGGLWAKGALVGKVGSVFTSTGTQhGGQETTITSTHTTLLHHGMVIVGLPYAFQGQMDVDEVTGGS 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 493862570 159 PYGATTIAGGDGSRQPSNEELSIARYQGEYVAGLAKKLNG 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 3.80e-114

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: 323.00  E-value: 3.80e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570    2 AKVLVLYYSMYGHIETMAHAVAEGANRVDGVEVVVKRVPETMQAEAFAKAGGKT-QNAPVATPQELADYDAIIFGTPTRF 80
Cdd:TIGR01755   1 VKVLVLYYSMYGHIETMARAVAEGAREVDGAEVVVKRVPETVPEEVAEKSHGKTdQTAPVATPQELADYDAIIFGTPTRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570   81 GNMSGQMRTFLDQTGGLWASGALYGKLASVFSSTGTG-GGQEQTITSTWTTLAHHGMVIVPIGYGAQELFDVSQVRGGTP 159
Cdd:TIGR01755  81 GNMASQMRNFLDQTGGLWASGALVGKVGSVFTSTGTQhGGQESTILSTWTTLLHHGMIIVPLPYAAQEQMGVDEVRGGSP 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 493862570  160 YGATTIAGGDGSRQPSNEELSIARYQGEYVAGLAKKL 196
Cdd:TIGR01755 161 YGATTIAGGDGSRQPSAEELDIARYQGRHVAGLAAKL 197
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 3-196 1.30e-49

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 158.94  E-value: 1.30e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570   3 KVLVLYYS--MYGHIETMAHAVAEGANRvDGVEVVVKRVPETMQAEAFAKAGGK---TQNAPVATPQELADYDAIIFGTP 77
Cdd:COG0655    1 KILVINGSprKNGNTAALAEAVAEGAEE-AGAEVELIRLADLDIKPCIGCGGTGkcvIKDDMNAIYEKLLEADGIIFGSP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570  78 TRFGNMSGQMRTFLDQTGGLWASGA-LYGKLASVFSSTGtGGGQEQTITSTWTTLAHHGMVIVPIGygaqelfdvsqvrg 156
Cdd:COG0655   80 TYFGNMSAQLKAFIDRLYALWAKGKlLKGKVGAVFTTGG-HGGAEATLLSLNTFLLHHGMIVVGLP-------------- 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 493862570 157 gtPYGAttIAGGDGSRQPSNEELSIARYQGEYVAGLAKKL 196
Cdd:COG0655  145 --PYGA--VGGGGPGDVLDEEGLATARELGKRLAELAKKL 180
NorV COG0426
Flavorubredoxin [Energy production and conversion];
3-119 1.63e-15

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 73.71  E-value: 1.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570   3 KVLVLYYSMYGHIETMAHAVAEGANRVdGVEVVVKRVPETMQAEAFAkaggktqnapvatpqELADYDAIIFGTPTRFGN 82
Cdd:COG0426  248 KVVIVYASMYGNTEKMAEAIAEGLTEE-GVKVKLYDLEKTDPSEIIT---------------EIFDAKGIVIGSPTYNGG 311

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 493862570  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 1.32e-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: 64.92  E-value: 1.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570   4 VLVLYYSMYGHIETMAHAVAEGANrVDGVEVVvkrvpetmqaeafakaggktqNAPVATPQELADYDAIIFGTPTRFGNM 83
Cdd:COG0716    1 ILIVYGSTTGNTEKVAEAIAEALG-AAGVDLF---------------------EIEDADLDDLEDYDLLILGTPTWAGEL 58

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 493862570  84 SGQMRTFLDQTGGLWAsgalyGKLASVFsstGTGGGQ 120
Cdd:COG0716   59 PDDWEDFLEELKEDLS-----GKKVALF---GTGDSS 87
FMN_red pfam03358
NADPH-dependent FMN reductase;
3-143 4.30e-12

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 61.10  E-value: 4.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570    3 KVLVLYYSMY--GHIETMAHAVAEGANRVDGVEVV-VKRVPETMQAEAFAKAGGKTQNAPVATPQeLADYDAIIFGTPTR 79
Cdd:pfam03358   2 KILAISGSPRkgSNTRKLARWAAELLEEGAEVELIdLADLILPLCDEDLEEEQGDPDDVQELREK-IAAADAIIIVTPEY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493862570   80 FGNMSGQMRTFLDQTGGLWASGALYGKLASVFSSTGTGGG----QEQTITStwttLAHHGMVIVPIGY 143
Cdd:pfam03358  81 NGSVSGLLKNAIDWLSRLRGGKELRGKPVAIVSTGGGRSGglraVEQLRQV----LAELGAIVVPSGQ 144
Flavodoxin_1 pfam00258
Flavodoxin;
6-135 3.81e-08

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 50.06  E-value: 3.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570    6 VLYYSMYGHIETMAHAVAEGANR--VDGVEVVVKRVPETMQ---AEAFAKAGGKTQNAPVATPQELADYDAIIFGTPTRF 80
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEagFEVDVVDLDDVDETLSeieEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFGTLED 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493862570   81 GNMSG---QMRTFLDQTGGL--WASGALYGKLASVFSST--GTGGGQEQTITSTWTTLAHHG 135
Cdd:pfam00258  81 GDLSGlkyAVFGLGDSGYEGfcGAAKKLDEKLSELGASRvgPLGEGDEDPQEDGLEEAFEAW 142
PRK05569 PRK05569
flavodoxin; Provisional
 1-93 1.30e-07

flavodoxin; Provisional


Pssm-ID: 135442 [Multi-domain]  Cd Length: 141  Bit Score: 48.68  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570   1 MAKVLVLYYSMYGHIETMAHAVAEGAnRVDGVEVVVKRVPEtmqaeafakaggktqnapvATPQELADYDAIIFGTPTRF 80
Cdd:PRK05569   1 MKKVSIIYWSCGGNVEVLANTIADGA-KEAGAEVTIKHVAD-------------------AKVEDVLEADAVAFGSPSMD 60

                         90
                 ....*....|....*
gi 493862570  81 GNMSGQ--MRTFLDQ 93
Cdd:PRK05569  61 NNNIEQeeMAPFLDQ 75
PRK05568 PRK05568
flavodoxin; Provisional
 1-120 5.60e-07

flavodoxin; Provisional


Pssm-ID: 235508 [Multi-domain]  Cd Length: 142  Bit Score: 47.11  E-value: 5.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570   1 MAKVLVLYYSMYGHIETMAHAVAEGAnRVDGVEVVVKRVPEtmqaeafakaggktqnapvATPQELADYDAIIFGTPTRF 80
Cdd:PRK05568   1 MKKINIIYWSGTGNTEAMANLIAEGA-KENGAEVKLLNVSE-------------------ASVDDVKGADVVALGSPAMG 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 493862570  81 GNM--SGQMRTFLDQTgglwaSGALYGKLASVFSSTGTGGGQ 120
Cdd:PRK05568  61 DEVleEGEMEPFVESI-----SSLVKGKKLVLFGSYGWGDGE 97
flav_short TIGR01753
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin ...
 4-118 1.10e-06

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: 46.18  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570    4 VLVLYYSMYGHIETMAHAVAEGANrvdgvevvvkrvpetmqaeafaKAGGKTQ--NAPVATPQELADYDAIIFGTPTrFG 81
Cdd:TIGR01753   1 ILIVYASMTGNTEEMANIIAEGLK----------------------EAGAEVDllEVADADAEDLLSYDAVLLGCST-WG 57

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 493862570   82 N---MSGQMRTFLDQTGGLWASgalyGKLASVFSSTGTGG 118
Cdd:TIGR01753  58 DedlEQDDFEPFFEELEDIDLG----GKKVALFGSGDWGY 93
HemG COG4635
Protoporphyrinogen IX oxidase, menaquinone-dependent (flavodoxin domain) [Coenzyme transport ...
 2-93 4.12e-05

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


Pssm-ID: 443673  Cd Length: 179  Bit Score: 42.19  E-value: 4.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570   2 AKVLVLYYSMYGHIETMAHAVAEGAnRVDGVEVVVKRVpetMQAEAFakaggktqnapvatpqELADYDAIIFGTPTRFG 81
Cdd:COG4635    1 MKVLILYASRDGQTRKIAERIAEVL-REAGHDVDLVDL---EDAPDL----------------DLAGYDAVVIGASIRYG 60

                         90
                 ....*....|..
gi 493862570  82 NMSGQMRTFLDQ 93
Cdd:COG4635   61 KWLPEAVRFVRR 72
PRK06756 PRK06756
flavodoxin; Provisional
 1-113 2.98e-04

flavodoxin; Provisional


Pssm-ID: 168663 [Multi-domain]  Cd Length: 148  Bit Score: 39.48  E-value: 2.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570   1 MAKVLVLYYSMYGHIETMAHAVAEGAnRVDGVEVVVKRVPETMQAeafakaggktqnapvatpQELADYDAIIFGTPTRF 80
Cdd:PRK06756   1 MSKLVMIFASMSGNTEEMADHIAGVI-RETENEIEVIDIMDSPEA------------------SILEQYDGIILGAYTWG 61

                         90       100       110
                 ....*....|....*....|....*....|....
gi 493862570  81 -GNMSGQMRTFLDQTGGLwasgALYGKLASVFSS 113
Cdd:PRK06756  62 dGDLPDDFLDFYDAMDSI----DLTGKKAAVFGS 91
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 3-134 1.20e-03

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: 38.08  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570    3 KVLVLYysmyGHIET------MAHAVAEGANRvDGVEVVV----KRVPETMQAEAFAKAGGKTQNAPVAT-PQELADYDA 71
Cdd:pfam02525   2 KILIIN----AHPRPgsfssrLADALVEALKA-AGHEVTVrdlyALFLPVLDAEDLADLTYPQGAADVESeQEELLAADV 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493862570   72 IIFGTPTRFGNMSGQMRTFLDQ----------TGGLWASGALYGKLASVFSSTGTGGGQEQTITSTWTTLAHH 134
Cdd:pfam02525  77 IVFQFPLYWFSVPALLKGWIDRvlragfafkyEEGGPGGGGLLGKKVLVIVTTGGPEYAYGKGGYNGFSLDEL 149
Flavodoxin_5 pfam12724
Flavodoxin domain; This is a family of flavodoxins. Flavodoxins are electron transfer proteins ...
 5-121 1.73e-03

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: 37.24  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570    5 LVLYYSMYGHIETMAHAVAEgANRVDGVEVVVKRVPETMqaeafakaggktqnapvatpqELADYDAIIFGTPTRFGNMS 84
Cdd:pfam12724   1 LILYSSRDGQTKKIAERIAE-ELREEGELVDVEDVEAGE---------------------DLSSYDAVVIGASIYYGKHL 58

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 493862570   85 GQMRTFLDQTGglwasGALYGKLASVFSSTGTGGGQE 121
Cdd:pfam12724  59 PELRQFVTKHR-----DELSSKPVAFFSVNLTARKPE 90
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
 3-116 2.90e-03

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


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 37.13  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570   3 KVLVLYysmyGHIE------TMAHAVAEGAnRVDGVEVVV-----KRVPETMQAEAFAKAGgkTQNAPVATPQE-LADYD 70
Cdd:COG2249    1 KILIIY----AHPDpssfnaALAEAAAEGL-EAAGHEVTVhdlyaEGFDPVLSAADFYRDG--PLPIDVAAEQElLLWAD 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 493862570  71 AIIFGTPTRFGNMSGQMRTFLDQ---------TGGLWASGALYGKLASVFSSTGT 116
Cdd:COG2249   74 HLVFQFPLWWYSMPALLKGWIDRvltpgfaygYGGGYPGGLLKGKKALLVVTTGG 128
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
64-150 9.29e-03

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 35.52  E-value: 9.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493862570  64 QELADYDAIIFGTPTRFGNMSGQMRTFLDqtgglWAS-GALYGKLASVFSSTGTGGGQEQTITSTWTTLAHHGMVIVPIG 142
Cdd:COG0431   65 EAIAAADGVVIVTPEYNGSYPGVLKNALD-----WLSrSELAGKPVALVSTSGGARGGLRALEHLRPVLSELGAVVLPPQ 139

                         90
                 ....*....|.
gi 493862570 143 Y---GAQELFD 150
Cdd:COG0431  140 VsipKAGEAFD 150
 
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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