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Conserved domains on  [gi|1308985323|gb|PKO90608|]
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oxidoreductase [Betaproteobacteria bacterium HGW-Betaproteobacteria-12]

Protein Classification

flavin reductase family protein( domain architecture ID 10786044)

flavin reductase family protein containing an N-terminal NAD(P) binding domain of flavin oxidoreductase-like proteins and a C-terminal 2Fe-2S iron-sulfur cluster binding domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 110-339 5.57e-97

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: 286.84  E-value: 5.57e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 110 FIDRKALTPDISLFTFASDGPAEFLAGQYAMIGIPALSQARAYSMSNIANEEGIWQFIIRRVPEGKVTAYLFDRLRLGDQ 189
Cdd:cd06190     1 LVDVRELTHDVAEFRFALDGPADFLPGQYALLALPGVEGARAYSMANLANASGEWEFIIKRKPGGAASNALFDNLEPGDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 190 LDLDGPYGIAYLRTDVTRPIVGIAGGSGLAPVLSVLQGAARSRCANGARPAMLYGGRTPTDIP--DVRQMATEAGIEVDF 267
Cdd:cd06190    81 LELDGPYGLAYLRPDEDRDIVCIAGGSGLAPMLSILRGAARSPYLSDRPVDLFYGGRTPSDLCalDELSALVALGARLRV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308985323 268 HPVISAPVNGVSVEWRGDIGFVHEFIAKKLAAPLPGYEYYLAGPPPMIEAAVRLLVAEHKVPTTQIHFDRFF 339
Cdd:cd06190   161 TPAVSDAGSGSAAGWDGPTGFVHEVVEATLGDRLAEFEFYFAGPPPMVDAVQRMLMIEGVVPFDQIHFDRFV 232
Fdx COG0633
Ferredoxin [Energy production and conversion];
6-92 3.17e-24

Ferredoxin [Energy production and conversion];


:

Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 94.53  E-value: 3.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323   6 RISLSGSETTYTGNTGDTLLRAGLRQGLGLAYECNVGACGSCKFDLIAGEVDDLfpEASGLRPKEREKGKRLACQCVPRS 85
Cdd:COG0633     3 KVTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHR--EEDALSDEERAAGSRLACQARPTS 80


                  ....*..
gi 1308985323  86 DCTIKIR 92
Cdd:COG0633    81 DLVVELP 87
 
Name Accession Description Interval E-value
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 110-339 5.57e-97

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: 286.84  E-value: 5.57e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 110 FIDRKALTPDISLFTFASDGPAEFLAGQYAMIGIPALSQARAYSMSNIANEEGIWQFIIRRVPEGKVTAYLFDRLRLGDQ 189
Cdd:cd06190     1 LVDVRELTHDVAEFRFALDGPADFLPGQYALLALPGVEGARAYSMANLANASGEWEFIIKRKPGGAASNALFDNLEPGDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 190 LDLDGPYGIAYLRTDVTRPIVGIAGGSGLAPVLSVLQGAARSRCANGARPAMLYGGRTPTDIP--DVRQMATEAGIEVDF 267
Cdd:cd06190    81 LELDGPYGLAYLRPDEDRDIVCIAGGSGLAPMLSILRGAARSPYLSDRPVDLFYGGRTPSDLCalDELSALVALGARLRV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308985323 268 HPVISAPVNGVSVEWRGDIGFVHEFIAKKLAAPLPGYEYYLAGPPPMIEAAVRLLVAEHKVPTTQIHFDRFF 339
Cdd:cd06190   161 TPAVSDAGSGSAAGWDGPTGFVHEVVEATLGDRLAEFEFYFAGPPPMVDAVQRMLMIEGVVPFDQIHFDRFV 232
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 4-339 7.36e-75

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: 235.91  E-value: 7.36e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323   4 SFRISLSGSETTYTGNTGDTLLRAGLRQGLGLAYECN-VGACGSCKFDLIAGEVDDLFPEASGLRPKEREKGKRLACQCV 82
Cdd:COG2871    34 EVKITINGDGKEIEVEEGQTLLDALLRQGIFLPSACGgGGTCGQCKVKVLEGGGDILPTETFHLSDRERKEGYRLACQVK 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323  83 PRSDCTIKIrsgDEylSAIPPARFKARFIDRKALTPDISLFTFASDGPAE--FLAGQYAMIGIPAL-------------- 146
Cdd:COG2871   114 VKSDMEIEV---PE--EVFGVKKWEATVVSNENVTTFIKELVLELPEGEEidFKAGQYIQIEVPPYevdfkdfdipeeek 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 147 ---------SQARAYSMSNIANEEGIWQFIIR------RVPEGKVTAYLFDrLRLGDQLDLDGPYGIAYLRtDVTRPIVG 211
Cdd:COG2871   189 fglfdkndeEVTRAYSMANYPAEKGIIELNIRiatppmDVPPGIGSSYIFS-LKPGDKVTISGPYGEFFLR-DSDREMVF 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 212 IAGGSGLAPVLSVLQGAARSRCANgaRPA-MLYGGRTPTDI---PDVRQMATEAGiEVDFHPVISAPVNGvsVEWRGDIG 287
Cdd:COG2871   267 IGGGAGMAPLRSHIFDLLERGKTD--RKItFWYGARSLRELfylEEFRELEKEHP-NFKFHPALSEPLPE--DNWDGETG 341

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1308985323 288 FVHEFIAKKLAAPLP---GYEYYLAGPPPMIEAAVRLLvAEHKVPTTQIHFDRFF 339
Cdd:COG2871   342 FIHEVLYENYLKDHPapeDCEAYLCGPPPMIDAVIKML-DDLGVEEENIYFDDFG 395
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 4-338 1.97e-59

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 194.32  E-value: 1.97e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323   4 SFRISLSGSETTYTGNTGDTLLRAGLRQGLGLAYECNVGACGSCKFDLIAGEVDDLFPEASGLRPKEREKGKRLACQCVP 83
Cdd:PRK07609    2 SFQVTLQPSGRQFTAEPDETILDAALRQGIHLPYGCKNGACGSCKGRLLEGEVEQGPHQASALSGEERAAGEALTCCAKP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323  84 RSDCTIKIRsgdEY--LSAIPPARFKARFIDRKALTPD---ISLFTFASDgPAEFLAGQYAMIgIPALSQARAYSMSNIA 158
Cdd:PRK07609   82 LSDLVLEAR---EVpaLGDIPVKKLPCRVASLERVAGDvmrLKLRLPATE-RLQYLAGQYIEF-ILKDGKRRSYSIANAP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 159 NEEGIWQFIIRRVPEGKVTAYLFDRLRLGDQLDLDGPYGIAYLRTDVTRPIVGIAGGSGLAPVLSVLQGAARSRCangAR 238
Cdd:PRK07609  157 HSGGPLELHIRHMPGGVFTDHVFGALKERDILRIEGPLGTFFLREDSDKPIVLLASGTGFAPIKSIVEHLRAKGI---QR 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 239 PAMLY-GGRTPTD---IPDVRQMATEAGiEVDFHPVISAPVNgvSVEWRGDIGFVHEFIAKKLAApLPGYEYYLAGPPPM 314
Cdd:PRK07609  234 PVTLYwGARRPEDlylSALAEQWAEELP-NFRYVPVVSDALD--DDAWTGRTGFVHQAVLEDFPD-LSGHQVYACGSPVM 309

                         330       340
                  ....*....|....*....|....
gi 1308985323 315 IEAAVRLLVaEHKVPTTQIHFDRF 338
Cdd:PRK07609  310 VYAARDDFV-AAGLPAEEFFADAF 332
BenC NF040810
benzoate 1,2-dioxygenase electron transfer component BenC;
19-338 3.92e-51

benzoate 1,2-dioxygenase electron transfer component BenC;


Pssm-ID: 468751 [Multi-domain]  Cd Length: 333  Bit Score: 172.70  E-value: 3.92e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323  19 NTGDTLLRAGLRQGLGLAYECNVGACGSCK-------FDLiaGevDDLFPEAsgLRPKEREKGKRLACQCVPRSDCTIKI 91
Cdd:NF040810   18 NAGETVLDAAYRQKINIPMDCRDGACGTCKcrcesgsYDL--G--DDYIEDA--LTEEEAAQGYVLTCQMVPQSDCVIRV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323  92 RSGDEyLSAIPPARFKARFIDRKALTPDISLFTFASDGPAE--FLAGQYAMIGIPALSQARAYSMSNIANEEGIwQFIIR 169
Cdd:NF040810   92 PASSA-ACKTGQATFEATVAAVEQLSDSTIELSLDLDDDAAlaFLPGQYVNIQVPGTGQTRSYSFSSLPGAREA-SFLIR 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 170 RVPEGKVTAYLFDRLRLGDQLDLDGPYGIAYLRtDVTRPIVGIAGGSGLAPVLSVLQGAARSRCANGARpaMLYGGRTPT 249
Cdd:NF040810  170 NVPGGLMSSYLTERAKPGDRLSLTGPLGSFYLR-EVTRPLLMLAGGTGLAPFLSMLEVLAEQGSEQPVH--LIYGVTRDA 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 250 DIPDVRQM-ATEAGIE-VDFHPVISAPVNGVSVEwrgdiGFVHEFIAkklAAPLPGYEY--YLAGPPPMIEaAVRLLVAE 325
Cdd:NF040810  247 DLVEVERLeAFAARLPnFTFRTCVADAASAHPRK-----GYVTQHIE---AEWLNDGDVdvYLCGPPPMVD-AVRGWFRE 317

                         330
                  ....*....|...
gi 1308985323 326 HKVPTTQIHFDRF 338
Cdd:NF040810  318 QGITPASFHYEKF 330
Fdx COG0633
Ferredoxin [Energy production and conversion];
6-92 3.17e-24

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 94.53  E-value: 3.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323   6 RISLSGSETTYTGNTGDTLLRAGLRQGLGLAYECNVGACGSCKFDLIAGEVDDLfpEASGLRPKEREKGKRLACQCVPRS 85
Cdd:COG0633     3 KVTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHR--EEDALSDEERAAGSRLACQARPTS 80


                  ....*..
gi 1308985323  86 DCTIKIR 92
Cdd:COG0633    81 DLVVELP 87
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 6-90 2.00e-21

2Fe-2S iron-sulfur cluster 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). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 86.68  E-value: 2.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323   6 RISLSGSETTYTGNTGDTLLRAGLRQGLGLAYECNVGACGSCKFDLIAGEVDDLfpEASGLRPKEREKGKRLACQCVPRS 85
Cdd:cd00207     2 TINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQS--DPSLLDEEEAEGGYVLACQTRVTD 79


                  ....*
gi 1308985323  86 DCTIK 90
Cdd:cd00207    80 GLVIE 84
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
107-197 4.31e-16

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 72.61  E-value: 4.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 107 KARFIDRKALTPDISLFTFASDGPAE---FLAGQYAMIGIPALSQA--RAYSMSNIANEEGIWQFIIRRVPEGKVTAYLf 181
Cdd:pfam00970   1 PLTLVEKELVSHDTRIFRFALPHPDQvlgLPVGQHLFLRLPIDGELviRSYTPISSDDDKGYLELLVKVYPGGKMSQYL- 79

                          90
                  ....*....|....*.
gi 1308985323 182 DRLRLGDQLDLDGPYG 197
Cdd:pfam00970  80 DELKIGDTIDFKGPLG 95
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
9-84 1.89e-12

2Fe-2S iron-sulfur cluster binding domain;


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 62.16  E-value: 1.89e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308985323   9 LSGSETTYTGNTGDT-LLRAGLRQGLGLAYECNVGACGSCKFDLIAGEVDDlfpEASGLRPKEREKGK-RLACQCVPR 84
Cdd:pfam00111   3 INGKGVTIEVPDGETtLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQS---DQSFLEDDELAAGYvVLACQTYPK 77
PTZ00038 PTZ00038
ferredoxin; Provisional
 24-96 4.56e-11

ferredoxin; Provisional


Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 61.01  E-value: 4.56e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308985323  24 LLRAGLRQGLGLAYECNVGACGSCKFDLIAGEVDDlfPEASGLRPKEREKGKRLACQCVPRSDCTIKIRSGDE 96
Cdd:PTZ00038  117 ILDAAERQGVELPYSCRGGSCSTCAAKLLEGEVDN--EDQSYLDDEQLKKGYCLLCTCYPKSDCTIETHKEDE 187
fdx_plant TIGR02008
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ...
 3-96 7.04e-10

ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ferredoxins. In general, these occur as a single domain proteins or with a chloroplast transit peptide. Species tend to be photosynthetic, but several forms may occur in one species and individually may not be associated with photocynthesis. Halobacterial forms differ somewhat in architecture; they score between trusted and noise cutoffs. Sequences scoring below the noise cutoff tend to be ferredoxin-related domains of larger proteins.


Pssm-ID: 273926 [Multi-domain]  Cd Length: 97  Bit Score: 55.54  E-value: 7.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323   3 ESFRISL---SGSETTYTGNTGDTLLRAGLRQGLGLAYECNVGACGSCKFDLIAGEVDDlfPEASGLRPKEREKGKRLAC 79
Cdd:TIGR02008   1 ATYKVTLvnpDGGEETIECPDDQYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQ--SDQSFLDDDQMEAGYVLTC 78

                          90
                  ....*....|....*..
gi 1308985323  80 QCVPRSDCTIKIRSGDE 96
Cdd:TIGR02008  79 VAYPTSDCTIETHKEED 95
 
Name Accession Description Interval E-value
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 110-339 5.57e-97

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: 286.84  E-value: 5.57e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 110 FIDRKALTPDISLFTFASDGPAEFLAGQYAMIGIPALSQARAYSMSNIANEEGIWQFIIRRVPEGKVTAYLFDRLRLGDQ 189
Cdd:cd06190     1 LVDVRELTHDVAEFRFALDGPADFLPGQYALLALPGVEGARAYSMANLANASGEWEFIIKRKPGGAASNALFDNLEPGDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 190 LDLDGPYGIAYLRTDVTRPIVGIAGGSGLAPVLSVLQGAARSRCANGARPAMLYGGRTPTDIP--DVRQMATEAGIEVDF 267
Cdd:cd06190    81 LELDGPYGLAYLRPDEDRDIVCIAGGSGLAPMLSILRGAARSPYLSDRPVDLFYGGRTPSDLCalDELSALVALGARLRV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308985323 268 HPVISAPVNGVSVEWRGDIGFVHEFIAKKLAAPLPGYEYYLAGPPPMIEAAVRLLVAEHKVPTTQIHFDRFF 339
Cdd:cd06190   161 TPAVSDAGSGSAAGWDGPTGFVHEVVEATLGDRLAEFEFYFAGPPPMVDAVQRMLMIEGVVPFDQIHFDRFV 232
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 4-339 7.36e-75

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: 235.91  E-value: 7.36e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323   4 SFRISLSGSETTYTGNTGDTLLRAGLRQGLGLAYECN-VGACGSCKFDLIAGEVDDLFPEASGLRPKEREKGKRLACQCV 82
Cdd:COG2871    34 EVKITINGDGKEIEVEEGQTLLDALLRQGIFLPSACGgGGTCGQCKVKVLEGGGDILPTETFHLSDRERKEGYRLACQVK 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323  83 PRSDCTIKIrsgDEylSAIPPARFKARFIDRKALTPDISLFTFASDGPAE--FLAGQYAMIGIPAL-------------- 146
Cdd:COG2871   114 VKSDMEIEV---PE--EVFGVKKWEATVVSNENVTTFIKELVLELPEGEEidFKAGQYIQIEVPPYevdfkdfdipeeek 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 147 ---------SQARAYSMSNIANEEGIWQFIIR------RVPEGKVTAYLFDrLRLGDQLDLDGPYGIAYLRtDVTRPIVG 211
Cdd:COG2871   189 fglfdkndeEVTRAYSMANYPAEKGIIELNIRiatppmDVPPGIGSSYIFS-LKPGDKVTISGPYGEFFLR-DSDREMVF 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 212 IAGGSGLAPVLSVLQGAARSRCANgaRPA-MLYGGRTPTDI---PDVRQMATEAGiEVDFHPVISAPVNGvsVEWRGDIG 287
Cdd:COG2871   267 IGGGAGMAPLRSHIFDLLERGKTD--RKItFWYGARSLRELfylEEFRELEKEHP-NFKFHPALSEPLPE--DNWDGETG 341

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1308985323 288 FVHEFIAKKLAAPLP---GYEYYLAGPPPMIEAAVRLLvAEHKVPTTQIHFDRFF 339
Cdd:COG2871   342 FIHEVLYENYLKDHPapeDCEAYLCGPPPMIDAVIKML-DDLGVEEENIYFDDFG 395
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 114-338 1.20e-59

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: 191.27  E-value: 1.20e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 114 KALTPDISLFTFASDGPAEFLAGQYAMIGIPAL-SQARAYSMSNIANEEGIWQFIIRRVPEGKVTAYLFDRLRLGDQLDL 192
Cdd:cd06187     5 ERLTHDIAVVRLQLDQPLPFWAGQYVNVTVPGRpRTWRAYSPANPPNEDGEIEFHVRAVPGGRVSNALHDELKVGDRVRL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 193 DGPYGIAYLRTDVTRPIVGIAGGSGLAPVLSVLQGAARSrcanGARP--AMLYGGRTPTDI---PDVRQMATEAGiEVDF 267
Cdd:cd06187    85 SGPYGTFYLRRDHDRPVLCIAGGTGLAPLRAIVEDALRR----GEPRpvHLFFGARTERDLydlEGLLALAARHP-WLRV 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308985323 268 HPVISAPVNGvsveWRGDIGFVHEFIAKKLAApLPGYEYYLAGPPPMIEAAVRLLVAEhKVPTTQIHFDRF 338
Cdd:cd06187   160 VPVVSHEEGA----WTGRRGLVTDVVGRDGPD-WADHDIYICGPPAMVDATVDALLAR-GAPPERIHFDKF 224
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 4-338 1.97e-59

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 194.32  E-value: 1.97e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323   4 SFRISLSGSETTYTGNTGDTLLRAGLRQGLGLAYECNVGACGSCKFDLIAGEVDDLFPEASGLRPKEREKGKRLACQCVP 83
Cdd:PRK07609    2 SFQVTLQPSGRQFTAEPDETILDAALRQGIHLPYGCKNGACGSCKGRLLEGEVEQGPHQASALSGEERAAGEALTCCAKP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323  84 RSDCTIKIRsgdEY--LSAIPPARFKARFIDRKALTPD---ISLFTFASDgPAEFLAGQYAMIgIPALSQARAYSMSNIA 158
Cdd:PRK07609   82 LSDLVLEAR---EVpaLGDIPVKKLPCRVASLERVAGDvmrLKLRLPATE-RLQYLAGQYIEF-ILKDGKRRSYSIANAP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 159 NEEGIWQFIIRRVPEGKVTAYLFDRLRLGDQLDLDGPYGIAYLRTDVTRPIVGIAGGSGLAPVLSVLQGAARSRCangAR 238
Cdd:PRK07609  157 HSGGPLELHIRHMPGGVFTDHVFGALKERDILRIEGPLGTFFLREDSDKPIVLLASGTGFAPIKSIVEHLRAKGI---QR 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 239 PAMLY-GGRTPTD---IPDVRQMATEAGiEVDFHPVISAPVNgvSVEWRGDIGFVHEFIAKKLAApLPGYEYYLAGPPPM 314
Cdd:PRK07609  234 PVTLYwGARRPEDlylSALAEQWAEELP-NFRYVPVVSDALD--DDAWTGRTGFVHQAVLEDFPD-LSGHQVYACGSPVM 309

                         330       340
                  ....*....|....*....|....
gi 1308985323 315 IEAAVRLLVaEHKVPTTQIHFDRF 338
Cdd:PRK07609  310 VYAARDDFV-AAGLPAEEFFADAF 332
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 106-338 1.17e-55

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: 180.97  E-value: 1.17e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 106 FKARFIDRKALTPDISLFTFASDGPAEFLAGQYAMIGIPALSQARAYSMSNIANEEGIWQFIIRRVPEGKVTAYLFDRLR 185
Cdd:cd06213     1 IRGTIVAQERLTHDIVRLTVQLDRPIAYKAGQYAELTLPGLPAARSYSFANAPQGDGQLSFHIRKVPGGAFSGWLFGADR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 186 LGDQLDLDGPYGIAYLRtDVTRPIVGIAGGSGLAPVLSVLQGAARSRCangARPA-MLYGGRTPTDI---PDVRQMATEA 261
Cdd:cd06213    81 TGERLTVRGPFGDFWLR-PGDAPILCIAGGSGLAPILAILEQARAAGT---KRDVtLLFGARTQRDLyalDEIAAIAARW 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308985323 262 GIEVDFHPVISAPVNGVSveWRGDIGFVHEFIAKKLaapLPGYEYYLAGPPPMIEAAVRLLVAeHKVPTTQIHFDRF 338
Cdd:cd06213   157 RGRFRFIPVLSEEPADSS--WKGARGLVTEHIAEVL---LAATEAYLCGPPAMIDAAIAVLRA-LGIAREHIHADRF 227
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 115-338 7.43e-54

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: 176.37  E-value: 7.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 115 ALTPDISLFTFASDGPAE--FLAGQYAMIGIPALSQARAYSMSNIANEEGIWQFIIRRVPEGKVTAYLFDRLRLGDQLDL 192
Cdd:cd06212    10 ALTHDIRRLRLRLEEPEPikFFAGQYVDITVPGTEETRSFSMANTPADPGRLEFIIKKYPGGLFSSFLDDGLAVGDPVTV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 193 DGPYGIAYLRTDVTRPIVGIAGGSGLAPVLSVLQGAARSRCANGARpaMLYGGRTPTDIPDVRQMAT--EAGIEVDFHPV 270
Cdd:cd06212    90 TGPYGTCTLRESRDRPIVLIGGGSGMAPLLSLLRDMAASGSDRPVR--FFYGARTARDLFYLEEIAAlgEKIPDFTFIPA 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308985323 271 ISAPvnGVSVEWRGDIGFVHEFIAKKLAApLPGYEYYLAGPPPMIEAAVRLLVAEHkVPTTQIHFDRF 338
Cdd:cd06212   168 LSES--PDDEGWSGETGLVTEVVQRNEAT-LAGCDVYLCGPPPMIDAALPVLEMSG-VPPDQIFYDKF 231
BenC NF040810
benzoate 1,2-dioxygenase electron transfer component BenC;
19-338 3.92e-51

benzoate 1,2-dioxygenase electron transfer component BenC;


Pssm-ID: 468751 [Multi-domain]  Cd Length: 333  Bit Score: 172.70  E-value: 3.92e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323  19 NTGDTLLRAGLRQGLGLAYECNVGACGSCK-------FDLiaGevDDLFPEAsgLRPKEREKGKRLACQCVPRSDCTIKI 91
Cdd:NF040810   18 NAGETVLDAAYRQKINIPMDCRDGACGTCKcrcesgsYDL--G--DDYIEDA--LTEEEAAQGYVLTCQMVPQSDCVIRV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323  92 RSGDEyLSAIPPARFKARFIDRKALTPDISLFTFASDGPAE--FLAGQYAMIGIPALSQARAYSMSNIANEEGIwQFIIR 169
Cdd:NF040810   92 PASSA-ACKTGQATFEATVAAVEQLSDSTIELSLDLDDDAAlaFLPGQYVNIQVPGTGQTRSYSFSSLPGAREA-SFLIR 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 170 RVPEGKVTAYLFDRLRLGDQLDLDGPYGIAYLRtDVTRPIVGIAGGSGLAPVLSVLQGAARSRCANGARpaMLYGGRTPT 249
Cdd:NF040810  170 NVPGGLMSSYLTERAKPGDRLSLTGPLGSFYLR-EVTRPLLMLAGGTGLAPFLSMLEVLAEQGSEQPVH--LIYGVTRDA 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 250 DIPDVRQM-ATEAGIE-VDFHPVISAPVNGVSVEwrgdiGFVHEFIAkklAAPLPGYEY--YLAGPPPMIEaAVRLLVAE 325
Cdd:NF040810  247 DLVEVERLeAFAARLPnFTFRTCVADAASAHPRK-----GYVTQHIE---AEWLNDGDVdvYLCGPPPMVD-AVRGWFRE 317

                         330
                  ....*....|...
gi 1308985323 326 HKVPTTQIHFDRF 338
Cdd:NF040810  318 QGITPASFHYEKF 330
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 106-338 4.97e-51

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: 169.43  E-value: 4.97e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 106 FKARFIDRKALTPDISLFTFASDGPA--EFLAGQYAMIGIPALSQARAYSMSNIANEEGIWQFIIRRVPEGKVTAYLFDR 183
Cdd:cd06211     7 FEGTVVEIEDLTPTIKGVRLKLDEPEeiEFQAGQYVNLQAPGYEGTRAFSIASSPSDAGEIELHIRLVPGGIATTYVHKQ 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 184 LRLGDQLDLDGPYGIAYLRTDVTRPIVGIAGGSGLAPVLSVLqgaARSRCANGARPAML-YGGRTPTDIPDVRQMATEAG 262
Cdd:cd06211    87 LKEGDELEISGPYGDFFVRDSDQRPIIFIAGGSGLSSPRSMI---LDLLERGDTRKITLfFGARTRAELYYLDEFEALEK 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308985323 263 IEVDFH--PVISAPVNGvsVEWRGDIGFVHEFIAKKLAAPLPGYEYYLAGPPPMIEAAVRLLVaEHKVPTTQIHFDRF 338
Cdd:cd06211   164 DHPNFKyvPALSREPPE--SNWKGFTGFVHDAAKKHFKNDFRGHKAYLCGPPPMIDACIKTLM-QGRLFERDIYYEKF 238
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
22-338 5.12e-50

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 169.92  E-value: 5.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323  22 DTLLRAGLRQGLGLAYECNVGACGSCKFDLIAGEVDDLFPEASGLRPKEREKGKRLACQCVPRSDCTIKIRSGDEYLSAI 101
Cdd:PRK11872   23 ELLLDAALRNGINLPLDCREGVCGTCQGRCESGIYSQDYVDEDALSERDLAQRKMLACQTRVKSDAAFYFDFDSSLCNAG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 102 PPARFKARFIDRKALTPDISLFTF---ASDGPAEFLAGQYAMIGIPALSQARAYSMSNIANEEGIWQFIIRRVPEGKVTA 178
Cdd:PRK11872  103 DTLKISGVVTAVELVSETTAILHLdasAHGRQLDFLPGQYARLQIPGTDDWRSYSFANRPNATNQLQFLIRLLPDGVMSN 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 179 YLFDRLRLGDQLDLDGPYGIAYLRtDVTRPIVGIAGGSGLAPVLSVLQGAARSRCangARPAMLYGG-RTPTDIPDVRQM 257
Cdd:PRK11872  183 YLRERCQVGDEILFEAPLGAFYLR-EVERPLVFVAGGTGLSAFLGMLDELAEQGC---SPPVHLYYGvRHAADLCELQRL 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 258 ATEAGIEVDF--HPVISAPvngvSVEWRGDIGFVHE-FIAKKLAAplPGYEYYLAGPPPMIEaAVRLLVAEHKVPTTQIH 334
Cdd:PRK11872  259 AAYAERLPNFryHPVVSKA----SADWQGKRGYIHEhFDKAQLRD--QAFDMYLCGPPPMVE-AVKQWLDEQALENYRLY 331


                  ....
gi 1308985323 335 FDRF 338
Cdd:PRK11872  332 YEKF 335
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
103-337 6.63e-48

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 161.11  E-value: 6.63e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 103 PARFKARFIDRKALTPDISLFTFASDGPAE---FLAGQYAMIGIPA--LSQARAYSMSNiANEEGIWQFIIRRVPEGKVT 177
Cdd:COG1018     1 AGFRPLRVVEVRRETPDVVSFTLEPPDGAPlprFRPGQFVTLRLPIdgKPLRRAYSLSS-APGDGRLEITVKRVPGGGGS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 178 AYLFDRLRLGDQLDLDGPYGIAYLRTDVTRPIVGIAGGSGLAPVLSVLQGAARsrcANGARP-AMLYGGRTPTDIP---D 253
Cdd:COG1018    80 NWLHDHLKVGDTLEVSGPRGDFVLDPEPARPLLLIAGGIGITPFLSMLRTLLA---RGPFRPvTLVYGARSPADLAfrdE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 254 VRQMATEAGiEVDFHPVISAPVNGVSvewrgdiGFVHEFIAKKLAAPLPGYEYYLAGPPPMIEAAVRLLvAEHKVPTTQI 333
Cdd:COG1018   157 LEALAARHP-RLRLHPVLSREPAGLQ-------GRLDAELLAALLPDPADAHVYLCGPPPMMEAVRAAL-AELGVPEERI 227


                  ....
gi 1308985323 334 HFDR 337
Cdd:COG1018   228 HFER 231
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 111-336 7.79e-48

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 161.57  E-value: 7.79e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 111 IDRKALTPDISLFTF-ASDGPAEFLAGQYAMIGIPALSQARAYSMSNIANEEGIWQFIIRRVpeGKVTAYLFdRLRLGDQ 189
Cdd:COG0543     3 VSVERLAPDVYLLRLeAPLIALKFKPGQFVMLRVPGDGLRRPFSIASAPREDGTIELHIRVV--GKGTRALA-ELKPGDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 190 LDLDGPYGIAYLRTDVTRPIVGIAGGSGLAPVLSVLQGAArsrcANGARPAMLYGGRTPTDIPDVRQMATEAGIEVDfhp 269
Cdd:COG0543    80 LDVRGPLGNGFPLEDSGRPVLLVAGGTGLAPLRSLAEALL----ARGRRVTLYLGARTPEDLYLLDELEALADFRVV--- 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308985323 270 visapvngVSVE--WRGDIGFVHEFIaKKLAAPLPGYEYYLAGPPPMIEAAVRLLvAEHKVPTTQIHFD 336
Cdd:COG0543   153 --------VTTDdgWYGRKGFVTDAL-KELLAEDSGDDVYACGPPPMMKAVAELL-LERGVPPERIYVS 211
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 114-338 7.84e-48

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: 160.79  E-value: 7.84e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 114 KALTPDISLFTFASDGPAEFLAGQYAMIGIPAlSQARAYSMSNIANEEGIWQFIIRRVPEGKVTAYLFDRLRLGDQLDLD 193
Cdd:cd06189     7 EPLNDDVYRVRLKPPAPLDFLAGQYLDLLLDD-GDKRPFSIASAPHEDGEIELHIRAVPGGSFSDYVFEELKENGLVRIE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 194 GPYGIAYLRTDVTRPIVGIAGGSGLAPVLSVLQGAARSRCangARPAMLY-GGRTPTDI--PDVRQMATEAGIEVDFHPV 270
Cdd:cd06189    86 GPLGDFFLREDSDRPLILIAGGTGFAPIKSILEHLLAQGS---KRPIHLYwGARTEEDLylDELLEAWAEAHPNFTYVPV 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308985323 271 ISAPVNGvsveWRGDIGFVHEFIAKKLAApLPGYEYYLAGPPPMIEAAVRLLVaEHKVPTTQIHFDRF 338
Cdd:cd06189   163 LSEPEEG----WQGRTGLVHEAVLEDFPD-LSDFDVYACGSPEMVYAARDDFV-EKGLPEENFFSDAF 224
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 126-338 2.48e-43

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: 149.28  E-value: 2.48e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 126 ASDGPAEFLAGQYAMIGIPALSQARAYSMSNIANEEGIwQFIIRRVPEGKVTAYLFDRLRLGDQLDLDGPYGIAYLRtDV 205
Cdd:cd06209    24 DEAGALAFLPGQYVNLQVPGTDETRSYSFSSAPGDPRL-EFLIRLLPGGAMSSYLRDRAQPGDRLTLTGPLGSFYLR-EV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 206 TRPIVGIAGGSGLAPVLSVLQGAARSRCangARPAML-YGGRTPTDIPDVRQMATEAG--IEVDFHPVISAPvngvsVEW 282
Cdd:cd06209   102 KRPLLMLAGGTGLAPFLSMLDVLAEDGS---AHPVHLvYGVTRDADLVELDRLEALAErlPGFSFRTVVADP-----DSW 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1308985323 283 RGDIGFVHEFIAKKLAAPlPGYEYYLAGPPPMIEAAVRLLvAEHKVPTTQIHFDRF 338
Cdd:cd06209   174 HPRKGYVTDHLEAEDLND-GDVDVYLCGPPPMVDAVRSWL-DEQGIEPANFYYEKF 227
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 116-336 2.18e-39

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: 138.73  E-value: 2.18e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 116 LTPDISLFTFASDGPAEFLAGQYAMIGIP--ALSQARAYSMSNIANEEGIWQFIIRRVPEGKVTAYLFDrLRLGDQLDLD 193
Cdd:cd00322     6 VTDDVRLFRLQLPNGFSFKPGQYVDLHLPgdGRGLRRAYSIASSPDEEGELELTVKIVPGGPFSAWLHD-LKPGDEVEVS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 194 GPYGIAYLRTDVTRPIVGIAGGSGLAPVLSVLQGAARSRcaNGARPAMLYGGRTPTDIP---DVRQMAtEAGIEVDFHPV 270
Cdd:cd00322    85 GPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADK--PGGEITLLYGARTPADLLfldELEELA-KEGPNFRLVLA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308985323 271 ISAPVNGvsvEWRGDIGFVHEFIAKKLAAPLPGYEYYLAGPPPMIEAAVRLLVaEHKVPTTQIHFD 336
Cdd:cd00322   162 LSRESEA---KLGPGGRIDREAEILALLPDDSGALVYICGPPAMAKAVREALV-SLGVPEERIHTE 223
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 124-338 7.16e-39

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: 137.86  E-value: 7.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 124 TFASDGPAEFLAGQYAMIGIPALSQARAYSMSNIANEEGIWQFIIRRVPEGKVTAYLFDRLRLGDQLDLDGPYGIAYLRT 203
Cdd:cd06210    26 AEGAGIAAEFVPGQFVEIEIPGTDTRRSYSLANTPNWDGRLEFLIRLLPGGAFSTYLETRAKVGQRLNLRGPLGAFGLRE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 204 DVTRPIVGIAGGSGLAPVLSVLQGAARSRCANGARpaMLYGGRTPTDIPDVRQMATEA----GIEVdfHPVISAPvngvS 279
Cdd:cd06210   106 NGLRPRWFVAGGTGLAPLLSMLRRMAEWGEPQEAR--LFFGVNTEAELFYLDELKRLAdslpNLTV--RICVWRP----G 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1308985323 280 VEWRGDIGFVHEFIAKKLAAPLPGYEYYLAGPPPMIEAAVRlLVAEHKVPTTQIHFDRF 338
Cdd:cd06210   178 GEWEGYRGTVVDALREDLASSDAKPDIYLCGPPGMVDAAFA-AAREAGVPDEQVYLEKF 235
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 117-338 2.27e-35

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: 128.54  E-value: 2.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 117 TPDISLFTFASDG--PAEFLAGQYAMIGIPAL---SQARAYSMSNIANEEGIWQFIIRRVPEGKVTAYLFDRLRLGDQLD 191
Cdd:cd06217    13 TPTVKTFRLAVPDgvPPPFLAGQHVDLRLTAIdgyTAQRSYSIASSPTQRGRVELTVKRVPGGEVSPYLHDEVKVGDLLE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 192 LDGPYGIAYLRTDVTRPIVGIAGGSGLAPVLSVLQgAARSRCANGaRPAMLYGGRTPTDIP---DVRQMATEA-GIEVDF 267
Cdd:cd06217    93 VRGPIGTFTWNPLHGDPVVLLAGGSGIVPLMSMIR-YRRDLGWPV-PFRLLYSARTAEDVIfrdELEQLARRHpNLHVTE 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308985323 268 hpVISAPvngVSVEWRGDIGFVHEFIAKKLAAPLPGYEYYLAGPPPMIEAAVRLLVaEHKVPTTQIHFDRF 338
Cdd:cd06217   171 --ALTRA---APADWLGPAGRITADLIAELVPPLAGRRVYVCGPPAFVEAATRLLL-ELGVPRDRIRTEAF 235
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
 118-338 8.88e-33

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: 123.18  E-value: 8.88e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 118 PDISLFTFA--SDGPAEFLAGQYAMIGIPA----------------------LSQ---------ARAYSMSNIANEEGIW 164
Cdd:cd06188    22 TFIKELVLKlpSGEEIAFKAGGYIQIEIPAyeiayadfdvaekyradwdkfgLWQlvfkhdepvSRAYSLANYPAEEGEL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 165 QFIIR---------RVPEGKVTAYLFDrLRLGDQLDLDGPYGIAYLRTDvTRPIVGIAGGSGLAPVLSVLQGAARSRcaN 235
Cdd:cd06188   102 KLNVRiatpppgnsDIPPGIGSSYIFN-LKPGDKVTASGPFGEFFIKDT-DREMVFIGGGAGMAPLRSHIFHLLKTL--K 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 236 GARPAML-YGGRTPTDIP---DVRQMATEAGiEVDFHPVISAPvnGVSVEWRGDIGFVHEFIA----KKLAAPlPGYEYY 307
Cdd:cd06188   178 SKRKISFwYGARSLKELFyqeEFEALEKEFP-NFKYHPVLSEP--QPEDNWDGYTGFIHQVLLenylKKHPAP-EDIEFY 253

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1308985323 308 LAGPPPMIEAAVRLLvAEHKVPTTQIHFDRF 338
Cdd:cd06188   254 LCGPPPMNSAVIKML-DDLGVPRENIAFDDF 283
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 111-334 8.71e-31

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: 116.15  E-value: 8.71e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 111 IDRKALTPDISLFTFASDGPA--EFLAGQYAMIGIPALSQA--RAYSMSNIANEEGIWQFIIRRVPEGKVTAYLFDRLRL 186
Cdd:cd06215     4 VKIIQETPDVKTFRFAAPDGSlfAYKPGQFLTLELEIDGETvyRAYTLSSSPSRPDSLSITVKRVPGGLVSNWLHDNLKV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 187 GDQLDLDGPYGIAYLRTDVTRPIVGIAGGSGLAPVLSVLQGAARSRCanGARPAMLYGGRTPTDIPDVRQMATEAGIEVD 266
Cdd:cd06215    84 GDELWASGPAGEFTLIDHPADKLLLLSAGSGITPMMSMARWLLDTRP--DADIVFIHSARSPADIIFADELEELARRHPN 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308985323 267 FHPVISAPVNGVSVeWRGDIGFVHEFIAKKLAAPLPGYEYYLAGPPPMIeAAVRLLVAEHKVPTTQIH 334
Cdd:cd06215   162 FRLHLILEQPAPGA-WGGYRGRLNAELLALLVPDLKERTVFVCGPAGFM-KAVKSLLAELGFPMSRFH 227
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 111-334 4.96e-29

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: 112.32  E-value: 4.96e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 111 IDRKALTPDISLFTFASDGPAE----FLAGQYAMIGIPALSQArAYSMSNIANEEGIWQFIIRRVpeGKVTAYLFdRLRL 186
Cdd:cd06221     2 VEVVDETEDIKTFTLRLEDDDEelftFKPGQFVMLSLPGVGEA-PISISSDPTRRGPLELTIRRV--GRVTEALH-ELKP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 187 GDQLDLDGPYGIAY-LRTDVTRPIVGIAGGSGLAPVLSVLQGAARSRcANGARPAMLYGGRTPTDIPDVRQMAT-EAGIE 264
Cdd:cd06221    78 GDTVGLRGPFGNGFpVEEMKGKDLLLVAGGLGLAPLRSLINYILDNR-EDYGKVTLLYGARTPEDLLFKEELKEwAKRSD 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 265 VDFHPVISAPVNGvsveWRGDIGFVHEFIAKKLAAPLPGYeYYLAGPPPMIEAAVRLLVaEHKVPTTQIH 334
Cdd:cd06221   157 VEVILTVDRAEEG----WTGNVGLVTDLLPELTLDPDNTV-AIVCGPPIMMRFVAKELL-KLGVPEEQIW 220
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 106-338 6.14e-27

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: 106.49  E-value: 6.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 106 FKARFIDRK-ALTPDISLFTFAS-DG--PAEFLAGQYAMIGIP----ALSQARAYSMSNIANEEGiWQFIIRRVPEGKVT 177
Cdd:cd06184     6 FRPFVVARKvAESEDITSFYLEPaDGgpLPPFLPGQYLSVRVKlpglGYRQIRQYSLSDAPNGDY-YRISVKREPGGLVS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 178 AYLFDRLRLGDQLDLDGPYGIAYLRTDVTRPIVGIAGGSGLAPVLSVLQGAARsrcANGARPA-MLYGGRTPTDIP---D 253
Cdd:cd06184    85 NYLHDNVKVGDVLEVSAPAGDFVLDEASDRPLVLISAGVGITPMLSMLEALAA---EGPGRPVtFIHAARNSAVHAfrdE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 254 VRQMATEAGiEVDFHPVISAPVNGVSVEWRGDIGFV-HEFIAKKLaaPLPGYEYYLAGPPPMIEAAVRLLVAEHkVPTTQ 332
Cdd:cd06184   162 LEELAARLP-NLKLHVFYSEPEAGDREEDYDHAGRIdLALLRELL--LPADADFYLCGPVPFMQAVREGLKALG-VPAER 237


                  ....*.
gi 1308985323 333 IHFDRF 338
Cdd:cd06184   238 IHYEVF 243
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 112-338 8.90e-27

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: 105.70  E-value: 8.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 112 DRKALTPDISLFTFasDGPAE------FLAGQY----AMIGipALSQARAYSMSNIAnEEGIWQFIIRRVPEGKVTAYLF 181
Cdd:cd06214     8 EVVRETADAVSITF--DVPEElrdafrYRPGQFltlrVPID--GEEVRRSYSICSSP-GDDELRITVKRVPGGRFSNWAN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 182 DRLRLGDQLDLDGPYGIAYLRTDV-TRPIVGIAGGSGLAPVLSVLQGA-ARSRcanGARPAMLYGGRTPTDI---PDVRQ 256
Cdd:cd06214    83 DELKAGDTLEVMPPAGRFTLPPLPgARHYVLFAAGSGITPVLSILKTAlAREP---ASRVTLVYGNRTEASVifrEELAD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 257 MATEAGIEVDFHPVISAPVNGVSV-EWRGDIGFVHEFIAKKLAAPLPgYEYYLAGPPPMIEAAVRLLvAEHKVPTTQIHF 335
Cdd:cd06214   160 LKARYPDRLTVIHVLSREQGDPDLlRGRLDAAKLNALLKNLLDATEF-DEAFLCGPEPMMDAVEAAL-LELGVPAERIHR 237


                  ...
gi 1308985323 336 DRF 338
Cdd:cd06214   238 ELF 240
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 109-320 2.83e-26

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: 104.19  E-value: 2.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 109 RFIDRKALTPDISLFTFASDGPAEFL---AGQYAMIGIPALSQ--ARAYSMSNIANEEGIWQFIIRRVPEGKVTAYLfDR 183
Cdd:cd06183     2 KLVSKEDISHDTRIFRFELPSPDQVLglpVGQHVELKAPDDGEqvVRPYTPISPDDDKGYFDLLIKIYPGGKMSQYL-HS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 184 LRLGDQLDLDGPYG-IAYLRTDVTRPIVGIAGGSGLAPVLSVLQGAARSRCANGaRPAMLYGGRTPTDIPDVRQ---MAT 259
Cdd:cd06183    81 LKPGDTVEIRGPFGkFEYKPNGKVKHIGMIAGGTGITPMLQLIRAILKDPEDKT-KISLLYANRTEEDILLREEldeLAK 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308985323 260 EAGIEVDFHPVISAPVNGvsveWRGDIGFVHEFIAKKLAAPLPGYEYY--LAGPPPMIEAAVR 320
Cdd:cd06183   160 KHPDRFKVHYVLSRPPEG----WKGGVGFITKEMIKEHLPPPPSEDTLvlVCGPPPMIEGAVK 218
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 95-338 6.45e-25

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: 100.76  E-value: 6.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323  95 DEYLSAIPPA----RFKARFIDRKALTPDISLFTFA-SDGPAEFLAGQYAMIGIP--ALSQARAYSMSNIANEE-GIWQF 166
Cdd:cd06216     3 DFYLELINPLwsarELRARVVAVRPETADMVTLTLRpNRGWPGHRAGQHVRLGVEidGVRHWRSYSLSSSPTQEdGTITL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 167 IIRRVPEGKVTAYLFDRLRLGDQLDLDGPYGIAYLRTDVTRPIVGIAGGSGLAPVLSVLqgaaRSRCANGARP--AMLYG 244
Cdd:cd06216    83 TVKAQPDGLVSNWLVNHLAPGDVVELSQPQGDFVLPDPLPPRLLLIAAGSGITPVMSML----RTLLARGPTAdvVLLYY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 245 GRTPTDIP---DVRQMATEagievdfHPvisapvnGVSVEWR----GDIGFVHEFIAKKLAAPLPGYEYYLAGPPPMIEA 317
Cdd:cd06216   159 ARTREDVIfadELRALAAQ-------HP-------NLRLHLLytreELDGRLSAAHLDAVVPDLADRQVYACGPPGFLDA 224

                         250       260
                  ....*....|....*....|.
gi 1308985323 318 AVRLLVAEHKVptTQIHFDRF 338
Cdd:cd06216   225 AEELLEAAGLA--DRLHTERF 243
Fdx COG0633
Ferredoxin [Energy production and conversion];
6-92 3.17e-24

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 94.53  E-value: 3.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323   6 RISLSGSETTYTGNTGDTLLRAGLRQGLGLAYECNVGACGSCKFDLIAGEVDDLfpEASGLRPKEREKGKRLACQCVPRS 85
Cdd:COG0633     3 KVTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHR--EEDALSDEERAAGSRLACQARPTS 80


                  ....*..
gi 1308985323  86 DCTIKIR 92
Cdd:COG0633    81 DLVVELP 87
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 116-339 4.35e-24

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: 98.11  E-value: 4.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 116 LTPDISLFTFASDGPAEFLAGQYAMIGIPALSqARAYSMSNIANEEGIWQFIIRRVPEGKVTAYLFDRLRLGDQLDLDGP 195
Cdd:cd06194     7 LSPDVLRVRLEPDRPLPYLPGQYVNLRRAGGL-ARSYSPTSLPDGDNELEFHIRRKPNGAFSGWLGEEARPGHALRLQGP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 196 YGIAYLRTDV-TRPIVGIAGGSGLAPVLSVLQgAARSRcaNGARPAMLY-GGRTPTDI---PDVRQMATEAGiEVDFHPV 270
Cdd:cd06194    86 FGQAFYRPEYgEGPLLLVGAGTGLAPLWGIAR-AALRQ--GHQGEIRLVhGARDPDDLylhPALLWLAREHP-NFRYIPC 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308985323 271 ISAPVNGVSVEWRGDigfvhefIAKKLAAPLPGYEYYLAGPPPMIEaAVRLLVAEHKVPTTQIHFDRFF 339
Cdd:cd06194   162 VSEGSQGDPRVRAGR-------IAAHLPPLTRDDVVYLCGAPSMVN-AVRRRAFLAGAPMKRIYADPFE 222
fre PRK08051
FMN reductase; Validated
 115-338 5.59e-22

FMN reductase; Validated


Pssm-ID: 236142 [Multi-domain]  Cd Length: 232  Bit Score: 92.61  E-value: 5.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 115 ALTPDISLFTFASDGPAEFLAGQYAMIgIPALSQARAYSMSNIANEEGIWQFIIRRVPEGKVTAYLFDRLRLGDQLDLDG 194
Cdd:PRK08051   12 AITDTVYRVRLVPEAPFSFRAGQYLMV-VMGEKDKRPFSIASTPREKGFIELHIGASELNLYAMAVMERILKDGEIEVDI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 195 PYGIAYLRTDVTRPIVGIAGGSGLAPVLSVLQGAARSrcaNGARPAMLY-GGRTPTDIPDVRQMA--TEAGIEVDFHPVI 271
Cdd:PRK08051   91 PHGDAWLREESERPLLLIAGGTGFSYARSILLTALAQ---GPNRPITLYwGGREEDHLYDLDELEalALKHPNLHFVPVV 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308985323 272 SAPVNGvsveWRGDIGFVHEFIAKKLAApLPGYEYYLAGPPPMIEAAVRLLVAEHKVPTTQIHFDRF 338
Cdd:PRK08051  168 EQPEEG----WQGKTGTVLTAVMQDFGS-LAEYDIYIAGRFEMAKIARELFCRERGAREEHLFGDAF 229
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 118-338 6.95e-22

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: 91.93  E-value: 6.95e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 118 PDISLFTFASDGPA-EFLAGQYA--MIGIPALSQARAYSMSNIANEEGIWQFIIRRVpeGKVTAYLFDRLRLGDQLDLDG 194
Cdd:cd06198     7 RPTTTLTLEPRGPAlGHRAGQFAflRFDASGWEEPHPFTISSAPDPDGRLRFTIKAL--GDYTRRLAERLKPGTRVTVEG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 195 PYGiAYLRTDVTRPIVGIAGGSGLAPVLSVLQGAARSRCANGARpaMLYGGRTPTDIPDV---RQMATEAGIEvdFHPVI 271
Cdd:cd06198    85 PYG-RFTFDDRRARQIWIAGGIGITPFLALLEALAARGDARPVT--LFYCVRDPEDAVFLdelRALAAAAGVV--LHVID 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308985323 272 SAPVNGVSvewrgdigfvHEFIAKKLAAPLPGYEYYLAGPPPMIEAAVRLLvAEHKVPTTQIHFDRF 338
Cdd:cd06198   160 SPSDGRLT----------LEQLVRALVPDLADADVWFCGPPGMADALEKGL-RALGVPARRFHYERF 215
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 6-90 2.00e-21

2Fe-2S iron-sulfur cluster 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). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 86.68  E-value: 2.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323   6 RISLSGSETTYTGNTGDTLLRAGLRQGLGLAYECNVGACGSCKFDLIAGEVDDLfpEASGLRPKEREKGKRLACQCVPRS 85
Cdd:cd00207     2 TINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQS--DPSLLDEEEAEGGYVLACQTRVTD 79


                  ....*
gi 1308985323  86 DCTIK 90
Cdd:cd00207    80 GLVIE 84
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 117-338 3.57e-19

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: 84.89  E-value: 3.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 117 TPDISLFTFASDGPAE--FLAGQYAMIGIPA--LSQARAYSMSNIANEEGIwQFIIRRVPEGKVTAYLFDRLRLGDQLDL 192
Cdd:cd06191    10 TPDAVTIVFAVPGPLQygFRPGQHVTLKLDFdgEELRRCYSLCSSPAPDEI-SITVKRVPGGRVSNYLREHIQPGMTVEV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 193 DGPYGIAYLRTDVTRPIVGIAGGSGLAPVLSVLqgAARSRCANGARPAMLYGGRTPTDIPDVRQMATEAGIEVDFHPVIS 272
Cdd:cd06191    89 MGPQGHFVYQPQPPGRYLLVAAGSGITPLMAMI--RATLQTAPESDFTLIHSARTPADMIFAQELRELADKPQRLRLLCI 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308985323 273 APVNGVSVEWRGDIGFVHEFIAKKLAAPLPGYEYYLAGPPPMIEAAVRLLVAEHKVPTTqIHFDRF 338
Cdd:cd06191   167 FTRETLDSDLLHGRIDGEQSLGAALIPDRLEREAFICGPAGMMDAVETALKELGMPPER-IHTERF 231
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 109-226 7.03e-18

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


Pssm-ID: 99792 [Multi-domain]  Cd Length: 241  Bit Score: 81.46  E-value: 7.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 109 RFIDRKALTPDISLFTFASDGPAEFLAGQYAMIGIPALSQ---ARAYSMSNIANEEGIwQFIIRRVPEGKVTAYLFdRLR 185
Cdd:cd06195     1 TVLKRRDWTDDLFSFRVTRDIPFRFQAGQFTKLGLPNDDGklvRRAYSIASAPYEENL-EFYIILVPDGPLTPRLF-KLK 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1308985323 186 LGDQLDLD-GPYGiaYLRTDVTRP---IVGIAGGSGLAPVLSVLQ 226
Cdd:cd06195    79 PGDTIYVGkKPTG--FLTLDEVPPgkrLWLLATGTGIAPFLSMLR 121
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 111-330 1.23e-16

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


Pssm-ID: 99814 [Multi-domain]  Cd Length: 246  Bit Score: 77.97  E-value: 1.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 111 IDRKALTPDISLFTFASDGPAE-FLAGQYAMIGIPALSQ---ARAYSMSNIANEEGIWQFIIRRVpeGKVTAYLfDRLRL 186
Cdd:cd06218     2 LSNREIADDIYRLVLEAPEIAAaAKPGQFVMLRVPDGSDpllRRPISIHDVDPEEGTITLLYKVV--GKGTRLL-SELKA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 187 GDQLDLDGPYGIAYLRTDVTRPIVGIAGGSGLAPVLsvlqGAARSRCANGARPAMLYGGRTPTDIPDVRQMATEAGievd 266
Cdd:cd06218    79 GDELDVLGPLGNGFDLPDDDGKVLLVGGGIGIAPLL----FLAKQLAERGIKVTVLLGFRSADDLFLVEEFEALGA---- 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308985323 267 fhPVISAPVNGvSVewrGDIGFVHEFIAKKLAAPLPGYeYYLAGPPPMIeAAVRLLVAEHKVPT 330
Cdd:cd06218   151 --EVYVATDDG-SA---GTKGFVTDLLKELLAEARPDV-VYACGPEPML-KAVAELAAERGVPC 206
PRK05713 PRK05713
iron-sulfur-binding ferredoxin reductase;
20-230 3.66e-16

iron-sulfur-binding ferredoxin reductase;


Pssm-ID: 235575 [Multi-domain]  Cd Length: 312  Bit Score: 77.84  E-value: 3.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323  20 TGDTLLRAGLRQGLGLAYECNVGACGSCKFDLIAGEVDDLFPEAsgLRPKEREKGKRLACQCVPRSDCTIKI----RSGd 95
Cdd:PRK05713   15 AGSNLLDALNAAGVAVPYSCRAGSCHACLVRCLQGEPEDALPEA--LAAEKREQGWRLACQCRVVGDLRVEVfdpqRDG- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323  96 eylsaiPPARFKArfIDRkaLTPDISLFTFASDGPAEFLAGQYAMIGIpALSQARAYSMSNIANEEGIWQFII--RRVPE 173
Cdd:PRK05713   92 ------LPARVVA--LDW--LGGDVLRLRLEPERPLRYRAGQHLVLWT-AGGVARPYSLASLPGEDPFLEFHIdcSRPGA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 174 GKVTAylfDRLRLGDQLDLDGPYGIAyLRTDV---TRPIVGIAGGSGLAPVLSVLQGAAR 230
Cdd:PRK05713  161 FCDAA---RQLQVGDLLRLGELRGGA-LHYDPdwqERPLWLLAAGTGLAPLWGILREALR 216
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
107-197 4.31e-16

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 72.61  E-value: 4.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 107 KARFIDRKALTPDISLFTFASDGPAE---FLAGQYAMIGIPALSQA--RAYSMSNIANEEGIWQFIIRRVPEGKVTAYLf 181
Cdd:pfam00970   1 PLTLVEKELVSHDTRIFRFALPHPDQvlgLPVGQHLFLRLPIDGELviRSYTPISSDDDKGYLELLVKVYPGGKMSQYL- 79

                          90
                  ....*....|....*.
gi 1308985323 182 DRLRLGDQLDLDGPYG 197
Cdd:pfam00970  80 DELKIGDTIDFKGPLG 95
PRK13289 PRK13289
NO-inducible flavohemoprotein;
129-339 6.38e-16

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 77.92  E-value: 6.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 129 GP-AEFLAGQYamIGI------PALSQARAYSMSNIANEEGiWQFIIRRVPEGKVTAYLFDRLRLGDQLDLDGPYGIAYL 201
Cdd:PRK13289  180 GPvADFKPGQY--LGVrldpegEEYQEIRQYSLSDAPNGKY-YRISVKREAGGKVSNYLHDHVNVGDVLELAAPAGDFFL 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 202 RTDVTRPIVGIAGGSGLAPVLSVLQGAARSR----------CANGARPAMlyggRTptdipDVRQMATEagievdfHPVI 271
Cdd:PRK13289  257 DVASDTPVVLISGGVGITPMLSMLETLAAQQpkrpvhfihaARNGGVHAF----RD-----EVEALAAR-------HPNL 320

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308985323 272 SAPV--NGVSVEWRGDIGFVHE-FI-AKKLAA--PLPGYEYYLAGPPPMIEAAVRLLVaEHKVPTTQIHFDrFF 339
Cdd:PRK13289  321 KAHTwyREPTEQDRAGEDFDSEgLMdLEWLEAwlPDPDADFYFCGPVPFMQFVAKQLL-ELGVPEERIHYE-FF 392
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 112-338 1.11e-14

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: 71.75  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 112 DRKALTPDISLFTFAS-DGPA--EFLAGqyAMIGI---PALSqaRAYSMSNIANEEGIWQFIIRRVPEGK-VTAYLFDRL 184
Cdd:cd06185     2 RIRDEAPDIRSFELEApDGAPlpAFEPG--AHIDVhlpNGLV--RQYSLCGDPADRDRYRIAVLREPASRgGSRYMHELL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 185 RLGDQLDLDGPYGIAYLRTDvTRPIVGIAGGSGLAPVLSVLQGAARSrcanGARPAMLYGGRTPTDIPDVRQMATEAGIE 264
Cdd:cd06185    78 RVGDELEVSAPRNLFPLDEA-ARRHLLIAGGIGITPILSMARALAAR----GADFELHYAGRSREDAAFLDELAALPGDR 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308985323 265 VDFHPvisapvngvsvewrgDIGFVHEFIAKKLAAPLPGYEYYLAGPPPMIEaAVRLLVAEHKVPTTQIHFDRF 338
Cdd:cd06185   153 VHLHF---------------DDEGGRLDLAALLAAPPAGTHVYVCGPEGMMD-AVRAAAAALGWPEARLHFERF 210
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 117-330 3.55e-14

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 71.06  E-value: 3.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 117 TPDISLFTFASDGPAEFLAGQYAMIGIPALSQA--RAYSMSNIANEEGIwqFIIRRVpeGKVTAYLFDrLRLGDQLDLDG 194
Cdd:PRK00054   16 APNIYTLVLDGEKVFDMKPGQFVMVWVPGVEPLleRPISISDIDKNEIT--ILYRKV--GEGTKKLSK-LKEGDELDIRG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 195 PYGIAYLRTDVTRPIVGIAGGSGLAPVLSVlqgaARSRCANGARPAMLYGGRTPTDIPDVRQMAteagiEVDfhPVISAP 274
Cdd:PRK00054   91 PLGNGFDLEEIGGKVLLVGGGIGVAPLYEL----AKELKKKGVEVTTVLGARTKDEVIFEEEFA-----KVG--DVYVTT 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1308985323 275 VNGVsvewRGDIGFVHEFIAKKLAAplpgYEY-YLAGPPPMIEAAVRLLvAEHKVPT 330
Cdd:PRK00054  160 DDGS----YGFKGFVTDVLDELDSE----YDAiYSCGPEIMMKKVVEIL-KEKKVPA 207
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 212-320 8.92e-14

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: 66.51  E-value: 8.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 212 IAGGSGLAPVLSVLQgAARSRCANGARPAMLYGGRTPTDI---PDVRQMATEAGIEVDFHPVISAPVNGvsveWRGDIGF 288
Cdd:pfam00175   2 IAGGTGIAPVRSMLR-AILEDPKDPTQVVLVFGNRNEDDIlyrEELDELAEKHPGRLTVVYVVSRPEAG----WTGGKGR 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1308985323 289 VHEFIAKKLA-APLPGYEYYLAGPPPMIEAAVR 320
Cdd:pfam00175  77 VQDALLEDHLsLPDEETHVYVCGPPGMIKAVRK 109
PLN02252 PLN02252
nitrate reductase [NADPH]
 102-320 3.27e-13

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 70.48  E-value: 3.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 102 PPARFKARFIDRKALTPDISLFTFASDGPAEFLagqyamiGIPA-----LSQA-------RAYSMSNIANEEGIWQFIIR 169
Cdd:PLN02252  631 PREKIPCRLVEKISLSHDVRLFRFALPSEDHVL-------GLPVgkhvfLCATingklcmRAYTPTSSDDEVGHFELVIK 703

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 170 --------RVPEG-KVTAYLfDRLRLGDQLDLDGPYG-IAYL---------RTDVTRPIVGIAGGSGLAPVLSVLQGAAR 230
Cdd:PLN02252  704 vyfknvhpKFPNGgLMSQYL-DSLPIGDTIDVKGPLGhIEYAgrgsflvngKPKFAKKLAMLAGGTGITPMYQVIQAILR 782

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 231 SRcANGARPAMLYGGRTPTDI---PDVRQMATEAGIEVDFHPVISAPvngVSVEWRGDIGFVHEFIAKKLAAPLPGYEYY 307
Cdd:PLN02252  783 DP-EDKTEMSLVYANRTEDDIllrEELDRWAAEHPDRLKVWYVVSQV---KREGWKYSVGRVTEAMLREHLPEGGDETLA 858

                         250
                  ....*....|....
gi 1308985323 308 LA-GPPPMIEAAVR 320
Cdd:PLN02252  859 LMcGPPPMIEFACQ 872
PTZ00319 PTZ00319
NADH-cytochrome B5 reductase; Provisional
 100-320 7.55e-13

NADH-cytochrome B5 reductase; Provisional


Pssm-ID: 173521 [Multi-domain]  Cd Length: 300  Bit Score: 67.93  E-value: 7.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 100 AIPPARFKA-RFIDRKALTPDISLFTFASDGPAEFLA---GQYAMI-------GIPALSQaRAYSMSNIANEEGIWQFII 168
Cdd:PTZ00319   27 ALDPDMFQHfKLIKKTEVTHDTFIFRFALHSPTQRLGlpiGQHIVFrcdcttpGKPETVQ-HSYTPISSDDEKGYVDFLI 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 169 R--------RVPEGKVTAYLFDRLRLGDQLDLDGPYG-IAYLRTDVTRPIVG--------------IAGGSGLAPVLSVL 225
Cdd:PTZ00319  106 KvyfkgvhpSFPNGGRLSQHLYHMKLGDKIEMRGPVGkFEYLGNGTYTVHKGkgglktmhvdafamIAGGTGITPMLQII 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 226 QGAARSRcANGARPAMLYGGRTPTDIPdVRQMATEAGIEVDFHpVISAPVNGVSVEWRGDIGFVHE-FIAKKLAAPLP-- 302
Cdd:PTZ00319  186 HAIKKNK-EDRTKVFLVYANQTEDDIL-LRKELDEAAKDPRFH-VWYTLDREATPEWKYGTGYVDEeMLRAHLPVPDPqn 262

                         250       260
                  ....*....|....*....|..
gi 1308985323 303 -GYEYYLA---GPPPMIEAAVR 320
Cdd:PTZ00319  263 sGIKKVMAlmcGPPPMLQMAVK 284
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
9-84 1.89e-12

2Fe-2S iron-sulfur cluster binding domain;


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 62.16  E-value: 1.89e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308985323   9 LSGSETTYTGNTGDT-LLRAGLRQGLGLAYECNVGACGSCKFDLIAGEVDDlfpEASGLRPKEREKGK-RLACQCVPR 84
Cdd:pfam00111   3 INGKGVTIEVPDGETtLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQS---DQSFLEDDELAAGYvVLACQTYPK 77
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 116-339 1.80e-11

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: 63.04  E-value: 1.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 116 LTPDISLFTFasDGPAEFLAGQYAMIGIPALSQaRAYSMSNIANEEGIwqfIIRRVpeGKVTAYLFDrLRLGDQLDLDGP 195
Cdd:cd06220     9 ETPTVKTFVF--DWDFDFKPGQFVMVWVPGVDE-IPMSLSYIDGPNSI---TVKKV--GEATSALHD-LKEGDKLGIRGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 196 YGIAYlrTDVTRPIVGIAGGSGLAPVLSVLqgaarSRCANGARPAMLYGGRTPTDI--------PDVRQMATEAGIEvdf 267
Cdd:cd06220    80 YGNGF--ELVGGKVLLIGGGIGIAPLAPLA-----ERLKKAADVTVLLGARTKEELlfldrlrkSDELIVTTDDGSY--- 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308985323 268 hpvisapvngvsvewrGDIGFVHEFIAKKLAAplpGYEY-YLAGPPPMIEAAVRLLVaEHKVPtTQIHFDRFF 339
Cdd:cd06220   150 ----------------GFKGFVTDLLKELDLE---EYDAiYVCGPEIMMYKVLEILD-ERGVR-AQFSLERYM 201
COG3894 COG3894
Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain ...
 1-122 3.61e-11

Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain [Function unknown];


Pssm-ID: 443101 [Multi-domain]  Cd Length: 621  Bit Score: 64.06  E-value: 3.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323   1 MTEsFRISLSGSETTYTGNTGDTLLRAGLRQGLGLAYECN-VGACGSCKFDLIAGEVDDL-FPEASGLRPKEREKGKRLA 78
Cdd:COG3894     1 MPK-VKVTFLPSGKRVEVEAGTTLLDAAREAGVDIDAPCGgRGTCGKCKVKVEEGEFSPVtEEERRLLSPEELAEGYRLA 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1308985323  79 CQCVPRSDCTIKIrsgdeylsaIPPARFKARFIDRKALTPDISL 122
Cdd:COG3894    80 CQARVLGDLVVEV---------PPESRLDKQKILKEGLEREIEL 114
PTZ00038 PTZ00038
ferredoxin; Provisional
 24-96 4.56e-11

ferredoxin; Provisional


Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 61.01  E-value: 4.56e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308985323  24 LLRAGLRQGLGLAYECNVGACGSCKFDLIAGEVDDlfPEASGLRPKEREKGKRLACQCVPRSDCTIKIRSGDE 96
Cdd:PTZ00038  117 ILDAAERQGVELPYSCRGGSCSTCAAKLLEGEVDN--EDQSYLDDEQLKKGYCLLCTCYPKSDCTIETHKEDE 187
fdx_plant TIGR02008
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ...
 3-96 7.04e-10

ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ferredoxins. In general, these occur as a single domain proteins or with a chloroplast transit peptide. Species tend to be photosynthetic, but several forms may occur in one species and individually may not be associated with photocynthesis. Halobacterial forms differ somewhat in architecture; they score between trusted and noise cutoffs. Sequences scoring below the noise cutoff tend to be ferredoxin-related domains of larger proteins.


Pssm-ID: 273926 [Multi-domain]  Cd Length: 97  Bit Score: 55.54  E-value: 7.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323   3 ESFRISL---SGSETTYTGNTGDTLLRAGLRQGLGLAYECNVGACGSCKFDLIAGEVDDlfPEASGLRPKEREKGKRLAC 79
Cdd:TIGR02008   1 ATYKVTLvnpDGGEETIECPDDQYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQ--SDQSFLDDDQMEAGYVLTC 78

                          90
                  ....*....|....*..
gi 1308985323  80 QCVPRSDCTIKIRSGDE 96
Cdd:TIGR02008  79 VAYPTSDCTIETHKEED 95
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 102-323 1.41e-09

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 58.28  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 102 PPARFKARFIDRKALTPDISLFTFASDGPA-----EFLAGQYAMIGIPALSQArAYSMSNIANEEGIWQFIIRRVpeGKV 176
Cdd:PRK08345    2 PYALHDAKILEVYDLTEREKLFLLRFEDPElaesfTFKPGQFVQVTIPGVGEV-PISICSSPTRKGFFELCIRRA--GRV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 177 TAYLfDRLRLGDQLDLDGPYGIAYLRTDVT-RPIVGIAGGSGLAPVLSVLQGAARSRCANGaRPAMLYGGRTPTDIPDVR 255
Cdd:PRK08345   79 TTVI-HRLKEGDIVGVRGPYGNGFPVDEMEgMDLLLIAGGLGMAPLRSVLLYAMDNRWKYG-NITLIYGAKYYEDLLFYD 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308985323 256 QMATEAGIEVDFHPVISAPVNgvsVEWRGDIGFVHEFI---AKKLAAPLPGYEYY--------LAGPPPMIEAAVRLLV 323
Cdd:PRK08345  157 ELIKDLAEAENVKIIQSVTRD---PEWPGCHGLPQGFIervCKGVVTDLFREANTdpkntyaaICGPPVMYKFVFKELI 232
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 148-324 2.64e-09

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: 56.48  E-value: 2.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 148 QARAYSMSNIaNEEGIWQFIIRRVPE-GKVTAYLfDRLRLGDQLDLDGPYG-IAYlrtdvTRPIVGIAGGSGLAPVLSVL 225
Cdd:cd06196    46 EKRPFTFTSL-PEDDVLEFVIKSYPDhDGVTEQL-GRLQPGDTLLIEDPWGaIEY-----KGPGVFIAGGAGITPFIAIL 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 226 QGAARSRCANGARpaMLYGGRTPTDI---PDVRQMATEAGIEVdfhpvisapvngVSVEwrGDIGFVH-----EFIaKKL 297
Cdd:cd06196   119 RDLAAKGKLEGNT--LIFANKTEKDIilkDELEKMLGLKFINV------------VTDE--KDPGYAHgridkAFL-KQH 181

                         170       180
                  ....*....|....*....|....*..
gi 1308985323 298 AAPLPGyEYYLAGPPPMIEAAVRLLVA 324
Cdd:cd06196   182 VTDFNQ-HFYVCGPPPMEEAINGALKE 207
petF CHL00134
ferredoxin; Validated
 4-96 2.72e-09

ferredoxin; Validated


Pssm-ID: 177056 [Multi-domain]  Cd Length: 99  Bit Score: 53.96  E-value: 2.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323   4 SFRISLSGSE----TTYTGNTGDTLLRAGLRQGLGLAYECNVGACGSCKFDLIAGEVDDlfPEASGLRPKEREKGKRLAC 79
Cdd:CHL00134    3 TYKVTLLSEEegidVTIDCPDDVYILDAAEEQGIDLPYSCRAGACSTCAGKVTEGTVDQ--SDQSFLDDDQLEAGFVLTC 80

                          90
                  ....*....|....*..
gi 1308985323  80 QCVPRSDCTIKIRSGDE 96
Cdd:CHL00134   81 VAYPTSDCTILTHQEEE 97
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 111-248 2.43e-08

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: 53.87  E-value: 2.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 111 IDRKALTPDISLFTF-ASDGPAEFLAGQYAMIGIPALSQ--ARAYSMSNIANEEGIWQFIIRRVpeGKVTAYLFdRLRLG 187
Cdd:cd06192     2 VKKEQLEPNLVLLTIkAPLAARLFRPGQFVFLRNFESPGleRIPLSLAGVDPEEGTISLLVEIR--GPKTKLIA-ELKPG 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308985323 188 DQLDLDGPYG--IAYLRTDVTrpIVGIAGGSGLAPVLSVlqgaARSRCANGARPAMLYGGRTP 248
Cdd:cd06192    79 EKLDVMGPLGngFEGPKKGGT--VLLVAGGIGLAPLLPI----AKKLAANGNKVTVLAGAKKA 135
PRK10713 PRK10713
2Fe-2S ferredoxin-like protein;
7-91 1.67e-05

2Fe-2S ferredoxin-like protein;


Pssm-ID: 182668 [Multi-domain]  Cd Length: 84  Bit Score: 42.79  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323   7 ISLSGSETTYTGNtGDTLLRAGLRQGLGLAYECNVGACGSCKFDLIAGEVDDLFPEASGLRPkerekGKRLACQCVPRSD 86
Cdd:PRK10713    6 LRITGTQLLCQDE-HPSLLAALESHNVAVEYQCREGYCGSCRTRLVAGQVDWIAEPLAFIQP-----GEILPCCCRAKGD 79


                  ....*
gi 1308985323  87 CTIKI 91
Cdd:PRK10713   80 IEIEM 84
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 118-226 2.18e-05

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: 44.99  E-value: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 118 PDISLFTFASDGPAEFLAGQYAMIGIPALS---QARAYSMSNIANEEGIW-QFIIRrvPEGKVTAYLFDRLRLGDQLD-- 191
Cdd:cd06186    10 SDVIRLTIPKPKPFKWKPGQHVYLNFPSLLsfwQSHPFTIASSPEDEQDTlSLIIR--AKKGFTTRLLRKALKSPGGGvs 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1308985323 192 ----LDGPYG--IAYLRTDVTrpIVGIAGGSGLAPVLSVLQ 226
Cdd:cd06186    88 lkvlVEGPYGssSEDLLSYDN--VLLVAGGSGITFVLPILR 126
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 117-339 2.39e-05

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 45.47  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 117 TPDISLFTFASDGPAEFLAGQYAMIGIPALSQA-RAYSMSNIANEEGIWQFIIRRVPEGKVTAYLFDRLRLGDQLDLDGP 195
Cdd:PRK10684   21 TPDVWTISLICHDFYPYRAGQYALVSIRNSAETlRAYTLSSTPGVSEFITLTVRRIDDGVGSQWLTRDVKRGDYLWLSDA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 196 YGIAYLRTDVTRPIVGIAGGSGLAPVLSVlqgaARSRCANgaRP----AMLYGGRTPTDIpdvrQMATEAGIEVDFHPVI 271
Cdd:PRK10684  101 MGEFTCDDKAEDKYLLLAAGCGVTPIMSM----RRWLLKN--RPqadvQVIFNVRTPQDV----IFADEWRQLKQRYPQL 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308985323 272 SAPVNGvsvEWRGDIGFVHEFIAKKL---AAP-LPGYEYYLAGPPPMIEaAVRLLVAEHKVPTTQIHFDRFF 339
Cdd:PRK10684  171 NLTLVA---ENNATEGFIAGRLTRELlqqAVPdLASRTVMTCGPAPYMD-WVEQEVKALGVTADRFFKEKFF 238
PLN03136 PLN03136
Ferredoxin; Provisional
 24-90 5.09e-05

Ferredoxin; Provisional


Pssm-ID: 178681 [Multi-domain]  Cd Length: 148  Bit Score: 42.81  E-value: 5.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308985323  24 LLRAGLRQGLGLAYECNVGACGSCKFDLIAGEVDDlfPEASGLRPKEREKGKRLACQCVPRSDCTIK 90
Cdd:PLN03136   76 VLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSIDQ--SDQSFLDDEQISEGYVLTCVAYPTSDVVIE 140
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 132-248 2.84e-04

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: 41.93  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 132 EFLAGQyaMIGI--PALSQARAYSMSNiANEEGIWQFIIRRVPEGKVTAYLFDrLRLGDQLDldgpygiAYLRTDVT--- 206
Cdd:cd06201    83 SFEAGD--LLGIlpPGSDVPRFYSLAS-SSSDGFLEICVRKHPGGLCSGYLHG-LKPGDTIK-------AFIRPNPSfrp 151

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1308985323 207 ----RPIVGIAGGSGLAPvlsvLQGAARsrcANGA-RPAMLY-GGRTP 248
Cdd:cd06201   152 akgaAPVILIGAGTGIAP----LAGFIR---ANAArRPMHLYwGGRDP 192
SiR_like1 cd06200
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 126-248 3.68e-04

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: 41.49  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 126 ASDGPAEFLAGQYAMIGIPALSQARAYSMSNIAnEEGIWQFIIRRVPE-----GKVTAYLFDRLRLGDQLDLDGPYGIAY 200
Cdd:cd06200    25 PPDAGAQWQAGDIAEIGPRHPLPHREYSIASLP-ADGALELLVRQVRHadgglGLGSGWLTRHAPIGASVALRLRENPGF 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1308985323 201 LRTDVTRPIVGIAGGSGLAPVLSVLQGAARsrcANGARPAMLYGGRTP 248
Cdd:cd06200   104 HLPDDGRPLILIGNGTGLAGLRSHLRARAR---AGRHRNWLLFGERQA 148
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
 102-272 4.20e-04

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: 41.54  E-value: 4.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 102 PPARFKARFIDRKALTPDISL-----FTFASDGPAEFLAGQyaMIGI-----------PALsqARAYSMSNIANEEG--- 162
Cdd:cd06208     5 PKNPLIGKVVSNTRLTGPDAPgevchIVIDHGGKLPYLEGQ--SIGIippgtdakngkPHK--LRLYSIASSRYGDDgdg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 163 -IWQFIIRRV----PEGKVTA------YLFDrLRLGDQLDLDGPYGIAYLR-TDVTRPIVGIAGGSGLAPVLSVLQGAAR 230
Cdd:cd06208    81 kTLSLCVKRLvytdPETDETKkgvcsnYLCD-LKPGDDVQITGPVGKTMLLpEDPNATLIMIATGTGIAPFRSFLRRLFR 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1308985323 231 SRCAN-GARP-AML-YGGRTPTDIP---DVRQMATEAGIEVDFHPVIS 272
Cdd:cd06208   160 EKHADyKFTGlAWLfFGVPNSDSLLyddELEKYPKQYPDNFRIDYAFS 207
CYPOR_like cd06182
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 113-250 6.42e-04

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: 40.78  E-value: 6.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 113 RKALTPDIS-------LFTFASDGPAEFLAGQYAMIgIPALS-QARAYSMSN-IANEEGIWQFIIRRV----PEGKV--- 176
Cdd:cd06182     5 NRKLTPPDSprstrhlEFDLSGNSVLKYQPGDHLGV-IPPNPlQPRYYSIASsPDVDPGEVHLCVRVVsyeaPAGRIrkg 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308985323 177 --TAYLfDRLRLGDQLDLDGPYGIAY-LRTDVTRPIVGIAGGSGLAPVLSVLQGAARSRCANGARPAM--LYGGRTPTD 250
Cdd:cd06182    84 vcSNFL-AGLQLGAKVTVFIRPAPSFrLPKDPTTPIIMVGPGTGIAPFRGFLQERAALRANGKARGPAwlFFGCRNFAS 161
PLN02292 PLN02292
ferric-chelate reductase
 173-226 9.91e-04

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 41.01  E-value: 9.91e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308985323 173 EGKVTAYLFDRLRLGDQLD-----LDGPYGIA---YLRTDvtrPIVGIAGGSGLAPVLSVLQ 226
Cdd:PLN02292  393 QGKWSTKLYHMLSSSDQIDrlavsVEGPYGPAstdFLRHE---SLVMVSGGSGITPFISIIR 451
PLN02631 PLN02631
ferric-chelate reductase
 95-226 9.99e-04

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 40.80  E-value: 9.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323  95 DEYLSAIPPARfKARFIDRKALTPDISLFTFASDGPAEFLAGQYAMIGIPALS--QARAYSMSNIAN-EEGIWQFIIRRv 171
Cdd:PLN02631  298 DRYLRFLQSTK-RSRLVSARILPSDNLELTFSKTPGLHYTPTSILFLHVPSISklQWHPFTITSSSNlEKDTLSVVIRR- 375

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 172 pEGKVTAYLFDRLRLG-DQLDL--DGPYGIAYLrtDVTR--PIVGIAGGSGLAPVLSVLQ 226
Cdd:PLN02631  376 -QGSWTQKLYTHLSSSiDSLEVstEGPYGPNSF--DVSRhnSLILVSGGSGITPFISVIR 432
FNR_like_2 cd06197
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) ...
 111-325 1.19e-03

FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (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 have a variety of physiological functions in a variety of organisms including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which varies 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 two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99794  Cd Length: 220  Bit Score: 39.68  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 111 IDRKALTPDISLFTFASDGPAEFL---AGQYAMIGIPALSQARAYSMSNIA----NEEGIWQFIIRRVPE---------- 173
Cdd:cd06197     1 IKSEVITPTLTRFTFELSPPDVVGkwtPGQYITLDFSSELDSGYSHMADDDpqslNDDFVRTFTVSSAPPhdpatdefei 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 174 -----GKVTAYLFDRLRLGDQLDL-------DGPYGIAYLRTDVTRPIVGIAGGSGLAPVLSVLQGAARSRcANGARPAM 241
Cdd:cd06197    81 tvrkkGPVTGFLFQVARRLREQGLevpvlgvGGEFTLSLPGEGAERKMVWIAGGVGITPFLAMLRAILSSR-NTTWDITL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 242 LYGGRTPtDIPDVRQmateagievDFHPVISAPVNgvsvewrgdigfVHEFIAKklaaplpgyEYYLAGPPPMIEAAVRL 321
Cdd:cd06197   160 LWSLRED-DLPLVMD---------TLVRFPGLPVS------------TTLFITS---------EVYLCGPPALEKAVLEW 208


                  ....
gi 1308985323 322 LVAE 325
Cdd:cd06197   209 LEGK 212
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 21-89 1.86e-03

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 39.69  E-value: 1.86e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308985323  21 GDTLLRAGLRQGLGLAYECNVGACGSCKFDLIAGEVddlfpEASG---LRPKEREKGKRLACQCVPRSDCTI 89
Cdd:PRK10684  265 GTTLLEALESNKVPVVAACRAGVCGCCKTKVVSGEY-----TVSStmtLTPAEIAQGYVLACSCHPQGDLVL 331
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 160-330 2.31e-03

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 39.73  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 160 EEGIWQFIIRRVpeGKVTAYLFDrLRLGDQL-DLDGPYG----IAYLRTdvtrpIVGIAGGSGLAPVLSVLQGAArsrcA 234
Cdd:PRK12778   55 EKGTITLVIQEV--GLSTTKLCE-LNEGDYItDVVGPLGnpseIENYGT-----VVCAGGGVGVAPMLPIVKALK----A 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 235 NGARPAMLYGGRTPTDI---PDVRQMATEAGIEVDfhpvisapvNGVsvewRGDIGFVHEFIaKKLAAPLPGYEYYLA-G 310
Cdd:PRK12778  123 AGNRVITILGGRSKELIileDEMRESSDEVIIMTD---------DGS----YGRKGLVTDGL-EEVIKRETKVDKVFAiG 188

                         170       180
                  ....*....|....*....|
gi 1308985323 311 PPPMIeAAVRLLVAEHKVPT 330
Cdd:PRK12778  189 PAIMM-KFVCLLTKKYGIPT 207
PTZ00274 PTZ00274
cytochrome b5 reductase; Provisional
 116-251 3.89e-03

cytochrome b5 reductase; Provisional


Pssm-ID: 140300  Cd Length: 325  Bit Score: 38.75  E-value: 3.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308985323 116 LTPDISLFTFASDGPAEF-------LAGQYAMiGIPALSQARAYSMSNIANE-EGIWQFIIRRVPEGKVTAYLFDrLRLG 187
Cdd:PTZ00274   63 ITHDTALFRFLLHSEEEFnlkpcstLQACYKY-GVQPMDQCQRFYTPVTANHtKGYFDIIVKRKKDGLMTNHLFG-MHVG 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308985323 188 DQLDLDG-PYGIAYlRTDVTRPIVGIAGGSGLAPVLSVLQGAARSRCANG----ARPAMLYGGRTPTDI 251
Cdd:PTZ00274  141 DKLLFRSvTFKIQY-RPNRWKHVGMIAGGTGFTPMLQIIRHSLTEPWDSGevdrTKLSFLFCNRTERHI 208
 
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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