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Conserved domains on  [gi|1082860120|gb|OGB73118|]
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ferric reductase [Burkholderiales bacterium RIFOXYC12_FULL_65_23]

Protein Classification

ferredoxin reductase family protein( domain architecture ID 11467864)

ferredoxin reductase family protein; ferredoxin reductase family protein may transfer electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH; contains a ferric reductase-like transmembrane domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
24-443 1.26e-137

Predicted ferric reductase [Inorganic ion transport and metabolism];


:

Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 401.96  E-value: 1.26e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120  24 SAALPLTQGLFPWRTLLVQYSGLLGMGVMSAAMLLAVRPAWLEHRLHGLDKMYRLHKWLGIAGLVLAILHWLISQGPKWL 103
Cdd:COG4097    26 ADPLPAPAGGRGLRTALGQLTGLLALALMSLQFLLAARPPWLERPFGGLDRLYRLHKWLGILALVLALAHPLLLLGPKWL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 104 IGAGLLERPVRgprplltdpvlAFLQSQRGLAEDLGEKAFYLAVALIALALIKR-FPYRHFFRTHRWIALAYLVLVWHSI 182
Cdd:COG4097   106 VGWGGLPARLA-----------ALLTLLRGLAELLGEWAFYLLLALVVLSLLRRrLPYELWRLTHRLLAVAYLLLAFHHL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 183 VLTSFGYWLQPVGVLHGLLLAGGTVAALISLTRRIGVRRKAVGEIEQLEYLEGvkvNAVSIRLK---SQWAGHEPGQFAF 259
Cdd:COG4097   175 LLGGPFYWSPPAGVLWAALAAAGLAAAVYSRLGRPLRSRRHPYRVESVEPEAG---DVVELTLRpegGRWLGHRAGQFAF 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 260 VTFDER---EGAHPFTISSAWQDDGRLMFLIKALGDYTHSLAAsLKLGDTVTVEGPYGRFQFD--GPARRQIWIGGGIGI 334
Cdd:COG4097   252 LRFDGSpfwEEAHPFSISSAPGGDGRLRFTIKALGDFTRRLGR-LKPGTRVYVEGPYGRFTFDrrDTAPRQVWIAGGIGI 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 335 SPFVARLKQLAQQS-DGREIDLFHATSEVDE-TALQRLQQHAQ-AAGVRLHLLISGRDGRLTGERLRALVPDWQQAELWF 411
Cdd:COG4097   331 TPFLALLRALAARPgDQRPVDLFYCVRDEEDaPFLEELRALAArLAGLRLHLVVSDEDGRLTAERLRRLVPDLAEADVFF 410

                         410       420       430
                  ....*....|....*....|....*....|..
gi 1082860120 412 CGPAAFGDAIRTDLCAQGLPAARFHQELFEMR 443
Cdd:COG4097   411 CGPPGMMDALRRDLRALGVPARRIHQERFEFR 442
 
Name Accession Description Interval E-value
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
24-443 1.26e-137

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 401.96  E-value: 1.26e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120  24 SAALPLTQGLFPWRTLLVQYSGLLGMGVMSAAMLLAVRPAWLEHRLHGLDKMYRLHKWLGIAGLVLAILHWLISQGPKWL 103
Cdd:COG4097    26 ADPLPAPAGGRGLRTALGQLTGLLALALMSLQFLLAARPPWLERPFGGLDRLYRLHKWLGILALVLALAHPLLLLGPKWL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 104 IGAGLLERPVRgprplltdpvlAFLQSQRGLAEDLGEKAFYLAVALIALALIKR-FPYRHFFRTHRWIALAYLVLVWHSI 182
Cdd:COG4097   106 VGWGGLPARLA-----------ALLTLLRGLAELLGEWAFYLLLALVVLSLLRRrLPYELWRLTHRLLAVAYLLLAFHHL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 183 VLTSFGYWLQPVGVLHGLLLAGGTVAALISLTRRIGVRRKAVGEIEQLEYLEGvkvNAVSIRLK---SQWAGHEPGQFAF 259
Cdd:COG4097   175 LLGGPFYWSPPAGVLWAALAAAGLAAAVYSRLGRPLRSRRHPYRVESVEPEAG---DVVELTLRpegGRWLGHRAGQFAF 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 260 VTFDER---EGAHPFTISSAWQDDGRLMFLIKALGDYTHSLAAsLKLGDTVTVEGPYGRFQFD--GPARRQIWIGGGIGI 334
Cdd:COG4097   252 LRFDGSpfwEEAHPFSISSAPGGDGRLRFTIKALGDFTRRLGR-LKPGTRVYVEGPYGRFTFDrrDTAPRQVWIAGGIGI 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 335 SPFVARLKQLAQQS-DGREIDLFHATSEVDE-TALQRLQQHAQ-AAGVRLHLLISGRDGRLTGERLRALVPDWQQAELWF 411
Cdd:COG4097   331 TPFLALLRALAARPgDQRPVDLFYCVRDEEDaPFLEELRALAArLAGLRLHLVVSDEDGRLTAERLRRLVPDLAEADVFF 410

                         410       420       430
                  ....*....|....*....|....*....|..
gi 1082860120 412 CGPAAFGDAIRTDLCAQGLPAARFHQELFEMR 443
Cdd:COG4097   411 CGPPGMMDALRRDLRALGVPARRIHQERFEFR 442
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 233-441 5.83e-79

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: 243.70  E-value: 5.83e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 233 LEGVKVNAVSIRLKSQWAGHEPGQFAFVTFDER--EGAHPFTISSAWQDDGRLMFLIKALGDYTHSLAASLKLGDTVTVE 310
Cdd:cd06198     4 TEVRPTTTLTLEPRGPALGHRAGQFAFLRFDASgwEEPHPFTISSAPDPDGRLRFTIKALGDYTRRLAERLKPGTRVTVE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 311 GPYGRFQFDGPARRQIWIGGGIGISPFVARLKQLAQQSDGREIDLFHATSEVDE-TALQRLQQHAQAAGVRLHLLISGRD 389
Cdd:cd06198    84 GPYGRFTFDDRRARQIWIAGGIGITPFLALLEALAARGDARPVTLFYCVRDPEDaVFLDELRALAAAAGVVLHVIDSPSD 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1082860120 390 GRLTGERL-RALVPDWQQAELWFCGPAAFGDAIRTDLCAQGLPAARFHQELFE 441
Cdd:cd06198   164 GRLTLEQLvRALVPDLADADVWFCGPPGMADALEKGLRALGVPARRFHYERFE 216
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
254-440 2.06e-10

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 61.68  E-value: 2.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 254 PGQFAFVTFDEREGAHPFTISSAWQDDGRLMFLIKALGDYTHS--LAASLKLGDTVTVEGPYGRFQFDGPARRQIWIGGG 331
Cdd:PRK11872  139 PGQYARLQIPGTDDWRSYSFANRPNATNQLQFLIRLLPDGVMSnyLRERCQVGDEILFEAPLGAFYLREVERPLVFVAGG 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 332 IGISPFVARLKQLAQQSDGREIDLFHA-TSEVDETALQRLQQHAQA-AGVRLHLLIS-------GRDGRLTGERLRALVP 402
Cdd:PRK11872  219 TGLSAFLGMLDELAEQGCSPPVHLYYGvRHAADLCELQRLAAYAERlPNFRYHPVVSkasadwqGKRGYIHEHFDKAQLR 298

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1082860120 403 DwQQAELWFCGPAAFGDAIRTDLCAQGLPAARFHQELF 440
Cdd:PRK11872  299 D-QAFDMYLCGPPPMVEAVKQWLDEQALENYRLYYEKF 335
FAD_binding_8 pfam08022
FAD-binding domain;
239-314 2.56e-07

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 48.87  E-value: 2.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 239 NAVSIRLK--SQWAGHEPGQFAFVTFDEREG---AHPFTISSAWQDDgRLMFLIKALGDYT-----HSLAASLKLGD--- 305
Cdd:pfam08022  15 NVLKLRVSkpKKPFKYKPGQYMFINFLPPLSflqSHPFTITSAPSDD-KLSLHIKVKGGWTrklanYLSSSCPKSPEngk 93

                          90
                  ....*....|..
gi 1082860120 306 ---TVTVEGPYG 314
Cdd:pfam08022  94 dkpRVLIEGPYG 105
 
Name Accession Description Interval E-value
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
24-443 1.26e-137

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 401.96  E-value: 1.26e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120  24 SAALPLTQGLFPWRTLLVQYSGLLGMGVMSAAMLLAVRPAWLEHRLHGLDKMYRLHKWLGIAGLVLAILHWLISQGPKWL 103
Cdd:COG4097    26 ADPLPAPAGGRGLRTALGQLTGLLALALMSLQFLLAARPPWLERPFGGLDRLYRLHKWLGILALVLALAHPLLLLGPKWL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 104 IGAGLLERPVRgprplltdpvlAFLQSQRGLAEDLGEKAFYLAVALIALALIKR-FPYRHFFRTHRWIALAYLVLVWHSI 182
Cdd:COG4097   106 VGWGGLPARLA-----------ALLTLLRGLAELLGEWAFYLLLALVVLSLLRRrLPYELWRLTHRLLAVAYLLLAFHHL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 183 VLTSFGYWLQPVGVLHGLLLAGGTVAALISLTRRIGVRRKAVGEIEQLEYLEGvkvNAVSIRLK---SQWAGHEPGQFAF 259
Cdd:COG4097   175 LLGGPFYWSPPAGVLWAALAAAGLAAAVYSRLGRPLRSRRHPYRVESVEPEAG---DVVELTLRpegGRWLGHRAGQFAF 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 260 VTFDER---EGAHPFTISSAWQDDGRLMFLIKALGDYTHSLAAsLKLGDTVTVEGPYGRFQFD--GPARRQIWIGGGIGI 334
Cdd:COG4097   252 LRFDGSpfwEEAHPFSISSAPGGDGRLRFTIKALGDFTRRLGR-LKPGTRVYVEGPYGRFTFDrrDTAPRQVWIAGGIGI 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 335 SPFVARLKQLAQQS-DGREIDLFHATSEVDE-TALQRLQQHAQ-AAGVRLHLLISGRDGRLTGERLRALVPDWQQAELWF 411
Cdd:COG4097   331 TPFLALLRALAARPgDQRPVDLFYCVRDEEDaPFLEELRALAArLAGLRLHLVVSDEDGRLTAERLRRLVPDLAEADVFF 410

                         410       420       430
                  ....*....|....*....|....*....|..
gi 1082860120 412 CGPAAFGDAIRTDLCAQGLPAARFHQELFEMR 443
Cdd:COG4097   411 CGPPGMMDALRRDLRALGVPARRIHQERFEFR 442
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 233-441 5.83e-79

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: 243.70  E-value: 5.83e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 233 LEGVKVNAVSIRLKSQWAGHEPGQFAFVTFDER--EGAHPFTISSAWQDDGRLMFLIKALGDYTHSLAASLKLGDTVTVE 310
Cdd:cd06198     4 TEVRPTTTLTLEPRGPALGHRAGQFAFLRFDASgwEEPHPFTISSAPDPDGRLRFTIKALGDYTRRLAERLKPGTRVTVE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 311 GPYGRFQFDGPARRQIWIGGGIGISPFVARLKQLAQQSDGREIDLFHATSEVDE-TALQRLQQHAQAAGVRLHLLISGRD 389
Cdd:cd06198    84 GPYGRFTFDDRRARQIWIAGGIGITPFLALLEALAARGDARPVTLFYCVRDPEDaVFLDELRALAAAAGVVLHVIDSPSD 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1082860120 390 GRLTGERL-RALVPDWQQAELWFCGPAAFGDAIRTDLCAQGLPAARFHQELFE 441
Cdd:cd06198   164 GRLTLEQLvRALVPDLADADVWFCGPPGMADALEKGLRALGVPARRFHYERFE 216
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
239-438 4.84e-28

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 110.65  E-value: 4.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 239 NAVSIRLK----SQWAGHEPGQFA--FVTFDEREGAHPFTISSAwQDDGRLMFLIKAL--GDYTHSLAASLKLGDTVTVE 310
Cdd:COG1018    17 DVVSFTLEppdgAPLPRFRPGQFVtlRLPIDGKPLRRAYSLSSA-PGDGRLEITVKRVpgGGGSNWLHDHLKVGDTLEVS 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 311 GPYGRFQFDGPARRqiwigggigiS-----------PFVARLKQLAQQSDGREIDLFHATSEVDETA-LQRLQQHAQA-A 377
Cdd:COG1018    96 GPRGDFVLDPEPAR----------PllliaggigitPFLSMLRTLLARGPFRPVTLVYGARSPADLAfRDELEALAARhP 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082860120 378 GVRLHLLIS----GRDGRLTGERLRALVPDWQQAELWFCGPAAFGDAIRTDLCAQGLPAARFHQE 438
Cdd:COG1018   166 RLRLHPVLSrepaGLQGRLDAELLAALLPDPADAHVYLCGPPPMMEAVRAALAELGVPEERIHFE 230
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 241-440 2.44e-26

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: 106.14  E-value: 2.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 241 VSIRLKSQWAGH---EPGQFAFVTFDEREGAH--PFTISSAWQDDGRLMFLIKAL--GDYTHSLAASLKLGDTVTVEGPY 313
Cdd:cd06215    14 KTFRFAAPDGSLfayKPGQFLTLELEIDGETVyrAYTLSSSPSRPDSLSITVKRVpgGLVSNWLHDNLKVGDELWASGPA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 314 GRFQ-FDGPARRQIWIGGGIGISPFVARLKQLAQQSDGREIDLFH-ATSEVDETALQRLQQ-HAQAAGVRLHLLIS---- 386
Cdd:cd06215    94 GEFTlIDHPADKLLLLSAGSGITPMMSMARWLLDTRPDADIVFIHsARSPADIIFADELEElARRHPNFRLHLILEqpap 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1082860120 387 ----GRDGRLTGERLRALVPDWQQAELWFCGPAAFGDAIRTDLCAQGLPAARFHQELF 440
Cdd:cd06215   174 gawgGYRGRLNAELLALLVPDLKERTVFVCGPAGFMKAVKSLLAELGFPMSRFHQESF 231
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 236-438 5.17e-24

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: 99.44  E-value: 5.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 236 VKVNAVSIRLK-SQWAGHEPGQFAFVTF--DEREGAHPFTISSAWQDDGRLMFLIKA--LGDYTHSLAaSLKLGDTVTVE 310
Cdd:cd00322     6 VTDDVRLFRLQlPNGFSFKPGQYVDLHLpgDGRGLRRAYSIASSPDEEGELELTVKIvpGGPFSAWLH-DLKPGDEVEVS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 311 GPYGRF-QFDGPARRQIWIGGGIGISPFVARLKQLAQQSDGREIDLFHATSEVDETA-LQRLQQHAQAAGVRLHLLISGR 388
Cdd:cd00322    85 GPGGDFfLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGEITLLYGARTPADLLfLDELEELAKEGPNFRLVLALSR 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1082860120 389 D---------GRLTGERLRALVPDWQQAELWFCGPAAFGDAIRTDLCAQGLPAARFHQE 438
Cdd:cd00322   165 EseaklgpggRIDREAEILALLPDDSGALVYICGPPAMAKAVREALVSLGVPEERIHTE 223
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 220-440 1.94e-22

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: 95.75  E-value: 1.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 220 RRKAVGEIEQLEYLEGvkvNAVSIRLK--SQWAGHEPGQFAFVTFdEREGAH---PFTISSAW-QDDGRLMFLIKAL--G 291
Cdd:cd06216    15 ARELRARVVAVRPETA---DMVTLTLRpnRGWPGHRAGQHVRLGV-EIDGVRhwrSYSLSSSPtQEDGTITLTVKAQpdG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 292 DYTHSLAASLKLGDTVTVEGPYGRFQFdgPARRQIWIGGGIGIS---PFVARLKQLAQQSDGREIDLFH-ATSEVDETAL 367
Cdd:cd06216    91 LVSNWLVNHLAPGDVVELSQPQGDFVL--PDPLPPRLLLIAAGSgitPVMSMLRTLLARGPTADVVLLYyARTREDVIFA 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082860120 368 QRLQQHA-QAAGVRLHLLIS--GRDGRLTGERLRALVPDWQQAELWFCGPAAFGDAIRTDLCAQGLpAARFHQELF 440
Cdd:cd06216   169 DELRALAaQHPNLRLHLLYTreELDGRLSAAHLDAVVPDLADRQVYACGPPGFLDAAEELLEAAGL-ADRLHTERF 243
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 252-436 1.44e-19

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 87.61  E-value: 1.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 252 HEPGQFAFVTFDEREGAHPFTISSAWQDDGRLMFLIKALGDYTHSLAAsLKLGDTVTVEGPYGR-FQFDGPARRQIwigg 330
Cdd:COG0543    26 FKPGQFVMLRVPGDGLRRPFSIASAPREDGTIELHIRVVGKGTRALAE-LKPGDELDVRGPLGNgFPLEDSGRPVL---- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 331 gigispFVAR------LKQLAQQ--SDGREIDLFHATSEVDETALqrLQQHAQAAGVRLHLLI----SGRDGRLTgERLR 398
Cdd:COG0543   101 ------LVAGgtglapLRSLAEAllARGRRVTLYLGARTPEDLYL--LDELEALADFRVVVTTddgwYGRKGFVT-DALK 171

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1082860120 399 ALVPDWQQAELWFCGPAAFGDAIRTDLCAQGLPAARFH 436
Cdd:COG0543   172 ELLAEDSGDDVYACGPPPMMKAVAELLLERGVPPERIY 209
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 254-440 4.49e-17

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: 79.94  E-value: 4.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 254 PGQFAFVTFDEREG-AHPFTISSAWQDDGRLMFLIKAL--GDYTHSLAASLKLGDTVTVEGPYGRFQFDGPARRQIWIGG 330
Cdd:cd06187    26 AGQYVNVTVPGRPRtWRAYSPANPPNEDGEIEFHVRAVpgGRVSNALHDELKVGDRVRLSGPYGTFYLRRDHDRPVLCIA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 331 GIG-ISPFVARLKQLAQQSDGREIDLFH-ATSEVDETALQRLQQHAQAAG-VRLHLLIS-------GRDGRLTgERLRAL 400
Cdd:cd06187   106 GGTgLAPLRAIVEDALRRGEPRPVHLFFgARTERDLYDLEGLLALAARHPwLRVVPVVSheegawtGRRGLVT-DVVGRD 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1082860120 401 VPDWQQAELWFCGPAAFGDAIRTDLCAQGLPAARFHQELF 440
Cdd:cd06187   185 GPDWADHDIYICGPPAMVDATVDALLARGAPPERIHFDKF 224
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 239-440 1.77e-14

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: 72.58  E-value: 1.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 239 NAVSI------RLKSQWAgHEPGQFafVTFDEREGAH----PFTISSAwQDDGRLMFLIKALGDYTHS--LAASLKLGDT 306
Cdd:cd06214    15 DAVSItfdvpeELRDAFR-YRPGQF--LTLRVPIDGEevrrSYSICSS-PGDDELRITVKRVPGGRFSnwANDELKAGDT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 307 VTVEGPYGRFQFDGPARRQiwigggigisPFVA------------RLKQ-LAQQSDGReIDLFHATSEVDET----ALQR 369
Cdd:cd06214    91 LEVMPPAGRFTLPPLPGAR----------HYVLfaagsgitpvlsILKTaLAREPASR-VTLVYGNRTEASVifreELAD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 370 LQ-QHAQaagvRLHLL---------ISGRDGRLTGERLRALVPDWQQAE---LWF-CGPAAFGDAIRTDLCAQGLPAARF 435
Cdd:cd06214   160 LKaRYPD----RLTVIhvlsreqgdPDLLRGRLDAAKLNALLKNLLDATefdEAFlCGPEPMMDAVEAALLELGVPAERI 235


                  ....*
gi 1082860120 436 HQELF 440
Cdd:cd06214   236 HRELF 240
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 253-438 1.22e-13

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: 69.96  E-value: 1.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 253 EPGQFAFVTFDE---REGAHPFTISSAwQDDGRLMFLIKALGDY---THSLAaSLKLGDTVTVEGPYGRFQFDGPArrqI 326
Cdd:cd06196    29 TPGQATEVAIDKpgwRDEKRPFTFTSL-PEDDVLEFVIKSYPDHdgvTEQLG-RLQPGDTLLIEDPWGAIEYKGPG---V 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 327 WIGGGIGISPFVARLKQLAQQSDGREIDLFHATSEVDETALQRLQQHAQaaGVRLHLLISGRD------GRLTGERLRAL 400
Cdd:cd06196   104 FIAGGAGITPFIAILRDLAAKGKLEGNTLIFANKTEKDIILKDELEKML--GLKFINVVTDEKdpgyahGRIDKAFLKQH 181

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1082860120 401 VPDWQQaELWFCGPAAFGDAIRTDLCAQGLPAARFHQE 438
Cdd:cd06196   182 VTDFNQ-HFYVCGPPPMEEAINGALKELGVPEDSIVFE 218
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 252-440 2.67e-13

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: 69.51  E-value: 2.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 252 HEPGQF--AFVTFDEREGAHP--FTISSAWqDDGRLMFLIK--ALGDYTHSLAASLKLGDTVTVEGPYGRFQFDGPARRq 325
Cdd:cd06184    37 FLPGQYlsVRVKLPGLGYRQIrqYSLSDAP-NGDYYRISVKrePGGLVSNYLHDNVKVGDVLEVSAPAGDFVLDEASDRp 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 326 iwig-ggigISPFVARLKQLAQQSDGREIDLFHATSEVDETAL-QRLQQHAQA-AGVRLHLLIS-----------GRDGR 391
Cdd:cd06184   116 lvlisagvgITPMLSMLEALAAEGPGRPVTFIHAARNSAVHAFrDELEELAARlPNLKLHVFYSepeagdreedyDHAGR 195

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1082860120 392 LTGERLRALVPDwQQAELWFCGPAAFGDAIRTDLCAQGLPAARFHQELF 440
Cdd:cd06184   196 IDLALLRELLLP-ADADFYLCGPVPFMQAVREGLKALGVPAERIHYEVF 243
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 249-440 5.02e-13

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: 68.32  E-value: 5.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 249 WAGHEPGQFAFV--TFDEREGAHPFTISSAWQDDgRLMFLIKAL--GDYTHSLAASLKLGDTVTVEGPYGRFQFD-GPAR 323
Cdd:cd06191    25 QYGFRPGQHVTLklDFDGEELRRCYSLCSSPAPD-EISITVKRVpgGRVSNYLREHIQPGMTVEVMGPQGHFVYQpQPPG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 324 RQIWIGGGIGISPFVARLKQLAQQSDGREIDLFH-ATSEVDETALQRLQQHAQAAG----VRLHLLISGR----DGRLTG 394
Cdd:cd06191   104 RYLLVAAGSGITPLMAMIRATLQTAPESDFTLIHsARTPADMIFAQELRELADKPQrlrlLCIFTRETLDsdllHGRIDG 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1082860120 395 ER--LRALVPDWQQAELWFCGPAAFGDAIRTDLCAQGLPAARFHQELF 440
Cdd:cd06191   184 EQslGAALIPDRLEREAFICGPAGMMDAVETALKELGMPPERIHTERF 231
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 225-440 4.73e-12

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: 65.31  E-value: 4.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 225 GEIEQLEYLEGvkvNAVSIRLK---SQWAGHEPGQFAFVTFDEREGAHPFTISSAwQDDGRLMFLIKALGDYTHS--LAA 299
Cdd:cd06209     4 ATVTEVERLSD---STIGLTLEldeAGALAFLPGQYVNLQVPGTDETRSYSFSSA-PGDPRLEFLIRLLPGGAMSsyLRD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 300 SLKLGDTVTVEGPYGRFQFDGPARRQIWIGGGIGISPFVARLKQLAQQSDGREIDL-FHATSEVDETALQRLQQHAQA-A 377
Cdd:cd06209    80 RAQPGDRLTLTGPLGSFYLREVKRPLLMLAGGTGLAPFLSMLDVLAEDGSAHPVHLvYGVTRDADLVELDRLEALAERlP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082860120 378 GVRLHLLIS------GRDGRLTG--ERLRALVPDwqqAELWFCGPAAFGDAIRTDLCAQGLPAARFHQELF 440
Cdd:cd06209   160 GFSFRTVVAdpdswhPRKGYVTDhlEAEDLNDGD---VDVYLCGPPPMVDAVRSWLDEQGIEPANFYYEKF 227
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 239-440 5.03e-12

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: 65.37  E-value: 5.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 239 NAVSIRLK-SQW--AGHEPGQFAFVTFDEREGAH---PFTISSAWQDDGRLMFLIKALGDYTHS--LAASLKLGDTVTVE 310
Cdd:cd06217    15 TVKTFRLAvPDGvpPPFLAGQHVDLRLTAIDGYTaqrSYSIASSPTQRGRVELTVKRVPGGEVSpyLHDEVKVGDLLEVR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 311 GPYGRFQFDGPARRQIWIGGGIG-ISPFVARLKQLAQQSDGREIDLFHA---TSEV---DEtaLQRLQqhAQAAGVRLHL 383
Cdd:cd06217    95 GPIGTFTWNPLHGDPVVLLAGGSgIVPLMSMIRYRRDLGWPVPFRLLYSartAEDVifrDE--LEQLA--RRHPNLHVTE 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082860120 384 LIS--------GRDGRLTGERLRALVPDWQQAELWFCGPAAFGDAIRTDLCAQGLPAARFHQELF 440
Cdd:cd06217   171 ALTraapadwlGPAGRITADLIAELVPPLAGRRVYVCGPPAFVEAATRLLLELGVPRDRIRTEAF 235
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 241-436 2.51e-11

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: 62.95  E-value: 2.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 241 VSIRLKS-QWAGHEPGQFAFVTFDEREGAhPFTISSAWQDDGRLMFLIKAL--GDYTHSLAASLKLGDTVTVEGPYGRFQ 317
Cdd:cd06189    14 YRVRLKPpAPLDFLAGQYLDLLLDDGDKR-PFSIASAPHEDGEIELHIRAVpgGSFSDYVFEELKENGLVRIEGPLGDFF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 318 FDGPARRQIWigggigispFVAR----------LKQLAQQSDGREIDLF-HATSEVDETALQRLQQ-HAQAAGVRLHLLI 385
Cdd:cd06189    93 LREDSDRPLI---------LIAGgtgfapiksiLEHLLAQGSKRPIHLYwGARTEEDLYLDELLEAwAEAHPNFTYVPVL 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1082860120 386 S----GRDGRlTG---ERLRALVPDWQQAELWFCGPAAFGDAIRTDLCAQGLPAARFH 436
Cdd:cd06189   164 SepeeGWQGR-TGlvhEAVLEDFPDLSDFDVYACGSPEMVYAARDDFVEKGLPEENFF 220
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 254-440 7.67e-11

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: 61.94  E-value: 7.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 254 PGQFAFVTFDEREGAHPFTISSAWQDDGRLMFLIKAL--GDYTHSLAASLKLGDTVTVEGPYGRFQFDGPARRQIWIGGG 331
Cdd:cd06213    30 AGQYAELTLPGLPAARSYSFANAPQGDGQLSFHIRKVpgGAFSGWLFGADRTGERLTVRGPFGDFWLRPGDAPILCIAGG 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 332 IGISPFVARLKQLAQQSDGREIDL-FHATSEVDETALQRLQQHAQAAGVRLHLL-----------ISGRDGRLTgERLRA 399
Cdd:cd06213   110 SGLAPILAILEQARAAGTKRDVTLlFGARTQRDLYALDEIAAIAARWRGRFRFIpvlseepadssWKGARGLVT-EHIAE 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1082860120 400 LVpdWQQAELWFCGPAAFGDAIRTDLCAQGLPAARFHQELF 440
Cdd:cd06213   189 VL--LAATEAYLCGPPAMIDAAIAVLRALGIAREHIHADRF 227
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
254-440 2.06e-10

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 61.68  E-value: 2.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 254 PGQFAFVTFDEREGAHPFTISSAWQDDGRLMFLIKALGDYTHS--LAASLKLGDTVTVEGPYGRFQFDGPARRQIWIGGG 331
Cdd:PRK11872  139 PGQYARLQIPGTDDWRSYSFANRPNATNQLQFLIRLLPDGVMSnyLRERCQVGDEILFEAPLGAFYLREVERPLVFVAGG 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 332 IGISPFVARLKQLAQQSDGREIDLFHA-TSEVDETALQRLQQHAQA-AGVRLHLLIS-------GRDGRLTGERLRALVP 402
Cdd:PRK11872  219 TGLSAFLGMLDELAEQGCSPPVHLYYGvRHAADLCELQRLAAYAERlPNFRYHPVVSkasadwqGKRGYIHEHFDKAQLR 298

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1082860120 403 DwQQAELWFCGPAAFGDAIRTDLCAQGLPAARFHQELF 440
Cdd:PRK11872  299 D-QAFDMYLCGPPPMVEAVKQWLDEQALENYRLYYEKF 335
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 253-440 2.86e-10

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: 60.05  E-value: 2.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 253 EPGQFAFVTFDEREGAHPFTISSAWQDDGRLMFLIKAL--GDYTHSLAASLKLGDTVTVEGPYGRFQ-FDGPARRQIWIG 329
Cdd:cd06210    36 VPGQFVEIEIPGTDTRRSYSLANTPNWDGRLEFLIRLLpgGAFSTYLETRAKVGQRLNLRGPLGAFGlRENGLRPRWFVA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 330 GGIGISPFVARLKQLAQQSDGREIDL-FHATSEVDETALQRLQQHAQA-AGVRLHLLISGRDGRLTGER---LRALVPDW 404
Cdd:cd06210   116 GGTGLAPLLSMLRRMAEWGEPQEARLfFGVNTEAELFYLDELKRLADSlPNLTVRICVWRPGGEWEGYRgtvVDALREDL 195

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1082860120 405 QQA----ELWFCGPAAFGDAIRTDLCAQGLPAARFHQELF 440
Cdd:cd06210   196 ASSdakpDIYLCGPPGMVDAAFAAAREAGVPDEQVYLEKF 235
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 254-440 3.69e-10

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: 59.65  E-value: 3.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 254 PGQFAFVTFDEREGAHPFTISSAWQDDGRLMFLIKAL--GDYTHSLAASLKLGDTVTVEGPYGRFQF-DGPARRQIWIGG 330
Cdd:cd06212    32 AGQYVDITVPGTEETRSFSMANTPADPGRLEFIIKKYpgGLFSSFLDDGLAVGDPVTVTGPYGTCTLrESRDRPIVLIGG 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 331 GIGISPFVARLKQLAQQSDGREIDLFH-ATSEVDETALQRLQQHAQA-AGVRLHLLIS---------GRDGRLTgERLRA 399
Cdd:cd06212   112 GSGMAPLLSLLRDMAASGSDRPVRFFYgARTARDLFYLEEIAALGEKiPDFTFIPALSespddegwsGETGLVT-EVVQR 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1082860120 400 LVPDWQQAELWFCGPAAFGDAIRTDLCAQGLPAARFHQELF 440
Cdd:cd06212   191 NEATLAGCDVYLCGPPPMIDAALPVLEMSGVPPDQIFYDKF 231
PRK13289 PRK13289
NO-inducible flavohemoprotein;
336-440 3.29e-09

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 58.27  E-value: 3.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 336 PFVARLKQLAQQSDGREIDLFHATSEVDETAL-QRLQQHAQA-AGVRLHLLIS--------GRD----GRLTGERLRALV 401
Cdd:PRK13289  275 PMLSMLETLAAQQPKRPVHFIHAARNGGVHAFrDEVEALAARhPNLKAHTWYRepteqdraGEDfdseGLMDLEWLEAWL 354

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1082860120 402 PDwQQAELWFCGPAAFGDAIRTDLCAQGLPAARFHQELF 440
Cdd:PRK13289  355 PD-PDADFYFCGPVPFMQFVAKQLLELGVPEERIHYEFF 392
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 241-440 4.22e-09

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: 56.16  E-value: 4.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 241 VSIRLKSQWaGHEPGQFAFVTFDEREG---AHPFTISSAWQDD-GRLMFLIKAL-GDYTHSLAASLKLGD-----TVTVE 310
Cdd:cd06186    15 LTIPKPKPF-KWKPGQHVYLNFPSLLSfwqSHPFTIASSPEDEqDTLSLIIRAKkGFTTRLLRKALKSPGggvslKVLVE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 311 GPYGR-----FQFD---------GparrqiwigggigISPFVARLKQLAQQSDGRE----IDLF-----HATSEVDETAL 367
Cdd:cd06186    94 GPYGSssedlLSYDnvllvaggsG-------------ITFVLPILRDLLRRSSKTSrtrrVKLVwvvrdREDLEWFLDEL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082860120 368 QRLQQHAQAAGVRLHllisgrdgrLTGerlralVPdwqqaelwFCGPAAFGDAIRTDLCAQGLPAARFHQELF 440
Cdd:cd06186   161 RAAQELEVDGEIEIY---------VTR------VV--------VCGPPGLVDDVRNAVAKKGGTGVEFHEESF 210
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 254-422 1.28e-08

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: 55.34  E-value: 1.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 254 PGQFAFVTFDEREGAHPFTISSAWQDDGRLMFLIKAL--GDYTHSLAASLKLGDTVTVEGPYGR--FQFDGPaRRQIWIG 329
Cdd:cd06190    26 PGQYALLALPGVEGARAYSMANLANASGEWEFIIKRKpgGAASNALFDNLEPGDELELDGPYGLayLRPDED-RDIVCIA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 330 GGIGISPFVARLKQLAQQS--DGREIDLFH-ATSEVDETALQRLQQH-AQAAGVRLHLLIS-----------GRDGRLTG 394
Cdd:cd06190   105 GGSGLAPMLSILRGAARSPylSDRPVDLFYgGRTPSDLCALDELSALvALGARLRVTPAVSdagsgsaagwdGPTGFVHE 184

                         170       180
                  ....*....|....*....|....*...
gi 1082860120 395 ERLRALVPDWQQAELWFCGPAAFGDAIR 422
Cdd:cd06190   185 VVEATLGDRLAEFEFYFAGPPPMVDAVQ 212
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 252-315 3.24e-08

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: 54.15  E-value: 3.24e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082860120 252 HEPGQFAFVT-FDEREGahPFTISSAWQDDGRLMFLIKALGDYTHSLAAsLKLGDTVTVEGPYGR 315
Cdd:cd06221    28 FKPGQFVMLSlPGVGEA--PISISSDPTRRGPLELTIRRVGRVTEALHE-LKPGDTVGLRGPFGN 89
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 299-440 3.93e-08

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: 53.64  E-value: 3.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 299 ASLKLGDTVTVEGPYGRFQFDGPARRQIWIGGGIGISPFVARLKQLAQQsdGREIDLFHATSEVDETA-LQRLqqhAQAA 377
Cdd:cd06185    75 ELLRVGDELEVSAPRNLFPLDEAARRHLLIAGGIGITPILSMARALAAR--GADFELHYAGRSREDAAfLDEL---AALP 149

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1082860120 378 GVRLHLLISGRDGRLtgeRLRALVPDWQQ-AELWFCGPAAFGDAIRTDLCAQGLPAARFHQELF 440
Cdd:cd06185   150 GDRVHLHFDDEGGRL---DLAALLAAPPAgTHVYVCGPEGMMDAVRAAAAALGWPEARLHFERF 210
FAD_binding_8 pfam08022
FAD-binding domain;
239-314 2.56e-07

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 48.87  E-value: 2.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 239 NAVSIRLK--SQWAGHEPGQFAFVTFDEREG---AHPFTISSAWQDDgRLMFLIKALGDYT-----HSLAASLKLGD--- 305
Cdd:pfam08022  15 NVLKLRVSkpKKPFKYKPGQYMFINFLPPLSflqSHPFTITSAPSDD-KLSLHIKVKGGWTrklanYLSSSCPKSPEngk 93

                          90
                  ....*....|..
gi 1082860120 306 ---TVTVEGPYG 314
Cdd:pfam08022  94 dkpRVLIEGPYG 105
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 253-315 8.37e-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: 50.02  E-value: 8.37e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082860120 253 EPGQFAFVTFDEREG--AHPFTISSAWQDDGRLMFLIKALGDYTHSLAaSLKLGDTVTVEGPYGR 315
Cdd:cd06192    26 RPGQFVFLRNFESPGleRIPLSLAGVDPEEGTISLLVEIRGPKTKLIA-ELKPGEKLDVMGPLGN 89
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 44-178 1.21e-06

Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.


Pssm-ID: 426438 [Multi-domain]  Cd Length: 121  Bit Score: 47.26  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120  44 SGLLGMGVMSAAMLLAVRPAWLEhRLHGL--DKMYRLHKWLGIAGLVLAILHWLISQGPKWLIGAGLLERPVRGPRPLLT 121
Cdd:pfam01794   1 LGILALALLPLLLLLALRNNPLE-WLTGLsyDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSLEGILDLLLKRPYNIL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1082860120 122 DpVLAFLqsqrglaedlgekaFYLAVALIALALIKRFPYRHFFRTHRWIALAYLVLV 178
Cdd:pfam01794  80 G-IIALV--------------LLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 390-440 1.47e-06

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 50.09  E-value: 1.47e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1082860120 390 GRLTGERLRALVPDWQQAELWFCGPAAFGDAIRTDLCAQGLPAARFHQELF 440
Cdd:PRK10684  187 GRLTRELLQQAVPDLASRTVMTCGPAPYMDWVEQEVKALGVTADRFFKEKF 237
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 253-320 6.12e-05

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: 44.16  E-value: 6.12e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082860120 253 EPGQFAFVtFDEREGAHPFTISSAwqdDGRLMFLIKALGDYTHSLAaSLKLGDTVTVEGPYGR-FQFDG 320
Cdd:cd06220    25 KPGQFVMV-WVPGVDEIPMSLSYI---DGPNSITVKKVGEATSALH-DLKEGDKLGIRGPYGNgFELVG 88
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 205-316 7.63e-05

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: 43.85  E-value: 7.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 205 GTVAALISLTRRI-GVRRKAVGEIEqleylegvkvnavsIRLKsqwaghePGQFAFVTFDEREGAHPFTISSAWQDDGRL 283
Cdd:cd06211     9 GTVVEIEDLTPTIkGVRLKLDEPEE--------------IEFQ-------AGQYVNLQAPGYEGTRAFSIASSPSDAGEI 67

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1082860120 284 MFLIK-----ALGDYTHSlaaSLKLGDTVTVEGPYGRF 316
Cdd:cd06211    68 ELHIRlvpggIATTYVHK---QLKEGDELEISGPYGDF 102
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
254-318 3.83e-04

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 39.49  E-value: 3.83e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082860120 254 PGQFAFVTF--DEREGAHPFTISSAWQDDGRLMFLIKAL--GDYTHSLAaSLKLGDTVTVEGPYGRFQF 318
Cdd:pfam00970  32 VGQHLFLRLpiDGELVIRSYTPISSDDDKGYLELLVKVYpgGKMSQYLD-ELKIGDTIDFKGPLGRFEY 99
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 271-316 7.12e-04

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: 41.77  E-value: 7.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1082860120 271 FTISSAWQDDGRLMFLIK-ALGD----------YTHSLaaslKLGDTVTVEGPYGRF 316
Cdd:COG2871   203 YSMANYPAEKGIIELNIRiATPPmdvppgigssYIFSL----KPGDKVTISGPYGEF 255
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 253-362 9.42e-04

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 40.63  E-value: 9.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082860120 253 EPGQFAFV------TFDERegahPFTISSAwqDDGRLMFLIKALGDYThSLAASLKLGDTVTVEGPYGR-FQFDGPARRQ 325
Cdd:PRK00054   33 KPGQFVMVwvpgvePLLER----PISISDI--DKNEITILYRKVGEGT-KKLSKLKEGDELDIRGPLGNgFDLEEIGGKV 105

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1082860120 326 IWIGGGIGISPFVARLKQLAQQSDGREIDLFHATSEV 362
Cdd:PRK00054  106 LLVGGGIGVAPLYELAKELKKKGVEVTTVLGARTKDE 142
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 251-320 6.85e-03

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: 37.93  E-value: 6.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082860120 251 GHEPGQFAFVTF--DEREGAHPFT-ISSAwQDDGRLMFLIKAL--GDYTHSLAaSLKLGDTVTVEGPYGRFQFDG 320
Cdd:cd06183    28 GLPVGQHVELKApdDGEQVVRPYTpISPD-DDKGYFDLLIKIYpgGKMSQYLH-SLKPGDTVEIRGPFGKFEYKP 100
 
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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