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Conserved domains on  [gi|1720401304|ref|XP_030108113|]
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NADPH-dependent diflavin oxidoreductase 1 isoform X13 [Mus musculus]

Protein Classification

ferredoxin reductase domain-containing protein( domain architecture ID 835)

ferredoxin reductase (FNR) domain-containing protein may bind FAD and/or NAD(P)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FNR_like super family cl06868
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 59-366 3.11e-103

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).


The actual alignment was detected with superfamily member cd06207:

Pssm-ID: 447143 [Multi-domain]  Cd Length: 382  Bit Score: 313.44  E-value: 3.11e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304  59 PVITNQRVTGPQHFQDVRLIEFDITDSNISFAAGDVVFILPSNSEAHTQQFCQVLCLDPNQFFTLKPREPGVPDPPgLPQ 138
Cdd:cd06207     1 KVTENKRLTPADYDRSTRHIEFDLGGSGLSYETGDNLGIYPENSDALVDEFLARLGLDGDDVVRVEPNEQQRGKPP-FPE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 139 PCTVWNLVSQYLDIASVPRRSFFELLACLSQHALEREKLLELSSARGQEElweYCSRPRRTILEVLCDFPHTAgaIPPDY 218
Cdd:cd06207    80 PISVRQLLKKFLDIFGKPTKKFLKLLSQLATDEEEKEDLYKLASREGRTE---YKRYEKYTYLEVLKDFPSVR--PTLEQ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 219 LLDLIPRIRPRAFSIASSLLAHPRRLQILVAVVKYQTRLKEPRHGLCSSWLASLNPGQagpvRVPLWVRPGSLVFPKTPD 298
Cdd:cd06207   155 LLELCPLIKPRYYSISSSPLKNPNEVHLLVSLVSWKTPSGRSRYGLCSSYLAGLKVGQ----RVTVFIKKSSFKLPKDPK 230

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720401304 299 TPIIMVGAGTGVAPFRAAIQERVAHGQTGN-----FLFFGCRQRDQDFYWQTEWQKLEQKGWLT-LVTAFSREQ 366
Cdd:cd06207   231 KPIIMVGPGTGLAPFRAFLQERAALLAQGPeigpvLLYFGCRHEDKDYLYKEELEEYEKSGVLTtLGTAFSRDQ 304
 
Name Accession Description Interval E-value
CyPoR_like cd06207
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 59-366 3.11e-103

NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99803 [Multi-domain]  Cd Length: 382  Bit Score: 313.44  E-value: 3.11e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304  59 PVITNQRVTGPQHFQDVRLIEFDITDSNISFAAGDVVFILPSNSEAHTQQFCQVLCLDPNQFFTLKPREPGVPDPPgLPQ 138
Cdd:cd06207     1 KVTENKRLTPADYDRSTRHIEFDLGGSGLSYETGDNLGIYPENSDALVDEFLARLGLDGDDVVRVEPNEQQRGKPP-FPE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 139 PCTVWNLVSQYLDIASVPRRSFFELLACLSQHALEREKLLELSSARGQEElweYCSRPRRTILEVLCDFPHTAgaIPPDY 218
Cdd:cd06207    80 PISVRQLLKKFLDIFGKPTKKFLKLLSQLATDEEEKEDLYKLASREGRTE---YKRYEKYTYLEVLKDFPSVR--PTLEQ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 219 LLDLIPRIRPRAFSIASSLLAHPRRLQILVAVVKYQTRLKEPRHGLCSSWLASLNPGQagpvRVPLWVRPGSLVFPKTPD 298
Cdd:cd06207   155 LLELCPLIKPRYYSISSSPLKNPNEVHLLVSLVSWKTPSGRSRYGLCSSYLAGLKVGQ----RVTVFIKKSSFKLPKDPK 230

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720401304 299 TPIIMVGAGTGVAPFRAAIQERVAHGQTGN-----FLFFGCRQRDQDFYWQTEWQKLEQKGWLT-LVTAFSREQ 366
Cdd:cd06207   231 KPIIMVGPGTGLAPFRAFLQERAALLAQGPeigpvLLYFGCRHEDKDYLYKEELEEYEKSGVLTtLGTAFSRDQ 304
CysJ COG0369
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ...
 24-366 1.91e-86

Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases [Nucleotide transport and metabolism, Inorganic ion transport and metabolism]; Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440138 [Multi-domain]  Cd Length: 561  Bit Score: 275.49  E-value: 1.91e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304  24 IFQFLQEVPSIGAEELNIASsAPQTPPSELQPFLAPVITNQRVTGPQHFQDVRLIEFDITDSNISFAAGDVVFILPSNSE 103
Cdd:COG0369   166 VLAALAEALGAAAAAAAAAA-AAAPAYSRKNPFPATVLENRELTGRGSAKETRHIEIDLPGSGLSYEPGDALGVWPENDP 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 104 AHTQQFCQVLCLDPNQFFTLKPrepgvpdppglpQPCTVWNLVSQYLDIaSVPRRSFFELLACLSQHalerEKLLELSSA 183
Cdd:COG0369   245 ALVDELLARLGLDGDEPVTLDG------------EPLSLREALTEHLEL-TRLTPPLLEKYAELTGN----AELAALLAD 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 184 RGQEELWEYCSRprRTILEVLCDFPhtAGAIPPDYLLDLIPRIRPRAFSIASSLLAHPRRLQILVAVVKYQTRlKEPRHG 263
Cdd:COG0369   308 EDKAALREYLAG--RQLLDLLREFP--AAELSAEELLELLRPLTPRLYSISSSPKAHPDEVHLTVGVVRYEAS-GRERKG 382

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 264 LCSSWLASLNPGQagpvRVPLWVRPgSLVF--PKTPDTPIIMVGAGTGVAPFRAAIQERVAHGQTG-NFLFFGCRQRDQD 340
Cdd:COG0369   383 VASTYLADLEEGD----TVPVFVEP-NPNFrlPADPDTPIIMIGPGTGIAPFRAFLQEREARGASGkNWLFFGDRHFTTD 457

                         330       340
                  ....*....|....*....|....*..
gi 1720401304 341 FYWQTEWQKLEQKGWLT-LVTAFSREQ 366
Cdd:COG0369   458 FLYQTELQAWLKDGVLTrLDLAFSRDQ 484
cysJ TIGR01931
sulfite reductase [NADPH] flavoprotein, alpha-component; This model describes an ...
 51-366 2.07e-48

sulfite reductase [NADPH] flavoprotein, alpha-component; This model describes an NADPH-dependent sulfite reductase flavoprotein subunit. Most members of this family are found in Cys biosynthesis gene clusters. The closest homologs below the trusted cutoff are designated as subunits nitrate reductase.


Pssm-ID: 273882 [Multi-domain]  Cd Length: 597  Bit Score: 175.27  E-value: 2.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304  51 SELQPFLAPVITNQRVTGPQHFQDVRLIEFDITDSNISFAAGDVVFILPSNSEAHTQQFCQVLCLDPNQFFTLKprepgv 130
Cdd:TIGR01931 230 SKQNPFRAEVLENQKITGRNSKKDVRHIEIDLEGSGLHYEPGDALGVWYKNDPALVKEILKLLNLDPDEKVTIG------ 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 131 pdppGLPQPCTVWnLVSQYlDIaSVPRRSFFELLACLSQHalerEKLLELSSarGQEELWEYCSRprRTILEVLCDFPht 210
Cdd:TIGR01931 304 ----GKTIPLFEA-LITHF-EL-TQNTKPLLKAYAELTGN----KELKALIA--DNEKLKAYIQN--TPLIDLIRDYP-- 366

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 211 aGAIPPDYLLDLIPRIRPRAFSIASSLLAHPRRLQILVAVVKYQTRLKEpRHGLCSSWLAS-LNPGQAgpvrVPLWVRPG 289
Cdd:TIGR01931 367 -ADLDAEQLISLLRPLTPRLYSISSSQSEVGDEVHLTVGVVRYQAHGRA-RLGGASGFLAErLKEGDT----VPVYIEPN 440

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 290 S-LVFPKTPDTPIIMVGAGTGVAPFRAAIQERVAHGQTG-NFLFFGCRQRDQDFYWQTEWQKLEQKGWLT-LVTAFSREQ 366
Cdd:TIGR01931 441 DnFRLPEDPDTPIIMIGPGTGVAPFRAFMQERAEDGAKGkNWLFFGNPHFTTDFLYQVEWQNYLKKGVLTkMDLAFSRDQ 520
FAD_binding_1 pfam00667
FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, ...
 49-268 2.71e-46

FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, Nitric oxide synthase and methionine synthase reductase.


Pssm-ID: 395540 [Multi-domain]  Cd Length: 219  Bit Score: 160.20  E-value: 2.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304  49 PPSELQPFLAPVITNQRVTGPQHFQDVRLIEFDITDSNISFAAGDVVFILPSNSEAHTQQFCQVLCLDP--NQFFTLKPR 126
Cdd:pfam00667   1 PFDAKKPFTAPVLSNRELTSPSSDRNCIHVELDISGSGLTYQTGDHLGVYPPNNEELVEELLERLGLDPkpDTVVLLKTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 127 EPGVPDPpgLPQPCTVWNLVSQYLDIASVPRRSFFELLACLSQHALEREKLLELSSARGQEELWEYCSRPRRTILEVLCD 206
Cdd:pfam00667  81 DERVKPP--RLPPTTYRQALKYYLDITGPPSKQLLRLLAQFAPEEEEKQRLEFLSSDAGAREYKRWKLNHAPTLLEVLEE 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720401304 207 FPHTagAIPPDYLLDLIPRIRPRAFSIASSLLAHPRRLQILVAVVKYQTRLKEP-RHGLCSSW 268
Cdd:pfam00667 159 FPSV--KLPADFLLTQLPQLQPRYYSISSSSKVHPNEVHLTVVVVEYETDGEGRiHYGVCSNW 219
PRK06214 PRK06214
sulfite reductase subunit alpha;
55-367 3.95e-42

sulfite reductase subunit alpha;


Pssm-ID: 235745 [Multi-domain]  Cd Length: 530  Bit Score: 157.16  E-value: 3.95e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304  55 PFLAPVITNQRVTGPQHFQDVRLIEFDITDSNISFAAGDVVFILPSNSEAHTQQFCQVLCLDPNqfftlKPREPGvpdpp 134
Cdd:PRK06214  168 PVEATFLSRRRLNKPGSEKETWHVEIDLAGSGLDYEVGDSLGLFPANDPALVDAVIAALGAPPE-----FPIGGK----- 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 135 glpqpcTVWNLVSQYLDIASVPRrSFFELLACLSQHAlEREKLLELSS---ARGQEELWEycsrprrtILEVLCDFPhta 211
Cdd:PRK06214  238 ------TLREALLEDVSLGPAPD-GLFELLSYITGGA-ARKKARALAAgedPDGDAATLD--------VLAALEKFP--- 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 212 GAIP-PDYLLDLIPRIRPRAFSIASSLLAHPRRLQILVAVVKYQTRlKEPRHGLCSSWLAS-LNPGQagPVRVplWVRPG 289
Cdd:PRK06214  299 GIRPdPEAFVEALDPLQPRLYSISSSPKATPGRVSLTVDAVRYEIG-SRLRLGVASTFLGErLAPGT--RVRV--YVQKA 373

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 290 -SLVFPKTPDTPIIMVGAGTGVAPFRAAIQERVAHGQTG-NFLFFGCRQRDQDFYWQTEWQKLEQKGWLT-LVTAFSREQ 366
Cdd:PRK06214  374 hGFALPADPNTPIIMVGPGTGIAPFRAFLHERAATKAPGrNWLFFGHQRSATDFFYEDELNGLKAAGVLTrLSLAWSRDG 453


                  .
gi 1720401304 367 S 367
Cdd:PRK06214  454 E 454
 
Name Accession Description Interval E-value
CyPoR_like cd06207
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 59-366 3.11e-103

NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99803 [Multi-domain]  Cd Length: 382  Bit Score: 313.44  E-value: 3.11e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304  59 PVITNQRVTGPQHFQDVRLIEFDITDSNISFAAGDVVFILPSNSEAHTQQFCQVLCLDPNQFFTLKPREPGVPDPPgLPQ 138
Cdd:cd06207     1 KVTENKRLTPADYDRSTRHIEFDLGGSGLSYETGDNLGIYPENSDALVDEFLARLGLDGDDVVRVEPNEQQRGKPP-FPE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 139 PCTVWNLVSQYLDIASVPRRSFFELLACLSQHALEREKLLELSSARGQEElweYCSRPRRTILEVLCDFPHTAgaIPPDY 218
Cdd:cd06207    80 PISVRQLLKKFLDIFGKPTKKFLKLLSQLATDEEEKEDLYKLASREGRTE---YKRYEKYTYLEVLKDFPSVR--PTLEQ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 219 LLDLIPRIRPRAFSIASSLLAHPRRLQILVAVVKYQTRLKEPRHGLCSSWLASLNPGQagpvRVPLWVRPGSLVFPKTPD 298
Cdd:cd06207   155 LLELCPLIKPRYYSISSSPLKNPNEVHLLVSLVSWKTPSGRSRYGLCSSYLAGLKVGQ----RVTVFIKKSSFKLPKDPK 230

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720401304 299 TPIIMVGAGTGVAPFRAAIQERVAHGQTGN-----FLFFGCRQRDQDFYWQTEWQKLEQKGWLT-LVTAFSREQ 366
Cdd:cd06207   231 KPIIMVGPGTGLAPFRAFLQERAALLAQGPeigpvLLYFGCRHEDKDYLYKEELEEYEKSGVLTtLGTAFSRDQ 304
CysJ COG0369
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ...
 24-366 1.91e-86

Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases [Nucleotide transport and metabolism, Inorganic ion transport and metabolism]; Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440138 [Multi-domain]  Cd Length: 561  Bit Score: 275.49  E-value: 1.91e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304  24 IFQFLQEVPSIGAEELNIASsAPQTPPSELQPFLAPVITNQRVTGPQHFQDVRLIEFDITDSNISFAAGDVVFILPSNSE 103
Cdd:COG0369   166 VLAALAEALGAAAAAAAAAA-AAAPAYSRKNPFPATVLENRELTGRGSAKETRHIEIDLPGSGLSYEPGDALGVWPENDP 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 104 AHTQQFCQVLCLDPNQFFTLKPrepgvpdppglpQPCTVWNLVSQYLDIaSVPRRSFFELLACLSQHalerEKLLELSSA 183
Cdd:COG0369   245 ALVDELLARLGLDGDEPVTLDG------------EPLSLREALTEHLEL-TRLTPPLLEKYAELTGN----AELAALLAD 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 184 RGQEELWEYCSRprRTILEVLCDFPhtAGAIPPDYLLDLIPRIRPRAFSIASSLLAHPRRLQILVAVVKYQTRlKEPRHG 263
Cdd:COG0369   308 EDKAALREYLAG--RQLLDLLREFP--AAELSAEELLELLRPLTPRLYSISSSPKAHPDEVHLTVGVVRYEAS-GRERKG 382

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 264 LCSSWLASLNPGQagpvRVPLWVRPgSLVF--PKTPDTPIIMVGAGTGVAPFRAAIQERVAHGQTG-NFLFFGCRQRDQD 340
Cdd:COG0369   383 VASTYLADLEEGD----TVPVFVEP-NPNFrlPADPDTPIIMIGPGTGIAPFRAFLQEREARGASGkNWLFFGDRHFTTD 457

                         330       340
                  ....*....|....*....|....*..
gi 1720401304 341 FYWQTEWQKLEQKGWLT-LVTAFSREQ 366
Cdd:COG0369   458 FLYQTELQAWLKDGVLTrLDLAFSRDQ 484
CYPOR cd06204
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 54-368 2.50e-84

NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99801 [Multi-domain]  Cd Length: 416  Bit Score: 265.66  E-value: 2.50e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304  54 QPFLAPVITNQRV-TGPQhfQDVRLIEFDITDSNISFAAGDVVFILPSNSEAHTQQFCQVLCLD-PNQFFTLKPREPGVP 131
Cdd:cd06204     4 NPFLAPVAVSRELfTGSD--RSCLHIEFDISGSGIRYQTGDHLAVWPTNPSEEVERLLKVLGLDdRDTVISLKSLDEPAS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 132 DPPGLPQPCTVWNLVSQYLDIASVPRRSffeLLACLSQHA---LEREKLLELSSArGQEELWEYCSRPRRTILEVLCDFP 208
Cdd:cd06204    82 KKVPFPCPTTYRTALRHYLDITAPVSRQ---VLAALAQFApdpEEKERLLKLASE-GKDEYAKWIVEPHRNLLEVLQDFP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 209 HTAGAIPP-DYLLDLIPRIRPRAFSIASSLLAHPRRLQILVAVVKYQTRLKEPRHGLCSSWLASLNPGQAGP-------- 279
Cdd:cd06204   158 SAKPTPPPfDFLIELLPRLQPRYYSISSSSKVHPNRIHITAVVVKYPTPTGRIIKGVATNWLLALKPALNGEkpptpyyl 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 280 ---------VRVPLWVRPGSLVFPKTPDTPIIMVGAGTGVAPFRAAIQERVAHGQTGN-----FLFFGCRQRDQDFYWQT 345
Cdd:cd06204   238 sgprkkgggSKVPVFVRRSNFRLPTKPSTPVIMIGPGTGVAPFRGFIQERAALKESGKkvgptLLFFGCRHPDEDFIYKD 317

                         330       340
                  ....*....|....*....|....
gi 1720401304 346 EWQKLEQKGWLT-LVTAFSREQSS 368
Cdd:cd06204   318 ELEEYAKLGGLLeLVTAFSREQPK 341
SiR cd06199
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 60-366 3.49e-62

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


Pssm-ID: 99796 [Multi-domain]  Cd Length: 360  Bit Score: 206.31  E-value: 3.49e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304  60 VITNQRVTGPQHFQDVRLIEFDITDSNISFAAGDVVFILPSNSEAHTQQFCQVLCLDPNqfftlkprEPgVPDPPGlpQP 139
Cdd:cd06199     2 VLENRLLTGPGSEKETRHIELDLEGSGLSYEPGDALGVYPTNDPALVDELLAALGLSGD--------EP-VSTVGG--GT 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 140 CTVWNLVSQYLDIASVPRRsffeLLACLSQHALEREKLlelssARGQEELWEycsrPRRTILEVLCDFPHTAGAIPPDYL 219
Cdd:cd06199    71 LPLREALIKHYEITTLLLA----LLESYAADTGALELL-----ALAALEAVL----AFAELRDVLDLLPIPPARLTAEEL 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 220 LDLIPRIRPRAFSIASSLLAHPRRLQILVAVVKYQTRlKEPRHGLCSSWLAS-LNPGQagpvRVPLWVRPG-SLVFPKTP 297
Cdd:cd06199   138 LDLLRPLQPRLYSIASSPKAVPDEVHLTVAVVRYESH-GRERKGVASTFLADrLKEGD----TVPVFVQPNpHFRLPEDP 212

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720401304 298 DTPIIMVGAGTGVAPFRAAIQERVAHGQTG-NFLFFGCRQRDQDFYWQTEWQKLEQKGWLT-LVTAFSREQ 366
Cdd:cd06199   213 DAPIIMVGPGTGIAPFRAFLQEREATGAKGkNWLFFGERHFATDFLYQDELQQWLKDGVLTrLDTAFSRDQ 283
Nitric_oxide_synthase cd06202
The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses ...
 89-366 8.98e-53

The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses with a heme-containing N-terminal oxidase domain. The reductase portion is similar in structure to NADPH dependent cytochrome-450 reductase (CYPOR), having an inserted connecting sub-domain within the FAD binding portion of FNR. NOS differs from CYPOR in a requirement for the cofactor tetrahydrobiopterin and unlike most CYPOR is dimeric. Nitric oxide synthase produces nitric oxide in the conversion of L-arginine to L-citruline. NOS has been implicated in a variety of processes including cytotoxicity, anti-inflamation, neurotransmission, and vascular smooth muscle relaxation.


Pssm-ID: 99799 [Multi-domain]  Cd Length: 406  Bit Score: 182.92  E-value: 8.98e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304  89 FAAGDVVFILPSNSEAHTQQFCQVL--CLDPNQFF---TLKPREPGVP-----DPPGLPQPCTVWNLVSQYLDIASVPRR 158
Cdd:cd06202    32 YQPGDHVGIFPANRPELVDALLDRLhdAPPPDQVIkleVLEERSTALGiiktwTPHERLPPCTLRQALTRYLDITTPPTP 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 159 SFFELLACLSQHALEREKLLELSSARGQEELWEYCSRPrrTILEVLCDFPHTAgaIPPDYLLDLIPRIRPRAFSIASSLL 238
Cdd:cd06202   112 QLLQLLATLATDEKDKERLEVLGKGSSEYEDWKWYKNP--NILEVLEEFPSLQ--VPASLLLTQLPLLQPRYYSISSSPD 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 239 AHPRRLQILVAVVKYQTRL-KEP-RHGLCSSWLASLNPGQAgpvrVPLWVRpGSLVF--PKTPDTPIIMVGAGTGVAPFR 314
Cdd:cd06202   188 MYPGEIHLTVAVVSYRTRDgQGPvHHGVCSTWLNGLTPGDT----VPCFVR-SAPSFhlPEDPSVPVIMVGPGTGIAPFR 262

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720401304 315 AAIQER-----VAHGQTGNF----LFFGCRQRDQDFYWQTEWQKLEQKGWLTLV-TAFSREQ 366
Cdd:cd06202   263 SFWQQRqydlrMSEDPGKKFgdmtLFFGCRNSTIDDIYKEETEEAKNKGVLTEVyTALSREP 324
bifunctional_CYPOR cd06206
These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase ...
 85-364 2.52e-51

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: 178.61  E-value: 2.52e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304  85 SNISFAAGDVVFILPSNSEAHTQQFCQVLCLDPNQFFTLKPREPGVPDPPGlpQPCTVWNLVSQYLDIASVPRRSFFELL 164
Cdd:cd06206    26 DGMTYRAGDYLAVLPRNPPELVRRALRRFGLAWDTVLTISASGSATGLPLG--TPISVSELLSSYVELSQPATRRQLAAL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 165 ACLSQHALEREKLLELSSARGQEELweycSRPRRTILEVLCDFPhtAGAIPPDYLLDLIPRIRPRAFSIASSLLAHPRRL 244
Cdd:cd06206   104 AEATRCPDTKALLERLAGEAYAAEV----LAKRVSVLDLLERFP--SIALPLATFLAMLPPMRPRQYSISSSPLVDPGHA 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 245 QILVAVVKYQTRLKEPRH-GLCSSWLASLNPGQagpvRVPLWVRPGSLVF--PKTPDTPIIMVGAGTGVAPFRAAIQERV 321
Cdd:cd06206   178 TLTVSVLDAPALSGQGRYrGVASSYLSSLRPGD----SIHVSVRPSHSAFrpPSDPSTPLIMIAAGTGLAPFRGFLQERA 253

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1720401304 322 AHGQTG-----NFLFFGCRQRDQDFYWQTEWQKLEQKGWLTLVTAFSR 364
Cdd:cd06206   254 ALLAQGrklapALLFFGCRHPDHDDLYRDELEEWEAAGVVSVRRAYSR 301
methionine_synthase_red cd06203
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ...
 75-370 3.13e-51

Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for the regeneration of methionine from homocysteine, as well as the coversion of methyltetrahydrofolate to tetrahydrofolate. In MSR, electrons are transferred from NADPH to FAD to FMN to cob(II)alamin. MSR resembles proteins of the cytochrome p450 family including nitric oxide synthase, the alpha subunit of sulfite reductase, but contains an extended hinge region. 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. CYPORs resemble ferredoxin reductase (FNR) but have a connecting subdomain inserted within the flavin binding region, which helps orient the FMN binding doamin with the FNR module. 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: 99800 [Multi-domain]  Cd Length: 398  Bit Score: 178.67  E-value: 3.13e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304  75 VRLIEFDITDSNISFAAGDVVFILPSNSEAHTQQFCQVLCLDP--NQFFTLKPREPGVPD----PPGLPQPCTVWNLVSQ 148
Cdd:cd06203    17 VVDLTLDLSPTGFDYQPGDTIGILPPNTASEVESLLKRLGLLEqaDQPCEVKVVPNTKKKnakvPVHIPKVVTLRTILTW 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 149 YLDIASVPRRSFFELLACLSQHALEREKLLELSSARGQEELWEYCSRPRRTILEVLCDFPHTAgaiPP-DYLLDLIPRIR 227
Cdd:cd06203    97 CLDIRAIPKKPLLRALAEFTSDDNEKRRLEELCSKQGSEDYTDFVRKRGLSLLDLLEAFPSCR---PPlSLLIEHLPRLQ 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 228 PRAFSIASSLLAHPRRLQILVAVVkyqtrlKEPRHGLCSSWLASL-NPGQAGPVRVPLWVRPgSLVFPKTPD---TPIIM 303
Cdd:cd06203   174 PRPYSIASSPLEGPGKLRFIFSVV------EFPAKGLCTSWLESLcLSASSHGVKVPFYLRS-SSRFRLPPDdlrRPIIM 246

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720401304 304 VGAGTGVAPFRAAIQER----VAHGQTGN---FLFFGCRQRDQDFYWQTEWQKLEQKGWLT-LVTAFSREQSSWS 370
Cdd:cd06203   247 VGPGTGVAPFLGFLQHReklkESHTETVFgeaWLFFGCRHRDRDYLFRDELEEFLEEGILTrLIVAFSRDENDGS 321
cysJ TIGR01931
sulfite reductase [NADPH] flavoprotein, alpha-component; This model describes an ...
 51-366 2.07e-48

sulfite reductase [NADPH] flavoprotein, alpha-component; This model describes an NADPH-dependent sulfite reductase flavoprotein subunit. Most members of this family are found in Cys biosynthesis gene clusters. The closest homologs below the trusted cutoff are designated as subunits nitrate reductase.


Pssm-ID: 273882 [Multi-domain]  Cd Length: 597  Bit Score: 175.27  E-value: 2.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304  51 SELQPFLAPVITNQRVTGPQHFQDVRLIEFDITDSNISFAAGDVVFILPSNSEAHTQQFCQVLCLDPNQFFTLKprepgv 130
Cdd:TIGR01931 230 SKQNPFRAEVLENQKITGRNSKKDVRHIEIDLEGSGLHYEPGDALGVWYKNDPALVKEILKLLNLDPDEKVTIG------ 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 131 pdppGLPQPCTVWnLVSQYlDIaSVPRRSFFELLACLSQHalerEKLLELSSarGQEELWEYCSRprRTILEVLCDFPht 210
Cdd:TIGR01931 304 ----GKTIPLFEA-LITHF-EL-TQNTKPLLKAYAELTGN----KELKALIA--DNEKLKAYIQN--TPLIDLIRDYP-- 366

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 211 aGAIPPDYLLDLIPRIRPRAFSIASSLLAHPRRLQILVAVVKYQTRLKEpRHGLCSSWLAS-LNPGQAgpvrVPLWVRPG 289
Cdd:TIGR01931 367 -ADLDAEQLISLLRPLTPRLYSISSSQSEVGDEVHLTVGVVRYQAHGRA-RLGGASGFLAErLKEGDT----VPVYIEPN 440

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 290 S-LVFPKTPDTPIIMVGAGTGVAPFRAAIQERVAHGQTG-NFLFFGCRQRDQDFYWQTEWQKLEQKGWLT-LVTAFSREQ 366
Cdd:TIGR01931 441 DnFRLPEDPDTPIIMIGPGTGVAPFRAFMQERAEDGAKGkNWLFFGNPHFTTDFLYQVEWQNYLKKGVLTkMDLAFSRDQ 520
FAD_binding_1 pfam00667
FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, ...
 49-268 2.71e-46

FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, Nitric oxide synthase and methionine synthase reductase.


Pssm-ID: 395540 [Multi-domain]  Cd Length: 219  Bit Score: 160.20  E-value: 2.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304  49 PPSELQPFLAPVITNQRVTGPQHFQDVRLIEFDITDSNISFAAGDVVFILPSNSEAHTQQFCQVLCLDP--NQFFTLKPR 126
Cdd:pfam00667   1 PFDAKKPFTAPVLSNRELTSPSSDRNCIHVELDISGSGLTYQTGDHLGVYPPNNEELVEELLERLGLDPkpDTVVLLKTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 127 EPGVPDPpgLPQPCTVWNLVSQYLDIASVPRRSFFELLACLSQHALEREKLLELSSARGQEELWEYCSRPRRTILEVLCD 206
Cdd:pfam00667  81 DERVKPP--RLPPTTYRQALKYYLDITGPPSKQLLRLLAQFAPEEEEKQRLEFLSSDAGAREYKRWKLNHAPTLLEVLEE 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720401304 207 FPHTagAIPPDYLLDLIPRIRPRAFSIASSLLAHPRRLQILVAVVKYQTRLKEP-RHGLCSSW 268
Cdd:pfam00667 159 FPSV--KLPADFLLTQLPQLQPRYYSISSSSKVHPNEVHLTVVVVEYETDGEGRiHYGVCSNW 219
PRK06214 PRK06214
sulfite reductase subunit alpha;
55-367 3.95e-42

sulfite reductase subunit alpha;


Pssm-ID: 235745 [Multi-domain]  Cd Length: 530  Bit Score: 157.16  E-value: 3.95e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304  55 PFLAPVITNQRVTGPQHFQDVRLIEFDITDSNISFAAGDVVFILPSNSEAHTQQFCQVLCLDPNqfftlKPREPGvpdpp 134
Cdd:PRK06214  168 PVEATFLSRRRLNKPGSEKETWHVEIDLAGSGLDYEVGDSLGLFPANDPALVDAVIAALGAPPE-----FPIGGK----- 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 135 glpqpcTVWNLVSQYLDIASVPRrSFFELLACLSQHAlEREKLLELSS---ARGQEELWEycsrprrtILEVLCDFPhta 211
Cdd:PRK06214  238 ------TLREALLEDVSLGPAPD-GLFELLSYITGGA-ARKKARALAAgedPDGDAATLD--------VLAALEKFP--- 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 212 GAIP-PDYLLDLIPRIRPRAFSIASSLLAHPRRLQILVAVVKYQTRlKEPRHGLCSSWLAS-LNPGQagPVRVplWVRPG 289
Cdd:PRK06214  299 GIRPdPEAFVEALDPLQPRLYSISSSPKATPGRVSLTVDAVRYEIG-SRLRLGVASTFLGErLAPGT--RVRV--YVQKA 373

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 290 -SLVFPKTPDTPIIMVGAGTGVAPFRAAIQERVAHGQTG-NFLFFGCRQRDQDFYWQTEWQKLEQKGWLT-LVTAFSREQ 366
Cdd:PRK06214  374 hGFALPADPNTPIIMVGPGTGIAPFRAFLHERAATKAPGrNWLFFGHQRSATDFFYEDELNGLKAAGVLTrLSLAWSRDG 453


                  .
gi 1720401304 367 S 367
Cdd:PRK06214  454 E 454
CYPOR_like cd06182
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 196-367 5.74e-42

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: 150.18  E-value: 5.74e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 196 PRRTILEVLCDFPHTAGAIPPDYLLDLIP--RIRPRAFSIASSLLAHPRRLQILVAVVKYQTRLKEPRHGLCSSWLASLN 273
Cdd:cd06182    14 PRSTRHLEFDLSGNSVLKYQPGDHLGVIPpnPLQPRYYSIASSPDVDPGEVHLCVRVVSYEAPAGRIRKGVCSNFLAGLQ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 274 PGQAgpvrVPLWVRPG-SLVFPKTPDTPIIMVGAGTGVAPFRAAIQERVAHGQTG-----NFLFFGCRQRDQDFYWQTEW 347
Cdd:cd06182    94 LGAK----VTVFIRPApSFRLPKDPTTPIIMVGPGTGIAPFRGFLQERAALRANGkargpAWLFFGCRNFASDYLYREEL 169

                         170       180
                  ....*....|....*....|.
gi 1720401304 348 QKLEQKGWLT-LVTAFSREQS 367
Cdd:cd06182   170 QEALKDGALTrLDVAFSREQA 190
cysJ PRK10953
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;
29-366 3.18e-36

NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;


Pssm-ID: 182862 [Multi-domain]  Cd Length: 600  Bit Score: 141.40  E-value: 3.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304  29 QEVPSIGAEELNIASSA----PQTPPSELQPFLAPVITNQRVTGPQHFQDVRLIEFDITDSNISFAAGDVVFILPSNSEA 104
Cdd:PRK10953  207 SRAPAVAAPSQSVATGAvneiHTSPYSKEAPLTASLSVNQKITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWYQNDPA 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 105 HTQQFCQVLcldpnqffTLKPREPGVPDPPGLPqpctvwnlVSQYLdiasvprRSFFELLACLSQ-----HALER-EKLL 178
Cdd:PRK10953  287 LVKELVELL--------WLKGDEPVTVDGKTLP--------LAEAL-------QWHFELTVNTANivenyATLTRsETLL 343

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 179 ELSSARGQeeLWEYCSRprRTILEVLCDFPhtaGAIPPDYLLDLIPRIRPRAFSIASSLLAHPRRLQILVAVVKYQTRLK 258
Cdd:PRK10953  344 PLVGDKAA--LQHYAAT--TPIVDMVRFAP---AQLDAEQLIGLLRPLTPRLYSIASSQAEVENEVHITVGVVRYDIEGR 416

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 259 ePRHGLCSSWLASlNPGQAGPVRVplWVRPG-SLVFPKTPDTPIIMVGAGTGVAPFRAAIQERVAHGQTG-NFLFFGCRQ 336
Cdd:PRK10953  417 -ARAGGASSFLAD-RLEEEGEVRV--FIEHNdNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADGAPGkNWLFFGNPH 492

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1720401304 337 RDQDFYWQTEWQKLEQKGWLTLVT-AFSREQ 366
Cdd:PRK10953  493 FTEDFLYQVEWQRYVKEGLLTRIDlAWSRDQ 523
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 197-369 1.15e-22

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: 95.98  E-value: 1.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 197 RRTILEVLCDFPHTAGaippDYL---LDLIPRIRPRAFSIASSllahPRRLQILVAVVKYQtrlkepRHGLCSSWLASLN 273
Cdd:cd00322    11 RLFRLQLPNGFSFKPG----QYVdlhLPGDGRGLRRAYSIASS----PDEEGELELTVKIV------PGGPFSAWLHDLK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 274 PGQAGPVRVPLwvrpGSLVFPKTPDTPIIMVGAGTGVAPFRAAIQERVAHGQTGNF-LFFGCRQRDQDFYWQtEWQKLEQ 352
Cdd:cd00322    77 PGDEVEVSGPG----GDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGEItLLYGARTPADLLFLD-ELEELAK 151

                         170
                  ....*....|....*...
gi 1720401304 353 KGW-LTLVTAFSREQSSW 369
Cdd:cd00322   152 EGPnFRLVLALSRESEAK 169
SiR_like1 cd06200
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 219-366 2.82e-20

Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues, and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule, which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99797  Cd Length: 245  Bit Score: 89.64  E-value: 2.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 219 LLDLIPRIR--PRAFSIASslLAHPRRLQILVAvvkyQTRLKEPRHGLCSSWLASLNPGQAgpvRVPLWVRPGSLVFPKT 296
Cdd:cd06200    37 IAEIGPRHPlpHREYSIAS--LPADGALELLVR----QVRHADGGLGLGSGWLTRHAPIGA---SVALRLRENPGFHLPD 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720401304 297 PDTPIIMVGAGTGVAPFRAAIQERVAHGQTGNFLFFGCRQRDQDFYWQTEWQKLEQKGWLT-LVTAFSREQ 366
Cdd:cd06200   108 DGRPLILIGNGTGLAGLRSHLRARARAGRHRNWLLFGERQAAHDFFCREELEAWQAAGHLArLDLAFSRDQ 178
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
207-373 2.34e-17

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 80.99  E-value: 2.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 207 FPHTAGAippdYL---LDLIPRIRPRAFSIASSllAHPRRLQILVavvkyqtrLKEPrHGLCSSWLA-SLNPGQagpvrv 282
Cdd:COG1018    32 PRFRPGQ----FVtlrLPIDGKPLRRAYSLSSA--PGDGRLEITV--------KRVP-GGGGSNWLHdHLKVGD------ 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 283 PLWVRP--GSLVFPKTPDTPIIMVGAGTGVAPFRAAIQERVAHGQTGNF-LFFGCRQRDqDFYWQTEWQKLEQK-GWLTL 358
Cdd:COG1018    91 TLEVSGprGDFVLDPEPARPLLLIAGGIGITPFLSMLRTLLARGPFRPVtLVYGARSPA-DLAFRDELEALAARhPRLRL 169

                         170
                  ....*....|....*
gi 1720401304 359 VTAFSREQSSWSLRL 373
Cdd:COG1018   170 HPVLSREPAGLQGRL 184
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
 209-368 8.77e-17

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: 80.44  E-value: 8.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 209 HTAGAIPPDylLDLI---PRIrPRAFSIASSLLAHPRRLQILVAVVK----YQTRLKEPRHGLCSSWLASLNPGQ----A 277
Cdd:cd06208    45 QSIGIIPPG--TDAKngkPHK-LRLYSIASSRYGDDGDGKTLSLCVKrlvyTDPETDETKKGVCSNYLCDLKPGDdvqiT 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 278 GPVrvplwvrpGS-LVFPKTPDTPIIMVGAGTGVAPFRAAIQERVAHGQ-----TGNF-LFFGCRQRDQDFYwQTEWQKL 350
Cdd:cd06208   122 GPV--------GKtMLLPEDPNATLIMIATGTGIAPFRSFLRRLFREKHadykfTGLAwLFFGVPNSDSLLY-DDELEKY 192

                         170       180
                  ....*....|....*....|
gi 1720401304 351 EQK--GWLTLVTAFSREQSS 368
Cdd:cd06208   193 PKQypDNFRIDYAFSREQKN 212
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 212-368 7.27e-15

Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99798 [Multi-domain]  Cd Length: 289  Bit Score: 75.06  E-value: 7.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 212 GAIPPDYLLdliprirPRAFSIASSllahpRRLQILVAVVKYQTrlkeprHGLCSSWLASLNPGQagpvRVPLWVRPGSL 291
Cdd:cd06201    91 GILPPGSDV-------PRFYSLASS-----SSDGFLEICVRKHP------GGLCSGYLHGLKPGD----TIKAFIRPNPS 148

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720401304 292 VFPKTPDTPIIMVGAGTGVAPFRAAIqeRVAHGQTGNFLFFGCRQRDQDFYWQTEWQKLEQKGWLT-LVTAFSREQSS 368
Cdd:cd06201   149 FRPAKGAAPVILIGAGTGIAPLAGFI--RANAARRPMHLYWGGRDPASDFLYEDELDQYLADGRLTqLHTAFSRTPDG 224
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 225-375 9.37e-13

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: 67.98  E-value: 9.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 225 RIRpRAFSIASSllAHPRRLQILVAVVkyqtrlkepRHGLCSSWLASLNPGQAgpvrvpLWVRP---GSLVFPKTPDTP- 300
Cdd:cd06195    42 LVR-RAYSIASA--PYEENLEFYIILV---------PDGPLTPRLFKLKPGDT------IYVGKkptGFLTLDEVPPGKr 103

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720401304 301 IIMVGAGTGVAPFRAAIQERVAHGQTGNF-LFFGCRQRDqDFYWQTEWQKLEQK--GWLTLVTAFSREQSSWSLRLRI 375
Cdd:cd06195   104 LWLLATGTGIAPFLSMLRDLEIWERFDKIvLVHGVRYAE-ELAYQDEIEALAKQynGKFRYVPIVSREKENGALTGRI 180
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 228-370 2.56e-12

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: 68.35  E-value: 2.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 228 PRAFSIASsllaHPRRLQILVAVVKYQTRLKEPRHGLCSSWLASLNPGQagPVRV--P---LWVRPGslvfpktpDTPII 302
Cdd:COG2871   200 TRAYSMAN----YPAEKGIIELNIRIATPPMDVPPGIGSSYIFSLKPGD--KVTIsgPygeFFLRDS--------DREMV 265

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720401304 303 MVGAGTGVAPFRAAIQERVAHGQTGN--FLFFGCRQRdQDFYWQTEWQKLEQKgW--LTLVTAFSREQ--SSWS 370
Cdd:COG2871   266 FIGGGAGMAPLRSHIFDLLERGKTDRkiTFWYGARSL-RELFYLEEFRELEKE-HpnFKFHPALSEPLpeDNWD 337
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 303-380 4.95e-11

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: 59.58  E-value: 4.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 303 MVGAGTGVAPFRAAIQERVAHGQTGNF--LFFGCRQrDQDFYWQTEWQKLEQK--GWLTLVTAFSREQSSWS-LRLRILT 377
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILEDPKDPTQvvLVFGNRN-EDDILYREELDELAEKhpGRLTVVYVVSRPEAGWTgGKGRVQD 79


                  ...
gi 1720401304 378 SVL 380
Cdd:pfam00175  80 ALL 82
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 228-361 2.57e-10

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 60.65  E-value: 2.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 228 PRAFSIASSLlAHPRRLQILVAVVkyqtrlkeprhGLCSSWLASLNPGQAgpVRV--PLwvrpGSLVFPKTPDTPIIMVG 305
Cdd:COG0543    42 RRPFSIASAP-REDGTIELHIRVV-----------GKGTRALAELKPGDE--LDVrgPL----GNGFPLEDSGRPVLLVA 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720401304 306 AGTGVAPFRAAIQERVAHGQ--TgnfLFFGCRQRDqDFYWQTEwqkLEQKGWLTLVTA 361
Cdd:COG0543   104 GGTGLAPLRSLAEALLARGRrvT---LYLGARTPE-DLYLLDE---LEALADFRVVVT 154
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 198-372 3.79e-10

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: 59.87  E-value: 3.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 198 RTILEVLCDFPHTAGaippDYLLDLIPRIRPRAFSIASSllahPRR-----LQILVAVvkyqtrlkeprHGLCSS-WLAS 271
Cdd:cd06189    15 RVRLKPPAPLDFLAG----QYLDLLLDDGDKRPFSIASA----PHEdgeieLHIRAVP-----------GGSFSDyVFEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 272 LNPGqaGPVRV--PL---WVRPGSlvfpktpDTPIIMVGAGTGVAPFRAAIQERVAHGQTGN-FLFFGCRQRDqDFYWQT 345
Cdd:cd06189    76 LKEN--GLVRIegPLgdfFLREDS-------DRPLILIAGGTGFAPIKSILEHLLAQGSKRPiHLYWGARTEE-DLYLDE 145

                         170       180
                  ....*....|....*....|....*...
gi 1720401304 346 EWQKL-EQKGWLTLVTAFSREQSSWSLR 372
Cdd:cd06189   146 LLEAWaEAHPNFTYVPVLSEPEEGWQGR 173
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 225-372 5.30e-10

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: 59.53  E-value: 5.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 225 RIRPRAFSIASSllahPRRLQILVAVVKYqtrlkePRHGLCSSWLAS-LNPGQagPVRV--PLwvrpGSLVFPKTPDTPI 301
Cdd:cd06187    38 PRTWRAYSPANP----PNEDGEIEFHVRA------VPGGRVSNALHDeLKVGD--RVRLsgPY----GTFYLRRDHDRPV 101

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720401304 302 IMVGAGTGVAPFRAAIQERVAHGQTGNF-LFFGCRQRdQDFYWQTEWQKLEQK-GWLTLVTAFSREQSSWSLR 372
Cdd:cd06187   102 LCIAGGTGLAPLRAIVEDALRRGEPRPVhLFFGARTE-RDLYDLEGLLALAARhPWLRVVPVVSHEEGAWTGR 173
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
 229-368 7.92e-10

ferredoxin--NADP(+) reductase; Provisional


Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 60.40  E-value: 7.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 229 RAFSIASSLL---AHPRRLQILVAVVKYQTRLKEPRHGLCSSWLASLNPGQA----GPVrvplwvrPGSLVFPKTPDTPI 301
Cdd:PLN03115  146 RLYSIASSALgdfGDSKTVSLCVKRLVYTNDQGEIVKGVCSNFLCDLKPGAEvkitGPV-------GKEMLMPKDPNATI 218

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720401304 302 IMVGAGTGVAPFRAAI-----QERVAHGQTG-NFLFFGCRQRDQDFYwQTEWQKLEQKGW--LTLVTAFSREQSS 368
Cdd:PLN03115  219 IMLATGTGIAPFRSFLwkmffEKHDDYKFNGlAWLFLGVPTSSSLLY-KEEFEKMKEKAPenFRLDFAVSREQTN 292
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 229-365 1.50e-09

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: 58.05  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 229 RAFSIASSllahPRRLQILVAVVKyqtRLKEprhGLCSSWLAS-LNPGQAGPVRVPLwvrpGSLVFPKTPDTPIIMVGAG 307
Cdd:cd06217    51 RSYSIASS----PTQRGRVELTVK---RVPG---GEVSPYLHDeVKVGDLLEVRGPI----GTFTWNPLHGDPVVLLAGG 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 308 TGVAPFRAAIQERVAHGQTGNF-LFFGCRQRDqDFYWQTEWQKLE-QKGWLTLVTAFSRE 365
Cdd:cd06217   117 SGIVPLMSMIRYRRDLGWPVPFrLLYSARTAE-DVIFRDELEQLArRHPNLHVTEALTRA 175
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
 229-353 1.92e-09

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: 58.47  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 229 RAFSIASsllaHPRRLQILVAVVKYQT---RLKEPRHGLCSSWLASLNPGQagPVRVplwVRPGSLVFPKTPDTPIIMVG 305
Cdd:cd06188    87 RAYSLAN----YPAEEGELKLNVRIATpppGNSDIPPGIGSSYIFNLKPGD--KVTA---SGPFGEFFIKDTDREMVFIG 157

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720401304 306 AGTGVAPFRAAIQERVAHGQTGN--FLFFGCRQRDQDFYwQTEWQKLEQK 353
Cdd:cd06188   158 GGAGMAPLRSHIFHLLKTLKSKRkiSFWYGARSLKELFY-QEEFEALEKE 206
PLN03116 PLN03116
ferredoxin--NADP+ reductase; Provisional
 228-366 1.66e-08

ferredoxin--NADP+ reductase; Provisional


Pssm-ID: 215586 [Multi-domain]  Cd Length: 307  Bit Score: 55.88  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 228 PRAFSIASS-----LLAHPRRLQILVAV-VKYQTRLKEP-RHGLCSSWLASLNPGQ----AGPVrvplwvrpGS-LVFPK 295
Cdd:PLN03116   81 VRLYSIASTrygddFDGKTASLCVRRAVyYDPETGKEDPaKKGVCSNFLCDAKPGDkvqiTGPS--------GKvMLLPE 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 296 T-PDTPIIMVGAGTGVAPFRAAIQ----ERVAHGQTGN--FLFFGCRQRDQDFYwQTEWQKLEQK--GWLTLVTAFSREQ 366
Cdd:PLN03116  153 EdPNATHIMVATGTGIAPFRGFLRrmfmEDVPAFKFGGlaWLFLGVANSDSLLY-DDEFERYLKDypDNFRYDYALSREQ 231
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 229-365 2.49e-08

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: 54.54  E-value: 2.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 229 RAFSIASSLLAHPRRLQILVAVVKyqtrlkeprHGLCSSWLAS-LNPGQagpvRVPLWVRPGSLVFPKTPDTPIIMVGAG 307
Cdd:cd06216    65 RSYSLSSSPTQEDGTITLTVKAQP---------DGLVSNWLVNhLAPGD----VVELSQPQGDFVLPDPLPPRLLLIAAG 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 308 TGVAPFRAAIQERVAHGQTGNFLFFGC-RQRDqDFYWQTEWQKL-EQKGWLTLVTAFSRE 365
Cdd:cd06216   132 SGITPVMSMLRTLLARGPTADVVLLYYaRTRE-DVIFADELRALaAQHPNLRLHLLYTRE 190
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 229-363 2.12e-07

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: 51.95  E-value: 2.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 229 RAFSIASSllahPRRLQILVAVVKyqtrlKEPrHGLCSSWLAS-LNPGQAGPVRVPLwvrpGSLVFPKTPDTPIIMVGAG 307
Cdd:cd06212    47 RSFSMANT----PADPGRLEFIIK-----KYP-GGLFSSFLDDgLAVGDPVTVTGPY----GTCTLRESRDRPIVLIGGG 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720401304 308 TGVAPFRAAIQERVAHGQTGNF-LFFGCRQRDqDFYWQTEWQKLEQK-GWLTLVTAFS 363
Cdd:cd06212   113 SGMAPLLSLLRDMAASGSDRPVrFFYGARTAR-DLFYLEEIAALGEKiPDFTFIPALS 169
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 228-369 2.35e-07

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


Pssm-ID: 99807  Cd Length: 238  Bit Score: 51.56  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 228 PRAFSIASSllahPRRLQIlvavVKYQTRLKEprHGLCSSWL-ASLNPGQAGPVRVPLwvrpGSLVFPKTPDTPIIMVGA 306
Cdd:cd06211    52 TRAFSIASS----PSDAGE----IELHIRLVP--GGIATTYVhKQLKEGDELEISGPY----GDFFVRDSDQRPIIFIAG 117

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720401304 307 GTGVAPFRAAIQERVAHGQTGN-FLFFGCRQRDqDFYWQTEWQKLEQKgW--LTLVTAFSR--EQSSW 369
Cdd:cd06211   118 GSGLSSPRSMILDLLERGDTRKiTLFFGARTRA-ELYYLDEFEALEKD-HpnFKYVPALSRepPESNW 183
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 227-370 4.57e-07

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: 50.77  E-value: 4.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 227 RPRAFSIASSllahPRRLQILVAVVkyqtrlkepRH---GLCSSWL-ASLNPGQAGPVRVPL---WVRPGslvfpktpDT 299
Cdd:cd06213    43 AARSYSFANA----PQGDGQLSFHI---------RKvpgGAFSGWLfGADRTGERLTVRGPFgdfWLRPG--------DA 101

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720401304 300 PIIMVGAGTGVAPFRAAIQERVAHGQTGNF-LFFGCRQRdQDFYWQTEWQKLEQKGW--LTLVTAFSRE--QSSWS 370
Cdd:cd06213   102 PILCIAGGSGLAPILAILEQARAAGTKRDVtLLFGARTQ-RDLYALDEIAAIAARWRgrFRFIPVLSEEpaDSSWK 176
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 230-370 2.38e-05

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: 45.68  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 230 AFSIASSllahPRRLQILVAVVKyqtrlkepRHGLCSSWLASLNPGQAGPVRVPLwvrpGSlVFP--KTPDTPIIMVGAG 307
Cdd:cd06221    45 PISISSD----PTRRGPLELTIR--------RVGRVTEALHELKPGDTVGLRGPF----GN-GFPveEMKGKDLLLVAGG 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720401304 308 TGVAPFRAAIQERVAHGQT-GNF-LFFGCRQRDqDFYWQTEWQKLEQKGWLTLVTAFSREQSSWS 370
Cdd:cd06221   108 LGLAPLRSLINYILDNREDyGKVtLLYGARTPE-DLLFKEELKEWAKRSDVEVILTVDRAEEGWT 171
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 229-372 1.77e-04

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: 42.97  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 229 RAFSIASslLAHPRRLQILVavvkyqtRLKEprHGLCSSWLASL-NPGQAGPVRVPLwvrpGSLvFPKTPDTPIIMVGAG 307
Cdd:cd06209    48 RSYSFSS--APGDPRLEFLI-------RLLP--GGAMSSYLRDRaQPGDRLTLTGPL----GSF-YLREVKRPLLMLAGG 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 308 TGVAPFRAAIQERVAHGQTGNF-LFFGCRqRDQDFYwqtEWQKLE----QKGWLTLVTAFSREqSSWSLR 372
Cdd:cd06209   112 TGLAPFLSMLDVLAEDGSAHPVhLVYGVT-RDADLV---ELDRLEalaeRLPGFSFRTVVADP-DSWHPR 176
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 297-349 2.05e-04

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 43.32  E-value: 2.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720401304 297 PDTPIIMVGAGTGVAPFRAAIQERVAHGQTGN-FLFFGCRQRdQDFY---WQTEWQK 349
Cdd:PRK07609  203 SDKPIVLLASGTGFAPIKSIVEHLRAKGIQRPvTLYWGARRP-EDLYlsaLAEQWAE 258
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 300-353 8.35e-04

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: 40.70  E-value: 8.35e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720401304 300 PIIMVGAGTGVAPFRAAIQERVAHGQTGNFLFFGCRQRDQDFYWQTEWQKLEQK 353
Cdd:cd06198    97 RQIWIAGGIGITPFLALLEALAARGDARPVTLFYCVRDPEDAVFLDELRALAAA 150
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 236-369 1.45e-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: 40.24  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 236 SLLAHPRRLQILVavvkyqtrlKEPRHGLCSSWLASLNPGQA----GPVrvPLWVRPGSLVFPKtpdtpIIMVGAGTGVA 311
Cdd:cd06183    54 SPDDDKGYFDLLI---------KIYPGGKMSQYLHSLKPGDTveirGPF--GKFEYKPNGKVKH-----IGMIAGGTGIT 117

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720401304 312 PF----RAAIQERVAHGQTgnFLFFGCRQRDqDFYWQTEWQKLEQKG------WLTLvtafSREQSSW 369
Cdd:cd06183   118 PMlqliRAILKDPEDKTKI--SLLYANRTEE-DILLREELDELAKKHpdrfkvHYVL----SRPPEGW 178
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 228-350 9.83e-03

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: 37.63  E-value: 9.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401304 228 PRAFSIASsLLAHPRRLQILVAVVkyqtrlkepRHGLCSSWLASL-NPGQAGPVRVPLwvrpGSLVFPKTP-DTPIIMVG 305
Cdd:cd06194    39 ARSYSPTS-LPDGDNELEFHIRRK---------PNGAFSGWLGEEaRPGHALRLQGPF----GQAFYRPEYgEGPLLLVG 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720401304 306 AGTGVAPFRAAIQERVAHGQTGN-FLFFGCRQRDqDFYWQTEWQKL 350
Cdd:cd06194   105 AGTGLAPLWGIARAALRQGHQGEiRLVHGARDPD-DLYLHPALLWL 149
 
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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