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Conserved domains on  [gi|490826269|ref|WP_004688359|]
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MULTISPECIES: NAD(P)H:quinone oxidoreductase type IV [Brucella]

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
 1-199 1.41e-131

NAD(P)H:quinone oxidoreductase; Provisional


:

Pssm-ID: 179647  Cd Length: 200  Bit Score: 367.32  E-value: 1.41e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826269   1 MVKMLVLYYSAYGHMEQMAKAAAEGARE-GGAEVTLKRVPELVPEEVAKASHYKIDQEAPIATPGELADYDAIIIGTATR 79
Cdd:PRK03767   1 MAKVLVLYYSMYGHIETMAEAVAEGAREvAGAEVTIKRVPETVPEEVAKKAGGKTDQAAPVATPDELADYDAIIFGTPTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826269  80 YGMMASQMKNFLDQTGGLWAKGALINKVGSVMVSTATQHGGAELALISTQWQMQHHGMIIVPLSYAYREQMGNDVVRGGA 159
Cdd:PRK03767  81 FGNMAGQMRNFLDQTGGLWAKGALVGKVGSVFTSTGTQHGGQETTITSTHTTLLHHGMVIVGLPYAFQGQMDVDEVTGGS 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 490826269 160 PYGMTTTADGDGSRQPSAQELDGARFQGRRVAEITAKLHG 199
Cdd:PRK03767 161 PYGATTIAGGDGSRQPSENELAGARYQGRHVAEIAAKLAG 200
 
Name Accession Description Interval E-value
PRK03767 PRK03767
NAD(P)H:quinone oxidoreductase; Provisional
 1-199 1.41e-131

NAD(P)H:quinone oxidoreductase; Provisional


Pssm-ID: 179647  Cd Length: 200  Bit Score: 367.32  E-value: 1.41e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826269   1 MVKMLVLYYSAYGHMEQMAKAAAEGARE-GGAEVTLKRVPELVPEEVAKASHYKIDQEAPIATPGELADYDAIIIGTATR 79
Cdd:PRK03767   1 MAKVLVLYYSMYGHIETMAEAVAEGAREvAGAEVTIKRVPETVPEEVAKKAGGKTDQAAPVATPDELADYDAIIFGTPTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826269  80 YGMMASQMKNFLDQTGGLWAKGALINKVGSVMVSTATQHGGAELALISTQWQMQHHGMIIVPLSYAYREQMGNDVVRGGA 159
Cdd:PRK03767  81 FGNMAGQMRNFLDQTGGLWAKGALVGKVGSVFTSTGTQHGGQETTITSTHTTLLHHGMVIVGLPYAFQGQMDVDEVTGGS 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 490826269 160 PYGMTTTADGDGSRQPSAQELDGARFQGRRVAEITAKLHG 199
Cdd:PRK03767 161 PYGATTIAGGDGSRQPSENELAGARYQGRHVAEIAAKLAG 200
flav_wrbA TIGR01755
NAD(P)H:quinone oxidoreductase, type IV; This model represents a protein, WrbA, related to and ...
 2-197 1.44e-125

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: 351.89  E-value: 1.44e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826269    2 VKMLVLYYSAYGHMEQMAKAAAEGAREG-GAEVTLKRVPELVPEEVAKASHYKIDQEAPIATPGELADYDAIIIGTATRY 80
Cdd:TIGR01755   1 VKVLVLYYSMYGHIETMARAVAEGAREVdGAEVVVKRVPETVPEEVAEKSHGKTDQTAPVATPQELADYDAIIFGTPTRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826269   81 GMMASQMKNFLDQTGGLWAKGALINKVGSVMVSTATQHGGAELALISTQWQMQHHGMIIVPLSYAYREQMGNDVVRGGAP 160
Cdd:TIGR01755  81 GNMASQMRNFLDQTGGLWASGALVGKVGSVFTSTGTQHGGQESTILSTWTTLLHHGMIIVPLPYAAQEQMGVDEVRGGSP 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 490826269  161 YGMTTTADGDGSRQPSAQELDGARFQGRRVAEITAKL 197
Cdd:TIGR01755 161 YGATTIAGGDGSRQPSAEELDIARYQGRHVAGLAAKL 197
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 3-197 4.22e-45

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 147.38  E-value: 4.22e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826269   3 KMLVLYYSA--YGHMEQMAKAAAEGAREGGAEVTLKRVPELV--PEEVAKASHYKIDQEAPIATPGELADYDAIIIGTAT 78
Cdd:COG0655    1 KILVINGSPrkNGNTAALAEAVAEGAEEAGAEVELIRLADLDikPCIGCGGTGKCVIKDDMNAIYEKLLEADGIIFGSPT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826269  79 RYGMMASQMKNFLDQTGGLWAKGA-LINKVGSVMVSTAtqHGGAELALISTQWQMQHHGMIIVplsyayreqmgndvvrG 157
Cdd:COG0655   81 YFGNMSAQLKAFIDRLYALWAKGKlLKGKVGAVFTTGG--HGGAEATLLSLNTFLLHHGMIVV----------------G 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 490826269 158 GAPYGMTTTADGDGSRQPsaQELDGARFQGRRVAEITAKL 197
Cdd:COG0655  143 LPPYGAVGGGGPGDVLDE--EGLATARELGKRLAELAKKL 180
FMN_red pfam03358
NADPH-dependent FMN reductase;
16-141 2.16e-13

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 64.57  E-value: 2.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826269   16 EQMAKAAAEGAREGgAEVTLKRVPELVPEevakasHYKIDQEAPIATPGE-------LADYDAIIIGTATRYGMMASQMK 88
Cdd:pfam03358  17 RKLARWAAELLEEG-AEVELIDLADLILP------LCDEDLEEEQGDPDDvqelrekIAAADAIIIVTPEYNGSVSGLLK 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 490826269   89 NFLDQTGGLWAKGALINKVGSVMVSTATQHGGAELALISTQWqMQHHGMIIVP 141
Cdd:pfam03358  90 NAIDWLSRLRGGKELRGKPVAIVSTGGGRSGGLRAVEQLRQV-LAELGAIVVP 141
 
Name Accession Description Interval E-value
PRK03767 PRK03767
NAD(P)H:quinone oxidoreductase; Provisional
 1-199 1.41e-131

NAD(P)H:quinone oxidoreductase; Provisional


Pssm-ID: 179647  Cd Length: 200  Bit Score: 367.32  E-value: 1.41e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826269   1 MVKMLVLYYSAYGHMEQMAKAAAEGARE-GGAEVTLKRVPELVPEEVAKASHYKIDQEAPIATPGELADYDAIIIGTATR 79
Cdd:PRK03767   1 MAKVLVLYYSMYGHIETMAEAVAEGAREvAGAEVTIKRVPETVPEEVAKKAGGKTDQAAPVATPDELADYDAIIFGTPTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826269  80 YGMMASQMKNFLDQTGGLWAKGALINKVGSVMVSTATQHGGAELALISTQWQMQHHGMIIVPLSYAYREQMGNDVVRGGA 159
Cdd:PRK03767  81 FGNMAGQMRNFLDQTGGLWAKGALVGKVGSVFTSTGTQHGGQETTITSTHTTLLHHGMVIVGLPYAFQGQMDVDEVTGGS 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 490826269 160 PYGMTTTADGDGSRQPSAQELDGARFQGRRVAEITAKLHG 199
Cdd:PRK03767 161 PYGATTIAGGDGSRQPSENELAGARYQGRHVAEIAAKLAG 200
flav_wrbA TIGR01755
NAD(P)H:quinone oxidoreductase, type IV; This model represents a protein, WrbA, related to and ...
 2-197 1.44e-125

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: 351.89  E-value: 1.44e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826269    2 VKMLVLYYSAYGHMEQMAKAAAEGAREG-GAEVTLKRVPELVPEEVAKASHYKIDQEAPIATPGELADYDAIIIGTATRY 80
Cdd:TIGR01755   1 VKVLVLYYSMYGHIETMARAVAEGAREVdGAEVVVKRVPETVPEEVAEKSHGKTDQTAPVATPQELADYDAIIFGTPTRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826269   81 GMMASQMKNFLDQTGGLWAKGALINKVGSVMVSTATQHGGAELALISTQWQMQHHGMIIVPLSYAYREQMGNDVVRGGAP 160
Cdd:TIGR01755  81 GNMASQMRNFLDQTGGLWASGALVGKVGSVFTSTGTQHGGQESTILSTWTTLLHHGMIIVPLPYAAQEQMGVDEVRGGSP 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 490826269  161 YGMTTTADGDGSRQPSAQELDGARFQGRRVAEITAKL 197
Cdd:TIGR01755 161 YGATTIAGGDGSRQPSAEELDIARYQGRHVAGLAAKL 197
WrbA COG0655
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ...
 3-197 4.22e-45

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


Pssm-ID: 440420 [Multi-domain]  Cd Length: 181  Bit Score: 147.38  E-value: 4.22e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826269   3 KMLVLYYSA--YGHMEQMAKAAAEGAREGGAEVTLKRVPELV--PEEVAKASHYKIDQEAPIATPGELADYDAIIIGTAT 78
Cdd:COG0655    1 KILVINGSPrkNGNTAALAEAVAEGAEEAGAEVELIRLADLDikPCIGCGGTGKCVIKDDMNAIYEKLLEADGIIFGSPT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826269  79 RYGMMASQMKNFLDQTGGLWAKGA-LINKVGSVMVSTAtqHGGAELALISTQWQMQHHGMIIVplsyayreqmgndvvrG 157
Cdd:COG0655   81 YFGNMSAQLKAFIDRLYALWAKGKlLKGKVGAVFTTGG--HGGAEATLLSLNTFLLHHGMIVV----------------G 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 490826269 158 GAPYGMTTTADGDGSRQPsaQELDGARFQGRRVAEITAKL 197
Cdd:COG0655  143 LPPYGAVGGGGPGDVLDE--EGLATARELGKRLAELAKKL 180
FMN_red pfam03358
NADPH-dependent FMN reductase;
16-141 2.16e-13

NADPH-dependent FMN reductase;


Pssm-ID: 427259 [Multi-domain]  Cd Length: 152  Bit Score: 64.57  E-value: 2.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826269   16 EQMAKAAAEGAREGgAEVTLKRVPELVPEevakasHYKIDQEAPIATPGE-------LADYDAIIIGTATRYGMMASQMK 88
Cdd:pfam03358  17 RKLARWAAELLEEG-AEVELIDLADLILP------LCDEDLEEEQGDPDDvqelrekIAAADAIIIVTPEYNGSVSGLLK 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 490826269   89 NFLDQTGGLWAKGALINKVGSVMVSTATQHGGAELALISTQWqMQHHGMIIVP 141
Cdd:pfam03358  90 NAIDWLSRLRGGKELRGKPVAIVSTGGGRSGGLRAVEQLRQV-LAELGAIVVP 141
NorV COG0426
Flavorubredoxin [Energy production and conversion];
5-113 4.18e-10

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 57.92  E-value: 4.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826269   5 LVLYYSAYGHMEQMAKAAAEGAREGGAEVTLKRVPELVPEEVAKashykidqeapiatpgELADYDAIIIGTATRYGMMA 84
Cdd:COG0426  250 VIVYASMYGNTEKMAEAIAEGLTEEGVKVKLYDLEKTDPSEIIT----------------EIFDAKGIVIGSPTYNGGAF 313

                         90       100
                 ....*....|....*....|....*....
gi 490826269  85 SQMKNFLDQTGGLWAKgaliNKVGSVMVS 113
Cdd:COG0426  314 PPIADLLGYLKGLAPK----NKLAGAFGS 338
FldA COG0716
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ...
 5-93 3.00e-09

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


Pssm-ID: 440480 [Multi-domain]  Cd Length: 135  Bit Score: 52.98  E-value: 3.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826269   5 LVLYYSAYGHMEQMAKAAAEGAreGGAEVTLKRVPElvpeevakashykidqeapiATPGELADYDAIIIGTATRYGMMA 84
Cdd:COG0716    2 LIVYGSTTGNTEKVAEAIAEAL--GAAGVDLFEIED--------------------ADLDDLEDYDLLILGTPTWAGELP 59


                 ....*....
gi 490826269  85 SQMKNFLDQ 93
Cdd:COG0716   60 DDWEDFLEE 68
flav_short TIGR01753
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin ...
 5-109 2.33e-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: 2.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826269    5 LVLYYSAYGHMEQMAKAAAEGAREGGAEVTLKRVPElvpeevakashykidqeapiATPGELADYDAIIIGTATrYGM-- 82
Cdd:TIGR01753   2 LIVYASMTGNTEEMANIIAEGLKEAGAEVDLLEVAD--------------------ADAEDLLSYDAVLLGCST-WGDed 60

                          90       100
                  ....*....|....*....|....*...
gi 490826269   83 -MASQMKNFLDQTGGLWAKGALINKVGS 109
Cdd:TIGR01753  61 lEQDDFEPFFEELEDIDLGGKKVALFGS 88
PRK05569 PRK05569
flavodoxin; Provisional
 1-49 3.55e-08

flavodoxin; Provisional


Pssm-ID: 135442 [Multi-domain]  Cd Length: 141  Bit Score: 50.22  E-value: 3.55e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 490826269   1 MVKMLVLYYSAYGHMEQMAKAAAEGAREGGAEVTLKRVPELVPEEVAKA 49
Cdd:PRK05569   1 MKKVSIIYWSCGGNVEVLANTIADGAKEAGAEVTIKHVADAKVEDVLEA 49
HemG COG4635
Protoporphyrinogen IX oxidase, menaquinone-dependent (flavodoxin domain) [Coenzyme transport ...
 3-93 1.13e-07

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


Pssm-ID: 443673  Cd Length: 179  Bit Score: 49.51  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826269   3 KMLVLYYSAYGHMEQMAKAAAEGAREGGAEVTL---KRVPELvpeevakashykidqeapiatpgELADYDAIIIGTATR 79
Cdd:COG4635    2 KVLILYASRDGQTRKIAERIAEVLREAGHDVDLvdlEDAPDL-----------------------DLAGYDAVVIGASIR 58

                         90
                 ....*....|....
gi 490826269  80 YGMMASQMKNFLDQ 93
Cdd:COG4635   59 YGKWLPEAVRFVRR 72
Flavodoxin_1 pfam00258
Flavodoxin;
6-78 1.04e-06

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 46.21  E-value: 1.04e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490826269    6 VLYYSAYGHMEQMAKAAAEGAREGGAEVTlkrvpelvpeeVAKASHYKIdqeapiaTPGELADYDAIIIGTAT 78
Cdd:pfam00258   1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVD-----------VVDLDDVDE-------TLSEIEEEDLLLVVVST 55
PRK05568 PRK05568
flavodoxin; Provisional
 1-49 1.12e-06

flavodoxin; Provisional


Pssm-ID: 235508 [Multi-domain]  Cd Length: 142  Bit Score: 46.34  E-value: 1.12e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 490826269   1 MVKMLVLYYSAYGHMEQMAKAAAEGAREGGAEVTLKRVPELVPEEVAKA 49
Cdd:PRK05568   1 MKKINIIYWSGTGNTEAMANLIAEGAKENGAEVKLLNVSEASVDDVKGA 49
Flavodoxin_5 pfam12724
Flavodoxin domain; This is a family of flavodoxins. Flavodoxins are electron transfer proteins ...
 5-93 9.47e-06

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: 43.79  E-value: 9.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826269    5 LVLYYSAYGHMEQMAKAAAEGAREGGAEVTLKRVPELVpeevakashykidqeapiatpgELADYDAIIIGTATRYGMMA 84
Cdd:pfam12724   1 LILYSSRDGQTKKIAERIAEELREEGELVDVEDVEAGE----------------------DLSSYDAVVIGASIYYGKHL 58


                  ....*....
gi 490826269   85 SQMKNFLDQ 93
Cdd:pfam12724  59 PELRQFVTK 67
PRK06756 PRK06756
flavodoxin; Provisional
 1-78 2.18e-04

flavodoxin; Provisional


Pssm-ID: 168663 [Multi-domain]  Cd Length: 148  Bit Score: 39.86  E-value: 2.18e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490826269   1 MVKMLVLYYSAYGHMEQMAKAAAEGAREGGAEVTLKRVpelvpeevakashykidQEAPIATpgELADYDAIIIGTAT 78
Cdd:PRK06756   1 MSKLVMIFASMSGNTEEMADHIAGVIRETENEIEVIDI-----------------MDSPEAS--ILEQYDGIILGAYT 59
SsuE COG0431
NAD(P)H-dependent FMN reductase [Energy production and conversion];
16-121 1.36e-03

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


Pssm-ID: 440200 [Multi-domain]  Cd Length: 162  Bit Score: 37.83  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826269  16 EQMAKAAAEGAREGGAEVTLKRVPELVPEevakasHYKIDQEAPIATPG------ELADYDAIIIGTATRYGMMASQMKN 89
Cdd:COG0431   17 RKLARAAAELAPAAGAEVELIDLRDLDLP------LYDEDLEADGAPPAvkalreAIAAADGVVIVTPEYNGSYPGVLKN 90

                         90       100       110
                 ....*....|....*....|....*....|...
gi 490826269  90 FLDqtgglWA-KGALINKVGSVMVSTATQHGGA 121
Cdd:COG0431   91 ALD-----WLsRSELAGKPVALVSTSGGARGGL 118
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
 17-124 7.60e-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: 35.77  E-value: 7.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826269   17 QMAKAAAEGAREGGAEVTL-----KRVPELVPEEVAkASHYKIDQEAPIATPGELADYDAIIIGTATRYGMMASQMKNFL 91
Cdd:pfam02525  18 RLADALVEALKAAGHEVTVrdlyaLFLPVLDAEDLA-DLTYPQGAADVESEQEELLAADVIVFQFPLYWFSVPALLKGWI 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 490826269   92 DQ----------TGGLWAKGALINKvgSVMVSTATqhGGAELA 124
Cdd:pfam02525  97 DRvlragfafkyEEGGPGGGGLLGK--KVLVIVTT--GGPEYA 135
 
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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