NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1002237022|ref|XP_015622711|]
View 

fruit protein pKIWI502 [Oryza sativa Japonica Group]

Protein Classification

FAD-dependent oxidoreductase( domain architecture ID 10085328)

FAD-dependent oxidoreductase, similar to ferredoxin- and rubredoxin-NAD(+) reductases including human oxidoreductase NAD-binding domain-containing protein 1, may act on an iron-sulfur protein as electron donor with NAD(+) or NADP(+) as acceptor

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 87-285 7.79e-37

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: 130.64  E-value: 7.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  87 PGQYLLIRVPGEDELKPAFMAIASPPG-GAAFEFLVKTVP-GTTAEKLCGLRDGDVLELGAIMGNGFPisrinPPDEAQT 164
Cdd:cd00322    25 PGQYVDLHLPGDGRGLRRAYSIASSPDeEGELELTVKIVPgGPFSAWLHDLKPGDEVEVSGPGGDFFL-----PLEESGP 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 165 VLLFATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQTMAYQDRFTNWESTG--LKIIPVLSRADDSWKGERGYVQDA 242
Cdd:cd00322   100 VVLIAGGIGITPFRSMLRHLAADKPGGEITLLYGARTPADLLFLDELEELAKEGpnFRLVLALSRESEAKLGPGGRIDRE 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1002237022 243 FLKAQNIANHFSTGAVLCGQKQMSEEITSALVADGVSPDKILT 285
Cdd:cd00322   180 AEILALLPDDSGALVYICGPPAMAKAVREALVSLGVPEERIHT 222
 
Name Accession Description Interval E-value
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 87-285 7.79e-37

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: 130.64  E-value: 7.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  87 PGQYLLIRVPGEDELKPAFMAIASPPG-GAAFEFLVKTVP-GTTAEKLCGLRDGDVLELGAIMGNGFPisrinPPDEAQT 164
Cdd:cd00322    25 PGQYVDLHLPGDGRGLRRAYSIASSPDeEGELELTVKIVPgGPFSAWLHDLKPGDEVEVSGPGGDFFL-----PLEESGP 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 165 VLLFATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQTMAYQDRFTNWESTG--LKIIPVLSRADDSWKGERGYVQDA 242
Cdd:cd00322   100 VVLIAGGIGITPFRSMLRHLAADKPGGEITLLYGARTPADLLFLDELEELAKEGpnFRLVLALSRESEAKLGPGGRIDRE 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1002237022 243 FLKAQNIANHFSTGAVLCGQKQMSEEITSALVADGVSPDKILT 285
Cdd:cd00322   180 AEILALLPDDSGALVYICGPPAMAKAVREALVSLGVPEERIHT 222
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 76-283 8.77e-34

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 123.43  E-value: 8.77e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  76 DATDLAASYTtPGQYLLIRVPGEDELKPafMAIASPPGGAA-FEFLVKTVpGTTAEKLCGLRDGDVLELGAIMGNGFPIs 154
Cdd:COG0543    18 EAPLIALKFK-PGQFVMLRVPGDGLRRP--FSIASAPREDGtIELHIRVV-GKGTRALAELKPGDELDVRGPLGNGFPL- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 155 rinpPDEAQTVLLFATGTGISPVRSLIEfgFAADQRADVRLYYGARNLQTMAYQDRFTNWESTGLKIIpvlsrADDSWKG 234
Cdd:COG0543    93 ----EDSGRPVLLVAGGTGLAPLRSLAE--ALLARGRRVTLYLGARTPEDLYLLDELEALADFRVVVT-----TDDGWYG 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1002237022 235 ERGYVQDAFLKAQNIANHFStgAVLCGQKQMSEEITSALVADGVSPDKI 283
Cdd:COG0543   162 RKGFVTDALKELLAEDSGDD--VYACGPPPMMKAVAELLLERGVPPERI 208
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 167-265 2.18e-16

Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity.


Pssm-ID: 425503 [Multi-domain]  Cd Length: 109  Bit Score: 73.06  E-value: 2.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 167 LFATGTGISPVRSLIEFGFAADQR-ADVRLYYGARNLQTMAYQDRFTNWEST---GLKIIPVLSRADDSWKGERGYVQDA 242
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILEDPKDpTQVVLVFGNRNEDDILYREELDELAEKhpgRLTVVYVVSRPEAGWTGGKGRVQDA 80

                          90       100
                  ....*....|....*....|....*...
gi 1002237022 243 FLKaqniaNHFSTG-----AVLCGQKQM 265
Cdd:pfam00175  81 LLE-----DHLSLPdeethVYVCGPPGM 103
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 70-283 3.85e-15

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 73.69  E-value: 3.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  70 FSVDLSDAtDLAASYT-TPGQYLLIRVPGEDELKPAFMAIASPPGgaAFEFLVKTVpGTTAEKLCGLRDGDVLELGAIMG 148
Cdd:PRK08345   23 FLLRFEDP-ELAESFTfKPGQFVQVTIPGVGEVPISICSSPTRKG--FFELCIRRA-GRVTTVIHRLKEGDIVGVRGPYG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 149 NGFPISRInppdEAQTVLLFATGTGISPVRSLieFGFAADQR---ADVRLYYGARNLQTMAYQDRFTN--WESTGLKIIP 223
Cdd:PRK08345   99 NGFPVDEM----EGMDLLLIAGGLGMAPLRSV--LLYAMDNRwkyGNITLIYGAKYYEDLLFYDELIKdlAEAENVKIIQ 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 224 VLSRaDDSWKG----ERGYVQDA------FLKAQNIANHFSTGAVLCGQKQMSEEITSALVADGVSPDKI 283
Cdd:PRK08345  173 SVTR-DPEWPGchglPQGFIERVckgvvtDLFREANTDPKNTYAAICGPPVMYKFVFKELINRGYRPERI 241
 
Name Accession Description Interval E-value
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 87-285 7.79e-37

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: 130.64  E-value: 7.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  87 PGQYLLIRVPGEDELKPAFMAIASPPG-GAAFEFLVKTVP-GTTAEKLCGLRDGDVLELGAIMGNGFPisrinPPDEAQT 164
Cdd:cd00322    25 PGQYVDLHLPGDGRGLRRAYSIASSPDeEGELELTVKIVPgGPFSAWLHDLKPGDEVEVSGPGGDFFL-----PLEESGP 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 165 VLLFATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQTMAYQDRFTNWESTG--LKIIPVLSRADDSWKGERGYVQDA 242
Cdd:cd00322   100 VVLIAGGIGITPFRSMLRHLAADKPGGEITLLYGARTPADLLFLDELEELAKEGpnFRLVLALSRESEAKLGPGGRIDRE 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1002237022 243 FLKAQNIANHFSTGAVLCGQKQMSEEITSALVADGVSPDKILT 285
Cdd:cd00322   180 AEILALLPDDSGALVYICGPPAMAKAVREALVSLGVPEERIHT 222
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 76-283 8.77e-34

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 123.43  E-value: 8.77e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  76 DATDLAASYTtPGQYLLIRVPGEDELKPafMAIASPPGGAA-FEFLVKTVpGTTAEKLCGLRDGDVLELGAIMGNGFPIs 154
Cdd:COG0543    18 EAPLIALKFK-PGQFVMLRVPGDGLRRP--FSIASAPREDGtIELHIRVV-GKGTRALAELKPGDELDVRGPLGNGFPL- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 155 rinpPDEAQTVLLFATGTGISPVRSLIEfgFAADQRADVRLYYGARNLQTMAYQDRFTNWESTGLKIIpvlsrADDSWKG 234
Cdd:COG0543    93 ----EDSGRPVLLVAGGTGLAPLRSLAE--ALLARGRRVTLYLGARTPEDLYLLDELEALADFRVVVT-----TDDGWYG 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1002237022 235 ERGYVQDAFLKAQNIANHFStgAVLCGQKQMSEEITSALVADGVSPDKI 283
Cdd:COG0543   162 RKGFVTDALKELLAEDSGDD--VYACGPPPMMKAVAELLLERGVPPERI 208
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
86-283 6.06e-31

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 115.27  E-value: 6.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  86 TPGQYLLIRVPGEDELKPAFMAIASPPGGAAFEFLVKTVP---GTTAekLC-GLRDGDVLELGAIMGNgFPIsrinPPDE 161
Cdd:COG1018    35 RPGQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVKRVPgggGSNW--LHdHLKVGDTLEVSGPRGD-FVL----DPEP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 162 AQTVLLFATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQTMAYQDRFTNWEST--GLKIIPVLSRADDswkGERGYV 239
Cdd:COG1018   108 ARPLLLIAGGIGITPFLSMLRTLLARGPFRPVTLVYGARSPADLAFRDELEALAARhpRLRLHPVLSREPA---GLQGRL 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1002237022 240 QDAFLKAqnIANHFSTGAV-LCGQKQMSEEITSALVADGVSPDKI 283
Cdd:COG1018   185 DAELLAA--LLPDPADAHVyLCGPPPMMEAVRAALAELGVPEERI 227
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 86-283 3.13e-28

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: 108.06  E-value: 3.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  86 TPGQYLLIRVPGEDELKPAFmAIASPPGGAAF-EFLVKTVP-GTTAEKLCG-LRDGDVLELGAIMGNgfpiSRINPPDEA 162
Cdd:cd06187    25 WAGQYVNVTVPGRPRTWRAY-SPANPPNEDGEiEFHVRAVPgGRVSNALHDeLKVGDRVRLSGPYGT----FYLRRDHDR 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 163 QtVLLFATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQTMAYQDRFTNWEST--GLKIIPVLSRADDSWKGERGYVQ 240
Cdd:cd06187   100 P-VLCIAGGTGLAPLRAIVEDALRRGEPRPVHLFFGARTERDLYDLEGLLALAARhpWLRVVPVVSHEEGAWTGRRGLVT 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1002237022 241 DAflkaqnIANHFSTGA----VLCGQKQMSEEITSALVADGVSPDKI 283
Cdd:cd06187   179 DV------VGRDGPDWAdhdiYICGPPAMVDATVDALLARGAPPERI 219
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 87-285 5.03e-28

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: 107.80  E-value: 5.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  87 PGQYLLIRVPGEDELKpAFmAIASPPGGAAF-EFLVKTVPGTTAEKLC--GLRDGDVLELgaimgNGfPISRINPPDEAQ 163
Cdd:cd06211    38 AGQYVNLQAPGYEGTR-AF-SIASSPSDAGEiELHIRLVPGGIATTYVhkQLKEGDELEI-----SG-PYGDFFVRDSDQ 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 164 TVLLF-ATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQTMAYQDRFTNWEST--GLKIIPVLSRA--DDSWKGERGY 238
Cdd:cd06211   110 RPIIFiAGGSGLSSPRSMILDLLERGDTRKITLFFGARTRAELYYLDEFEALEKDhpNFKYVPALSREppESNWKGFTGF 189

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002237022 239 VQDAflkaqnIANHFS---TG--AVLCGQKQMSEEITSALVADGVSPDKILT 285
Cdd:cd06211   190 VHDA------AKKHFKndfRGhkAYLCGPPPMIDACIKTLMQGRLFERDIYY 235
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 62-285 4.03e-23

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: 94.98  E-value: 4.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  62 TADGSLVHFSVDLSDATDLAAsytTPGQYLLIRVPGEDElKPafMAIASPPGGA-AFEFLVKTVpGTTAEKLCGLRDGDV 140
Cdd:cd06221     8 TEDIKTFTLRLEDDDEELFTF---KPGQFVMLSLPGVGE-AP--ISISSDPTRRgPLELTIRRV-GRVTEALHELKPGDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 141 LELGAIMGNGFPISRInppdEAQTVLLFATGTGISPVRSLIEfgFAADQRAD---VRLYYGARNLQTMAYQDRFTNWE-S 216
Cdd:cd06221    81 VGLRGPFGNGFPVEEM----KGKDLLLVAGGLGLAPLRSLIN--YILDNREDygkVTLLYGARTPEDLLFKEELKEWAkR 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 217 TGLKIIPVLSRADDSWKGERGYVQDAFLKAQ-NIANhfsTGAVLCGQKQMSEEITSALVADGVSPDKILT 285
Cdd:cd06221   155 SDVEVILTVDRAEEGWTGNVGLVTDLLPELTlDPDN---TVAIVCGPPIMMRFVAKELLKLGVPEEQIWV 221
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 87-283 1.25e-22

NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron transfer from iron complexes or iron proteins. Structurally similar to ferredoxin reductases, but with only 15% sequence identity, flavin reductases reduce FAD, FMN, or riboflavin via NAD(P)H. Flavin is used as a substrate, rather than a tightly bound prosthetic group as in flavoenzymes; weaker binding is due to the absence of a binding site for the AMP moeity of FAD.


Pssm-ID: 99786 [Multi-domain]  Cd Length: 224  Bit Score: 93.00  E-value: 1.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  87 PGQYLLIRVPGEDelKPAFmAIASPPGGAAF-EFLVKTVPGT--TAEKLCGLRDGDVLELGAIMGNGFpisrINPPDEAQ 163
Cdd:cd06189    28 AGQYLDLLLDDGD--KRPF-SIASAPHEDGEiELHIRAVPGGsfSDYVFEELKENGLVRIEGPLGDFF----LREDSDRP 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 164 TVLLfATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQTMAYQDRFTNWEST--GLKIIPVLSRADDSWKGERGYVQD 241
Cdd:cd06189   101 LILI-AGGTGFAPIKSILEHLLAQGSKRPIHLYWGARTEEDLYLDELLEAWAEAhpNFTYVPVLSEPEEGWQGRTGLVHE 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1002237022 242 AFLkaQNIANHFSTGAVLCGQKQMSEEITSALVADGVSPDKI 283
Cdd:cd06189   180 AVL--EDFPDLSDFDVYACGSPEMVYAARDDFVEKGLPEENF 219
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 86-281 3.39e-22

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: 92.24  E-value: 3.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  86 TPGQYLLIRVPGEDElKPAFMA--IASPPGGAAFEFLVKTVP-GTTAEKLCGLRDGDVLELGA-IMGNgFPISRINPPDe 161
Cdd:cd06195    26 QAGQFTKLGLPNDDG-KLVRRAysIASAPYEENLEFYIILVPdGPLTPRLFKLKPGDTIYVGKkPTGF-LTLDEVPPGK- 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 162 aqTVLLFATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQTMAYQDRFTNWESTG---LKIIPVLSRADDSWkGERGY 238
Cdd:cd06195   103 --RLWLLATGTGIAPFLSMLRDLEIWERFDKIVLVHGVRYAEELAYQDEIEALAKQYngkFRYVPIVSREKENG-ALTGR 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002237022 239 VQDaFLKAQNIANHF-------STGAVLCGQKQMSEEITSALVADGVSPD 281
Cdd:cd06195   180 IPD-LIESGELEEHAglpldpeTSHVMLCGNPQMIDDTQELLKEKGFSKN 228
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 66-284 8.71e-22

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: 91.12  E-value: 8.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  66 SLVHFSVDLSDATDLAasyTTPGQYLLIRVPGEDELKPAFMaiASPPGGAAFEFLVKTVPG----TTAEKLCglRDGDVL 141
Cdd:cd06209    15 STIGLTLELDEAGALA---FLPGQYVNLQVPGTDETRSYSF--SSAPGDPRLEFLIRLLPGgamsSYLRDRA--QPGDRL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 142 ELGAIMGNGF--PISRinPpdeaqtVLLFATGTGISPVRSLIEFgFAADQRA-DVRLYYGARNLQTMAYQDR---FTNWe 215
Cdd:cd06209    88 TLTGPLGSFYlrEVKR--P------LLMLAGGTGLAPFLSMLDV-LAEDGSAhPVHLVYGVTRDADLVELDRleaLAER- 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002237022 216 STGLKIIPVLSRAdDSWKGERGYVQDAFLKAqnianHFSTGAV---LCGQKQMSEEITSALVADGVSPDKIL 284
Cdd:cd06209   158 LPGFSFRTVVADP-DSWHPRKGYVTDHLEAE-----DLNDGDVdvyLCGPPPMVDAVRSWLDEQGIEPANFY 223
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 86-283 2.83e-20

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: 87.00  E-value: 2.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  86 TPGQYLLIRVPGEDELKPAFMAiASPPGGAAFEFLVKTVP-GTTAEKLC-GLRDGDVLELGAIMGNGFpiSRINPPdeaQ 163
Cdd:cd06212    31 FAGQYVDITVPGTEETRSFSMA-NTPADPGRLEFIIKKYPgGLFSSFLDdGLAVGDPVTVTGPYGTCT--LRESRD---R 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 164 TVLLFATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQTMAYQDRFtnwESTGLKI-----IPVLSRADDS--WKGER 236
Cdd:cd06212   105 PIVLIGGGSGMAPLLSLLRDMAASGSDRPVRFFYGARTARDLFYLEEI---AALGEKIpdftfIPALSESPDDegWSGET 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1002237022 237 GYVQDAFlkAQNIANHFSTGAVLCGQKQMSEEITSALVADGVSPDKI 283
Cdd:cd06212   182 GLVTEVV--QRNEATLAGCDVYLCGPPPMIDAALPVLEMSGVPPDQI 226
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 67-283 6.28e-20

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. 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 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: 99809  Cd Length: 227  Bit Score: 85.83  E-value: 6.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  67 LVHFSVDLSDATDLAASYTtPGQYLLIRVPGEDElkPAFMAIASPPGGAA-FEFLVKTVPGT--TAEKLCGLRDGDVLEL 143
Cdd:cd06213    11 LTHDIVRLTVQLDRPIAYK-AGQYAELTLPGLPA--ARSYSFANAPQGDGqLSFHIRKVPGGafSGWLFGADRTGERLTV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 144 GAIMGNgFpisRINPPDEaqTVLLFATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQTMAYQDRF----TNWEStGL 219
Cdd:cd06213    88 RGPFGD-F---WLRPGDA--PILCIAGGSGLAPILAILEQARAAGTKRDVTLLFGARTQRDLYALDEIaaiaARWRG-RF 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002237022 220 KIIPVLSR--ADDSWKGERGYVQDAFlkAQNIANhfSTGAVLCGQKQMSEEITSALVADGVSPDKI 283
Cdd:cd06213   161 RFIPVLSEepADSSWKGARGLVTEHI--AEVLLA--ATEAYLCGPPAMIDAAIAVLRALGIAREHI 222
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 87-285 3.19e-19

Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and conversion]; Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase


Pssm-ID: 442118 [Multi-domain]  Cd Length: 396  Bit Score: 86.45  E-value: 3.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  87 PGQYLLIRVPGED--------ELKPAFMA-------------IASPPG-GAAFEFLVK------TVPG---TTAekLCGL 135
Cdd:COG2871   163 AGQYIQIEVPPYEvdfkdfdiPEEEKFGLfdkndeevtraysMANYPAeKGIIELNIRiatppmDVPPgigSSY--IFSL 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 136 RDGDVLELGAIMGNGFPisrinpPDEAQTVLLFATGTGISPVRSLIEFGFAAD--QRaDVRLYYGARNLQTMAYQDRFTN 213
Cdd:COG2871   241 KPGDKVTISGPYGEFFL------RDSDREMVFIGGGAGMAPLRSHIFDLLERGktDR-KITFWYGARSLRELFYLEEFRE 313

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002237022 214 WEST--GLKIIPVLSRA--DDSWKGERGYVQDAfLKAQNIANHFSTG---AVLCGQKQMSEEITSALVADGVSPDKILT 285
Cdd:COG2871   314 LEKEhpNFKFHPALSEPlpEDNWDGETGFIHEV-LYENYLKDHPAPEdceAYLCGPPPMIDAVIKMLDDLGVEEENIYF 391
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 62-283 2.13e-18

NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation oxidoreductase. PA oxidoreductases of E. coli hydroxylate PA-CoA in the second step of PA degradation. Members of this group typically fuse a ferredoxin reductase-like domain with an iron-sulfur binding cluster domain. Ferredoxins 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 portion may contain a flavin prosthetic group, as in flavoenzymes, or use flavin as a substrate. 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 and 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: 99810 [Multi-domain]  Cd Length: 241  Bit Score: 82.21  E-value: 2.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  62 TADGSLVHFSVDlsdaTDLAASYT-TPGQYLLIRVPGEDELKPAFMAIASPPGGAAFEFLVKTVPGTTAEK-LCG-LRDG 138
Cdd:cd06214    13 TADAVSITFDVP----EELRDAFRyRPGQFLTLRVPIDGEEVRRSYSICSSPGDDELRITVKRVPGGRFSNwANDeLKAG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 139 DVLELGAIMGNGFPisrinPPD-EAQTVLLFATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQTM-----------A 206
Cdd:cd06214    89 DTLEVMPPAGRFTL-----PPLpGARHYVLFAAGSGITPVLSILKTALAREPASRVTLVYGNRTEASVifreeladlkaR 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 207 YQDRFTnwestglkIIPVLSRADDSWKGERGYVQDAFLKA---QNIANHFSTGAVLCGQKQMSEEITSALVADGVSPDKI 283
Cdd:cd06214   164 YPDRLT--------VIHVLSREQGDPDLLRGRLDAAKLNAllkNLLDATEFDEAFLCGPEPMMDAVEAALLELGVPAERI 235
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
 108-284 1.52e-16

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: 77.73  E-value: 1.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 108 IASPPGGAAfeflvKTVPGTTAEKLCGLRDGDVLElgaIMGngfPISRINPPDEAQTVLLFATGTGISPVRSLIEFGFAA 187
Cdd:cd06188   107 IATPPPGNS-----DIPPGIGSSYIFNLKPGDKVT---ASG---PFGEFFIKDTDREMVFIGGGAGMAPLRSHIFHLLKT 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 188 D-QRADVRLYYGARNLQTMAYQDRFTN--WESTGLKIIPVLSRA--DDSWKGERGYVQDAFLKAQnIANHFSTGAV---L 259
Cdd:cd06188   176 LkSKRKISFWYGARSLKELFYQEEFEAleKEFPNFKYHPVLSEPqpEDNWDGYTGFIHQVLLENY-LKKHPAPEDIefyL 254

                         170       180
                  ....*....|....*....|....*
gi 1002237022 260 CGQKQMSEEITSALVADGVSPDKIL 284
Cdd:cd06188   255 CGPPPMNSAVIKMLDDLGVPRENIA 279
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 167-265 2.18e-16

Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity.


Pssm-ID: 425503 [Multi-domain]  Cd Length: 109  Bit Score: 73.06  E-value: 2.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 167 LFATGTGISPVRSLIEFGFAADQR-ADVRLYYGARNLQTMAYQDRFTNWEST---GLKIIPVLSRADDSWKGERGYVQDA 242
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILEDPKDpTQVVLVFGNRNEDDILYREELDELAEKhpgRLTVVYVVSRPEAGWTGGKGRVQDA 80

                          90       100
                  ....*....|....*....|....*...
gi 1002237022 243 FLKaqniaNHFSTG-----AVLCGQKQM 265
Cdd:pfam00175  81 LLE-----DHLSLPdeethVYVCGPPGM 103
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 87-285 1.99e-15

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: 73.84  E-value: 1.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  87 PGQYLLIRVPGED--ELKPAFmAIASPPGGAAF-EFLVKTVPG-------TTAeklcgLRDGDVLELGAIMGnGFpisrI 156
Cdd:cd06217    33 AGQHVDLRLTAIDgyTAQRSY-SIASSPTQRGRvELTVKRVPGgevspylHDE-----VKVGDLLEVRGPIG-TF----T 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 157 NPPDEAQTVLLFATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQTMAYQDRFTNWEST--GLKIIPVLSRADD-SWK 233
Cdd:cd06217   102 WNPLHGDPVVLLAGGSGIVPLMSMIRYRRDLGWPVPFRLLYSARTAEDVIFRDELEQLARRhpNLHVTEALTRAAPaDWL 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002237022 234 GERGYVqDAFLKAQNIANHFSTGAVLCGQKQMSEEITSALVADGVSPDKILT 285
Cdd:cd06217   182 GPAGRI-TADLIAELVPPLAGRRVYVCGPPAFVEAATRLLLELGVPRDRIRT 232
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 70-283 3.85e-15

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 73.69  E-value: 3.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  70 FSVDLSDAtDLAASYT-TPGQYLLIRVPGEDELKPAFMAIASPPGgaAFEFLVKTVpGTTAEKLCGLRDGDVLELGAIMG 148
Cdd:PRK08345   23 FLLRFEDP-ELAESFTfKPGQFVQVTIPGVGEVPISICSSPTRKG--FFELCIRRA-GRVTTVIHRLKEGDIVGVRGPYG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 149 NGFPISRInppdEAQTVLLFATGTGISPVRSLieFGFAADQR---ADVRLYYGARNLQTMAYQDRFTN--WESTGLKIIP 223
Cdd:PRK08345   99 NGFPVDEM----EGMDLLLIAGGLGMAPLRSV--LLYAMDNRwkyGNITLIYGAKYYEDLLFYDELIKdlAEAENVKIIQ 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 224 VLSRaDDSWKG----ERGYVQDA------FLKAQNIANHFSTGAVLCGQKQMSEEITSALVADGVSPDKI 283
Cdd:PRK08345  173 SVTR-DPEWPGchglPQGFIERVckgvvtDLFREANTDPKNTYAAICGPPVMYKFVFKELINRGYRPERI 241
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 87-278 5.12e-15

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: 72.67  E-value: 5.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  87 PGQYLLIRVPGEDElKPafMAIASPPGGAAfeFLVKTVpGTTAEKLCGLRDGDVLELGAIMGNGFPIsrinppdEAQTVL 166
Cdd:cd06220    26 PGQFVMVWVPGVDE-IP--MSLSYIDGPNS--ITVKKV-GEATSALHDLKEGDKLGIRGPYGNGFEL-------VGGKVL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 167 LFATGTGISPVRSLIEFgfaADQRADVRLYYGARNLQTMAYQDRFtnweSTGLKIIPVlsrADDSWKGERGYVQDAfLKA 246
Cdd:cd06220    93 LIGGGIGIAPLAPLAER---LKKAADVTVLLGARTKEELLFLDRL----RKSDELIVT---TDDGSYGFKGFVTDL-LKE 161

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1002237022 247 QNIANHfsTGAVLCGQKQMSEEITSALVADGV 278
Cdd:cd06220   162 LDLEEY--DAIYVCGPEIMMYKVLEILDERGV 191
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 87-285 4.16e-14

Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with a C-terminal iron-sulfur binding cluster domain. FNR 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 methnae assimilation in a variety of 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: 99788 [Multi-domain]  Cd Length: 231  Bit Score: 69.86  E-value: 4.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  87 PGQYLLIRVPGEDELKPAFMAIASPPGGAAFEFLVKTVPGTTAEKLC--GLRDGDVLELGAIMGNgFpisrINPPDEAQT 164
Cdd:cd06191    30 PGQHVTLKLDFDGEELRRCYSLCSSPAPDEISITVKRVPGGRVSNYLreHIQPGMTVEVMGPQGH-F----VYQPQPPGR 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 165 VLLFATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQTMAYQDRFTNWES--TGLKIIPVLSR--ADDSWKGERGYVQ 240
Cdd:cd06191   105 YLLVAAGSGITPLMAMIRATLQTAPESDFTLIHSARTPADMIFAQELRELADkpQRLRLLCIFTRetLDSDLLHGRIDGE 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1002237022 241 DAFLKAQnIANHFSTGAVLCGQKQMSEEITSALVADGVSPDKILT 285
Cdd:cd06191   185 QSLGAAL-IPDRLEREAFICGPAGMMDAVETALKELGMPPERIHT 228
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 79-265 4.88e-14

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: 69.88  E-value: 4.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  79 DLAASYTTPGQYLLIRVPGEDEL---KPafMAIAS--PPGGAaFEFLVKTVpGTTAEKLCGLRDGDVLELGAIMGNGFPI 153
Cdd:cd06218    19 PEIAAAAKPGQFVMLRVPDGSDPllrRP--ISIHDvdPEEGT-ITLLYKVV-GKGTRLLSELKAGDELDVLGPLGNGFDL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 154 srinpPDEAQTVLLFATGTGISPVRSLIEFgfAADQRADVRLYYGARNLQTMAYQDRFTNWestglkIIPVLSRADDSWK 233
Cdd:cd06218    95 -----PDDDGKVLLVGGGIGIAPLLFLAKQ--LAERGIKVTVLLGFRSADDLFLVEEFEAL------GAEVYVATDDGSA 161

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1002237022 234 GERGYVQDAfLKAQNIANHFstGAVL-CGQKQM 265
Cdd:cd06218   162 GTKGFVTDL-LKELLAEARP--DVVYaCGPEPM 191
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
87-269 1.84e-13

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 69.39  E-value: 1.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  87 PGQYLLIRVPGEDELKpAFMAIASPPGGAAFEFLVKTVPGTTAEKLcgLRD----GDVLELGAIMGnGFPISRINPPdea 162
Cdd:PRK11872  139 PGQYARLQIPGTDDWR-SYSFANRPNATNQLQFLIRLLPDGVMSNY--LRErcqvGDEILFEAPLG-AFYLREVERP--- 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 163 qtVLLFATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQTMAYQDRFTNWEST--GLKIIPVLSRADDSWKGERGYVQ 240
Cdd:PRK11872  212 --LVFVAGGTGLSAFLGMLDELAEQGCSPPVHLYYGVRHAADLCELQRLAAYAERlpNFRYHPVVSKASADWQGKRGYIH 289

                         170       180
                  ....*....|....*....|....*....
gi 1002237022 241 DAFLKAQNIANHFSTgaVLCGQKQMSEEI 269
Cdd:PRK11872  290 EHFDKAQLRDQAFDM--YLCGPPPMVEAV 316
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 87-281 1.37e-12

CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 66.82  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  87 PGQYL-LIRVPGedelKPAFMAIASPPGGAAF-EFLVKTVP-GTTAEKLCG-LRDGDVLELGAIMGNGFPISRINPPdea 162
Cdd:PRK07609  134 AGQYIeFILKDG----KRRSYSIANAPHSGGPlELHIRHMPgGVFTDHVFGaLKERDILRIEGPLGTFFLREDSDKP--- 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 163 qtVLLFATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQTMaYQDRFTN-WEST--GLKIIPVLS--RADDSWKGERG 237
Cdd:PRK07609  207 --IVLLASGTGFAPIKSIVEHLRAKGIQRPVTLYWGARRPEDL-YLSALAEqWAEElpNFRYVPVVSdaLDDDAWTGRTG 283

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1002237022 238 YVQDAFLkaqniANHFSTGAVL---CGQKQMSEEITSALVADGVSPD 281
Cdd:PRK07609  284 FVHQAVL-----EDFPDLSGHQvyaCGSPVMVYAARDDFVAAGLPAE 325
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 86-283 1.77e-12

FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain containing a B-type heme fused with a ferredoxin reductase-like FAD/NAD-binding domain. Flavohemoglobins detoxify nitric oxide (NO) via an NO dioxygenase reaction. The hemoglobin domain adopts a globin fold with an embedded heme molecule. Flavohemoglobins also have a C-terminal reductase domain with bindiing sites for FAD and NAD(P)H. This domain catalyzes the conversion of NO + O2 + NAD(P)H to NO3- + NAD(P)+. Instead of the oxygen transport function of hemoglobins, flavohemoglobins seem to act in NO dioxygenation and NO signalling.


Pssm-ID: 99781  Cd Length: 247  Bit Score: 65.66  E-value: 1.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  86 TPGQYLLIRVPGEDELKPAFMA--IASPPGGAAFEFLVKTVP-GTTAEKLCG-LRDGDVLELGAIMGNgFPIsrinPPDE 161
Cdd:cd06184    38 LPGQYLSVRVKLPGLGYRQIRQysLSDAPNGDYYRISVKREPgGLVSNYLHDnVKVGDVLEVSAPAGD-FVL----DEAS 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 162 AQTVLLFATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQTMAYQDRFTNWEST--GLKIIPVLSRADDSWKGE---- 235
Cdd:cd06184   113 DRPLVLISAGVGITPMLSMLEALAAEGPGRPVTFIHAARNSAVHAFRDELEELAARlpNLKLHVFYSEPEAGDREEdydh 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1002237022 236 RGYVQDAFLKAQNIANHFSTgaVLCGQKQMSEEITSALVADGVSPDKI 283
Cdd:cd06184   193 AGRIDLALLRELLLPADADF--YLCGPVPFMQAVREGLKALGVPAERI 238
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 117-285 1.85e-12

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: 65.28  E-value: 1.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 117 FEFLVKTVP-GTTAEKLCGLRDGDVLELGAIMGNgFPISRINPPDEaqtVLLFATGTGISPVRSLIEFgfAADQRAD--- 192
Cdd:cd06183    62 FDLLIKIYPgGKMSQYLHSLKPGDTVEIRGPFGK-FEYKPNGKVKH---IGMIAGGTGITPMLQLIRA--ILKDPEDktk 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 193 VRLYYGARNLQTMAYQDRFTNWESTG---LKIIPVLSRADDSWKGERGYVQDAFLKaQNIANH--FSTGAVLCG-QKQMS 266
Cdd:cd06183   136 ISLLYANRTEEDILLREELDELAKKHpdrFKVHYVLSRPPEGWKGGVGFITKEMIK-EHLPPPpsEDTLVLVCGpPPMIE 214

                         170
                  ....*....|....*....
gi 1002237022 267 EEITSALVADGVSPDKILT 285
Cdd:cd06183   215 GAVKGLLKELGYKKDNVFK 233
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
 88-275 1.96e-12

These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but lack the FAD-binding region connecting sub-domain. Ferredoxin-NADP+ reductase (FNR) 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. CYPOR serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases, sulfite reducatase, and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPOR has a C-terminal FNR-like FAD and NAD binding module, an FMN-binding domain, and an additional connecting domain (inserted within the FAD binding region) that orients the FNR and FMN -binding domains. 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: 99804 [Multi-domain]  Cd Length: 286  Bit Score: 65.81  E-value: 1.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  88 GQYLLIRVPGEDEL-----KPAFMAIASP-----PGGAAFEFLVKTVPGTTAEK-----------LCGLRDGDVLELGAI 146
Cdd:cd06208    44 GQSIGIIPPGTDAKngkphKLRLYSIASSrygddGDGKTLSLCVKRLVYTDPETdetkkgvcsnyLCDLKPGDDVQITGP 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 147 MGNGFpisrINPPDEAQTVLLFATGTGISPVRSLIEFGFAADQR-----ADVRLYYGARNLQTMAYQDRFTNWESTG--- 218
Cdd:cd06208   124 VGKTM----LLPEDPNATLIMIATGTGIAPFRSFLRRLFREKHAdykftGLAWLFFGVPNSDSLLYDDELEKYPKQYpdn 199

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002237022 219 LKIIPVLSRADDSWKGERGYVQDAFLK-AQNIANHFSTGAV---LCGQKQMSEEITSALVA 275
Cdd:cd06208   200 FRIDYAFSREQKNADGGKMYVQDRIAEyAEEIWNLLDKDNThvyICGLKGMEPGVDDALTS 260
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 87-281 3.29e-12

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: 64.67  E-value: 3.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  87 PGQYLLIRVPGEDELKPAFMAIASPPGGAaFEFLVKTVPGTTAEKLCGLRD--GDVLELGAIMGnGFPISRinppDEAQT 164
Cdd:cd06210    37 PGQFVEIEIPGTDTRRSYSLANTPNWDGR-LEFLIRLLPGGAFSTYLETRAkvGQRLNLRGPLG-AFGLRE----NGLRP 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 165 VLLFATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQTMAYQDRFTNWEST--GLKIIPVLSRADDSWKGERGYVQDA 242
Cdd:cd06210   111 RWFVAGGTGLAPLLSMLRRMAEWGEPQEARLFFGVNTEAELFYLDELKRLADSlpNLTVRICVWRPGGEWEGYRGTVVDA 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1002237022 243 FLKaqnianHFSTGAV-----LCGQKQMSEEITSALVADGVsPD 281
Cdd:cd06210   191 LRE------DLASSDAkpdiyLCGPPGMVDAAFAAAREAGV-PD 227
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 87-280 6.08e-12

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: 63.81  E-value: 6.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  87 PGQYLLIRVPGeDELKPAFmAIASPPGGAAF-EFLVKTVPGTTA-EKLCG-LRDGDVLELGAIMGNGFpiSRinpPDEAQ 163
Cdd:cd06190    26 PGQYALLALPG-VEGARAY-SMANLANASGEwEFIIKRKPGGAAsNALFDnLEPGDELELDGPYGLAY--LR---PDEDR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 164 TVLLFATGTGISPVRSLIEFGFAADQRAD--VRLYYGARNLQTMAYQDRFTNWESTG--LKIIPVLSRADDS----WKGE 235
Cdd:cd06190    99 DIVCIAGGSGLAPMLSILRGAARSPYLSDrpVDLFYGGRTPSDLCALDELSALVALGarLRVTPAVSDAGSGsaagWDGP 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002237022 236 RGYVQDAflkaqnIANHFSTG-----AVLCGQKQMSEEITSALVADGVSP 280
Cdd:cd06190   179 TGFVHEV------VEATLGDRlaefeFYFAGPPPMVDAVQRMLMIEGVVP 222
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 86-265 9.15e-12

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 63.74  E-value: 9.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  86 TPGQYLLIRVPGEDEL--KPafMAIASpPGGAAFEFLVKTV-PGTtaEKLCGLRDGDVLELGAIMGNGFPISRINppdea 162
Cdd:PRK00054   33 KPGQFVMVWVPGVEPLleRP--ISISD-IDKNEITILYRKVgEGT--KKLSKLKEGDELDIRGPLGNGFDLEEIG----- 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 163 QTVLLFATGTGISPVRSLIEfgFAADQRADVRLYYGARNLQTMAYQDRFtnwESTGlKIIPVlsrADDSWKGERGYVQDA 242
Cdd:PRK00054  103 GKVLLVGGGIGVAPLYELAK--ELKKKGVEVTTVLGARTKDEVIFEEEF---AKVG-DVYVT---TDDGSYGFKGFVTDV 173

                         170       180
                  ....*....|....*....|...
gi 1002237022 243 FlkaQNIANHFSTGAVlCGQKQM 265
Cdd:PRK00054  174 L---DELDSEYDAIYS-CGPEIM 192
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 86-273 6.96e-11

Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. 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: 99798 [Multi-domain]  Cd Length: 289  Bit Score: 61.58  E-value: 6.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  86 TPGQYLLIRVPGEDelKPAFMAIASPPGGAAFEFLVKTVP-GTTAEKLCGLRDGDVLElGAIMGNgfpiSRINPPDEAQT 164
Cdd:cd06201    85 EAGDLLGILPPGSD--VPRFYSLASSSSDGFLEICVRKHPgGLCSGYLHGLKPGDTIK-AFIRPN----PSFRPAKGAAP 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 165 VLLFATGTGISPvrsLIEFGFAADQRADVRLYYGARNLQTMA-YQDRFTNWESTGlkiiPVLS-RADDSWKGERGYVQDA 242
Cdd:cd06201   158 VILIGAGTGIAP---LAGFIRANAARRPMHLYWGGRDPASDFlYEDELDQYLADG----RLTQlHTAFSRTPDGAYVQDR 230

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1002237022 243 FLK-AQNIANHFSTGAVL--CGQKQMSEEITSAL 273
Cdd:cd06201   231 LRAdAERLRRLIEDGAQImvCGSRAMAQGVAAVL 264
fre PRK08051
FMN reductase; Validated
 87-242 7.21e-11

FMN reductase; Validated


Pssm-ID: 236142 [Multi-domain]  Cd Length: 232  Bit Score: 60.64  E-value: 7.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  87 PGQYLLIrVPGEDELKPaFmAIASPPggaafeflvktvpgttaeklcglRDGDVLEL--GAIMGNGFP---ISRIN---- 157
Cdd:PRK08051   32 AGQYLMV-VMGEKDKRP-F-SIASTP-----------------------REKGFIELhiGASELNLYAmavMERILkdge 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 158 -----PPDEAQ-------TVLLFATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQTMAYQDRFTNWES--TGLKIIP 223
Cdd:PRK08051   86 ievdiPHGDAWlreeserPLLLIAGGTGFSYARSILLTALAQGPNRPITLYWGGREEDHLYDLDELEALALkhPNLHFVP 165

                         170
                  ....*....|....*....
gi 1002237022 224 VLSRADDSWKGERGYVQDA 242
Cdd:PRK08051  166 VVEQPEEGWQGKTGTVLTA 184
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 86-285 7.31e-11

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 varies in orientation with respect to the NAD(P) binding domain. The N-terminal region 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: 99793 [Multi-domain]  Cd Length: 218  Bit Score: 60.72  E-value: 7.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  86 TPGQ--YLLIRVPG-EDELKPAFMAiaSPPGGAAFEFLVKTVP---GTTaEKLCGLRDGDVLELGAIMGNgfpISRINPP 159
Cdd:cd06196    29 TPGQatEVAIDKPGwRDEKRPFTFT--SLPEDDVLEFVIKSYPdhdGVT-EQLGRLQPGDTLLIEDPWGA---IEYKGPG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 160 deaqtvLLFATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQTMAYQDRFTNWEstGLKIIPVLSRADDSwKGERGYV 239
Cdd:cd06196   103 ------VFIAGGAGITPFIAILRDLAAKGKLEGNTLIFANKTEKDIILKDELEKML--GLKFINVVTDEKDP-GYAHGRI 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1002237022 240 QDAFLKaQNIANhFSTGAVLCGQKQMSEEITSALVADGVSPDKILT 285
Cdd:cd06196   174 DKAFLK-QHVTD-FNQHFYVCGPPPMEEAINGALKELGVPEDSIVF 217
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 87-283 1.11e-10

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 portion of the FAD/NAD binding domain contains most of the NADP(H) binding residues and the N-terminal sub-domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. In this ferredoxin like sub-group, the FAD/NAD sub-domains is typically fused to a C-terminal iron-sulfur binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins which act as electron carriers in photosynthesis and ferredoxins which participate in redox chains from bacteria to mammals. Ferredoxin 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: 99811 [Multi-domain]  Cd Length: 231  Bit Score: 60.30  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  87 PGQYLLIRVPGEDELKPAFMAIASPPGGA-AFEFLVKTVPGttaeklcG---------LRDGDVLELGAIMGnGFpiSRI 156
Cdd:cd06215    30 PGQFLTLELEIDGETVYRAYTLSSSPSRPdSLSITVKRVPG-------GlvsnwlhdnLKVGDELWASGPAG-EF--TLI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 157 NPPdeAQTVLLFATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQTMAYQDRftnWES-----TGLKIIPVLSR-ADD 230
Cdd:cd06215   100 DHP--ADKLLLLSAGSGITPMMSMARWLLDTRPDADIVFIHSARSPADIIFADE---LEElarrhPNFRLHLILEQpAPG 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002237022 231 SWKGERGYVQDAFLkaQNIANHFSTGAV-LCGQKQMSEEITSALVADGVSPDKI 283
Cdd:cd06215   175 AWGGYRGRLNAELL--ALLVPDLKERTVfVCGPAGFMKAVKSLLAELGFPMSRF 226
CYPOR_like cd06182
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 60-284 5.16e-09

NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPOR has a C-terminal ferredoxin reducatase (FNR)- like FAD and NAD binding module, an FMN-binding domain, and an additional conecting domain (inserted within the FAD binding region) that orients the FNR and FMN binding domains. 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 and 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: 99779 [Multi-domain]  Cd Length: 267  Bit Score: 55.81  E-value: 5.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  60 PATADGSLVHFSVDLSDATDLaasYTTPGQYLLIRVPGEdeLKPAFMAIASPPGGAA--FEFLVKTVPGTTAEK------ 131
Cdd:cd06182    10 PPDSPRSTRHLEFDLSGNSVL---KYQPGDHLGVIPPNP--LQPRYYSIASSPDVDPgeVHLCVRVVSYEAPAGrirkgv 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 132 ----LCGLRDGDVLELGAIMGNGFPIsrinPPDEAQTVLLFATGTGISPVRSLIEfGFAADQRADVR-----LYYGARN- 201
Cdd:cd06182    85 csnfLAGLQLGAKVTVFIRPAPSFRL----PKDPTTPIIMVGPGTGIAPFRGFLQ-ERAALRANGKArgpawLFFGCRNf 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 202 LQTMAYQDRFTNWESTGlkiipVLSRADDSW----KGERGYVQDAFLK-AQNIANHFSTGAVL--CGQ-KQMS---EEIT 270
Cdd:cd06182   160 ASDYLYREELQEALKDG-----ALTRLDVAFsreqAEPKVYVQDKLKEhAEELRRLLNEGAHIyvCGDaKSMAkdvEDAL 234

                         250
                  ....*....|....
gi 1002237022 271 SALVADGVSPDKIL 284
Cdd:cd06182   235 VKIIAKAGGVDESD 248
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 86-283 1.63e-08

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: 53.80  E-value: 1.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  86 TPGQYLLIRVPGEDELKPAFMAIASPPGGAA-FEFLVKTV------------PGTTAeklcglrdgdvlelgAIMGngfP 152
Cdd:cd06198    24 RAGQFAFLRFDASGWEEPHPFTISSAPDPDGrLRFTIKALgdytrrlaerlkPGTRV---------------TVEG---P 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 153 ISRINPPDEAQTVLLFATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQTMAYQDRFTNWESTGLKIIPVLSRADDSW 232
Cdd:cd06198    86 YGRFTFDDRRARQIWIAGGIGITPFLALLEALAARGDARPVTLFYCVRDPEDAVFLDELRALAAAAGVVLHVIDSPSDGR 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1002237022 233 KGERGYVQDAFLKAQNiANHFstgavLCGQKQMSEEITSALVADGVSPDKI 283
Cdd:cd06198   166 LTLEQLVRALVPDLAD-ADVW-----FCGPPGMADALEKGLRALGVPARRF 210
bifunctional_CYPOR cd06206
These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase ...
 158-274 2.94e-08

These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase (CYPOR). NADPH cytochrome p450 reductase serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. 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: 99802 [Multi-domain]  Cd Length: 384  Bit Score: 54.19  E-value: 2.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 158 PPDEAQTVLLFATGTGISPVRsliefGFAADQRADVR---------LYYGARN-----LqtmaYQDRFTNWESTG-LKII 222
Cdd:cd06206   226 PSDPSTPLIMIAAGTGLAPFR-----GFLQERAALLAqgrklapalLFFGCRHpdhddL----YRDELEEWEAAGvVSVR 296

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002237022 223 PVLSRADDSWkgeRGYVQDAFLK-AQNIANHFSTGAVL--CGQKQMSEEITSALV 274
Cdd:cd06206   297 RAYSRPPGGG---CRYVQDRLWAeREEVWELWEQGARVyvCGDGRMAPGVREVLK 348
SiR_like1 cd06200
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 108-275 6.29e-08

Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. 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: 99797  Cd Length: 245  Bit Score: 52.28  E-value: 6.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 108 IASPPGGAAFEFLVKTVPgtTAEKLCGL---------RDGDVLELGAIMGNGFPisrinPPDEAQTVLLFATGTGISPVR 178
Cdd:cd06200    53 IASLPADGALELLVRQVR--HADGGLGLgsgwltrhaPIGASVALRLRENPGFH-----LPDDGRPLILIGNGTGLAGLR 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 179 SLIEFGFAADQRADvRLYYGARNLQ-TMAYQDRFTNWESTGlkiipVLSRADDSW---KGERGYVQDAFL-KAQNIANHF 253
Cdd:cd06200   126 SHLRARARAGRHRN-WLLFGERQAAhDFFCREELEAWQAAG-----HLARLDLAFsrdQAQKRYVQDRLRaAADELRAWV 199

                         170       180
                  ....*....|....*....|....*
gi 1002237022 254 STGAVL--CGQKQ-MSEEITSALVA 275
Cdd:cd06200   200 AEGAAIyvCGSLQgMAPGVDAVLDE 224
CyPoR_like cd06207
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 101-274 6.35e-08

NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. 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: 99803 [Multi-domain]  Cd Length: 382  Bit Score: 53.05  E-value: 6.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 101 LKPAFMAIASPP--GGAAFEFLVKTVPGTTAEK-----LC-----GLRDGDVLElGAIMGNGFPIsrinPPDEAQTVLLF 168
Cdd:cd06207   162 IKPRYYSISSSPlkNPNEVHLLVSLVSWKTPSGrsrygLCssylaGLKVGQRVT-VFIKKSSFKL----PKDPKKPIIMV 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 169 ATGTGISPVRSLIEF-GFAADQ---RADVRLYYGARNLQT-MAYQDRFTNWES--TGLKIIPVLSRADDswkgERGYVQD 241
Cdd:cd06207   237 GPGTGLAPFRAFLQErAALLAQgpeIGPVLLYFGCRHEDKdYLYKEELEEYEKsgVLTTLGTAFSRDQP----KKVYVQD 312

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1002237022 242 AFLK-AQNIANHFSTGAV---LCGQKQ-MSEEITSALV 274
Cdd:cd06207   313 LIREnSDLVYQLLEEGAGviyVCGSTWkMPPDVQEAFE 350
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 87-209 1.95e-07

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 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: 99812 [Multi-domain]  Cd Length: 243  Bit Score: 50.69  E-value: 1.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  87 PGQYLLIRVPGEDELKPAFMAIASPPGGAA--FEFLVKTVP-GTTAEKLCG-LRDGDVLELGAIMGNgFPIsrinPPDEA 162
Cdd:cd06216    48 AGQHVRLGVEIDGVRHWRSYSLSSSPTQEDgtITLTVKAQPdGLVSNWLVNhLAPGDVVELSQPQGD-FVL----PDPLP 122

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1002237022 163 QTVLLFATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQTMAYQD 209
Cdd:cd06216   123 PRLLLIAAGSGITPVMSMLRTLLARGPTADVVLLYYARTREDVIFAD 169
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 87-203 4.22e-07

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: 49.57  E-value: 4.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  87 PGQYLLIRVPGeDELKPafMAIASPPGGAAF-EFLVKTVP-GTTAEKLCGL-RDGDVLELGAIMGNGFpiSRINPPDeaQ 163
Cdd:cd06194    26 PGQYVNLRRAG-GLARS--YSPTSLPDGDNElEFHIRRKPnGAFSGWLGEEaRPGHALRLQGPFGQAF--YRPEYGE--G 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1002237022 164 TVLLFATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQ 203
Cdd:cd06194    99 PLLLVGAGTGLAPLWGIARAALRQGHQGEIRLVHGARDPD 138
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 87-273 5.03e-07

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: 49.63  E-value: 5.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  87 PGQYLLIRVPGEDEL--KPAFMAIASPPGGAaFEFLVKTVPGTTAeKLCGLRDGDVLELGAIMGNGFPIsrinpPDEAQT 164
Cdd:cd06192    27 PGQFVFLRNFESPGLerIPLSLAGVDPEEGT-ISLLVEIRGPKTK-LIAELKPGEKLDVMGPLGNGFEG-----PKKGGT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 165 VLLFATGTGISPVRSLIEfgFAADQRADVRLYYGARNLQTMAYQDRFtNWESTGLKIIpvlsrADDSWKGERGYVQDAFL 244
Cdd:cd06192   100 VLLVAGGIGLAPLLPIAK--KLAANGNKVTVLAGAKKAKEEFLDEYF-ELPADVEIWT-----TDDGELGLEGKVTDSDK 171

                         170       180
                  ....*....|....*....|....*....
gi 1002237022 245 kaqNIANHFSTGAVLCGQKQMSEEITSAL 273
Cdd:cd06192   172 ---PIPLEDVDRIIVAGSDIMMKAVVEAL 197
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 135-213 6.61e-07

Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron transfer from NADH to FMN to an iron sulfur cluster. PDR has an an N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding domain and a C-terminal iron-sulfur [2Fe-2S] cluster domain. Although structurally homologous to FNR, PDR binds FMN rather than FAD in it's FNR-like domain. Electron transfer between pyrimidines and iron-sulfur clusters (Rieske center [2Fe-2S]) or heme groups is mediated by flavins in respiration, photosynthesis, and oxygenase systems. Type I dioxygenase systems, including the hydroxylate phthalate system, have 2 components, a monomeric reductase consisting of a flavin and a 2Fe-2S center and a multimeric oxygenase. In contrast to other Rieske dioxygenases the ferredoxin like domain is C-, not N-terminal.


Pssm-ID: 99782 [Multi-domain]  Cd Length: 211  Bit Score: 49.02  E-value: 6.61e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002237022 135 LRDGDVLELGAImGNGFPISrinppDEAQTVLLFATGTGISPVRSLIEFgfAADQRADVRLYYGARNLQTMAYQDRFTN 213
Cdd:cd06185    77 LRVGDELEVSAP-RNLFPLD-----EAARRHLLIAGGIGITPILSMARA--LAARGADFELHYAGRSREDAAFLDELAA 147
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
 122-278 2.61e-06

ferredoxin--NADP(+) reductase; Provisional


Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 48.07  E-value: 2.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 122 KTVPGTTAEKLCGLRDGDVLELGAIMGNgfpiSRINPPDEAQTVLLFATGTGISPVRSLIEFGFaADQRADVR------L 195
Cdd:PLN03115  179 EIVKGVCSNFLCDLKPGAEVKITGPVGK----EMLMPKDPNATIIMLATGTGIAPFRSFLWKMF-FEKHDDYKfnglawL 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 196 YYGARNLQTMAYQDRFTNWESTG---LKIIPVLSRADDSWKGERGYVQD----------AFLKAQNianhfsTGAVLCGQ 262
Cdd:PLN03115  254 FLGVPTSSSLLYKEEFEKMKEKApenFRLDFAVSREQTNAKGEKMYIQTrmaeyaeelwELLKKDN------TYVYMCGL 327

                         170       180
                  ....*....|....*....|
gi 1002237022 263 KQMSEEITSALVA----DGV 278
Cdd:PLN03115  328 KGMEKGIDDIMVSlaakDGI 347
PRK10926 PRK10926
ferredoxin-NADP reductase; Provisional
 86-265 2.04e-05

ferredoxin-NADP reductase; Provisional


Pssm-ID: 182844  Cd Length: 248  Bit Score: 45.08  E-value: 2.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  86 TPGQY--LLIRVPGEdELKPAFmAIASPPGGAAFEFLVKTVP-GTTAEKLCGLRDGDVLELGAIMGNGFPISRInpPDeA 162
Cdd:PRK10926   32 TAGQFtkLGLEIDGE-RVQRAY-SYVNAPDNPDLEFYLVTVPeGKLSPRLAALKPGDEVQVVSEAAGFFVLDEV--PD-C 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 163 QTVLLFATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQTMAY-------QDRFTNwestGLKIIPVLSR--ADDSWK 233
Cdd:PRK10926  107 ETLWMLATGTAIGPYLSILQEGKDLERFKNLVLVHAARYAADLSYlplmqelEQRYEG----KLRIQTVVSRetAPGSLT 182

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1002237022 234 G------ERGYVQDAF-LKAQNIANHfstgAVLCGQKQM 265
Cdd:PRK10926  183 GrvpaliESGELEAAVgLPMDAETSH----VMLCGNPQM 217
PLN03116 PLN03116
ferredoxin--NADP+ reductase; Provisional
 123-273 2.24e-05

ferredoxin--NADP+ reductase; Provisional


Pssm-ID: 215586 [Multi-domain]  Cd Length: 307  Bit Score: 45.09  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 123 TVPGTTAEKLCGLRDGDVLEL----GAIMgngfpisRINPPDEAQTVLLFATGTGISPVRSLIEFGFAADQRA-----DV 193
Cdd:PLN03116  120 AKKGVCSNFLCDAKPGDKVQItgpsGKVM-------LLPEEDPNATHIMVATGTGIAPFRGFLRRMFMEDVPAfkfggLA 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 194 RLYYGARNLQTMAYQDRFTNWestgLKIIP-------VLSRADDSWKGERGYVQDAFLK-AQNIANHFSTGAVL--CGQK 263
Cdd:PLN03116  193 WLFLGVANSDSLLYDDEFERY----LKDYPdnfrydyALSREQKNKKGGKMYVQDKIEEySDEIFKLLDNGAHIyfCGLK 268

                         170
                  ....*....|
gi 1002237022 264 QMSEEITSAL 273
Cdd:PLN03116  269 GMMPGIQDTL 278
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 87-272 5.98e-04

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: 39.98  E-value: 5.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022  87 PGQYLLIRVPGedeLKPAFMA----IASPPGGAA--FEFLVKTVPGTTAEKLCGLRDGDvlelgaimGNGFPI------- 153
Cdd:cd06186    27 PGQHVYLNFPS---LLSFWQShpftIASSPEDEQdtLSLIIRAKKGFTTRLLRKALKSP--------GGGVSLkvlvegp 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 154 --SRINPPDEAQTVLLFATGTGISPV----RSLIEFGFAADQRADVRLYYGARNlqtmayqdrftnwestglkiipvlsR 227
Cdd:cd06186    96 ygSSSEDLLSYDNVLLVAGGSGITFVlpilRDLLRRSSKTSRTRRVKLVWVVRD-------------------------R 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002237022 228 ADDSWkgergyVQDAFLKAQNIANHFS-----TGAVLCGQKQMSEEITSA 272
Cdd:cd06186   151 EDLEW------FLDELRAAQELEVDGEieiyvTRVVVCGPPGLVDDVRNA 194
PRK05713 PRK05713
iron-sulfur-binding ferredoxin reductase;
107-203 3.18e-03

iron-sulfur-binding ferredoxin reductase;


Pssm-ID: 235575 [Multi-domain]  Cd Length: 312  Bit Score: 38.55  E-value: 3.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 107 AIASPPGGAAF-EFLVK-TVPGTTAEKLCGLRDGDVLELGAIMGNGFpisRINPPDEAQTVLLFATGTGISPVRSLIEFG 184
Cdd:PRK05713  138 SLASLPGEDPFlEFHIDcSRPGAFCDAARQLQVGDLLRLGELRGGAL---HYDPDWQERPLWLLAAGTGLAPLWGILREA 214

                          90
                  ....*....|....*....
gi 1002237022 185 FAADQRADVRLYYGARNLQ 203
Cdd:PRK05713  215 LRQGHQGPIRLLHLARDSA 233
PRK06214 PRK06214
sulfite reductase subunit alpha;
158-274 4.69e-03

sulfite reductase subunit alpha;


Pssm-ID: 235745 [Multi-domain]  Cd Length: 530  Bit Score: 38.13  E-value: 4.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 158 PPDEAQTVLLFATGTGISPVRSLIEfgfaadQRADVR------LYYGArnlQTMAYqDRFTNWESTGLKIIPVLSRADDS 231
Cdd:PRK06214  379 PADPNTPIIMVGPGTGIAPFRAFLH------ERAATKapgrnwLFFGH---QRSAT-DFFYEDELNGLKAAGVLTRLSLA 448

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002237022 232 WK---GERGYVQDAFLK-AQNIANHFSTGAVL--CGQ-KQMSEEITSALV 274
Cdd:PRK06214  449 WSrdgEEKTYVQDRMREnGAELWKWLEEGAHFyvCGDaKRMAKDVERALV 498
SiR cd06199
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 158-241 5.35e-03

Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain.


Pssm-ID: 99796 [Multi-domain]  Cd Length: 360  Bit Score: 37.98  E-value: 5.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237022 158 PPDEAQTVLLFATGTGISPVRSLIEFGFAADQRADVRLYYGARNLQT-MAYQDRFTNWESTGlkiipVLSRADDSW---K 233
Cdd:cd06199   209 PEDPDAPIIMVGPGTGIAPFRAFLQEREATGAKGKNWLFFGERHFATdFLYQDELQQWLKDG-----VLTRLDTAFsrdQ 283


                  ....*...
gi 1002237022 234 GERGYVQD 241
Cdd:cd06199   284 AEKVYVQD 291
 
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