NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|671551678|ref|WP_031534348|]
View 

MULTISPECIES: dihydroorotate dehydrogenase electron transfer subunit [Bacillaceae]

Protein Classification

dihydroorotate dehydrogenase electron transfer subunit( domain architecture ID 11477869)

dihydroorotate dehydrogenase electron transfer subunit is part of the enzyme complex that catalyzes the ubiquinone-mediated oxidation of (D)-dihydroorotate to orotate, an essential step in pyrimidine de novo biosynthesis

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 1-259 6.08e-116

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


:

Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 332.22  E-value: 6.08e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   1 MIKNEICTVVEQKEIAENIMELTLTGELVSEMnEPGQFVHIKVSDnATPLLRRPISICRIDQESKTFTmiYRAEGAGTKL 80
Cdd:PRK00054   1 MMKPENMKIVENKEIAPNIYTLVLDGEKVFDM-KPGQFVMVWVPG-VEPLLERPISISDIDKNEITIL--YRKVGEGTKK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  81 LAQKTAGEAVDILGPLGNGFPVEASksGQTALLVGGGIGVPPLYELANRLVAKGVKVVAVLGFQTESVAFYEEKFASFGD 160
Cdd:PRK00054  77 LSKLKEGDELDIRGPLGNGFDLEEI--GGKVLLVGGGIGVAPLYELAKELKKKGVEVTTVLGARTKDEVIFEEEFAKVGD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678 161 TYIATVDGSHGTQGFVTDVIFQENLEFDVLYSCGPTPMLKNLEKTFPTKK--VFISLEERMGCGIGACFACVCHTADDpt 238
Cdd:PRK00054 155 VYVTTDDGSYGFKGFVTDVLDELDSEYDAIYSCGPEIMMKKVVEILKEKKvpAYVSLERRMKCGIGACGACVCDTETG-- 232

                        250       260
                 ....*....|....*....|.
gi 671551678 239 gfsYKKVCTDGPVFRTGEVVL 259
Cdd:PRK00054 233 ---GKRVCKDGPVFSGGELVL 250
 
Name Accession Description Interval E-value
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 1-259 6.08e-116

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 332.22  E-value: 6.08e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   1 MIKNEICTVVEQKEIAENIMELTLTGELVSEMnEPGQFVHIKVSDnATPLLRRPISICRIDQESKTFTmiYRAEGAGTKL 80
Cdd:PRK00054   1 MMKPENMKIVENKEIAPNIYTLVLDGEKVFDM-KPGQFVMVWVPG-VEPLLERPISISDIDKNEITIL--YRKVGEGTKK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  81 LAQKTAGEAVDILGPLGNGFPVEASksGQTALLVGGGIGVPPLYELANRLVAKGVKVVAVLGFQTESVAFYEEKFASFGD 160
Cdd:PRK00054  77 LSKLKEGDELDIRGPLGNGFDLEEI--GGKVLLVGGGIGVAPLYELAKELKKKGVEVTTVLGARTKDEVIFEEEFAKVGD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678 161 TYIATVDGSHGTQGFVTDVIFQENLEFDVLYSCGPTPMLKNLEKTFPTKK--VFISLEERMGCGIGACFACVCHTADDpt 238
Cdd:PRK00054 155 VYVTTDDGSYGFKGFVTDVLDELDSEYDAIYSCGPEIMMKKVVEILKEKKvpAYVSLERRMKCGIGACGACVCDTETG-- 232

                        250       260
                 ....*....|....*....|.
gi 671551678 239 gfsYKKVCTDGPVFRTGEVVL 259
Cdd:PRK00054 233 ---GKRVCKDGPVFSGGELVL 250
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 9-253 7.51e-113

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.


Pssm-ID: 99814 [Multi-domain]  Cd Length: 246  Bit Score: 324.11  E-value: 7.51e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   9 VVEQKEIAENIMELTLTGELVSEMNEPGQFVHIKVSDNATPLLRRPISICRIDQESKTFTMIYRAEGAGTKLLAQKTAGE 88
Cdd:cd06218    1 VLSNREIADDIYRLVLEAPEIAAAAKPGQFVMLRVPDGSDPLLRRPISIHDVDPEEGTITLLYKVVGKGTRLLSELKAGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  89 AVDILGPLGNGFPVEAskSGQTALLVGGGIGVPPLYELANRLVAKGVKVVAVLGFQTESVAFYEEKFASFG-DTYIATVD 167
Cdd:cd06218   81 ELDVLGPLGNGFDLPD--DDGKVLLVGGGIGIAPLLFLAKQLAERGIKVTVLLGFRSADDLFLVEEFEALGaEVYVATDD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678 168 GSHGTQGFVTDVI--FQENLEFDVLYSCGPTPMLKNLEKTFPTKKV--FISLEERMGCGIGACFACVCHTADDPTGfsYK 243
Cdd:cd06218  159 GSAGTKGFVTDLLkeLLAEARPDVVYACGPEPMLKAVAELAAERGVpcQVSLEERMACGIGACLGCVVKTKDDEGG--YK 236

                        250
                 ....*....|
gi 671551678 244 KVCTDGPVFR 253
Cdd:cd06218  237 RVCKDGPVFD 246
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 8-259 5.35e-80

NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 240.92  E-value: 5.35e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   8 TVVEQKEIAENIMELTLTGELVSEMNEPGQFVHIKVSDNatpLLRRPISICRIDQESKTFTMIYRAEGAGTKLLAQKTAG 87
Cdd:COG0543    1 KVVSVERLAPDVYLLRLEAPLIALKFKPGQFVMLRVPGD---GLRRPFSIASAPREDGTIELHIRVVGKGTRALAELKPG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  88 EAVDILGPLGNGFPVEasKSGQTALLVGGGIGVPPLYELANRLVAKGVKVVAVLGFQTESVAFYEEKFASFGD--TYIAT 165
Cdd:COG0543   78 DELDVRGPLGNGFPLE--DSGRPVLLVAGGTGLAPLRSLAEALLARGRRVTLYLGARTPEDLYLLDELEALADfrVVVTT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678 166 VDGSHGTQGFVTDVI--FQENLEFDVLYSCGPTPMLKNLEKTF-----PTKKVFISLEERMGCGIGACFACVCHTADdpt 238
Cdd:COG0543  156 DDGWYGRKGFVTDALkeLLAEDSGDDVYACGPPPMMKAVAELLlergvPPERIYVSLERRMACGIGMCGGCVVPVGG--- 232

                        250       260
                 ....*....|....*....|.
gi 671551678 239 gfsykkVCTDGPVFRTGEVVL 259
Cdd:COG0543  233 ------GCKDGPVFDAAEVDW 247
DHODB_Fe-S_bind pfam10418
Iron-sulfur cluster binding domain of dihydroorotate dehydrogenase B; Lactococcus lactis is ...
 216-257 7.53e-17

Iron-sulfur cluster binding domain of dihydroorotate dehydrogenase B; Lactococcus lactis is one of the few organizms with two dihydroorotate dehydrogenases, DHODs, A and B. The B enzyme is a prototype for DHODs in Gram-positive bacteria that use NAD+ as the second substrate. DHODB is a hetero-tetramer composed of a central homodimer of PyrDB subunits resembling the DHODA structure and two PyrK subunits along with three different cofactors: FMN, FAD, and a [2Fe-2S] cluster. The [2Fe-2S] iron-sulfur cluster binds to this C-terminal domain of the PyrK subunit, which is at the interface between the flavin and NAD binding domains and contains three beta-strands. The four cysteine residues at the N-terminal part of this domain are the ones that bind, in pairs, to the iron-sulfur cluster. The conformation of the whole molecule means that the iron-sulfur cluster is localized in a well-ordered part of this domain close to the FAD binding site. The FAD and and NAD binding domains are FAD_binding_6, pfam00970 and NAD_binding_1, pfam00175.


Pssm-ID: 463084 [Multi-domain]  Cd Length: 40  Bit Score: 71.86  E-value: 7.53e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 671551678  216 EERMGCGIGACFACVCHTADDPTgfSYKKVCTDGPVFRTGEV 257
Cdd:pfam10418   1 EERMACGVGACGGCVVKTKGGDG--EYKRVCVDGPVFDADEV 40
 
Name Accession Description Interval E-value
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 1-259 6.08e-116

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 332.22  E-value: 6.08e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   1 MIKNEICTVVEQKEIAENIMELTLTGELVSEMnEPGQFVHIKVSDnATPLLRRPISICRIDQESKTFTmiYRAEGAGTKL 80
Cdd:PRK00054   1 MMKPENMKIVENKEIAPNIYTLVLDGEKVFDM-KPGQFVMVWVPG-VEPLLERPISISDIDKNEITIL--YRKVGEGTKK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  81 LAQKTAGEAVDILGPLGNGFPVEASksGQTALLVGGGIGVPPLYELANRLVAKGVKVVAVLGFQTESVAFYEEKFASFGD 160
Cdd:PRK00054  77 LSKLKEGDELDIRGPLGNGFDLEEI--GGKVLLVGGGIGVAPLYELAKELKKKGVEVTTVLGARTKDEVIFEEEFAKVGD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678 161 TYIATVDGSHGTQGFVTDVIFQENLEFDVLYSCGPTPMLKNLEKTFPTKK--VFISLEERMGCGIGACFACVCHTADDpt 238
Cdd:PRK00054 155 VYVTTDDGSYGFKGFVTDVLDELDSEYDAIYSCGPEIMMKKVVEILKEKKvpAYVSLERRMKCGIGACGACVCDTETG-- 232

                        250       260
                 ....*....|....*....|.
gi 671551678 239 gfsYKKVCTDGPVFRTGEVVL 259
Cdd:PRK00054 233 ---GKRVCKDGPVFSGGELVL 250
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 9-253 7.51e-113

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.


Pssm-ID: 99814 [Multi-domain]  Cd Length: 246  Bit Score: 324.11  E-value: 7.51e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   9 VVEQKEIAENIMELTLTGELVSEMNEPGQFVHIKVSDNATPLLRRPISICRIDQESKTFTMIYRAEGAGTKLLAQKTAGE 88
Cdd:cd06218    1 VLSNREIADDIYRLVLEAPEIAAAAKPGQFVMLRVPDGSDPLLRRPISIHDVDPEEGTITLLYKVVGKGTRLLSELKAGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  89 AVDILGPLGNGFPVEAskSGQTALLVGGGIGVPPLYELANRLVAKGVKVVAVLGFQTESVAFYEEKFASFG-DTYIATVD 167
Cdd:cd06218   81 ELDVLGPLGNGFDLPD--DDGKVLLVGGGIGIAPLLFLAKQLAERGIKVTVLLGFRSADDLFLVEEFEALGaEVYVATDD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678 168 GSHGTQGFVTDVI--FQENLEFDVLYSCGPTPMLKNLEKTFPTKKV--FISLEERMGCGIGACFACVCHTADDPTGfsYK 243
Cdd:cd06218  159 GSAGTKGFVTDLLkeLLAEARPDVVYACGPEPMLKAVAELAAERGVpcQVSLEERMACGIGACLGCVVKTKDDEGG--YK 236

                        250
                 ....*....|
gi 671551678 244 KVCTDGPVFR 253
Cdd:cd06218  237 RVCKDGPVFD 246
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 8-259 5.35e-80

NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 240.92  E-value: 5.35e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   8 TVVEQKEIAENIMELTLTGELVSEMNEPGQFVHIKVSDNatpLLRRPISICRIDQESKTFTMIYRAEGAGTKLLAQKTAG 87
Cdd:COG0543    1 KVVSVERLAPDVYLLRLEAPLIALKFKPGQFVMLRVPGD---GLRRPFSIASAPREDGTIELHIRVVGKGTRALAELKPG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  88 EAVDILGPLGNGFPVEasKSGQTALLVGGGIGVPPLYELANRLVAKGVKVVAVLGFQTESVAFYEEKFASFGD--TYIAT 165
Cdd:COG0543   78 DELDVRGPLGNGFPLE--DSGRPVLLVAGGTGLAPLRSLAEALLARGRRVTLYLGARTPEDLYLLDELEALADfrVVVTT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678 166 VDGSHGTQGFVTDVI--FQENLEFDVLYSCGPTPMLKNLEKTF-----PTKKVFISLEERMGCGIGACFACVCHTADdpt 238
Cdd:COG0543  156 DDGWYGRKGFVTDALkeLLAEDSGDDVYACGPPPMMKAVAELLlergvPPERIYVSLERRMACGIGMCGGCVVPVGG--- 232

                        250       260
                 ....*....|....*....|.
gi 671551678 239 gfsykkVCTDGPVFRTGEVVL 259
Cdd:COG0543  233 ------GCKDGPVFDAAEVDW 247
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 9-253 6.78e-61

FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99789 [Multi-domain]  Cd Length: 243  Bit Score: 192.16  E-value: 6.78e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   9 VVEQKEIAENIMELTLTGELVSEMNEPGQFVHIKVSDNAtPLLRRPISICRIDQESKTFTMIYRAEGAGTKLLAQKTAGE 88
Cdd:cd06192    1 IVKKEQLEPNLVLLTIKAPLAARLFRPGQFVFLRNFESP-GLERIPLSLAGVDPEEGTISLLVEIRGPKTKLIAELKPGE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  89 AVDILGPLGNGFPVEasKSGQTALLVGGGIGVPPLYELANRLVAKGVKVVAVLGFQTESVAFYEEKFASFGDT-YIATVD 167
Cdd:cd06192   80 KLDVMGPLGNGFEGP--KKGGTVLLVAGGIGLAPLLPIAKKLAANGNKVTVLAGAKKAKEEFLDEYFELPADVeIWTTDD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678 168 GSHGTQGFVTDVIFQENLE-FDVLYSCGPTPMLK----NLEKTFPTKKVFISLEERMGCGIGACFACVCHTADdptgfSY 242
Cdd:cd06192  158 GELGLEGKVTDSDKPIPLEdVDRIIVAGSDIMMKavveALDEWLQLIKASVSNNSPMCCGIGICGACTIETKH-----GV 232

                        250
                 ....*....|.
gi 671551678 243 KKVCTDGPVFR 253
Cdd:cd06192  233 KRLCKDGPVFR 243
DHOD_e_trans_like1 cd06219
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 8-252 5.45e-42

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group, as in flavoenzymes, or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD, forming FADH2 via a semiquinone intermediate, and then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99815 [Multi-domain]  Cd Length: 248  Bit Score: 143.87  E-value: 5.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   8 TVVEQKEIAENIMELTLTGELVSEMNEPGQFVHIKVSDNATpllRRPISICRIDQESKTFTMIYRAEGAGTKLLAQKTAG 87
Cdd:cd06219    2 KILEKEELAPNVKLFEIEAPLIAKKAKPGQFVIVRADEKGE---RIPLTIADWDPEKGTITIVVQVVGKSTRELATLEEG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  88 EAV-DILGPLGNGFPVEASKsgqTALLVGGGIGVPPLYELANRLVAKGVKVVAVLGFQTESVAFYEEKFASFGDT-YIAT 165
Cdd:cd06219   79 DKIhDVVGPLGKPSEIENYG---TVVFVGGGVGIAPIYPIAKALKEAGNRVITIIGARTKDLVILEDEFRAVSDElIITT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678 166 VDGSHGTQGFVTDV---IFQENLEFDVLYSCGPTPMLKNL-EKTFPTK-KVFISLEERMGCGIGACFACVChTADDPTGF 240
Cdd:cd06219  156 DDGSYGEKGFVTDPlkeLIESGEKVDLVIAIGPPIMMKAVsELTRPYGiPTVVSLNPIMVDGTGMCGACRV-TVGGETKF 234

                        250
                 ....*....|..
gi 671551678 241 sykkVCTDGPVF 252
Cdd:cd06219  235 ----ACVDGPEF 242
PRK06222 PRK06222
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;
8-252 3.62e-41

sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;


Pssm-ID: 235747 [Multi-domain]  Cd Length: 281  Bit Score: 142.63  E-value: 3.62e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   8 TVVEQKEIAENIMELTLTGELVSEMNEPGQFVHIKVSDNATpllRRPISICRIDQESKTFTMIYRAEGAGTKLLAQKTAG 87
Cdd:PRK06222   3 KILEKEELAPNVFLMEIEAPRVAKKAKPGQFVIVRIDEKGE---RIPLTIADYDREKGTITIVFQAVGKSTRKLAELKEG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  88 EAV-DILGPLGNgfPVEASKSGqTALLVGGGIGVPPLYELANRLVAKGVKVVAVLGFQTESVAFYEEKFASFGDT-YIAT 165
Cdd:PRK06222  80 DSIlDVVGPLGK--PSEIEKFG-TVVCVGGGVGIAPVYPIAKALKEAGNKVITIIGARNKDLLILEDEMKAVSDElYVTT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678 166 VDGSHGTQGFVTDVI---FQENLEFDVLYSCGPTPMLKNLEKTfpTK----KVFISLEERMGCGIGACFACVChTADDPT 238
Cdd:PRK06222 157 DDGSYGRKGFVTDVLkelLESGKKVDRVVAIGPVIMMKFVAEL--TKpygiKTIVSLNPIMVDGTGMCGACRV-TVGGET 233

                        250
                 ....*....|....
gi 671551678 239 GFsykkVCTDGPVF 252
Cdd:PRK06222 234 KF----ACVDGPEF 243
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 14-252 4.12e-41

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.


Pssm-ID: 99816 [Multi-domain]  Cd Length: 233  Bit Score: 140.85  E-value: 4.12e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  14 EIAENIMELTLTGELVSEMN---EPGQFVHIKVsdnatPLL-RRPISICRIDQEsKTFTMiyRAEGAGTKLLAQKTAGEA 89
Cdd:cd06220    2 TIKEVIDETPTVKTFVFDWDfdfKPGQFVMVWV-----PGVdEIPMSLSYIDGP-NSITV--KKVGEATSALHDLKEGDK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  90 VDILGPLGNGFPVEASKsgqtALLVGGGIGVPPLYELANRLVAKGVKVVAvLGFQTESVAFYEEKFASFGDTYIATVDGS 169
Cdd:cd06220   74 LGIRGPYGNGFELVGGK----VLLIGGGIGIAPLAPLAERLKKAADVTVL-LGARTKEELLFLDRLRKSDELIVTTDDGS 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678 170 HGTQGFVTDVIFQENLE-FDVLYSCGPTPMLKNLEKTFPTKKVF--ISLEERMGCGIGACFACVChtadDPTGFsykKVC 246
Cdd:cd06220  149 YGFKGFVTDLLKELDLEeYDAIYVCGPEIMMYKVLEILDERGVRaqFSLERYMKCGIGICGSCCI----DPTGL---RVC 221


                 ....*.
gi 671551678 247 TDGPVF 252
Cdd:cd06220  222 RDGPVF 227
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 9-257 6.80e-35

bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 132.17  E-value: 6.80e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   9 VVEQKEIAENIMELTLTGELVSEMNEPGQFVHIKVSDNATpllRRPISICRIDQESKTFTMIYRAEGAGTKLLAQKTAGE 88
Cdd:PRK12778   4 IVEKEIFSEKVFLLEIEAPLIAKSRKPGQFVIVRVGEKGE---RIPLTIADADPEKGTITLVIQEVGLSTTKLCELNEGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  89 AV-DILGPLGNgfPVEASKSGqTALLVGGGIGVPPLYELANRLVAKGVKVVAVLGFQTESVAFYEEKFASFGD-TYIATV 166
Cdd:PRK12778  81 YItDVVGPLGN--PSEIENYG-TVVCAGGGVGVAPMLPIVKALKAAGNRVITILGGRSKELIILEDEMRESSDeVIIMTD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678 167 DGSHGTQGFVTDV---IFQENLEFDVLYSCGPTPMLKNLEKTfpTKKVFI----SLEERMGCGIGACFACVChTADDPTG 239
Cdd:PRK12778 158 DGSYGRKGLVTDGleeVIKRETKVDKVFAIGPAIMMKFVCLL--TKKYGIptivSLNTIMVDGTGMCGACRV-TVGGKTK 234

                        250
                 ....*....|....*...
gi 671551678 240 FsykkVCTDGPVFRTGEV 257
Cdd:PRK12778 235 F----ACVDGPEFDGHLV 248
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 9-253 2.70e-32

Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural similarity to ferredoxin reductase and sequence similarity to dihydroorotate dehydrogenases. Clostridium pasteurianum inducible dissimilatory type sulfite reductase is linked to ferredoxin and reduces NH2OH and SeO3 at a lesser rate than it's normal substate SO3(2-). Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+.


Pssm-ID: 99817 [Multi-domain]  Cd Length: 253  Bit Score: 118.86  E-value: 2.70e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   9 VVEQKEIAENIMELTLTGELVSEMN---EPGQFVHI---KVSDnatpllrRPISICRIDQESKTFTMIYRAEGAGTKLLA 82
Cdd:cd06221    1 IVEVVDETEDIKTFTLRLEDDDEELftfKPGQFVMLslpGVGE-------APISISSDPTRRGPLELTIRRVGRVTEALH 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  83 QKTAGEAVDILGPLGNGFPVEASKsGQTALLVGGGIGVPPL-----YELANRlvAKGVKVVAVLGFQTES-VAFYEEKF- 155
Cdd:cd06221   74 ELKPGDTVGLRGPFGNGFPVEEMK-GKDLLLVAGGLGLAPLrslinYILDNR--EDYGKVTLLYGARTPEdLLFKEELKe 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678 156 --ASFGDTYIATVD----GSHGTQGFVTDVIFQENL--EFDVLYSCGPTPMLKN-----LEKTFPTKKVFISLEERMGCG 222
Cdd:cd06221  151 waKRSDVEVILTVDraeeGWTGNVGLVTDLLPELTLdpDNTVAIVCGPPIMMRFvakelLKLGVPEEQIWVSLERRMKCG 230

                        250       260       270
                 ....*....|....*....|....*....|.
gi 671551678 223 IGACFACVChtaddptGFSYkkVCTDGPVFR 253
Cdd:cd06221  231 VGKCGHCQI-------GPKY--VCKDGPVFS 252
PRK12775 PRK12775
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ...
 34-252 1.15e-25

putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional


Pssm-ID: 183738 [Multi-domain]  Cd Length: 1006  Bit Score: 105.79  E-value: 1.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   34 EPGQFVHIKVSDNATpllRRPISICRIDQESKTFTMIYRAEGAGTKLLAQK-TAGEA-VDILGPLGngFPVEASKSGQTa 111
Cdd:PRK12775   29 EPGHFVMLRLYEGAE---RIPLTVADFDRKKGTITMVVQALGKTTREMMTKfKAGDTfEDFVGPLG--LPQHIDKAGHV- 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  112 LLVGGGIGVPPLYELANRLVAKGVKVVAVLGFQTESVAFYEEKFASFGDTYI-ATVDGSHGTQGFVTDVIFQ--ENLEFD 188
Cdd:PRK12775  103 VLVGGGLGVAPVYPQLRAFKEAGARTTGIIGFRNKDLVFWEDKFGKYCDDLIvCTDDGSYGKPGFVTAALKEvcEKDKPD 182

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 671551678  189 VLYSCGPTPMLKN-LEKTFPTK-KVFISLEERMGCGIGACFACVChtaddPTGFSYKKVCTDGPVF 252
Cdd:PRK12775  183 LVVAIGPLPMMNAcVETTRPFGvKTMVSLNAIMVDGTGMCGSCRV-----TVGGEVKFACVDGPDF 243
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 35-252 6.46e-25

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 99.88  E-value: 6.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  35 PGQFVHIKVSDNAtpllRRPISICRIDQESKTFTMIYRAEGAGTKLLAQKTAGEAVDILGPLGNGFPVEASKsGQTALLV 114
Cdd:PRK08345  40 PGQFVQVTIPGVG----EVPISICSSPTRKGFFELCIRRAGRVTTVIHRLKEGDIVGVRGPYGNGFPVDEME-GMDLLLI 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678 115 GGGIGVPPL-----YELANRLVAKGVKVVAVLGFQtESVAFYEEKFASFGD----------TYIATVDGSHG-------- 171
Cdd:PRK08345 115 AGGLGMAPLrsvllYAMDNRWKYGNITLIYGAKYY-EDLLFYDELIKDLAEaenvkiiqsvTRDPEWPGCHGlpqgfier 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678 172 -TQGFVTDVIFQENLEFDVLYS--CGPTPMLKN-----LEKTFPTKKVFISLEERMGCGIGACFACVCHTADdptgfSYK 243
Cdd:PRK08345 194 vCKGVVTDLFREANTDPKNTYAaiCGPPVMYKFvfkelINRGYRPERIYVTLERRMRCGIGKCGHCIVGTST-----SIK 268


                 ....*....
gi 671551678 244 KVCTDGPVF 252
Cdd:PRK08345 269 YVCKDGPVF 277
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 10-200 1.57e-20

Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99778 [Multi-domain]  Cd Length: 223  Bit Score: 86.73  E-value: 1.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  10 VEQKEIAENIMELTLTGELVSEMnEPGQFVHIKVsDNATPLLRRPISICRIDQESKTFTMIYRAE--GAGTKLLAQKTAG 87
Cdd:cd00322    1 VATEDVTDDVRLFRLQLPNGFSF-KPGQYVDLHL-PGDGRGLRRAYSIASSPDEEGELELTVKIVpgGPFSAWLHDLKPG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  88 EAVDILGPLGNGFPVEASKsgQTALLVGGGIGVPPLYELANRLVAKGVKVVAVL--GFQTESVAFYEEKFASFGDT---- 161
Cdd:cd00322   79 DEVEVSGPGGDFFLPLEES--GPVVLIAGGIGITPFRSMLRHLAADKPGGEITLlyGARTPADLLFLDELEELAKEgpnf 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 671551678 162 --YIATVDGSHGTQGFVTDVIFQENLEFDVL-------YSCGPTPMLK 200
Cdd:cd00322  157 rlVLALSRESEAKLGPGGRIDREAEILALLPddsgalvYICGPPAMAK 204
PRK12779 PRK12779
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ...
 8-250 1.04e-17

putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional


Pssm-ID: 183740 [Multi-domain]  Cd Length: 944  Bit Score: 82.19  E-value: 1.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   8 TVVEQKEIAENIMELTLTGELVSEMNEPGQFVHIKVSDNATPLlrrPISICRIDQESKTFTMIYRAEGAGTKLLAQKTAG 87
Cdd:PRK12779 652 TIVGKVQLAGGIVEFTVRAPMVARSAQAGQFVRVLPWEKGELI---PLTLADWDAEKGTIDLVVQGMGTSSLEINRMAIG 728

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  88 EAVD-ILGPLGNGFPVEASKSGQTALLVGGGIGVPPLY-------ELANRLVAKGVKVVAVLGFQTESVAFYEEKFASFG 159
Cdd:PRK12779 729 DAFSgIAGPLGRASELHRYEGNQTVVFCAGGVGLPPVYpimrahlRLGNHVTLISGFRAKEFLFWTGDDERVGKLKAEFG 808

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678 160 DTY---IATVDGSHGTQGFVT---DVIFQENLEFD-----VLYSCGPTPMLK---NLEKTFPTKKVfISLEERMGCGIGA 225
Cdd:PRK12779 809 DQLdviYTTNDGSFGVKGFVTgplEEMLKANQQGKgrtiaEVIAIGPPLMMRavsDLTKPYGVKTV-ASLNSIMVDATGM 887

                        250       260
                 ....*....|....*....|....*
gi 671551678 226 CFACVCHTADDPTgFSYKKVCTDGP 250
Cdd:PRK12779 888 CGACMVPVTIDGK-MVRKHACIDGP 911
DHODB_Fe-S_bind pfam10418
Iron-sulfur cluster binding domain of dihydroorotate dehydrogenase B; Lactococcus lactis is ...
 216-257 7.53e-17

Iron-sulfur cluster binding domain of dihydroorotate dehydrogenase B; Lactococcus lactis is one of the few organizms with two dihydroorotate dehydrogenases, DHODs, A and B. The B enzyme is a prototype for DHODs in Gram-positive bacteria that use NAD+ as the second substrate. DHODB is a hetero-tetramer composed of a central homodimer of PyrDB subunits resembling the DHODA structure and two PyrK subunits along with three different cofactors: FMN, FAD, and a [2Fe-2S] cluster. The [2Fe-2S] iron-sulfur cluster binds to this C-terminal domain of the PyrK subunit, which is at the interface between the flavin and NAD binding domains and contains three beta-strands. The four cysteine residues at the N-terminal part of this domain are the ones that bind, in pairs, to the iron-sulfur cluster. The conformation of the whole molecule means that the iron-sulfur cluster is localized in a well-ordered part of this domain close to the FAD binding site. The FAD and and NAD binding domains are FAD_binding_6, pfam00970 and NAD_binding_1, pfam00175.


Pssm-ID: 463084 [Multi-domain]  Cd Length: 40  Bit Score: 71.86  E-value: 7.53e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 671551678  216 EERMGCGIGACFACVCHTADDPTgfSYKKVCTDGPVFRTGEV 257
Cdd:pfam10418   1 EERMACGVGACGGCVVKTKGGDG--EYKRVCVDGPVFDADEV 40
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
8-205 4.40e-13

Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 66.74  E-value: 4.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   8 TVVEQKEIAENIMELTLT---GELVSEMnEPGQFVHIKVSDNATPLlRRPISICRI-DQESKTFTMIYRAEGAGTKLLAQ 83
Cdd:COG1018    7 RVVEVRRETPDVVSFTLEppdGAPLPRF-RPGQFVTLRLPIDGKPL-RRAYSLSSApGDGRLEITVKRVPGGGGSNWLHD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  84 K-TAGEAVDILGPLGNgFPVEASkSGQTALLVGGGIGVPPLYELANRLVAKGVKVVAVL--GFQTESVAFYEEKFASFGD 160
Cdd:COG1018   85 HlKVGDTLEVSGPRGD-FVLDPE-PARPLLLIAGGIGITPFLSMLRTLLARGPFRPVTLvyGARSPADLAFRDELEALAA 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 671551678 161 -----TYIATV-DGSHGTQGFVTDVIFQE---NLEFDVLYSCGPTPMLKNLEKT 205
Cdd:COG1018  163 rhprlRLHPVLsREPAGLQGRLDAELLAAllpDPADAHVYLCGPPPMMEAVRAA 216
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 8-199 1.67e-12

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. These flavoprotein monooxygenases use molecular oxygen as a substrate and require reduced FAD. One atom of oxygen is incorportated into the aromatic compond, while the other is used to form a molecule of water. In contrast dioxygenases add both atoms of oxygen to the substrate.


Pssm-ID: 99808 [Multi-domain]  Cd Length: 232  Bit Score: 65.04  E-value: 1.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   8 TVVEQKEIAENIMELTLTGELVSEMN-EPGQFVHIKVSDNATpllRRPISICRIDQESKTFTMIYRA--EGAGTKLLAQK 84
Cdd:cd06212    4 TVVAVEALTHDIRRLRLRLEEPEPIKfFAGQYVDITVPGTEE---TRSFSMANTPADPGRLEFIIKKypGGLFSSFLDDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  85 TA-GEAVDILGPLGnGFPVEASKSGQtALLVGGGIGVPPLYELANRLVAKGVKVVAVL--GFQTESVAFYEEKFASFGD- 160
Cdd:cd06212   81 LAvGDPVTVTGPYG-TCTLRESRDRP-IVLIGGGSGMAPLLSLLRDMAASGSDRPVRFfyGARTARDLFYLEEIAALGEk 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 671551678 161 ----TYIATV------DGSHGTQGFVTDVIfQENLE----FDVlYSCGPTPML 199
Cdd:cd06212  159 ipdfTFIPALsespddEGWSGETGLVTEVV-QRNEAtlagCDV-YLCGPPPMI 209
PRK05802 PRK05802
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;
7-236 9.58e-12

sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;


Pssm-ID: 235613 [Multi-domain]  Cd Length: 320  Bit Score: 63.84  E-value: 9.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   7 CTVVEQKEIAENIMELTL--TGELVSEMNEPGQFVHIKvSDNATPLLRRPISICRIDQESKTFTMIYRAEGAGTKLLAQK 84
Cdd:PRK05802  67 CKIIKKENIEDNLIILTLkvPHKLARDLVYPGSFVFLR-NKNSSSFFDVPISIMEADTEENIIKVAIEIRGVKTKKIAKL 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  85 TAGEAVDILGPLGNGF----PVEASKSGqTALLVGGGIGVPPLYELANRLVAKGVKVVAVLGFQTESVAFYEEKFASFGD 160
Cdd:PRK05802 146 NKGDEILLRGPYWNGIlglkNIKSTKNG-KSLVIARGIGQAPGVPVIKKLYSNGNKIIVIIDKGPFKNNFIKEYLELYNI 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678 161 TYIATV---DGSHGTQG--FVTDVIfqENLEFDVLYSCGP----TPMLKNLEKTFPTKKVFISLEERMGCGIGACFACVC 231
Cdd:PRK05802 225 EIIELNlldDGELSEEGkdILKEII--KKEDINLIHCGGSdilhYKIIEYLDKLNEKIKLSCSNNAKMCCGEGICGACTV 302


                 ....*
gi 671551678 232 HTADD 236
Cdd:PRK05802 303 RYGGH 307
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
8-206 3.08e-10

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 59.91  E-value: 3.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   8 TVVEQKEIAENIMELTLTGELVSEMN-EPGQFVHIKVSDnaTPLLRR--PISICRIDQESKTFTMIYRAEGAGTKLLAQK 84
Cdd:COG4097  218 RVESVEPEAGDVVELTLRPEGGRWLGhRAGQFAFLRFDG--SPFWEEahPFSISSAPGGDGRLRFTIKALGDFTRRLGRL 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  85 TAGEAVDILGPLGNgFPVEASKSGQTALLVGGGIGVPP----LYELANRlVAKGVKVVAVLGFQTESVAFYEEKF----A 156
Cdd:COG4097  296 KPGTRVYVEGPYGR-FTFDRRDTAPRQVWIAGGIGITPflalLRALAAR-PGDQRPVDLFYCVRDEEDAPFLEELralaA 373

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 671551678 157 SFGDTYIATVDGSHgtQGFVTDVIFQENL----EFDVlYSCGPTPMLKNLEKTF 206
Cdd:COG4097  374 RLAGLRLHLVVSDE--DGRLTAERLRRLVpdlaEADV-FFCGPPGMMDALRRDL 424
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 9-198 5.64e-08

Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent hydroxylation of methane to methanol. This multicomponent enzyme mediates electron transfer via a hydroxylase (MMOH), a coupling protein, and a reductase which is comprised of an N-terminal [2Fe-2S] ferredoxin domain, an FAD binding subdomain, and an NADH binding subdomain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. Dioxygenases add both atom of oxygen to the substrate, while mono-oxygenases add one atom to the substrate and one atom to water.


Pssm-ID: 99806  Cd Length: 236  Bit Score: 51.96  E-value: 5.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   9 VVEQKEIAENIMELTLTGELVSEMN-----EPGQFVHIKVSDNatpLLRRPISICRI--DQESKTFTMIYRAEGAGTKLL 81
Cdd:cd06210    6 IVAVDRVSSNVVRLRLQPDDAEGAGiaaefVPGQFVEIEIPGT---DTRRSYSLANTpnWDGRLEFLIRLLPGGAFSTYL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  82 AQKT-AGEAVDILGPLGnGFPVEASkSGQTALLVGGGIGVPPLYELANRLVAKGVKVVAVL--GFQTESVAFYEEKFASF 158
Cdd:cd06210   83 ETRAkVGQRLNLRGPLG-AFGLREN-GLRPRWFVAGGTGLAPLLSMLRRMAEWGEPQEARLffGVNTEAELFYLDELKRL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 671551678 159 GDT------YIAT-VDGSH--GTQGFVTDvIFQENLEF-----DVlYSCGPTPM 198
Cdd:cd06210  161 ADSlpnltvRICVwRPGGEweGYRGTVVD-ALREDLASsdakpDI-YLCGPPGM 212
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 35-206 1.97e-07

NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) domain, which varies in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99795 [Multi-domain]  Cd Length: 216  Bit Score: 50.33  E-value: 1.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  35 PGQFVHIKVsdnATPLLRR--PISICRIDQESKTFTMIYRAEGAGTKLLAQKT-AGEAVDILGPLGnGFPVEASKSGQta 111
Cdd:cd06198   25 AGQFAFLRF---DASGWEEphPFTISSAPDPDGRLRFTIKALGDYTRRLAERLkPGTRVTVEGPYG-RFTFDDRRARQ-- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678 112 LLVGGGIGVPPLYELANRLVAKGVKVVAVL--GFQTESVAFYEEKFASfgdtyIATVDG------SHGTQGFVTDVIFQE 183
Cdd:cd06198   99 IWIAGGIGITPFLALLEALAARGDARPVTLfyCVRDPEDAVFLDELRA-----LAAAAGvvlhviDSPSDGRLTLEQLVR 173

                        170       180
                 ....*....|....*....|....*..
gi 671551678 184 NLEFDV----LYSCGPTPMLKNLEKTF 206
Cdd:cd06198  174 ALVPDLadadVWFCGPPGMADALEKGL 200
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 8-212 5.32e-07

Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use molecular oxygen as a substrate in the microbial degredation of phenol. This protein is encoded by a single gene and uses a tightly bound FAD cofactor in the NAD(P)H dependent conversion of phenol and O2 to catechol and H2O. This group is related to the NAD binding ferredoxin reductases.


Pssm-ID: 99807  Cd Length: 238  Bit Score: 49.25  E-value: 5.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   8 TVVEQKEIAENIMELTLtgELVSEMN---EPGQFVHIKVSDNATPllrRPISICRIDQESKTFTMIYR--AEGAGTKLL- 81
Cdd:cd06211   10 TVVEIEDLTPTIKGVRL--KLDEPEEiefQAGQYVNLQAPGYEGT---RAFSIASSPSDAGEIELHIRlvPGGIATTYVh 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  82 AQKTAGEAVDILGPLGNgFPVEASkSGQTALLVGGGIGVPPLYELANRLVAKGVKVVAVLGFQTESVA--FYEEKFASFG 159
Cdd:cd06211   85 KQLKEGDELEISGPYGD-FFVRDS-DQRPIIFIAGGSGLSSPRSMILDLLERGDTRKITLFFGARTRAelYYLDEFEALE 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 671551678 160 D-----TYIATVDGSH------GTQGFVTDVI---FQENLEFDVLYSCGPTPMLKNLEKTFPTKKVF 212
Cdd:cd06211  163 KdhpnfKYVPALSREPpesnwkGFTGFVHDAAkkhFKNDFRGHKAYLCGPPPMIDACIKTLMQGRLF 229
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 8-198 6.34e-07

Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. As a Class I bacterial dioxygenases, benzoate dioxygenase like proteins combine an [2Fe-2S] cluster containing N-terminal ferredoxin at the end fused to an FAD/NADP(P) domain. In dioxygenase FAD/NAD(P) binding domain, the reductase transfers 2 electrons from NAD(P)H to the oxygenase which insert into an aromatic substrate, an initial step in microbial aerobic degradation of aromatic rings. Flavin oxidoreductases use flavins as substrates, unlike flavoenzymes which have a flavin prosthetic group.


Pssm-ID: 99805 [Multi-domain]  Cd Length: 228  Bit Score: 48.74  E-value: 6.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   8 TVVEQKEIAENIMELTLTgelVSEMNE----PGQFVHIKV--SDnatplLRRPISI-CRIDQESKTFTMIYRAEGAGTKL 80
Cdd:cd06209    5 TVTEVERLSDSTIGLTLE---LDEAGAlaflPGQYVNLQVpgTD-----ETRSYSFsSAPGDPRLEFLIRLLPGGAMSSY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  81 LAQKTA-GEAVDILGPLGNGF--PVEASksgqtALLVGGGIGVPPLYELANRLVAKGVKVVAVL--G-------FQTESV 148
Cdd:cd06209   77 LRDRAQpGDRLTLTGPLGSFYlrEVKRP-----LLMLAGGTGLAPFLSMLDVLAEDGSAHPVHLvyGvtrdadlVELDRL 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 671551678 149 AFYEEKFASFgdTYIATV---DGSHGTQGFVTDVIFQENL---EFDVlYSCGPTPM 198
Cdd:cd06209  152 EALAERLPGF--SFRTVVadpDSWHPRKGYVTDHLEAEDLndgDVDV-YLCGPPPM 204
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 34-200 1.24e-05

Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor. Like ferredoxin reductases, these proteins have an N-terminal FAD binding subdomain and a C-terminal NADH binding subdomain, separated by a cleft, which accepts FAD. The NADH-binding moiety interacts with part of the FAD and resembles a Rossmann fold. However, NAD is bound differently than in canonical Rossmann fold proteins. Nitrate reductases, flavoproteins similar to pyridine nucleotide cytochrome reductases, catalyze the reduction of nitrate to nitrite. The enzyme can be divided into three functional fragments that bind the cofactors molybdopterin, heme-iron, and FAD/NADH.


Pssm-ID: 99780 [Multi-domain]  Cd Length: 234  Bit Score: 45.25  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  34 EPGQFVHIKVSDNATPLLR--RPISIcriDQESKTFTM---IYRaEGAGTKLLAQKTAGEAVDILGPLGNgFPVEASKSG 108
Cdd:cd06183   30 PVGQHVELKAPDDGEQVVRpyTPISP---DDDKGYFDLlikIYP-GGKMSQYLHSLKPGDTVEIRGPFGK-FEYKPNGKV 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678 109 QTALLVGGGIGVPPLYELANR-LVAKGVKVVAVL--GFQTE-SVAFYEE--KFASFGD-----TYIAT--VDGSHGTQGF 175
Cdd:cd06183  105 KHIGMIAGGTGITPMLQLIRAiLKDPEDKTKISLlyANRTEeDILLREEldELAKKHPdrfkvHYVLSrpPEGWKGGVGF 184

                        170       180       190
                 ....*....|....*....|....*....|
gi 671551678 176 VTDVIFQENLEFD-----VLYSCGPTPMLK 200
Cdd:cd06183  185 ITKEMIKEHLPPPpsedtLVLVCGPPPMIE 214
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 9-198 2.25e-05

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons using oxygen as the oxidant. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate, while mono-oxygenases (aka mixed oxygenases) add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate.


Pssm-ID: 99784 [Multi-domain]  Cd Length: 224  Bit Score: 44.12  E-value: 2.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   9 VVEQKEIAENIMELTLtgELVSEMN-EPGQFVHIKVSDnaTPLLRRPISICRIDQESKTFTMIYRA--EGAGTKLLAQKT 85
Cdd:cd06187    1 VVSVERLTHDIAVVRL--QLDQPLPfWAGQYVNVTVPG--RPRTWRAYSPANPPNEDGEIEFHVRAvpGGRVSNALHDEL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  86 -AGEAVDILGPLGnGFPVEASKSGQTaLLVGGGIGVPPLYELANRLVAKGVKVVAVL--GFQTESVAFYEEKFASFGD-- 160
Cdd:cd06187   77 kVGDRVRLSGPYG-TFYLRRDHDRPV-LCIAGGTGLAPLRAIVEDALRRGEPRPVHLffGARTERDLYDLEGLLALAArh 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 671551678 161 ---TYIATV----DGSHGTQGFVTDVI--FQENL-EFDVlYSCGPTPM 198
Cdd:cd06187  155 pwlRVVPVVsheeGAWTGRRGLVTDVVgrDGPDWaDHDI-YICGPPAM 201
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
 2-204 7.44e-05

Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) provides a means of storing redox reaction energy via the transmembrane translocation of Na2+ ions. The C-terminal domain resembles ferredoxin:NADP+ oxidoreductase, and has NADH and FAD binding sites. (Na+-NQR) is distinct from H+-translocating NADH:quinone oxidoreductases and noncoupled NADH:quinone oxidoreductases. The NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain of this group typically contains an iron-sulfur cluster binding domain.


Pssm-ID: 99785 [Multi-domain]  Cd Length: 283  Bit Score: 43.06  E-value: 7.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   2 IKNEICTVVEQKEIAENIMELTLtgELVS--EMN-EPGQFVHI-----------------------------KVSDNATP 49
Cdd:cd06188    7 AKKWECTVISNDNVATFIKELVL--KLPSgeEIAfKAGGYIQIeipayeiayadfdvaekyradwdkfglwqLVFKHDEP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  50 LLRRpISICRIDQESKTFTMIYR-----------AEGAGTKLLAQKTAGEAVDILGPLGNGFpveASKSGQTALLVGGGI 118
Cdd:cd06188   85 VSRA-YSLANYPAEEGELKLNVRiatpppgnsdiPPGIGSSYIFNLKPGDKVTASGPFGEFF---IKDTDREMVFIGGGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678 119 GVPPL----YELANRLVAKGVKVVAvLGFQTESVAFYEEKFASFGD-----TYIATV------DGSHGTQGFVTDVIFQ- 182
Cdd:cd06188  161 GMAPLrshiFHLLKTLKSKRKISFW-YGARSLKELFYQEEFEALEKefpnfKYHPVLsepqpeDNWDGYTGFIHQVLLEn 239

                        250       260       270
                 ....*....|....*....|....*....|
gi 671551678 183 --------ENLEFdvlYSCGPTPMLKNLEK 204
Cdd:cd06188  240 ylkkhpapEDIEF---YLCGPPPMNSAVIK 266
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 9-127 1.16e-04

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an N-terminal Iron-Sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99791 [Multi-domain]  Cd Length: 222  Bit Score: 42.26  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   9 VVEQKEIAENIMELTLTGELVSEMnEPGQFVHIKVSDNATpllrRPISICRIDQESKTFTM---IYRAEGAGTKLLAQKT 85
Cdd:cd06194    1 VVSLQRLSPDVLRVRLEPDRPLPY-LPGQYVNLRRAGGLA----RSYSPTSLPDGDNELEFhirRKPNGAFSGWLGEEAR 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 671551678  86 AGEAVDILGPLGNGFPVEASKSGqTALLVGGGIGVPPLYELA 127
Cdd:cd06194   76 PGHALRLQGPFGQAFYRPEYGEG-PLLLVGAGTGLAPLWGIA 116
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 35-198 1.32e-04

Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates toluene and forms p-cresol as part of a three component toluene-4-monoxygenase system. Electron transfer is from NADH to an NADH:ferredoxin oxidoreductase (TmoF in P. mendocina) to ferredoxin to an iron-containing oxygenase. TmoF is homologous to other mono- and dioxygenase systems within the ferredoxin reductase family.


Pssm-ID: 99787  Cd Length: 232  Bit Score: 42.24  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  35 PGQFVHIKVsdnatPLL--RRPISICRIDQESKTFTMIYRA--EGAGTKLLAQKT-AGEAVDILGPLGNGF--PVEASKS 107
Cdd:cd06190   26 PGQYALLAL-----PGVegARAYSMANLANASGEWEFIIKRkpGGAASNALFDNLePGDELELDGPYGLAYlrPDEDRDI 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678 108 gqtaLLVGGGIGVPPLYELANRLVAKGVKVVAVL----GFQTESVAFYEEKFAS---FGDT---YIATVDGSHGTQ---- 173
Cdd:cd06190  101 ----VCIAGGSGLAPMLSILRGAARSPYLSDRPVdlfyGGRTPSDLCALDELSAlvaLGARlrvTPAVSDAGSGSAagwd 176

                        170       180       190
                 ....*....|....*....|....*....|..
gi 671551678 174 ---GFVTDVI---FQENL-EFDVlYSCGPTPM 198
Cdd:cd06190  177 gptGFVHEVVeatLGDRLaEFEF-YFAGPPPM 207
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 34-205 2.00e-03

NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 38.44  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  34 EPGQFVHIKVsdnatPLLRR-----PISICRI-DQESKTFTMIYRAEGAGTKLLAQKTAGEAVDIL-------GPLGNgf 100
Cdd:cd06186   26 KPGQHVYLNF-----PSLLSfwqshPFTIASSpEDEQDTLSLIIRAKKGFTTRLLRKALKSPGGGVslkvlveGPYGS-- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678 101 PVEASKSGQTALLVGGGIGVPPLYELANRLVAKGVKvvavlGFQTESVAFY-----EEKFASFGD--TYIATVDGSHGTQ 173
Cdd:cd06186   99 SSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSSK-----TSRTRRVKLVwvvrdREDLEWFLDelRAAQELEVDGEIE 173

                        170       180       190
                 ....*....|....*....|....*....|..
gi 671551678 174 GFVTDVIfqenlefdvlySCGPTPMLKNLEKT 205
Cdd:cd06186  174 IYVTRVV-----------VCGPPGLVDDVRNA 194
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 8-122 4.01e-03

Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99792 [Multi-domain]  Cd Length: 241  Bit Score: 37.54  E-value: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678   8 TVVEQKEIAENIMELTLTGELVSEMnEPGQFVHIKVSDNATPLLRRPISI-CRIDQESKTFTMIYRAEGAGTKLLAQKTA 86
Cdd:cd06195    1 TVLKRRDWTDDLFSFRVTRDIPFRF-QAGQFTKLGLPNDDGKLVRRAYSIaSAPYEENLEFYIILVPDGPLTPRLFKLKP 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 671551678  87 GEAVDI-LGPLGNgFPVEASKSGQTALLVGGGIGVPP 122
Cdd:cd06195   80 GDTIYVgKKPTGF-LTLDEVPPGKRLWLLATGTGIAP 115
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 34-123 6.44e-03

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap between the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99813 [Multi-domain]  Cd Length: 235  Bit Score: 36.86  E-value: 6.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671551678  34 EPGQFVHIKVSDNATPLLRRPISICRIDQESKTF-TMIYRAEGA--GTKLLAQKTAGEAVDILGPLGnGF---PVEasks 107
Cdd:cd06217   32 LAGQHVDLRLTAIDGYTAQRSYSIASSPTQRGRVeLTVKRVPGGevSPYLHDEVKVGDLLEVRGPIG-TFtwnPLH---- 106

                         90
                 ....*....|....*.
gi 671551678 108 GQTALLVGGGIGVPPL 123
Cdd:cd06217  107 GDPVVLLAGGSGIVPL 122
 
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