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Conserved domains on  [gi|848893825|ref|XP_012846955|]
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PREDICTED: fruit protein pKIWI502-like [Erythranthe guttata]

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

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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 ...
 40-269 7.55e-35

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: 124.87  E-value: 7.55e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  40 IKVTPAAESHFHITIDvadsPDLASSYtKAGQYLQLRLRD---PYARPtfLAIASPPsiaASKGVFEFLVK-SIAGSTAE 115
Cdd:cd00322    1 VATEDVTDDVRLFRLQ----LPNGFSF-KPGQYVDLHLPGdgrGLRRA--YSIASSP---DEEGELELTVKiVPGGPFSA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 116 LLCGLQRGDVVELSTAIGNGFdidqiSPPENYQTVLIFATGSGISPIRSLIEAGFGADKRADVRLYYGARNLSRMAYRER 195
Cdd:cd00322   71 WLHDLKPGDEVEVSGPGGDFF-----LPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGEITLLYGARTPADLLFLDE 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 848893825 196 FRDWESSGINI--VPVLSKPEDSWTGERGFVQAAFARAKRILNPQSTGAVLCGRRQMTEEVTSILVSDGVASEKIL 269
Cdd:cd00322  146 LEELAKEGPNFrlVLALSRESEAKLGPGGRIDREAEILALLPDDSGALVYICGPPAMAKAVREALVSLGVPEERIH 221
 
Name Accession Description Interval E-value
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 40-269 7.55e-35

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: 124.87  E-value: 7.55e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  40 IKVTPAAESHFHITIDvadsPDLASSYtKAGQYLQLRLRD---PYARPtfLAIASPPsiaASKGVFEFLVK-SIAGSTAE 115
Cdd:cd00322    1 VATEDVTDDVRLFRLQ----LPNGFSF-KPGQYVDLHLPGdgrGLRRA--YSIASSP---DEEGELELTVKiVPGGPFSA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 116 LLCGLQRGDVVELSTAIGNGFdidqiSPPENYQTVLIFATGSGISPIRSLIEAGFGADKRADVRLYYGARNLSRMAYRER 195
Cdd:cd00322   71 WLHDLKPGDEVEVSGPGGDFF-----LPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGEITLLYGARTPADLLFLDE 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 848893825 196 FRDWESSGINI--VPVLSKPEDSWTGERGFVQAAFARAKRILNPQSTGAVLCGRRQMTEEVTSILVSDGVASEKIL 269
Cdd:cd00322  146 LEELAKEGPNFrlVLALSRESEAKLGPGGRIDREAEILALLPDDSGALVYICGPPAMAKAVREALVSLGVPEERIH 221
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 38-268 8.16e-35

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 125.36  E-value: 8.16e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  38 RLIKVTPAAESHFHITIDVadsPDLASSYtKAGQYLQLRLRDPY-ARPtfLAIASPPsiaASKGVFEFLVKsIAGSTAEL 116
Cdd:COG0543    1 KVVSVERLAPDVYLLRLEA---PLIALKF-KPGQFVMLRVPGDGlRRP--FSIASAP---REDGTIELHIR-VVGKGTRA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 117 LCGLQRGDVVELSTAIGNGFDIdqispPENYQTVLIFATGSGISPIRSLIEAGFGADKRadVRLYYGARNLSRMAYRERF 196
Cdd:COG0543   71 LAELKPGDELDVRGPLGNGFPL-----EDSGRPVLLVAGGTGLAPLRSLAEALLARGRR--VTLYLGARTPEDLYLLDEL 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 848893825 197 RDWesSGINIVpVLSkpEDSWTGERGFVQAAFaraKRILNPQSTGAV-LCGRRQMTEEVTSILVSDGVASEKI 268
Cdd:COG0543  144 EAL--ADFRVV-VTT--DDGWYGRKGFVTDAL---KELLAEDSGDDVyACGPPPMMKAVAELLLERGVPPERI 208
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 154-250 3.17e-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: 72.68  E-value: 3.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  154 ATGSGISPIRSLIEAGF-GADKRADVRLYYGARNLSRMAYRERFRDWE---SSGINIVPVLSKPEDSWTGERGFVQAAFA 229
Cdd:pfam00175   3 AGGTGIAPVRSMLRAILeDPKDPTQVVLVFGNRNEDDILYREELDELAekhPGRLTVVYVVSRPEAGWTGGKGRVQDALL 82

                          90       100
                  ....*....|....*....|.
gi 848893825  230 RAKRILNPQSTGAVLCGRRQM 250
Cdd:pfam00175  83 EDHLSLPDEETHVYVCGPPGM 103
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 36-268 5.81e-13

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 67.14  E-value: 5.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  36 PTRLIKVTPAAESHFHITIDVADsPDLASSYT-KAGQYLQLRLRDPYARPtfLAIASPPSiaaSKGVFEFLVKSiAGSTA 114
Cdd:PRK08345   7 DAKILEVYDLTEREKLFLLRFED-PELAESFTfKPGQFVQVTIPGVGEVP--ISICSSPT---RKGFFELCIRR-AGRVT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 115 ELLCGLQRGDVVELSTAIGNGFDIDQISPpenyQTVLIFATGSGISPIRS-LIEAGFGADKRADVRLYYGARNLSRMAYR 193
Cdd:PRK08345  80 TVIHRLKEGDIVGVRGPYGNGFPVDEMEG----MDLLLIAGGLGMAPLRSvLLYAMDNRWKYGNITLIYGAKYYEDLLFY 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 194 -ERFRDW-ESSGINIVPVLSKpEDSWTG----ERGFVQ------AAFARAKRILNPQSTGAVLCGRRQMTEEVTSILVSD 261
Cdd:PRK08345 156 dELIKDLaEAENVKIIQSVTR-DPEWPGchglPQGFIErvckgvVTDLFREANTDPKNTYAAICGPPVMYKFVFKELINR 234


                 ....*..
gi 848893825 262 GVASEKI 268
Cdd:PRK08345 235 GYRPERI 241
nqrF TIGR01941
NADH:ubiquinone oxidoreductase, Na(+)-translocating, F subunit; This model represents the NqrF ...
 50-269 3.13e-11

NADH:ubiquinone oxidoreductase, Na(+)-translocating, F subunit; This model represents the NqrF subunit of the six-protein, Na(+)-pumping NADH-quinone reductase of a number of marine and pathogenic Gram-negative bacteria. This oxidoreductase complex functions primarily as a sodium ion pump. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130996 [Multi-domain]  Cd Length: 405  Bit Score: 62.89  E-value: 3.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825   50 FHITIDVADSPDLASS---YTKAGQYLQLRLRdpYARPTFLAIASPPSIAASKgVFEflvksiagstaellcgLQRGDVV 126
Cdd:TIGR01941 195 FDLVSKVDEETVRAYSmanYPAEKGIIKLNVR--IATPPFINSDIPPGIMSSY-IFS----------------LKPGDKV 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  127 ELSTAIGNGFDIDQISPpenyqtvLIF-ATGSGISPIRSLIEAGFGADK-RADVRLYYGARNLSRMAYRERFRDWESSGI 204
Cdd:TIGR01941 256 TISGPFGEFFAKDTDAE-------MVFiGGGAGMAPMRSHIFDQLKRLKsKRKISFWYGARSLREMFYQEDFDQLEAENP 328

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 848893825  205 NIV--PVLS--KPEDSWTGERGFVQAAF--ARAKRILNPQSTGAVLCGRRQMTEEVTSILVSDGVASEKIL 269
Cdd:TIGR01941 329 NFVwhVALSdpQPEDNWTGYTGFIHNVLyeNYLKDHDAPEDCEFYMCGPPMMNAAVIKMLEDLGVERENIL 399
 
Name Accession Description Interval E-value
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 40-269 7.55e-35

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: 124.87  E-value: 7.55e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  40 IKVTPAAESHFHITIDvadsPDLASSYtKAGQYLQLRLRD---PYARPtfLAIASPPsiaASKGVFEFLVK-SIAGSTAE 115
Cdd:cd00322    1 VATEDVTDDVRLFRLQ----LPNGFSF-KPGQYVDLHLPGdgrGLRRA--YSIASSP---DEEGELELTVKiVPGGPFSA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 116 LLCGLQRGDVVELSTAIGNGFdidqiSPPENYQTVLIFATGSGISPIRSLIEAGFGADKRADVRLYYGARNLSRMAYRER 195
Cdd:cd00322   71 WLHDLKPGDEVEVSGPGGDFF-----LPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGEITLLYGARTPADLLFLDE 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 848893825 196 FRDWESSGINI--VPVLSKPEDSWTGERGFVQAAFARAKRILNPQSTGAVLCGRRQMTEEVTSILVSDGVASEKIL 269
Cdd:cd00322  146 LEELAKEGPNFrlVLALSRESEAKLGPGGRIDREAEILALLPDDSGALVYICGPPAMAKAVREALVSLGVPEERIH 221
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 38-268 8.16e-35

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 125.36  E-value: 8.16e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  38 RLIKVTPAAESHFHITIDVadsPDLASSYtKAGQYLQLRLRDPY-ARPtfLAIASPPsiaASKGVFEFLVKsIAGSTAEL 116
Cdd:COG0543    1 KVVSVERLAPDVYLLRLEA---PLIALKF-KPGQFVMLRVPGDGlRRP--FSIASAP---REDGTIELHIR-VVGKGTRA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 117 LCGLQRGDVVELSTAIGNGFDIdqispPENYQTVLIFATGSGISPIRSLIEAGFGADKRadVRLYYGARNLSRMAYRERF 196
Cdd:COG0543   71 LAELKPGDELDVRGPLGNGFPL-----EDSGRPVLLVAGGTGLAPLRSLAEALLARGRR--VTLYLGARTPEDLYLLDEL 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 848893825 197 RDWesSGINIVpVLSkpEDSWTGERGFVQAAFaraKRILNPQSTGAV-LCGRRQMTEEVTSILVSDGVASEKI 268
Cdd:COG0543  144 EAL--ADFRVV-VTT--DDGWYGRKGFVTDAL---KELLAEDSGDDVyACGPPPMMKAVAELLLERGVPPERI 208
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 68-268 6.58e-29

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: 109.72  E-value: 6.58e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  68 KAGQYLQLRLrDPYARPTFLAIASPPSiaaSKGVFEFLVKSIAGSTAELLC--GLQRGDVVELSTAIGNGFDIDqisppE 145
Cdd:cd06211   37 QAGQYVNLQA-PGYEGTRAFSIASSPS---DAGEIELHIRLVPGGIATTYVhkQLKEGDELEISGPYGDFFVRD-----S 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 146 NYQTVLIFATGSGISPIRSLIEAGFGADKRADVRLYYGARNLSRMAYRERFRDWESSGINI--VPVLS--KPEDSWTGER 221
Cdd:cd06211  108 DQRPIIFIAGGSGLSSPRSMILDLLERGDTRKITLFFGARTRAELYYLDEFEALEKDHPNFkyVPALSrePPESNWKGFT 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 848893825 222 GFVQAAfarAKRILNPQSTG--AVLCGRRQMTEEVTSILVSDGVASEKI 268
Cdd:cd06211  188 GFVHDA---AKKHFKNDFRGhkAYLCGPPPMIDACIKTLMQGRLFERDI 233
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
34-268 1.44e-27

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 106.03  E-value: 1.44e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  34 WTPTRLIKVTPAAESHFHITIDVADSPDLASSytKAGQYLQLRLR---DPYARPtfLAIASPPSiaasKGVFEFLVKSIA 110
Cdd:COG1018    3 FRPLRVVEVRRETPDVVSFTLEPPDGAPLPRF--RPGQFVTLRLPidgKPLRRA--YSLSSAPG----DGRLEITVKRVP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 111 GS--TAELLCGLQRGDVVELSTAIGNgFDIDqispPENYQTVLIFATGSGISPIRSLIEAGFGADKRADVRLYYGARNLS 188
Cdd:COG1018   75 GGggSNWLHDHLKVGDTLEVSGPRGD-FVLD----PEPARPLLLIAGGIGITPFLSMLRTLLARGPFRPVTLVYGARSPA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 189 RMAYRERFRDW--ESSGINIVPVLSKPEDswtGERGFVQAAFARAkrILNPQSTGAV-LCGRRQMTEEVTSILVSDGVAS 265
Cdd:COG1018  150 DLAFRDELEALaaRHPRLRLHPVLSREPA---GLQGRLDAELLAA--LLPDPADAHVyLCGPPPMMEAVRAALAELGVPE 224


                 ...
gi 848893825 266 EKI 268
Cdd:COG1018  225 ERI 227
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 68-268 6.94e-26

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: 101.47  E-value: 6.94e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  68 KAGQYLQLRLRDPYARPtFlAIASPPSiaaSKGVFEFLVKSIAGS--TAELLCGLQRGDVVELSTAIGNGFdidqISPPE 145
Cdd:cd06189   27 LAGQYLDLLLDDGDKRP-F-SIASAPH---EDGEIELHIRAVPGGsfSDYVFEELKENGLVRIEGPLGDFF----LREDS 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 146 NYQTVLIfATGSGISPIRSLIEAGFGADKRADVRLYYGARNLSRMAYRERFRDWES--SGINIVPVLSKPEDSWTGERGF 223
Cdd:cd06189   98 DRPLILI-AGGTGFAPIKSILEHLLAQGSKRPIHLYWGARTEEDLYLDELLEAWAEahPNFTYVPVLSEPEEGWQGRTGL 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 848893825 224 VQAAFarAKRILNPQSTGAVLCGRRQMTEEVTSILVSDGVASEKI 268
Cdd:cd06189  177 VHEAV--LEDFPDLSDFDVYACGSPEMVYAARDDFVEKGLPEENF 219
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 39-268 8.19e-25

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: 99.22  E-value: 8.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  39 LIKVTPAAESHFHITIDVADsPDLASSYTKAGQYLQLRLRDPYARPtfLAIASPPsiaASKGVFEFLVKsIAGSTAELLC 118
Cdd:cd06221    1 IVEVVDETEDIKTFTLRLED-DDEELFTFKPGQFVMLSLPGVGEAP--ISISSDP---TRRGPLELTIR-RVGRVTEALH 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 119 GLQRGDVVELSTAIGNGFdidqisPPENYQT--VLIFATGSGISPIRSLIEAgFGA--DKRADVRLYYGARNLSRMAYRE 194
Cdd:cd06221   74 ELKPGDTVGLRGPFGNGF------PVEEMKGkdLLLVAGGLGLAPLRSLINY-ILDnrEDYGKVTLLYGARTPEDLLFKE 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 848893825 195 RFRDWE-SSGINIVPVLSKPEDSWTGERGFVQAAFARAKriLNPQSTGAVLCGRRQMTEEVTSILVSDGVASEKI 268
Cdd:cd06221  147 ELKEWAkRSDVEVILTVDRAEEGWTGNVGLVTDLLPELT--LDPDNTVAIVCGPPIMMRFVAKELLKLGVPEEQI 219
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 68-269 2.54e-24

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: 100.32  E-value: 2.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  68 KAGQYLQLR--------------------LRDPYARPTFLA--IASPPsiaASKGVFEFLVKsIA----------GSTae 115
Cdd:COG2871  162 KAGQYIQIEvppyevdfkdfdipeeekfgLFDKNDEEVTRAysMANYP---AEKGIIELNIR-IAtppmdvppgiGSS-- 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 116 LLCGLQRGDVVELSTAIGNGFDIDqiSPPEnyqtvLIF-ATGSGISPIRSLIEAGF--GADKRaDVRLYYGARNLSRMAY 192
Cdd:COG2871  236 YIFSLKPGDKVTISGPYGEFFLRD--SDRE-----MVFiGGGAGMAPLRSHIFDLLerGKTDR-KITFWYGARSLRELFY 307

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 193 RERFRDWESSGIN--IVPVLS--KPEDSWTGERGFV-QAAFAR-AKRILNPQSTGAVLCGRRQMTEEVTSILVSDGVASE 266
Cdd:COG2871  308 LEEFRELEKEHPNfkFHPALSepLPEDNWDGETGFIhEVLYENyLKDHPAPEDCEAYLCGPPPMIDAVIKMLDDLGVEEE 387


                 ...
gi 848893825 267 KIL 269
Cdd:COG2871  388 NIY 390
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 68-268 8.57e-22

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: 90.34  E-value: 8.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  68 KAGQYLQLRLrdPYARPT--FLAIASPPSiaaSKGVFEFLVKSIAG--STAELLCGLQRGDVVELSTAIGnGFDIDqisp 143
Cdd:cd06187   25 WAGQYVNVTV--PGRPRTwrAYSPANPPN---EDGEIEFHVRAVPGgrVSNALHDELKVGDRVRLSGPYG-TFYLR---- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 144 PENYQTVLIFATGSGISPIRSLIEAGFGADKRADVRLYYGARNLSRMAYRERFRDWESSGIN--IVPVLSKPEDSWTGER 221
Cdd:cd06187   95 RDHDRPVLCIAGGTGLAPLRAIVEDALRRGEPRPVHLFFGARTERDLYDLEGLLALAARHPWlrVVPVVSHEEGAWTGRR 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 848893825 222 GFVQAAFARAkrILNPQSTGAVLCGRRQMTEEVTSILVSDGVASEKI 268
Cdd:cd06187  175 GLVTDVVGRD--GPDWADHDIYICGPPAMVDATVDALLARGAPPERI 219
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 68-268 1.55e-19

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: 84.67  E-value: 1.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  68 KAGQYLQLRLR-DPYARPtfLAIASPPSiaaSKGVFEFLVKSIAGS--TAELLCGLQRGDVVELSTAIGNgFDIDQISPP 144
Cdd:cd06213   29 KAGQYAELTLPgLPAARS--YSFANAPQ---GDGQLSFHIRKVPGGafSGWLFGADRTGERLTVRGPFGD-FWLRPGDAP 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 145 enyqtVLIFATGSGISPIRSLIEAGFGADKRADVRLYYGARN------LSRM-AYRERFRdwesSGINIVPVLS-KPEDS 216
Cdd:cd06213  103 -----ILCIAGGSGLAPILAILEQARAAGTKRDVTLLFGARTqrdlyaLDEIaAIAARWR----GRFRFIPVLSeEPADS 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 848893825 217 -WTGERGFVQAAFARakriLNPQSTGAVLCGRRQMTEEVTSILVSDGVASEKI 268
Cdd:cd06213  174 sWKGARGLVTEHIAE----VLLAATEAYLCGPPAMIDAAIAVLRALGIAREHI 222
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
 44-270 2.66e-19

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: 85.05  E-value: 2.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  44 PAAESHFHiTIDVADSpdLASSYTKAGQylqLRLRDPYARPTFLA--IASPPsiaASKGVFEFLVKsIA----------- 110
Cdd:cd06188   50 PAYEIAYA-DFDVAEK--YRADWDKFGL---WQLVFKHDEPVSRAysLANYP---AEEGELKLNVR-IAtpppgnsdipp 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 111 GSTAELLCGLQRGDVVELSTAIGngfdiDQISPPENYQTVLIFAtGSGISPIRSLIEAGFGADKRA-DVRLYYGARNLSR 189
Cdd:cd06188  120 GIGSSYIFNLKPGDKVTASGPFG-----EFFIKDTDREMVFIGG-GAGMAPLRSHIFHLLKTLKSKrKISFWYGARSLKE 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 190 MAYRERFR--DWESSGINIVPVLSKP--EDSWTGERGFVQAAFAR--AKRILNPQSTGAVLCGRRQMTEEVTSILVSDGV 263
Cdd:cd06188  194 LFYQEEFEalEKEFPNFKYHPVLSEPqpEDNWDGYTGFIHQVLLEnyLKKHPAPEDIEFYLCGPPPMNSAVIKMLDDLGV 273


                 ....*..
gi 848893825 264 ASEKILK 270
Cdd:cd06188  274 PRENIAF 280
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 68-268 6.08e-19

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: 83.15  E-value: 6.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  68 KAGQYLQLRLRDPYARPTFlAIASPPSiaaSKGVFEFLVKSIAGS--TAELLCGLQRGDVVELSTAIGNGFDIDQISPPe 145
Cdd:cd06212   31 FAGQYVDITVPGTEETRSF-SMANTPA---DPGRLEFIIKKYPGGlfSSFLDDGLAVGDPVTVTGPYGTCTLRESRDRP- 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 146 nyqTVLIfATGSGISPI----RSLIEAGfgadKRADVRLYYGARNLSRMAYRERFRDWESS--GINIVPVLSK--PEDSW 217
Cdd:cd06212  106 ---IVLI-GGGSGMAPLlsllRDMAASG----SDRPVRFFYGARTARDLFYLEEIAALGEKipDFTFIPALSEspDDEGW 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 848893825 218 TGERGFVQAAFARakRILNPQSTGAVLCGRRQMTEEVTSILVSDGVASEKI 268
Cdd:cd06212  178 SGETGLVTEVVQR--NEATLAGCDVYLCGPPPMIDAALPVLEMSGVPPDQI 226
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 38-262 3.71e-18

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: 81.07  E-value: 3.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  38 RLIKVTPAAESHFHITIDvadsPDLASSYtKAGQYLQLRLRDPYARPTFLA--IASPPSiaasKGVFEF---LVKSiaGS 112
Cdd:cd06195    1 TVLKRRDWTDDLFSFRVT----RDIPFRF-QAGQFTKLGLPNDDGKLVRRAysIASAPY----EENLEFyiiLVPD--GP 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 113 TAELLCGLQRGDVVELSTAIGNGFDIDQISPPENYqtvLIFATGSGISPIRSLIEAGFGADKRADVRLYYGARNLSRMAY 192
Cdd:cd06195   70 LTPRLFKLKPGDTIYVGKKPTGFLTLDEVPPGKRL---WLLATGTGIAPFLSMLRDLEIWERFDKIVLVHGVRYAEELAY 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 848893825 193 RERFRDWESSG---INIVPVLSKPEDSWtGERGFVQAAFA------RAKRILNPQSTGAVLCGRRQMTEEVTSILVSDG 262
Cdd:cd06195  147 QDEIEALAKQYngkFRYVPIVSREKENG-ALTGRIPDLIEsgeleeHAGLPLDPETSHVMLCGNPQMIDDTQELLKEKG 224
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 37-268 4.40e-17

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: 77.97  E-value: 4.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  37 TRLIKVTPAAEShfhITIDVADspDLASSYT-KAGQYLQLR-------LRDPYArptflaIASPPSiaasKGVFEFLVKS 108
Cdd:cd06214    7 AEVVRETADAVS---ITFDVPE--ELRDAFRyRPGQFLTLRvpidgeeVRRSYS------ICSSPG----DDELRITVKR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 109 IAGSTA-ELLCG-LQRGDVVELSTAIGNgFDIDQISPPENYqtvLIFATGSGISPIRSLIEAGFGADKRADVRLYYGARN 186
Cdd:cd06214   72 VPGGRFsNWANDeLKAGDTLEVMPPAGR-FTLPPLPGARHY---VLFAAGSGITPVLSILKTALAREPASRVTLVYGNRT 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 187 LSRM-----------AYRERFRdwessginIVPVLSKPEDSWTGERGFVQAAFARA--KRILNPQS-TGAVLCGRRQMTE 252
Cdd:cd06214  148 EASVifreeladlkaRYPDRLT--------VIHVLSREQGDPDLLRGRLDAAKLNAllKNLLDATEfDEAFLCGPEPMMD 219

                        250
                 ....*....|....*.
gi 848893825 253 EVTSILVSDGVASEKI 268
Cdd:cd06214  220 AVEAALLELGVPAERI 235
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 154-250 3.17e-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: 72.68  E-value: 3.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  154 ATGSGISPIRSLIEAGF-GADKRADVRLYYGARNLSRMAYRERFRDWE---SSGINIVPVLSKPEDSWTGERGFVQAAFA 229
Cdd:pfam00175   3 AGGTGIAPVRSMLRAILeDPKDPTQVVLVFGNRNEDDILYREELDELAekhPGRLTVVYVVSRPEAGWTGGKGRVQDALL 82

                          90       100
                  ....*....|....*....|.
gi 848893825  230 RAKRILNPQSTGAVLCGRRQM 250
Cdd:pfam00175  83 EDHLSLPDEETHVYVCGPPGM 103
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 38-270 1.44e-15

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: 73.76  E-value: 1.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  38 RLIKVTPAAE--SHFHITIDVADSpdlaSSYTKAGQYLQLRLRD-------PYaRPTflaiaSPPSiaaSKGVFEFLVKS 108
Cdd:cd06183    2 KLVSKEDISHdtRIFRFELPSPDQ----VLGLPVGQHVELKAPDdgeqvvrPY-TPI-----SPDD---DKGYFDLLIKI 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 109 -IAGSTAELLCGLQRGDVVELSTAIGNgfdiDQISPPENYQTVLIFATGSGISPIRSLIEA--GFGADKRaDVRLYYGAR 185
Cdd:cd06183   69 yPGGKMSQYLHSLKPGDTVEIRGPFGK----FEYKPNGKVKHIGMIAGGTGITPMLQLIRAilKDPEDKT-KISLLYANR 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 186 NLSRMAYRERFRDWESSG---INIVPVLSKPEDSWTGERGFVQAAFarAKRILNPQSTGAVL---CGRRQMTE-EVTSIL 258
Cdd:cd06183  144 TEEDILLREELDELAKKHpdrFKVHYVLSRPPEGWKGGVGFITKEM--IKEHLPPPPSEDTLvlvCGPPPMIEgAVKGLL 221

                        250
                 ....*....|..
gi 848893825 259 VSDGVASEKILK 270
Cdd:cd06183  222 KELGYKKDNVFK 233
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 40-258 1.77e-15

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: 73.73  E-value: 1.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  40 IKVTPAAESHFHITIDvadSPDLASSyTKAGQYLQLRLRDPYA----RPtfLAIASppsIAASKGVFEFLVKsIAGSTAE 115
Cdd:cd06218    2 LSNREIADDIYRLVLE---APEIAAA-AKPGQFVMLRVPDGSDpllrRP--ISIHD---VDPEEGTITLLYK-VVGKGTR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 116 LLCGLQRGDVVELSTAIGNGFDIdqispPENYQTVLIFATGSGISP----IRSLIEAGfgadkrADVRLYYGARNLSRMA 191
Cdd:cd06218   72 LLSELKAGDELDVLGPLGNGFDL-----PDDDGKVLLVGGGIGIAPllflAKQLAERG------IKVTVLLGFRSADDLF 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 848893825 192 YRERFRDWessginIVPVLSKPEDSWTGERGFVQAAFARAKRILNPqstGAVL-CGRRQMTEEVTSIL 258
Cdd:cd06218  141 LVEEFEAL------GAEVYVATDDGSAGTKGFVTDLLKELLAEARP---DVVYaCGPEPMLKAVAELA 199
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 69-268 2.77e-13

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: 67.29  E-value: 2.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  69 AGQYLQLRLRDP----YARPtfLAIASPPsiaASKGVFEFLVKSIAGSTAE--LLCGLQRGDVVELSTAIGnGFdidQIS 142
Cdd:cd06217   33 AGQHVDLRLTAIdgytAQRS--YSIASSP---TQRGRVELTVKRVPGGEVSpyLHDEVKVGDLLEVRGPIG-TF---TWN 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 143 PPENYQTVLIfATGSGISPIRSLIEAGFGADKRADVRLYYGARNLSRMAYRERFRDWES--SGINIVPVLSKPED-SWTG 219
Cdd:cd06217  104 PLHGDPVVLL-AGGSGIVPLMSMIRYRRDLGWPVPFRLLYSARTAEDVIFRDELEQLARrhPNLHVTEALTRAAPaDWLG 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 848893825 220 ERGFVQAAFaRAKRILNPQSTGAVLCGRRQMTEEVTSILVSDGVASEKI 268
Cdd:cd06217  183 PAGRITADL-IAELVPPLAGRRVYVCGPPAFVEAATRLLLELGVPRDRI 230
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 36-268 5.81e-13

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 67.14  E-value: 5.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  36 PTRLIKVTPAAESHFHITIDVADsPDLASSYT-KAGQYLQLRLRDPYARPtfLAIASPPSiaaSKGVFEFLVKSiAGSTA 114
Cdd:PRK08345   7 DAKILEVYDLTEREKLFLLRFED-PELAESFTfKPGQFVQVTIPGVGEVP--ISICSSPT---RKGFFELCIRR-AGRVT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 115 ELLCGLQRGDVVELSTAIGNGFDIDQISPpenyQTVLIFATGSGISPIRS-LIEAGFGADKRADVRLYYGARNLSRMAYR 193
Cdd:PRK08345  80 TVIHRLKEGDIVGVRGPYGNGFPVDEMEG----MDLLLIAGGLGMAPLRSvLLYAMDNRWKYGNITLIYGAKYYEDLLFY 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 194 -ERFRDW-ESSGINIVPVLSKpEDSWTG----ERGFVQ------AAFARAKRILNPQSTGAVLCGRRQMTEEVTSILVSD 261
Cdd:PRK08345 156 dELIKDLaEAENVKIIQSVTR-DPEWPGchglPQGFIErvckgvVTDLFREANTDPKNTYAAICGPPVMYKFVFKELINR 234


                 ....*..
gi 848893825 262 GVASEKI 268
Cdd:PRK08345 235 GYRPERI 241
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 92-266 3.41e-12

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: 64.19  E-value: 3.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  92 PPSIAASKGVFEFLVKsIAGSTAELLCGLQRGDVVELSTAIGNGFDIDQisppenyQTVLIFATGSGISPIRSLIEAgfg 171
Cdd:cd06220   41 PMSLSYIDGPNSITVK-KVGEATSALHDLKEGDKLGIRGPYGNGFELVG-------GKVLLIGGGIGIAPLAPLAER--- 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 172 ADKRADVRLYYGARNLSRMAYRERFRdwesSGINIVPVlskPEDSWTGERGFVQAAFaraKRILNPQSTGAVLCGRRQMT 251
Cdd:cd06220  110 LKKAADVTVLLGARTKEELLFLDRLR----KSDELIVT---TDDGSYGFKGFVTDLL---KELDLEEYDAIYVCGPEIMM 179

                        170
                 ....*....|....*
gi 848893825 252 EEVTSILVSDGVASE 266
Cdd:cd06220  180 YKVLEILDERGVRAQ 194
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 69-227 3.46e-12

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 65.28  E-value: 3.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  69 AGQYLQLRLRDpyARPTFLAIASPPSiaaSKGVFEFLVKSIAG--STAELLCGLQRGDVVELSTAIGNGFDIDQISPPen 146
Cdd:PRK07609 134 AGQYIEFILKD--GKRRSYSIANAPH---SGGPLELHIRHMPGgvFTDHVFGALKERDILRIEGPLGTFFLREDSDKP-- 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 147 yqTVLIfATGSGISPIRSLIEAGFGADKRADVRLYYGARNLSRMAYRERFRDW--ESSGINIVPVLSK--PEDSWTGERG 222
Cdd:PRK07609 207 --IVLL-ASGTGFAPIKSIVEHLRAKGIQRPVTLYWGARRPEDLYLSALAEQWaeELPNFRYVPVVSDalDDDAWTGRTG 283


                 ....*
gi 848893825 223 FVQAA 227
Cdd:PRK07609 284 FVHQA 288
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
 117-260 8.18e-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: 63.88  E-value: 8.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 117 LCGLQRGDVVELSTAIGNGFdidqiSPPENYQTVLIF-ATGSGISPIRSLIEAGFgADKRADVR------LYYGARNLSR 189
Cdd:cd06208  109 LCDLKPGDDVQITGPVGKTM-----LLPEDPNATLIMiATGTGIAPFRSFLRRLF-REKHADYKftglawLFFGVPNSDS 182

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 848893825 190 MAYRERFRDWES---SGINIVPVLSKPEDSWTGERGFVQ-AAFARAKRILNPQSTGAV---LCGRRQMTEEVTSILVS 260
Cdd:cd06208  183 LLYDDELEKYPKqypDNFRIDYAFSREQKNADGGKMYVQdRIAEYAEEIWNLLDKDNThvyICGLKGMEPGVDDALTS 260
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 100-266 2.53e-11

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: 61.89  E-value: 2.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 100 GVFEFLVKSI---AGSTAeLLCGLQRGDVVELSTAIGNGFdidqISPPENYQTVLIfATGSGISPI----RSLIEAGFGA 172
Cdd:cd06190   53 GEWEFIIKRKpggAASNA-LFDNLEPGDELELDGPYGLAY----LRPDEDRDIVCI-AGGSGLAPMlsilRGAARSPYLS 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 173 DKRADvrLYYGARNLSRMAYRERFRDWESSG--INIVPVLSKPEDS----WTGERGFVQAAFARAKRIlNPQSTGAVLCG 246
Cdd:cd06190  127 DRPVD--LFYGGRTPSDLCALDELSALVALGarLRVTPAVSDAGSGsaagWDGPTGFVHEVVEATLGD-RLAEFEFYFAG 203

                        170       180
                 ....*....|....*....|
gi 848893825 247 RRQMTEEVTSILVSDGVASE 266
Cdd:cd06190  204 PPPMVDAVQRMLMIEGVVPF 223
nqrF TIGR01941
NADH:ubiquinone oxidoreductase, Na(+)-translocating, F subunit; This model represents the NqrF ...
 50-269 3.13e-11

NADH:ubiquinone oxidoreductase, Na(+)-translocating, F subunit; This model represents the NqrF subunit of the six-protein, Na(+)-pumping NADH-quinone reductase of a number of marine and pathogenic Gram-negative bacteria. This oxidoreductase complex functions primarily as a sodium ion pump. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130996 [Multi-domain]  Cd Length: 405  Bit Score: 62.89  E-value: 3.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825   50 FHITIDVADSPDLASS---YTKAGQYLQLRLRdpYARPTFLAIASPPSIAASKgVFEflvksiagstaellcgLQRGDVV 126
Cdd:TIGR01941 195 FDLVSKVDEETVRAYSmanYPAEKGIIKLNVR--IATPPFINSDIPPGIMSSY-IFS----------------LKPGDKV 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  127 ELSTAIGNGFDIDQISPpenyqtvLIF-ATGSGISPIRSLIEAGFGADK-RADVRLYYGARNLSRMAYRERFRDWESSGI 204
Cdd:TIGR01941 256 TISGPFGEFFAKDTDAE-------MVFiGGGAGMAPMRSHIFDQLKRLKsKRKISFWYGARSLREMFYQEDFDQLEAENP 328

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 848893825  205 NIV--PVLS--KPEDSWTGERGFVQAAF--ARAKRILNPQSTGAVLCGRRQMTEEVTSILVSDGVASEKIL 269
Cdd:TIGR01941 329 NFVwhVALSdpQPEDNWTGYTGFIHNVLyeNYLKDHDAPEDCEFYMCGPPMMNAAVIKMLEDLGVERENIL 399
fre PRK08051
FMN reductase; Validated
 41-227 3.57e-11

FMN reductase; Validated


Pssm-ID: 236142 [Multi-domain]  Cd Length: 232  Bit Score: 61.41  E-value: 3.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  41 KVTPAAESHFHITIdvadSPDLASSYtKAGQYLQLRLRDPYARPtFlAIASPPSiaaSKGVFEFLVksiaGSTAELLCGL 120
Cdd:PRK08051   9 SVEAITDTVYRVRL----VPEAPFSF-RAGQYLMVVMGEKDKRP-F-SIASTPR---EKGFIELHI----GASELNLYAM 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 121 QrgdVVElstAIGNGFDIDqISPP--------ENYQTVLIFATGSGISPIRSLIEAGFGADKRADVRLYYGARNLSRMAY 192
Cdd:PRK08051  75 A---VME---RILKDGEIE-VDIPhgdawlreESERPLLLIAGGTGFSYARSILLTALAQGPNRPITLYWGGREEDHLYD 147

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 848893825 193 RERFRDWES--SGINIVPVLSKPEDSWTGERGFVQAA 227
Cdd:PRK08051 148 LDELEALALkhPNLHFVPVVEQPEEGWQGKTGTVLTA 184
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 68-268 3.66e-11

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: 61.12  E-value: 3.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  68 KAGQYLQLRLRDPYARPtflaiASPPSIAAS---KGVFEFLVKSIAGSTAELLCGLQRGDVVELSTAIGnGFDIDQISPP 144
Cdd:cd06198   24 RAGQFAFLRFDASGWEE-----PHPFTISSApdpDGRLRFTIKALGDYTRRLAERLKPGTRVTVEGPYG-RFTFDDRRAR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 145 EnyqtVLIfATGSGISPIRSLIEAGFGADKRADVRLYYGARNLSRMAYRERFRDW-ESSGINIVPVLSkPEDSWTGERGF 223
Cdd:cd06198   98 Q----IWI-AGGIGITPFLALLEALAARGDARPVTLFYCVRDPEDAVFLDELRALaAAAGVVLHVIDS-PSDGRLTLEQL 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 848893825 224 VQAafarakRILNPQSTGAVLCGRRQMTEEVTSILVSDGVASEKI 268
Cdd:cd06198  172 VRA------LVPDLADADVWFCGPPGMADALEKGLRALGVPARRF 210
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 38-268 1.13e-10

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: 60.23  E-value: 1.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  38 RLIKVTPaaESHFHITIdVADSPDLASSYTKAGQYLQLRLR-DPYARPTFLAIASPPSiaasKGVFEFLVKSIAGS--TA 114
Cdd:cd06191    2 RVAEVRS--ETPDAVTI-VFAVPGPLQYGFRPGQHVTLKLDfDGEELRRCYSLCSSPA----PDEISITVKRVPGGrvSN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 115 ELLCGLQRGDVVELSTAIGngfdiDQISPPENYQTVLIFATGSGISPIRSLIEAGFGADKRADVRLYYGARNLSRMAYRE 194
Cdd:cd06191   75 YLREHIQPGMTVEVMGPQG-----HFVYQPQPPGRYLLVAAGSGITPLMAMIRATLQTAPESDFTLIHSARTPADMIFAQ 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 848893825 195 RFRDWESS--GINIVPVLSK--PEDSWTGERGFVQAAFARAkrILNPQST-GAVLCGRRQMTEEVTSILVSDGVASEKI 268
Cdd:cd06191  150 ELRELADKpqRLRLLCIFTRetLDSDLLHGRIDGEQSLGAA--LIPDRLErEAFICGPAGMMDAVETALKELGMPPERI 226
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
 91-262 1.28e-10

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 61.72  E-value: 1.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825   91 SPPSIAASKGVFEFLVKSIAGSTAELLCGLQRGDVVELStAIGnGFDIDQiSPPENY---------QTVLIfATGSGISP 161
Cdd:PTZ00306  970 SPITLPDDLGVISILARGDKGTLKEWISALRPGDSVEMK-ACG-GLRIER-RPADKQfvfrghvirKLALI-AGGTGVAP 1045

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  162 IRSLIEAGFG---ADKRADVRLYYGARNLSRMAYR---ERFRDWESSGINIVPVLSKPEDSWTGERGFVQAAFARAkrIL 235
Cdd:PTZ00306 1046 MLQIIRAALKkpyVDSIESIRLIYAAEDVSELTYRellESYRKENPGKFKCHFVLNNPPEGWTDGVGFVDRALLQS--AL 1123

                         170       180
                  ....*....|....*....|....*....
gi 848893825  236 NPQSTG--AVLCGRRQMTEEVTSILVSDG 262
Cdd:PTZ00306 1124 QPPSKDllVAICGPPVMQRAVKADLLALG 1152
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 68-197 3.10e-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 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: 58.78  E-value: 3.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  68 KAGQYLQL-------RLRDPYArptflaIASPPsiAASKGVFEFLVKSIAGS--TAELLCGLQRGDVVELSTAIGNgFDI 138
Cdd:cd06216   47 RAGQHVRLgveidgvRHWRSYS------LSSSP--TQEDGTITLTVKAQPDGlvSNWLVNHLAPGDVVELSQPQGD-FVL 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 848893825 139 DQISPPEnyqtVLIFATGSGISPIRSLIEAGFGADKRADVRLYYGARNLSRMAYRERFR 197
Cdd:cd06216  118 PDPLPPR----LLLIAAGSGITPVMSMLRTLLARGPTADVVLLYYARTREDVIFADELR 172
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 68-198 1.19e-09

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 57.19  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  68 KAGQYLQLRLRDPYA---RPtfLAIASPpsiaaSKGVFEFLVKsIAGSTAELLCGLQRGDVVELSTAIGNGFDIDQISpp 144
Cdd:PRK00054  33 KPGQFVMVWVPGVEPlleRP--ISISDI-----DKNEITILYR-KVGEGTKKLSKLKEGDELDIRGPLGNGFDLEEIG-- 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 848893825 145 enyQTVLIFATGSGISPIRSLIEAgfGADKRADVRLYYGARNLSRMAYRERFRD 198
Cdd:PRK00054 103 ---GKVLLVGGGIGVAPLYELAKE--LKKKGVEVTTVLGARTKDEVIFEEEFAK 151
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 69-268 8.07e-09

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: 54.58  E-value: 8.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  69 AGQYLQLRLRDPYARPtfLAIASPPsiaASKGVFEFLVKSI-AGSTAELLCGLQR-GDVVELSTAIGNGFDidqispPEN 146
Cdd:cd06194   26 PGQYVNLRRAGGLARS--YSPTSLP---DGDNELEFHIRRKpNGAFSGWLGEEARpGHALRLQGPFGQAFY------RPE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 147 YQT--VLIFATGSGISPIRSLIEAGFGADKRADVRLYYGARNLSRMAYRERFRdW---ESSGINIVPVLSKPEDSWTGER 221
Cdd:cd06194   95 YGEgpLLLVGAGTGLAPLWGIARAALRQGHQGEIRLVHGARDPDDLYLHPALL-WlarEHPNFRYIPCVSEGSQGDPRVR 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 848893825 222 GFVQAafarAKRILNPQSTGAVLCGRRQMTEEVTSILVSDGVASEKI 268
Cdd:cd06194  174 AGRIA----AHLPPLTRDDVVYLCGAPSMVNAVRRRAFLAGAPMKRI 216
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
 109-263 8.71e-09

ferredoxin--NADP(+) reductase; Provisional


Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 55.39  E-value: 8.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 109 IAGSTAELLCGLQRGDVVELSTAIGNgfdiDQISPPENYQTVLIFATGSGISPIRSLIEAGFgADKRADVR------LYY 182
Cdd:PLN03115 181 VKGVCSNFLCDLKPGAEVKITGPVGK----EMLMPKDPNATIIMLATGTGIAPFRSFLWKMF-FEKHDDYKfnglawLFL 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 183 GARNLSRMAYRERF---RDWESSGINIVPVLSKPEDSWTGERGFVQAAFARAK----RILNPQSTGAVLCGRRQMTEEVT 255
Cdd:PLN03115 256 GVPTSSSLLYKEEFekmKEKAPENFRLDFAVSREQTNAKGEKMYIQTRMAEYAeelwELLKKDNTYVYMCGLKGMEKGID 335

                        170
                 ....*....|..
gi 848893825 256 SILVS----DGV 263
Cdd:PLN03115 336 DIMVSlaakDGI 347
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
121-254 3.69e-08

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 53.59  E-value: 3.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 121 QRGDVVELSTAIGnGFDIDQISPPenyqtVLIFATGSGISPIRSLIEAGFGADKRADVRLYYGARN------LSRM-AYR 193
Cdd:PRK11872 189 QVGDEILFEAPLG-AFYLREVERP-----LVFVAGGTGLSAFLGMLDELAEQGCSPPVHLYYGVRHaadlceLQRLaAYA 262

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 848893825 194 ERFrdwesSGINIVPVLSKPEDSWTGERGFVQAAFARAKriLNPQSTGAVLCGRRQMTEEV 254
Cdd:PRK11872 263 ERL-----PNFRYHPVVSKASADWQGKRGYIHEHFDKAQ--LRDQAFDMYLCGPPPMVEAV 316
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 69-269 4.12e-08

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


Pssm-ID: 99806  Cd Length: 236  Bit Score: 52.73  E-value: 4.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  69 AGQYLQLRLRDPYARPTFlaiaSPPSIAASKGVFEFLVKSIAGS--TAELLCGLQRGDVVELSTAIGnGFDIDQISPpen 146
Cdd:cd06210   37 PGQFVEIEIPGTDTRRSY----SLANTPNWDGRLEFLIRLLPGGafSTYLETRAKVGQRLNLRGPLG-AFGLRENGL--- 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 147 yQTVLIFATGSGISPIRSLIE--AGFGADKRAdvRLYYGARNLSRMAYRERFRDWESS--GINIVPVLSKPEDSWTGERG 222
Cdd:cd06210  109 -RPRWFVAGGTGLAPLLSMLRrmAEWGEPQEA--RLFFGVNTEAELFYLDELKRLADSlpNLTVRICVWRPGGEWEGYRG 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 848893825 223 FVQAAFARAKrilnpQSTGAV----LCGRRQMTEEVTSILVSDGVASEKIL 269
Cdd:cd06210  186 TVVDALREDL-----ASSDAKpdiyLCGPPGMVDAAFAAAREAGVPDEQVY 231
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 68-263 2.14e-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 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: 50.67  E-value: 2.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  68 KAGQYLQLRLR---DPYARPtfLAIASPPSiaaSKGVFEFLVKSIAGSTAE--LLCGLQRGDVVELSTAIG--NGFDIDQ 140
Cdd:cd06215   29 KPGQFLTLELEidgETVYRA--YTLSSSPS---RPDSLSITVKRVPGGLVSnwLHDNLKVGDELWASGPAGefTLIDHPA 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 141 isppenyQTVLIFATGSGISPIRSLIEAGFGADKRADVRLYYGARN---------LSRMAYRErfrdwesSGINIVPVLS 211
Cdd:cd06215  104 -------DKLLLLSAGSGITPMMSMARWLLDTRPDADIVFIHSARSpadiifadeLEELARRH-------PNFRLHLILE 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 848893825 212 KP-EDSWTGERGFVQAA-FARAKRILNPQStgAVLCGRRQMTEEVTSILVSDGV 263
Cdd:cd06215  170 QPaPGAWGGYRGRLNAElLALLVPDLKERT--VFVCGPAGFMKAVKSLLAELGF 221
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 120-268 8.01e-07

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: 49.09  E-value: 8.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 120 LQRGDVVELSTAIGNgFDIDQISP-PenyqTVLIfATGSGISPIRSLIEAGFGADKRADVRLYYGARNLSRMAYRERFRD 198
Cdd:cd06184   91 VKVGDVLEVSAPAGD-FVLDEASDrP----LVLI-SAGVGITPMLSMLEALAAEGPGRPVTFIHAARNSAVHAFRDELEE 164

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 848893825 199 WESSGINI--VPVLSKPEDSWTGE----RGFVQAAFARakRILNPQSTGAVLCGRRQMTEEVTSILVSDGVASEKI 268
Cdd:cd06184  165 LAARLPNLklHVFYSEPEAGDREEdydhAGRIDLALLR--ELLLPADADFYLCGPVPFMQAVREGLKALGVPAERI 238
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 59-225 1.19e-06

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: 48.48  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  59 SPDLASSYtKAGQYLQLRLrdpYARPTFLAIA-SPPSIAASKGVFEFLVKsIAGSTAELLCGLQRGDVVELSTAIGNGFD 137
Cdd:cd06192   18 APLAARLF-RPGQFVFLRN---FESPGLERIPlSLAGVDPEEGTISLLVE-IRGPKTKLIAELKPGEKLDVMGPLGNGFE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 138 IdqispPENYQTVLIFATGSGISPIRSLIEAgFGADKRaDVRLYYGARNLSrmayrERFRDWESSGINIVPVLSKpEDSW 217
Cdd:cd06192   93 G-----PKKGGTVLLVAGGIGLAPLLPIAKK-LAANGN-KVTVLAGAKKAK-----EEFLDEYFELPADVEIWTT-DDGE 159


                 ....*...
gi 848893825 218 TGERGFVQ 225
Cdd:cd06192  160 LGLEGKVT 167
DHOD_e_trans_like1 cd06219
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 38-197 1.94e-06

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


Pssm-ID: 99815 [Multi-domain]  Cd Length: 248  Bit Score: 47.96  E-value: 1.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  38 RLIKVTPAAESHFHITIDvadSPDLASSyTKAGQYLQLRLrDPYARPTFLAIASppsIAASKGVFEFLVKSIaGSTAELL 117
Cdd:cd06219    2 KILEKEELAPNVKLFEIE---APLIAKK-AKPGQFVIVRA-DEKGERIPLTIAD---WDPEKGTITIVVQVV-GKSTREL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 118 CGLQRGDVVE-LSTAIGNGFDIdqisppENYQTVLIFATGSGISPI----RSLIEAGfgadkrADVRLYYGARNLSRMAY 192
Cdd:cd06219   73 ATLEEGDKIHdVVGPLGKPSEI------ENYGTVVFVGGGVGIAPIypiaKALKEAG------NRVITIIGARTKDLVIL 140


                 ....*
gi 848893825 193 RERFR 197
Cdd:cd06219  141 EDEFR 145
CYPOR_like cd06182
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 44-205 2.19e-05

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: 44.64  E-value: 2.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  44 PAAESHFHITIDVADSPDLassYTKAGQYLQLRLRDPYaRPTFLAIASppSIAASKGVFEFLVKSI----------AGST 113
Cdd:cd06182   12 DSPRSTRHLEFDLSGNSVL---KYQPGDHLGVIPPNPL-QPRYYSIAS--SPDVDPGEVHLCVRVVsyeapagrirKGVC 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 114 AELLCGLQRGDVVELSTAIGNGFdidqiSPPENYQTVLIF-ATGSGISPIRSLIEAgFGADKRADVR-----LYYGARN- 186
Cdd:cd06182   86 SNFLAGLQLGAKVTVFIRPAPSF-----RLPKDPTTPIIMvGPGTGIAPFRGFLQE-RAALRANGKArgpawLFFGCRNf 159

                        170
                 ....*....|....*....
gi 848893825 187 LSRMAYRERFRDWESSGIN 205
Cdd:cd06182  160 ASDYLYREELQEALKDGAL 178
PRK10926 PRK10926
ferredoxin-NADP reductase; Provisional
 34-258 7.95e-05

ferredoxin-NADP reductase; Provisional


Pssm-ID: 182844  Cd Length: 248  Bit Score: 43.15  E-value: 7.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  34 WTPTRLIKVTPAAESHFHITIDVADSPDLASSYTKagqyLQLRLRDPYARPTFLAIASPpsiaaSKGVFEF-LVKSIAGS 112
Cdd:PRK10926   4 WVTGKVTKVQNWTDALFSLTVHAPVDPFTAGQFTK----LGLEIDGERVQRAYSYVNAP-----DNPDLEFyLVTVPEGK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 113 TAELLCGLQRGDVVELSTAIGNGFDIDQISPPEnyqTVLIFATGSGISPIRSLIEAGFGADKRADVRLYYGARNLSRMAY 192
Cdd:PRK10926  75 LSPRLAALKPGDEVQVVSEAAGFFVLDEVPDCE---TLWMLATGTAIGPYLSILQEGKDLERFKNLVLVHAARYAADLSY 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 193 -------RERFRDwessGINIVPVLSKPE--DSWTG------ERGFVQAAFARAkriLNPQSTGAVLCGRRQMTEEVTSI 257
Cdd:PRK10926 152 lplmqelEQRYEG----KLRIQTVVSRETapGSLTGrvpaliESGELEAAVGLP---MDAETSHVMLCGNPQMVRDTQQL 224


                 .
gi 848893825 258 L 258
Cdd:PRK10926 225 L 225
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 120-197 2.23e-04

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: 41.31  E-value: 2.23e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 848893825 120 LQRGDVVELStAIGNGFDIDQISPPenyqTVLIfATGSGISPIRSLIEAGfgADKRADVRLYYGARNLSRMAYRERFR 197
Cdd:cd06185   77 LRVGDELEVS-APRNLFPLDEAARR----HLLI-AGGIGITPILSMARAL--AARGADFELHYAGRSREDAAFLDELA 146
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 68-254 1.26e-03

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


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 39.21  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825  68 KAGQYLqlRLRDPyARPTFLA-----IASPPSiaASKGVFEFLVKSIAGSTAELLCGLQRGDVVELSTAIGngfdID--- 139
Cdd:cd06186   26 KPGQHV--YLNFP-SLLSFWQshpftIASSPE--DEQDTLSLIIRAKKGFTTRLLRKALKSPGGGVSLKVL----VEgpy 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 140 --QISPPENYQTVLIFATGSGISP----IRSLIEAGFGADKRADVRLYYGARNLsrmAYRERFRDWESSGINIVPVLSkp 213
Cdd:cd06186   97 gsSSEDLLSYDNVLLVAGGSGITFvlpiLRDLLRRSSKTSRTRRVKLVWVVRDR---EDLEWFLDELRAAQELEVDGE-- 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 848893825 214 edswtgERGFVqaafarakrilnpqsTGAVLCGRRQMTEEV 254
Cdd:cd06186  172 ------IEIYV---------------TRVVVCGPPGLVDDV 191
bifunctional_CYPOR cd06206
These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase ...
 143-259 1.68e-03

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: 39.16  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 848893825 143 PPENYQTVLI-FATGSGISPIRslieaGFGADKRADVR---------LYYGARN--LSRMaYRERFRDWESSGI-NIVPV 209
Cdd:cd06206  225 PPSDPSTPLImIAAGTGLAPFR-----GFLQERAALLAqgrklapalLFFGCRHpdHDDL-YRDELEEWEAAGVvSVRRA 298

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 848893825 210 LSKPEDSWtgeRGFVQ-AAFARAKRILNPQSTGAVL--CGRRQMTEEVTSILV 259
Cdd:cd06206  299 YSRPPGGG---CRYVQdRLWAEREEVWELWEQGARVyvCGDGRMAPGVREVLK 348
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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