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Conserved domains on  [gi|2022570156|dbj|BCF34802|]
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oxidoreductase [Bradyrhizobium diazoefficiens]

Protein Classification

hybrid-cluster NAD(P)-dependent oxidoreductase; FAD-binding oxidoreductase( domain architecture ID 10082242)

NAD(P)-dependent oxidoreductase that is a hybrid-cluster protein containing both [2Fe-2S] (or [4Fe-4S]) and [4Fe-2S-2O] clusters, may transfer electrons to carrier proteins such as ferredoxin; FAD-binding oxidoreductase catalyzes the oxidation or reduction of a specific substrate using flavin adenine dinucleotide (FAD) as a cofactor; also contains a major facilitator superfamily (MFS) transporter domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 109-342 2.60e-148

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: 417.12  E-value: 2.60e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 109 FTGTVTSVSALTHDIRRLEITLEQP--LKFWAGQYVDITLPGPEtITRSFSMANSPGESQNLAFIIKKYPNGRFSSRLDG 186
Cdd:cd06212     1 FVGTVVAVEALTHDIRRLRLRLEEPepIKFFAGQYVDITVPGTE-ETRSFSMANTPADPGRLEFIIKKYPGGLFSSFLDD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 187 DLAVGTEVGIKGPYGTCFRRENKTGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDLFYLDHFAELAAKH 266
Cdd:cd06212    80 GLAVGDPVTVTGPYGTCTLRESRDRPIVLIGGGSGMAPLLSLLRDMAASGSDRPVRFFYGARTARDLFYLEEIAALGEKI 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2022570156 267 PEFTFVPVLSHAADDTAWGGAKGFVHEAVGEHLRGADygeDVDVYACGPSPMIEALTPVLQMSDVESDRIFFDKFT 342
Cdd:cd06212   160 PDFTFIPALSESPDDEGWSGETGLVTEVVQRNEATLA---GCDVYLCGPPPMIDAALPVLEMSGVPPDQIFYDKFT 232
Fdx COG0633
Ferredoxin [Energy production and conversion];
8-92 1.50e-25

Ferredoxin [Energy production and conversion];


:

Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 98.00  E-value: 1.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156   8 VRLQPVGIEFEVEENETVLDAAFRQGIALPHGCKEGQCSACKCVLTGGDVELKKYStfALNEMERGQDYILLCRTLAYSD 87
Cdd:COG0633     4 VTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREED--ALSDEERAAGSRLACQARPTSD 81


                  ....*
gi 2022570156  88 LEVEL 92
Cdd:COG0633    82 LVVEL 86
 
Name Accession Description Interval E-value
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 109-342 2.60e-148

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: 417.12  E-value: 2.60e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 109 FTGTVTSVSALTHDIRRLEITLEQP--LKFWAGQYVDITLPGPEtITRSFSMANSPGESQNLAFIIKKYPNGRFSSRLDG 186
Cdd:cd06212     1 FVGTVVAVEALTHDIRRLRLRLEEPepIKFFAGQYVDITVPGTE-ETRSFSMANTPADPGRLEFIIKKYPGGLFSSFLDD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 187 DLAVGTEVGIKGPYGTCFRRENKTGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDLFYLDHFAELAAKH 266
Cdd:cd06212    80 GLAVGDPVTVTGPYGTCTLRESRDRPIVLIGGGSGMAPLLSLLRDMAASGSDRPVRFFYGARTARDLFYLEEIAALGEKI 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2022570156 267 PEFTFVPVLSHAADDTAWGGAKGFVHEAVGEHLRGADygeDVDVYACGPSPMIEALTPVLQMSDVESDRIFFDKFT 342
Cdd:cd06212   160 PDFTFIPALSESPDDEGWSGETGLVTEVVQRNEATLA---GCDVYLCGPPPMIDAALPVLEMSGVPPDQIFYDKFT 232
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 8-343 2.48e-138

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: 398.08  E-value: 2.48e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156   8 VRLQPVGIEFEVEENETVLDAAFRQGIALPHGC-KEGQCSACKCVLTGGDVELKKYSTFALNEMERGQDYILLCRTLAYS 86
Cdd:COG2871    37 ITINGDGKEIEVEEGQTLLDALLRQGIFLPSACgGGGTCGQCKVKVLEGGGDILPTETFHLSDRERKEGYRLACQVKVKS 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156  87 DLEVELlnyDEEVLsksiPVKDFTGTVTSVSALTHDIRRLEITLEQ--PLKFWAGQYVDITLPG---------------- 148
Cdd:COG2871   117 DMEIEV---PEEVF----GVKKWEATVVSNENVTTFIKELVLELPEgeEIDFKAGQYIQIEVPPyevdfkdfdipeeekf 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 149 ------PETITRSFSMANSPGESQNLAFIIK------KYPNGRFSSRLDGdLAVGTEVGIKGPYGTCFRRENkTGAMILV 216
Cdd:COG2871   190 glfdknDEEVTRAYSMANYPAEKGIIELNIRiatppmDVPPGIGSSYIFS-LKPGDKVTISGPYGEFFLRDS-DREMVFI 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 217 GGGSGMSPLWSILHDHISSGEV-RPVRFFYGARTQNDLFYLDHFAELAAKHPEFTFVPVLSHAADDTAWGGAKGFVHEAV 295
Cdd:COG2871   268 GGGAGMAPLRSHIFDLLERGKTdRKITFWYGARSLRELFYLEEFRELEKEHPNFKFHPALSEPLPEDNWDGETGFIHEVL 347

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2022570156 296 GEH-LRGADYGEDVDVYACGPSPMIEALTPVLQMSDVESDRIFFDKFTP 343
Cdd:COG2871   348 YENyLKDHPAPEDCEAYLCGPPPMIDAVIKMLDDLGVEEENIYFDDFGG 396
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 8-344 1.77e-93

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 282.14  E-value: 1.77e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156   8 VRLQPVGIEFEVEENETVLDAAFRQGIALPHGCKEGQCSACKCVLTGGDVELKKYSTFALNEMERGQDYILLCRTLAYSD 87
Cdd:PRK07609    5 VTLQPSGRQFTAEPDETILDAALRQGIHLPYGCKNGACGSCKGRLLEGEVEQGPHQASALSGEERAAGEALTCCAKPLSD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156  88 LEVELlnydEEVL-SKSIPVKDFTGTVTSVSALTHDIRRLEITL--EQPLKFWAGQYVDITLPGPETitRSFSMANSPGE 164
Cdd:PRK07609   85 LVLEA----REVPaLGDIPVKKLPCRVASLERVAGDVMRLKLRLpaTERLQYLAGQYIEFILKDGKR--RSYSIANAPHS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 165 SQNLAFIIKKYPNGRFSSRLDGDLAVGTEVGIKGPYGTCFRRENKTGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFF 244
Cdd:PRK07609  159 GGPLELHIRHMPGGVFTDHVFGALKERDILRIEGPLGTFFLREDSDKPIVLLASGTGFAPIKSIVEHLRAKGIQRPVTLY 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 245 YGARTQNDLFYLDHFAELAAKHPEFTFVPVLSHAADDTAWGGAKGFVHEAVGEHLrgADYgEDVDVYACGPSPMIEALTP 324
Cdd:PRK07609  239 WGARRPEDLYLSALAEQWAEELPNFRYVPVVSDALDDDAWTGRTGFVHQAVLEDF--PDL-SGHQVYACGSPVMVYAARD 315

                         330       340
                  ....*....|....*....|
gi 2022570156 325 VLQMSDVESDRIFFDKFTPA 344
Cdd:PRK07609  316 DFVAAGLPAEEFFADAFTYA 335
Fdx COG0633
Ferredoxin [Energy production and conversion];
8-92 1.50e-25

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 98.00  E-value: 1.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156   8 VRLQPVGIEFEVEENETVLDAAFRQGIALPHGCKEGQCSACKCVLTGGDVELKKYStfALNEMERGQDYILLCRTLAYSD 87
Cdd:COG0633     4 VTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREED--ALSDEERAAGSRLACQARPTSD 81


                  ....*
gi 2022570156  88 LEVEL 92
Cdd:COG0633    82 LVVEL 86
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 215-321 2.42e-24

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: 95.40  E-value: 2.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 215 LVGGGSGMSPLWSILHdHI--SSGEVRPVRFFYGARTQNDLFYLDHFAELAAKHPE-FTFVPVLSHAADDtaWGGAKGFV 291
Cdd:pfam00175   1 MIAGGTGIAPVRSMLR-AIleDPKDPTQVVLVFGNRNEDDILYREELDELAEKHPGrLTVVYVVSRPEAG--WTGGKGRV 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 2022570156 292 HEAVGEHLRGADyGEDVDVYACGPSPMIEA 321
Cdd:pfam00175  78 QDALLEDHLSLP-DEETHVYVCGPPGMIKA 106
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 14-91 8.67e-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: 85.14  E-value: 8.67e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2022570156  14 GIEFEVEENETVLDAAFRQGIALPHGCKEGQCSACKCVLTGGDVELKkySTFALNEMERGQDYILLCRTLAYSDLEVE 91
Cdd:cd00207     9 GVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQS--DPSLLDEEEAEGGYVLACQTRVTDGLVIE 84
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
8-84 1.99e-15

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 70.25  E-value: 1.99e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2022570156   8 VRLQPVGIEFEVEENET-VLDAAFRQGIALPHGCKEGQCSACKCVLTGGDVELKkySTFALNEMERGQDYILLCRTLA 84
Cdd:pfam00111   1 VTINGKGVTIEVPDGETtLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSD--QSFLEDDELAAGYVVLACQTYP 76
PTZ00038 PTZ00038
ferredoxin; Provisional
 16-91 4.27e-11

ferredoxin; Provisional


Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 61.39  E-value: 4.27e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2022570156  16 EFEVEENETVLDAAFRQGIALPHGCKEGQCSACKCVLTGGDVELKKYSTFALNEMERGqdYILLCRTLAYSDLEVE 91
Cdd:PTZ00038  108 VIECDEDEYILDAAERQGVELPYSCRGGSCSTCAAKLLEGEVDNEDQSYLDDEQLKKG--YCLLCTCYPKSDCTIE 181
 
Name Accession Description Interval E-value
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 109-342 2.60e-148

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: 417.12  E-value: 2.60e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 109 FTGTVTSVSALTHDIRRLEITLEQP--LKFWAGQYVDITLPGPEtITRSFSMANSPGESQNLAFIIKKYPNGRFSSRLDG 186
Cdd:cd06212     1 FVGTVVAVEALTHDIRRLRLRLEEPepIKFFAGQYVDITVPGTE-ETRSFSMANTPADPGRLEFIIKKYPGGLFSSFLDD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 187 DLAVGTEVGIKGPYGTCFRRENKTGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDLFYLDHFAELAAKH 266
Cdd:cd06212    80 GLAVGDPVTVTGPYGTCTLRESRDRPIVLIGGGSGMAPLLSLLRDMAASGSDRPVRFFYGARTARDLFYLEEIAALGEKI 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2022570156 267 PEFTFVPVLSHAADDTAWGGAKGFVHEAVGEHLRGADygeDVDVYACGPSPMIEALTPVLQMSDVESDRIFFDKFT 342
Cdd:cd06212   160 PDFTFIPALSESPDDEGWSGETGLVTEVVQRNEATLA---GCDVYLCGPPPMIDAALPVLEMSGVPPDQIFYDKFT 232
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 8-343 2.48e-138

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: 398.08  E-value: 2.48e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156   8 VRLQPVGIEFEVEENETVLDAAFRQGIALPHGC-KEGQCSACKCVLTGGDVELKKYSTFALNEMERGQDYILLCRTLAYS 86
Cdd:COG2871    37 ITINGDGKEIEVEEGQTLLDALLRQGIFLPSACgGGGTCGQCKVKVLEGGGDILPTETFHLSDRERKEGYRLACQVKVKS 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156  87 DLEVELlnyDEEVLsksiPVKDFTGTVTSVSALTHDIRRLEITLEQ--PLKFWAGQYVDITLPG---------------- 148
Cdd:COG2871   117 DMEIEV---PEEVF----GVKKWEATVVSNENVTTFIKELVLELPEgeEIDFKAGQYIQIEVPPyevdfkdfdipeeekf 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 149 ------PETITRSFSMANSPGESQNLAFIIK------KYPNGRFSSRLDGdLAVGTEVGIKGPYGTCFRRENkTGAMILV 216
Cdd:COG2871   190 glfdknDEEVTRAYSMANYPAEKGIIELNIRiatppmDVPPGIGSSYIFS-LKPGDKVTISGPYGEFFLRDS-DREMVFI 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 217 GGGSGMSPLWSILHDHISSGEV-RPVRFFYGARTQNDLFYLDHFAELAAKHPEFTFVPVLSHAADDTAWGGAKGFVHEAV 295
Cdd:COG2871   268 GGGAGMAPLRSHIFDLLERGKTdRKITFWYGARSLRELFYLEEFRELEKEHPNFKFHPALSEPLPEDNWDGETGFIHEVL 347

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2022570156 296 GEH-LRGADYGEDVDVYACGPSPMIEALTPVLQMSDVESDRIFFDKFTP 343
Cdd:COG2871   348 YENyLKDHPAPEDCEAYLCGPPPMIDAVIKMLDDLGVEEENIYFDDFGG 396
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 8-344 1.77e-93

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 282.14  E-value: 1.77e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156   8 VRLQPVGIEFEVEENETVLDAAFRQGIALPHGCKEGQCSACKCVLTGGDVELKKYSTFALNEMERGQDYILLCRTLAYSD 87
Cdd:PRK07609    5 VTLQPSGRQFTAEPDETILDAALRQGIHLPYGCKNGACGSCKGRLLEGEVEQGPHQASALSGEERAAGEALTCCAKPLSD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156  88 LEVELlnydEEVL-SKSIPVKDFTGTVTSVSALTHDIRRLEITL--EQPLKFWAGQYVDITLPGPETitRSFSMANSPGE 164
Cdd:PRK07609   85 LVLEA----REVPaLGDIPVKKLPCRVASLERVAGDVMRLKLRLpaTERLQYLAGQYIEFILKDGKR--RSYSIANAPHS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 165 SQNLAFIIKKYPNGRFSSRLDGDLAVGTEVGIKGPYGTCFRRENKTGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFF 244
Cdd:PRK07609  159 GGPLELHIRHMPGGVFTDHVFGALKERDILRIEGPLGTFFLREDSDKPIVLLASGTGFAPIKSIVEHLRAKGIQRPVTLY 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 245 YGARTQNDLFYLDHFAELAAKHPEFTFVPVLSHAADDTAWGGAKGFVHEAVGEHLrgADYgEDVDVYACGPSPMIEALTP 324
Cdd:PRK07609  239 WGARRPEDLYLSALAEQWAEELPNFRYVPVVSDALDDDAWTGRTGFVHQAVLEDF--PDL-SGHQVYACGSPVMVYAARD 315

                         330       340
                  ....*....|....*....|
gi 2022570156 325 VLQMSDVESDRIFFDKFTPA 344
Cdd:PRK07609  316 DFVAAGLPAEEFFADAFTYA 335
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 113-341 4.06e-85

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: 256.37  E-value: 4.06e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 113 VTSVSALTHDIRRLEITLEQPLKFWAGQYVDITLPGPETITRSFSMANSPGESQNLAFIIKKYPNGRFSSRLDGDLAVGT 192
Cdd:cd06187     1 VVSVERLTHDIAVVRLQLDQPLPFWAGQYVNVTVPGRPRTWRAYSPANPPNEDGEIEFHVRAVPGGRVSNALHDELKVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 193 EVGIKGPYGTCFRRENKTGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDLFYLDHFAELAAKHPEFTFV 272
Cdd:cd06187    81 RVRLSGPYGTFYLRRDHDRPVLCIAGGTGLAPLRAIVEDALRRGEPRPVHLFFGARTERDLYDLEGLLALAARHPWLRVV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2022570156 273 PVLSHAADdtAWGGAKGFVHEAVGEHLRGadyGEDVDVYACGPSPMIEALTPVLQMSDVESDRIFFDKF 341
Cdd:cd06187   161 PVVSHEEG--AWTGRRGLVTDVVGRDGPD---WADHDIYICGPPAMVDATVDALLARGAPPERIHFDKF 224
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 105-341 7.04e-78

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: 238.38  E-value: 7.04e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 105 PVKDFTGTVTSVSALTHDIRRLEITLEQP--LKFWAGQYVDITLPGPETiTRSFSMANSPGESQNLAFIIKKYPNGRFSS 182
Cdd:cd06211     3 NVKDFEGTVVEIEDLTPTIKGVRLKLDEPeeIEFQAGQYVNLQAPGYEG-TRAFSIASSPSDAGEIELHIRLVPGGIATT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 183 RLDGDLAVGTEVGIKGPYGTCFRRENKTGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDLFYLDHFAEL 262
Cdd:cd06211    82 YVHKQLKEGDELEISGPYGDFFVRDSDQRPIIFIAGGSGLSSPRSMILDLLERGDTRKITLFFGARTRAELYYLDEFEAL 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2022570156 263 AAKHPEFTFVPVLSHAADDTAWGGAKGFVHEAVGEHLRGADYGEdvDVYACGPSPMIEALTPVLQMSDVESDRIFFDKF 341
Cdd:cd06211   162 EKDHPNFKYVPALSREPPESNWKGFTGFVHDAAKKHFKNDFRGH--KAYLCGPPPMIDACIKTLMQGRLFERDIYYEKF 238
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 109-341 7.51e-68

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: 212.56  E-value: 7.51e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 109 FTGTVTSVSALTHDIRRLEITLEQPLKFWAGQYVDITLPGPETiTRSFSMANSPGESQNLAFIIKKYPNGRFSSRLDGDL 188
Cdd:cd06213     1 IRGTIVAQERLTHDIVRLTVQLDRPIAYKAGQYAELTLPGLPA-ARSYSFANAPQGDGQLSFHIRKVPGGAFSGWLFGAD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 189 AVGTEVGIKGPYGTcFRRENKTGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDLFYLDHFAELAAK-HP 267
Cdd:cd06213    80 RTGERLTVRGPFGD-FWLRPGDAPILCIAGGSGLAPILAILEQARAAGTKRDVTLLFGARTQRDLYALDEIAAIAARwRG 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2022570156 268 EFTFVPVLSHAADDTAWGGAKGFVHeavgEHLRgADYGEDVDVYACGPSPMIEALTPVLQMSDVESDRIFFDKF 341
Cdd:cd06213   159 RFRFIPVLSEEPADSSWKGARGLVT----EHIA-EVLLAATEAYLCGPPAMIDAAIAVLRALGIAREHIHADRF 227
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 113-341 1.03e-66

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: 209.33  E-value: 1.03e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 113 VTSVSALTHDIRRLEITLEQPLKFWAGQYVDITLPGPETitRSFSMANSPGESQNLAFIIKKYPNGRFSSRLDGDLAVGT 192
Cdd:cd06189     3 VESIEPLNDDVYRVRLKPPAPLDFLAGQYLDLLLDDGDK--RPFSIASAPHEDGEIELHIRAVPGGSFSDYVFEELKENG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 193 EVGIKGPYGTCFRRENKTGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDLFYLDHFAELAAKHPEFTFV 272
Cdd:cd06189    81 LVRIEGPLGDFFLREDSDRPLILIAGGTGFAPIKSILEHLLAQGSKRPIHLYWGARTEEDLYLDELLEAWAEAHPNFTYV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2022570156 273 PVLSHAADDtaWGGAKGFVHEAVGEhlrgaDYG--EDVDVYACGPSPMIEALTPVLQMSDVESDRIFFDKF 341
Cdd:cd06189   161 PVLSEPEEG--WQGRTGLVHEAVLE-----DFPdlSDFDVYACGSPEMVYAARDDFVEKGLPEENFFSDAF 224
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 113-341 2.92e-64

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: 203.64  E-value: 2.92e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 113 VTSVSALTHDIRRLEITLEQPLKFWAGQYVDITLPGPETiTRSFSMANSPGESQNLAFIIKKYPNGRFSSRLDGDLAVGT 192
Cdd:cd06190     1 LVDVRELTHDVAEFRFALDGPADFLPGQYALLALPGVEG-ARAYSMANLANASGEWEFIIKRKPGGAASNALFDNLEPGD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 193 EVGIKGPYGTCFRRENKTGAMILVGGGSGMSPLWSILHDHISSG--EVRPVRFFYGARTQNDLFYLDHFAELAAKHPEFT 270
Cdd:cd06190    80 ELELDGPYGLAYLRPDEDRDIVCIAGGSGLAPMLSILRGAARSPylSDRPVDLFYGGRTPSDLCALDELSALVALGARLR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2022570156 271 FVPVLSHAADDTA--WGGAKGFVHEAVGEHLRGADygEDVDVYACGPSPMIEALTPVLQMSD-VESDRIFFDKF 341
Cdd:cd06190   160 VTPAVSDAGSGSAagWDGPTGFVHEVVEATLGDRL--AEFEFYFAGPPPMVDAVQRMLMIEGvVPFDQIHFDRF 231
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 114-339 6.88e-60

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: 191.89  E-value: 6.88e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 114 TSVSALTHDIRRLEITLEQPLKFWAGQYVDITLPGPET-ITRSFSMANSPGESQNLAFIIKKYPNGRFSSRLDgDLAVGT 192
Cdd:cd00322     1 VATEDVTDDVRLFRLQLPNGFSFKPGQYVDLHLPGDGRgLRRAYSIASSPDEEGELELTVKIVPGGPFSAWLH-DLKPGD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 193 EVGIKGPYGTCFRRENKTGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDLFYLDHFAELAAKHPEFTFV 272
Cdd:cd00322    80 EVEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGEITLLYGARTPADLLFLDELEELAKEGPNFRLV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2022570156 273 PVLSHAADDTAWGGAKGFVHEAVGEHLRGADygeDVDVYACGPSPMIEALTPVLQMSDVESDRIFFD 339
Cdd:cd00322   160 LALSRESEAKLGPGGRIDREAEILALLPDDS---GALVYICGPPAMAKAVREALVSLGVPEERIHTE 223
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 109-342 1.41e-59

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: 191.27  E-value: 1.41e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 109 FTGTVTSVSALTHDIRRLEITLE--QPLKFWAGQYVDITLPGPEtITRSFSMANSPGESQnLAFIIKKYPNGRFSSRLDG 186
Cdd:cd06209     2 FEATVTEVERLSDSTIGLTLELDeaGALAFLPGQYVNLQVPGTD-ETRSYSFSSAPGDPR-LEFLIRLLPGGAMSSYLRD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 187 DLAVGTEVGIKGPYGTCFRREnKTGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDLFYLDHFAELAAKH 266
Cdd:cd06209    80 RAQPGDRLTLTGPLGSFYLRE-VKRPLLMLAGGTGLAPFLSMLDVLAEDGSAHPVHLVYGVTRDADLVELDRLEALAERL 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2022570156 267 PEFTFVPVLSHAAddtAWGGAKGFVHeavgEHLRGADY-GEDVDVYACGPSPMIEALTPVLQMSDVESDRIFFDKFT 342
Cdd:cd06209   159 PGFSFRTVVADPD---SWHPRKGYVT----DHLEAEDLnDGDVDVYLCGPPPMVDAVRSWLDEQGIEPANFYYEKFT 228
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 112-339 5.33e-59

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 190.46  E-value: 5.33e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 112 TVTSVSALTHDIRRLEITL-EQPLKFWAGQYVDITLPGpETITRSFSMANSPGESQNLAFIIKKYpnGRFSSRLdGDLAV 190
Cdd:COG0543     1 KVVSVERLAPDVYLLRLEApLIALKFKPGQFVMLRVPG-DGLRRPFSIASAPREDGTIELHIRVV--GKGTRAL-AELKP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 191 GTEVGIKGPYGTCFRRENKTGAMILVGGGSGMSPLWSILHDHISSGevRPVRFFYGARTQNDLFYLDHFAELAakhpEFT 270
Cdd:COG0543    77 GDELDVRGPLGNGFPLEDSGRPVLLVAGGTGLAPLRSLAEALLARG--RRVTLYLGARTPEDLYLLDELEALA----DFR 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2022570156 271 FVpVLShaadDTAWGGAKGFVHEAVGEHLrgaDYGEDVDVYACGPSPMIEALTPVLQMSDVESDRIFFD 339
Cdd:COG0543   151 VV-VTT----DDGWYGRKGFVTDALKELL---AEDSGDDVYACGPPPMMKAVAELLLERGVPPERIYVS 211
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
17-345 4.08e-56

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 186.10  E-value: 4.08e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156  17 FEVEENETVLDAAFRQGIALPHGCKEGQCSACKCVLTGGDVELKKYSTFALNEMERGQDYILLCRTLAYSDLEVeLLNYD 96
Cdd:PRK11872   17 FPVGKDELLLDAALRNGINLPLDCREGVCGTCQGRCESGIYSQDYVDEDALSERDLAQRKMLACQTRVKSDAAF-YFDFD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156  97 EEVLSKSIPVKdFTGTVTSVSALTHDIRRLEITL---EQPLKFWAGQYVDITLPGPETiTRSFSMANSPGESQNLAFIIK 173
Cdd:PRK11872   96 SSLCNAGDTLK-ISGVVTAVELVSETTAILHLDAsahGRQLDFLPGQYARLQIPGTDD-WRSYSFANRPNATNQLQFLIR 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 174 KYPNGRFSSRLDGDLAVGTEVGIKGPYGTCFRREnKTGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDL 253
Cdd:PRK11872  174 LLPDGVMSNYLRERCQVGDEILFEAPLGAFYLRE-VERPLVFVAGGTGLSAFLGMLDELAEQGCSPPVHLYYGVRHAADL 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 254 FYLDHFAELAAKHPEFTFVPVLSHAADDtaWGGAKGFVHeavgEHLRGADYGE-DVDVYACGPSPMIEALTPVLQMSDVE 332
Cdd:PRK11872  253 CELQRLAAYAERLPNFRYHPVVSKASAD--WQGKRGYIH----EHFDKAQLRDqAFDMYLCGPPPMVEAVKQWLDEQALE 326

                         330
                  ....*....|...
gi 2022570156 333 SDRIFFDKFTPAN 345
Cdd:PRK11872  327 NYRLYYEKFTQSN 339
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
109-340 5.02e-53

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 174.59  E-value: 5.02e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 109 FTGTVTSVSALTHDIRRLEITLEQPLK---FWAGQYVDITLP-GPETITRSFSMANSPGESQnLAFIIKKYPNGRFSSRL 184
Cdd:COG1018     4 RPLRVVEVRRETPDVVSFTLEPPDGAPlprFRPGQFVTLRLPiDGKPLRRAYSLSSAPGDGR-LEITVKRVPGGGGSNWL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 185 DGDLAVGTEVGIKGPYGTCFRRENKTGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDLFYLDHFAELAA 264
Cdd:COG1018    83 HDHLKVGDTLEVSGPRGDFVLDPEPARPLLLIAGGIGITPFLSMLRTLLARGPFRPVTLVYGARSPADLAFRDELEALAA 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2022570156 265 KHPEFTFVPVLSHAADdtawgGAKGFV-HEAVGEHLRGAdygEDVDVYACGPSPMIEALTPVLQMSDVESDRIFFDK 340
Cdd:COG1018   163 RHPRLRLHPVLSREPA-----GLQGRLdAELLAALLPDP---ADAHVYLCGPPPMMEAVRAALAELGVPEERIHFER 231
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 108-342 6.17e-52

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: 171.76  E-value: 6.17e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 108 DFTGTVTSVSALTHDIRRLEI------TLEQPLKFWAGQYVDITLPGPETiTRSFSMANSPGESQNLAFIIKKYPNGRFS 181
Cdd:cd06210     1 VREAEIVAVDRVSSNVVRLRLqpddaeGAGIAAEFVPGQFVEIEIPGTDT-RRSYSLANTPNWDGRLEFLIRLLPGGAFS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 182 SRLDGDLAVGTEVGIKGPYGTCFRRENKTGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDLFYLDHFAE 261
Cdd:cd06210    80 TYLETRAKVGQRLNLRGPLGAFGLRENGLRPRWFVAGGTGLAPLLSMLRRMAEWGEPQEARLFFGVNTEAELFYLDELKR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 262 LAAKHPEFTFVPVLSHAADDtaWGGAKGFVHEAVGEHLRGADYGEdvDVYACGPSPMIEALTPVLQMSDVESDRIFFDKF 341
Cdd:cd06210   160 LADSLPNLTVRICVWRPGGE--WEGYRGTVVDALREDLASSDAKP--DIYLCGPPGMVDAAFAAAREAGVPDEQVYLEKF 235


                  .
gi 2022570156 342 T 342
Cdd:cd06210   236 L 236
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
 97-341 1.78e-51

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: 172.10  E-value: 1.78e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156  97 EEVLSksipVKDFTGTVTSVSALTHDIR--RLEITLEQPLKFWAGQYVDITLPGP------------------------- 149
Cdd:cd06188     2 EEVLG----AKKWECTVISNDNVATFIKelVLKLPSGEEIAFKAGGYIQIEIPAYeiayadfdvaekyradwdkfglwql 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 150 -----ETITRSFSMANSPGESQNLAFIIK---------KYPNGRFSSRLdGDLAVGTEVGIKGPYGTCFRRENKTgAMIL 215
Cdd:cd06188    78 vfkhdEPVSRAYSLANYPAEEGELKLNVRiatpppgnsDIPPGIGSSYI-FNLKPGDKVTASGPFGEFFIKDTDR-EMVF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 216 VGGGSGMSPLWS-ILHDHISSGEVRPVRFFYGARTQNDLFYLDHFAELAAKHPEFTFVPVLSHAADDTAWGGAKGFVHEA 294
Cdd:cd06188   156 IGGGAGMAPLRShIFHLLKTLKSKRKISFWYGARSLKELFYQEEFEALEKEFPNFKYHPVLSEPQPEDNWDGYTGFIHQV 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2022570156 295 VGEH-LRGADYGEDVDVYACGPSPMIEALTPVLQMSDVESDRIFFDKF 341
Cdd:cd06188   236 LLENyLKKHPAPEDIEFYLCGPPPMNSAVIKMLDDLGVPRENIAFDDF 283
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 113-341 5.59e-50

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: 166.29  E-value: 5.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 113 VTSVSALTHDIRRLEITLEQPLKFWAGQYVDITLPGpeTITRSFSMANSPGESQNLAFIIKKYPNGRFSSRLDGDLAVGT 192
Cdd:cd06194     1 VVSLQRLSPDVLRVRLEPDRPLPYLPGQYVNLRRAG--GLARSYSPTSLPDGDNELEFHIRRKPNGAFSGWLGEEARPGH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 193 EVGIKGPYGTCFRR-ENKTGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDLFYLDHFAELAAKHPEFTF 271
Cdd:cd06194    79 ALRLQGPFGQAFYRpEYGEGPLLLVGAGTGLAPLWGIARAALRQGHQGEIRLVHGARDPDDLYLHPALLWLAREHPNFRY 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 272 VPVLSHAADDtawGGAKGFVHEAVGEHLRGADygeDVdVYACGPSPMIEALTPVLQMSDVESDRIFFDKF 341
Cdd:cd06194   159 IPCVSEGSQG---DPRVRAGRIAAHLPPLTRD---DV-VYLCGAPSMVNAVRRRAFLAGAPMKRIYADPF 221
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 109-341 6.57e-44

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: 150.88  E-value: 6.57e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 109 FTGTVTSVSALTHDIR--RLEITLEQPLKFWAGQYVDITLPGPE--TITRSFSMANSPGESQNLAFIIKKYPNGRFSSRL 184
Cdd:cd06217     2 RVLRVTEIIQETPTVKtfRLAVPDGVPPPFLAGQHVDLRLTAIDgyTAQRSYSIASSPTQRGRVELTVKRVPGGEVSPYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 185 DGDLAVGTEVGIKGPYGTCFRRENKTGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDLFYLDHFAELAA 264
Cdd:cd06217    82 HDEVKVGDLLEVRGPIGTFTWNPLHGDPVVLLAGGSGIVPLMSMIRYRRDLGWPVPFRLLYSARTAEDVIFRDELEQLAR 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2022570156 265 KHPEFTFVPVLShAADDTAWGGAKGFVHEAVGEHLRGADygEDVDVYACGPSPMIEALTPVLQMSDVESDRIFFDKF 341
Cdd:cd06217   162 RHPNLHVTEALT-RAAPADWLGPAGRITADLIAELVPPL--AGRRVYVCGPPAFVEAATRLLLELGVPRDRIRTEAF 235
fre PRK08051
FMN reductase; Validated
 110-341 8.10e-38

FMN reductase; Validated


Pssm-ID: 236142 [Multi-domain]  Cd Length: 232  Bit Score: 134.98  E-value: 8.10e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 110 TGTVTSVSALTHDIRRLEITLEQPLKFWAGQYVDITLPgpETITRSFSMANSPGESQNL-----AFIIKKYPngrfssrl 184
Cdd:PRK08051    4 SCKVTSVEAITDTVYRVRLVPEAPFSFRAGQYLMVVMG--EKDKRPFSIASTPREKGFIelhigASELNLYA-------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 185 dgdLAV------GTEVGIKGPYGTCFRRENKTGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDLFYLDH 258
Cdd:PRK08051   74 ---MAVmerilkDGEIEVDIPHGDAWLREESERPLLLIAGGTGFSYARSILLTALAQGPNRPITLYWGGREEDHLYDLDE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 259 FAELAAKHPEFTFVPVLSHAADDtaWGGAKGFVHEAVGEhlrgaDYG--EDVDVYACGPSPMIEALTPVL-QMSDVESDR 335
Cdd:PRK08051  151 LEALALKHPNLHFVPVVEQPEEG--WQGKTGTVLTAVMQ-----DFGslAEYDIYIAGRFEMAKIARELFcRERGAREEH 223


                  ....*.
gi 2022570156 336 IFFDKF 341
Cdd:PRK08051  224 LFGDAF 229
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 112-341 6.94e-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 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: 127.32  E-value: 6.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 112 TVTSVSALTHDIR--RLEITLEQPLKFWAGQYVDITLP-GPETITRSFSMANSPGESQNLAFIIKKYPNGRFSSRLDGDL 188
Cdd:cd06215     2 RCVKIIQETPDVKtfRFAAPDGSLFAYKPGQFLTLELEiDGETVYRAYTLSSSPSRPDSLSITVKRVPGGLVSNWLHDNL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 189 AVGTEVGIKGPYG--TCFRRENKTgaMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDLFYLDHFAELAAKH 266
Cdd:cd06215    82 KVGDELWASGPAGefTLIDHPADK--LLLLSAGSGITPMMSMARWLLDTRPDADIVFIHSARSPADIIFADELEELARRH 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2022570156 267 PEFTFVPVLShAADDTAWGGAKGFVHEavgEHLRGA--DYGEDvDVYACGPSPMIEALTPVLQMSDVESDRIFFDKF 341
Cdd:cd06215   160 PNFRLHLILE-QPAPGAWGGYRGRLNA---ELLALLvpDLKER-TVFVCGPAGFMKAVKSLLAELGFPMSRFHQESF 231
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 112-337 8.09e-34

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: 124.60  E-value: 8.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 112 TVTSVSALTHDIRRLEITLEQPLKFW---AGQYVDITLP-GPETITRSFSMANSPGESQNLAFIIKKYPNGRFSSRLDgD 187
Cdd:cd06183     2 KLVSKEDISHDTRIFRFELPSPDQVLglpVGQHVELKAPdDGEQVVRPYTPISPDDDKGYFDLLIKIYPGGKMSQYLH-S 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 188 LAVGTEVGIKGPYGTCFRREN-KTGAMILVGGGSGMSPLWSILHdHISSGEVRP--VRFFYGARTQNDLFYLDHFAELAA 264
Cdd:cd06183    81 LKPGDTVEIRGPFGKFEYKPNgKVKHIGMIAGGTGITPMLQLIR-AILKDPEDKtkISLLYANRTEEDILLREELDELAK 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2022570156 265 KHPE-FTFVPVLSHAADDtaWGGAKGFVHEAVGEHLRGADYGEDVDVYACGPSPMIE-ALTPVLQMSDVESDRIF 337
Cdd:cd06183   160 KHPDrFKVHYVLSRPPEG--WKGGVGFITKEMIKEHLPPPPSEDTLVLVCGPPPMIEgAVKGLLKELGYKKDNVF 232
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 106-341 1.84e-32

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: 121.18  E-value: 1.84e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 106 VKDFTGTVTSVSALTHDIRRLEItleQPLKFW----AGQYVDITLP--GpETITRSFSMANSPGESQN-LAFIIKKYPNG 178
Cdd:cd06216    15 ARELRARVVAVRPETADMVTLTL---RPNRGWpghrAGQHVRLGVEidG-VRHWRSYSLSSSPTQEDGtITLTVKAQPDG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 179 RFSSRLDGDLAVGTEVGIKGPYGtCFRRENK-TGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDLFYLD 257
Cdd:cd06216    91 LVSNWLVNHLAPGDVVELSQPQG-DFVLPDPlPPRLLLIAAGSGITPVMSMLRTLLARGPTADVVLLYYARTREDVIFAD 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 258 HFAELAAKHPEFTFvpVLSHAADdtawgGAKGFVHEavgEHLRG--ADYgEDVDVYACGPSPMIEALTPVLQMSDVEsDR 335
Cdd:cd06216   170 ELRALAAQHPNLRL--HLLYTRE-----ELDGRLSA---AHLDAvvPDL-ADRQVYACGPPGFLDAAEELLEAAGLA-DR 237


                  ....*.
gi 2022570156 336 IFFDKF 341
Cdd:cd06216   238 LHTERF 243
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 112-342 6.43e-32

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: 119.57  E-value: 6.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 112 TVTSVSALTHDIRrlEITLEQP------LKFWAGQYVDI-TLPGPETITRSFSMANSPGESQnLAFIIKKYPNGRFSSRL 184
Cdd:cd06214     5 TVAEVVRETADAV--SITFDVPeelrdaFRYRPGQFLTLrVPIDGEEVRRSYSICSSPGDDE-LRITVKRVPGGRFSNWA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 185 DGDLAVGTEVGIKGPYGT-CFRRENKTGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDLFYLDHFAELA 263
Cdd:cd06214    82 NDELKAGDTLEVMPPAGRfTLPPLPGARHYVLFAAGSGITPVLSILKTALAREPASRVTLVYGNRTEASVIFREELADLK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 264 AKHPE-FTFVPVLShaADDTAWGGAKGFVHEA-VGEHLRGADYGEDVD-VYACGPSPMIEALTPVLQMSDVESDRIFFDK 340
Cdd:cd06214   162 ARYPDrLTVIHVLS--REQGDPDLLRGRLDAAkLNALLKNLLDATEFDeAFLCGPEPMMDAVEAALLELGVPAERIHREL 239


                  ..
gi 2022570156 341 FT 342
Cdd:cd06214   240 FT 241
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 126-342 1.28e-31

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: 118.13  E-value: 1.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 126 LEITLEQP-LKFWAGQYVDITLPGPETIT-RSFSMANSPGESQNLAFIIKkyPNGRFSSRLDGDLAVGTEVGIKGPYGtC 203
Cdd:cd06198    12 LTLEPRGPaLGHRAGQFAFLRFDASGWEEpHPFTISSAPDPDGRLRFTIK--ALGDYTRRLAERLKPGTRVTVEGPYG-R 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 204 FRRENKTGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDLFYLDHFAELAAKHpEFTFVpVLSHAADDta 283
Cdd:cd06198    89 FTFDDRRARQIWIAGGIGITPFLALLEALAARGDARPVTLFYCVRDPEDAVFLDELRALAAAA-GVVLH-VIDSPSDG-- 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2022570156 284 WGGAKGFVHEAVGEHlrgadygEDVDVYACGPSPMIEALTPVLQMSDVESDRIFFDKFT 342
Cdd:cd06198   165 RLTLEQLVRALVPDL-------ADADVWFCGPPGMADALEKGLRALGVPARRFHYERFE 216
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 111-341 4.29e-30

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: 114.55  E-value: 4.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 111 GTVTSVSALTHDIRRLEITLEQPLK--FWAGQYVDITLP-GPETITRSFSMANSPGESQnLAFIIKKYPNGRFSSRLDGD 187
Cdd:cd06191     1 LRVAEVRSETPDAVTIVFAVPGPLQygFRPGQHVTLKLDfDGEELRRCYSLCSSPAPDE-ISITVKRVPGGRVSNYLREH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 188 LAVGTEVGIKGPYGTCFRRENKTGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDLFYLDHFAELAAKHP 267
Cdd:cd06191    80 IQPGMTVEVMGPQGHFVYQPQPPGRYLLVAAGSGITPLMAMIRATLQTAPESDFTLIHSARTPADMIFAQELRELADKPQ 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2022570156 268 EFTFVPVLSHAADDTAWGGAKGFVHEAVGEHLrGADYGEDvDVYACGPSPMIEALTPVLQMSDVESDRIFFDKF 341
Cdd:cd06191   160 RLRLLCIFTRETLDSDLLHGRIDGEQSLGAAL-IPDRLER-EAFICGPAGMMDAVETALKELGMPPERIHTERF 231
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 134-344 5.24e-29

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: 112.27  E-value: 5.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 134 LKFWAGQY--VDITLPGPE-TITRSFSMANSPGESQnLAFIIKKYPNGRFSSRLDGDLAVGTEVGIKGPYGTCFRRENKT 210
Cdd:cd06184    35 PPFLPGQYlsVRVKLPGLGyRQIRQYSLSDAPNGDY-YRISVKREPGGLVSNYLHDNVKVGDVLEVSAPAGDFVLDEASD 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 211 GAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDLFYLDHFAELAAKHPEFTFVPVLSHAADDTAWGG--AK 288
Cdd:cd06184   114 RPLVLISAGVGITPMLSMLEALAAEGPGRPVTFIHAARNSAVHAFRDELEELAARLPNLKLHVFYSEPEAGDREEDydHA 193

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2022570156 289 GFV-HEAVGEHLRGADYgedvDVYACGPSPMIEALTPVLQMSDVESDRIFFDKFTPA 344
Cdd:cd06184   194 GRIdLALLRELLLPADA----DFYLCGPVPFMQAVREGLKALGVPAERIHYEVFGPG 246
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 112-276 1.56e-26

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: 105.34  E-value: 1.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 112 TVTSVSALTHDIRRLEITLEQPLKFWAGQYVDITLPGPET--ITRSFSMANSPGEsQNLAFIIKKYPNGRFSSRLdGDLA 189
Cdd:cd06195     1 TVLKRRDWTDDLFSFRVTRDIPFRFQAGQFTKLGLPNDDGklVRRAYSIASAPYE-ENLEFYIILVPDGPLTPRL-FKLK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 190 VGTEVGI-KGPYGT-CFRRENKTGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDLFYLDHFAELAAKHP 267
Cdd:cd06195    79 PGDTIYVgKKPTGFlTLDEVPPGKRLWLLATGTGIAPFLSMLRDLEIWERFDKIVLVHGVRYAEELAYQDEIEALAKQYN 158

                         170
                  ....*....|
gi 2022570156 268 E-FTFVPVLS 276
Cdd:cd06195   159 GkFRYVPIVS 168
Fdx COG0633
Ferredoxin [Energy production and conversion];
8-92 1.50e-25

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 98.00  E-value: 1.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156   8 VRLQPVGIEFEVEENETVLDAAFRQGIALPHGCKEGQCSACKCVLTGGDVELKKYStfALNEMERGQDYILLCRTLAYSD 87
Cdd:COG0633     4 VTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREED--ALSDEERAAGSRLACQARPTSD 81


                  ....*
gi 2022570156  88 LEVEL 92
Cdd:COG0633    82 LVVEL 86
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 215-321 2.42e-24

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: 95.40  E-value: 2.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 215 LVGGGSGMSPLWSILHdHI--SSGEVRPVRFFYGARTQNDLFYLDHFAELAAKHPE-FTFVPVLSHAADDtaWGGAKGFV 291
Cdd:pfam00175   1 MIAGGTGIAPVRSMLR-AIleDPKDPTQVVLVFGNRNEDDILYREELDELAEKHPGrLTVVYVVSRPEAG--WTGGKGRV 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 2022570156 292 HEAVGEHLRGADyGEDVDVYACGPSPMIEA 321
Cdd:pfam00175  78 QDALLEDHLSLP-DEETHVYVCGPPGMIKA 106
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 113-337 3.43e-24

Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural similarity to ferredoxin reductase and sequence similarity to dihydroorotate dehydrogenases. Clostridium pasteurianum inducible dissimilatory type sulfite reductase is linked to ferredoxin and reduces NH2OH and SeO3 at a lesser rate than it's normal substate SO3(2-). Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+.


Pssm-ID: 99817 [Multi-domain]  Cd Length: 253  Bit Score: 99.22  E-value: 3.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 113 VTSVSALTHDIR----RLEITLEQPLKFWAGQYVDITLPGPETITrsFSMANSPGESQNLAFIIKKYpnGRFSSRLDgDL 188
Cdd:cd06221     1 IVEVVDETEDIKtftlRLEDDDEELFTFKPGQFVMLSLPGVGEAP--ISISSDPTRRGPLELTIRRV--GRVTEALH-EL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 189 AVGTEVGIKGPYGTCFRRENKTGA-MILVGGGSGMSPLWSILHDHISSGE-VRPVRFFYGARTQNDLFYLDHFAELAAKH 266
Cdd:cd06221    76 KPGDTVGLRGPFGNGFPVEEMKGKdLLLVAGGLGLAPLRSLINYILDNREdYGKVTLLYGARTPEDLLFKEELKEWAKRS 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2022570156 267 PEFTFVPVlshAADDTAWGGAKGFVHEAVgEHLRGADygEDVDVYACGPSPMIEALTPVLQMSDVESDRIF 337
Cdd:cd06221   156 DVEVILTV---DRAEEGWTGNVGLVTDLL-PELTLDP--DNTVAIVCGPPIMMRFVAKELLKLGVPEEQIW 220
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 112-338 4.16e-24

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 98.79  E-value: 4.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 112 TVTSVSALTHDIRRLEITLEQPLKFWAGQYVDITLPGPETITR---SFSMANSpgesQNLAFIIKKYpnGRFSSRLdGDL 188
Cdd:PRK00054    8 KIVENKEIAPNIYTLVLDGEKVFDMKPGQFVMVWVPGVEPLLErpiSISDIDK----NEITILYRKV--GEGTKKL-SKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 189 AVGTEVGIKGPYGTCFRRENKTGAMILVGGGSGMSPLWSILHDHISSGEVrpVRFFYGARTQNDLFYLDHFAELAAKHPe 268
Cdd:PRK00054   81 KEGDELDIRGPLGNGFDLEEIGGKVLLVGGGIGVAPLYELAKELKKKGVE--VTTVLGARTKDEVIFEEEFAKVGDVYV- 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 269 ftfvpvlshAADDTAWgGAKGFVHEAVGEHLRGADYgedvdVYACGPSPMIEAltpVLQMSDVESDRIFF 338
Cdd:PRK00054  158 ---------TTDDGSY-GFKGFVTDVLDELDSEYDA-----IYSCGPEIMMKK---VVEILKEKKVPAYV 209
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 128-322 6.88e-23

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: 95.39  E-value: 6.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 128 ITLEQPLKFWAGQYVDITLPGPETITRSFSmanspGESQNLAFIIKKYpnGRFSSRLdGDLAVGTEVGIKGPYGTCFRRE 207
Cdd:cd06220    16 FVFDWDFDFKPGQFVMVWVPGVDEIPMSLS-----YIDGPNSITVKKV--GEATSAL-HDLKEGDKLGIRGPYGNGFELV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 208 NktGAMILVGGGSGMSPLWSILhDHISSGEVrpVRFFYGARTQNDLFYLDHFAELAAKHPeftfvpvlshAADDTAWgGA 287
Cdd:cd06220    88 G--GKVLLIGGGIGIAPLAPLA-ERLKKAAD--VTVLLGARTKEELLFLDRLRKSDELIV----------TTDDGSY-GF 151

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2022570156 288 KGFVHEAVGEHLrgadyGEDVD-VYACGPSPMIEAL 322
Cdd:cd06220   152 KGFVTDLLKELD-----LEEYDaIYVCGPEIMMYKV 182
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 14-91 8.67e-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: 85.14  E-value: 8.67e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2022570156  14 GIEFEVEENETVLDAAFRQGIALPHGCKEGQCSACKCVLTGGDVELKkySTFALNEMERGQDYILLCRTLAYSDLEVE 91
Cdd:cd00207     9 GVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQS--DPSLLDEEEAEGGYVLACQTRVTDGLVIE 84
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 113-322 6.34e-20

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: 87.22  E-value: 6.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 113 VTSVSALTHDIRRLEITLEQPLK-FWAGQYVDITLPGPETIT--RSFSMANSPGESQNLAFIIKKYpnGRFSSRLDGdLA 189
Cdd:cd06218     1 VLSNREIADDIYRLVLEAPEIAAaAKPGQFVMLRVPDGSDPLlrRPISIHDVDPEEGTITLLYKVV--GKGTRLLSE-LK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 190 VGTEVGIKGPYGTCFRRENKTGAMILVGGGSGMSPLWSILHDHISSGevRPVRFFYGARTQNDLFYLDHFAELAAKHpef 269
Cdd:cd06218    78 AGDELDVLGPLGNGFDLPDDDGKVLLVGGGIGIAPLLFLAKQLAERG--IKVTVLLGFRSADDLFLVEEFEALGAEV--- 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2022570156 270 tfvpvlsHAADDTAWGGAKGFVHEAVGEHLrgADYGEDVdVYACGPSPMIEAL 322
Cdd:cd06218   153 -------YVATDDGSAGTKGFVTDLLKELL--AEARPDV-VYACGPEPMLKAV 195
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 109-339 9.06e-20

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: 86.14  E-value: 9.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 109 FTGTVTSVSALTHDIRRLeiTLEQP--LKFWAGQYVDITL--PGPETITRSFSMANSPGESQnLAFIIKKYPN-GRFSSR 183
Cdd:cd06196     1 HTVTLLSIEPVTHDVKRL--RFDKPegYDFTPGQATEVAIdkPGWRDEKRPFTFTSLPEDDV-LEFVIKSYPDhDGVTEQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 184 LdGDLAVGTEVGIKGPYGTCFRRenktGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDLFYLDHFAELa 263
Cdd:cd06196    78 L-GRLQPGDTLLIEDPWGAIEYK----GPGVFIAGGAGITPFIAILRDLAAKGKLEGNTLIFANKTEKDIILKDELEKM- 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2022570156 264 akhPEFTFVPVLShaaDDTAWGGAKGFVHEA-VGEHLrgADYGEDVdvYACGPSPMIEALTPVLQMSDVESDRIFFD 339
Cdd:cd06196   152 ---LGLKFINVVT---DEKDPGYAHGRIDKAfLKQHV--TDFNQHF--YVCGPPPMEEAINGALKELGVPEDSIVFE 218
PRK05713 PRK05713
iron-sulfur-binding ferredoxin reductase;
26-283 1.36e-19

iron-sulfur-binding ferredoxin reductase;


Pssm-ID: 235575 [Multi-domain]  Cd Length: 312  Bit Score: 87.86  E-value: 1.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156  26 LDAAFRQGIALPHGCKEGQCSAC--KCVltGGDVELKKYStfALNEMERGQDYILLCRTLAYSDLEVELLNydeevlsks 103
Cdd:PRK05713   20 LDALNAAGVAVPYSCRAGSCHAClvRCL--QGEPEDALPE--ALAAEKREQGWRLACQCRVVGDLRVEVFD--------- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 104 iPVKD-FTGTVTSVSALTHDIRRLEITLEQPLKFWAGQYVDITLPGPetITRSFSMANSPGESQNLAFIIKKYPNGRFSS 182
Cdd:PRK05713   87 -PQRDgLPARVVALDWLGGDVLRLRLEPERPLRYRAGQHLVLWTAGG--VARPYSLASLPGEDPFLEFHIDCSRPGAFCD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 183 RLDGdLAVGTEVGIKGPYGTCFRREN--KTGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARtQNDLFYL-DHF 259
Cdd:PRK05713  164 AARQ-LQVGDLLRLGELRGGALHYDPdwQERPLWLLAAGTGLAPLWGILREALRQGHQGPIRLLHLAR-DSAGHYLaEPL 241

                         250       260
                  ....*....|....*....|....
gi 2022570156 260 AELAAKHPEFTfVPVLSHAADDTA 283
Cdd:PRK05713  242 AALAGRHPQLS-VELVTAAQLPAA 264
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
111-202 7.28e-19

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 80.32  E-value: 7.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 111 GTVTSVSALTHDIRRLEITLEQP---LKFWAGQYVDITLPGP-ETITRSFSMANSPGESQNLAFIIKKYPNGRFSSRLDG 186
Cdd:pfam00970   2 LTLVEKELVSHDTRIFRFALPHPdqvLGLPVGQHLFLRLPIDgELVIRSYTPISSDDDKGYLELLVKVYPGGKMSQYLDE 81

                          90
                  ....*....|....*.
gi 2022570156 187 dLAVGTEVGIKGPYGT 202
Cdd:pfam00970  82 -LKIGDTIDFKGPLGR 96
PTZ00319 PTZ00319
NADH-cytochrome B5 reductase; Provisional
 119-337 1.42e-16

NADH-cytochrome B5 reductase; Provisional


Pssm-ID: 173521 [Multi-domain]  Cd Length: 300  Bit Score: 79.11  E-value: 1.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 119 LTHDIRRLEITLEQP---LKFWAGQY----VDITLPG-PETITRSFSMANSPGESQNLAFIIKKY--------PNG-RFS 181
Cdd:PTZ00319   44 VTHDTFIFRFALHSPtqrLGLPIGQHivfrCDCTTPGkPETVQHSYTPISSDDEKGYVDFLIKVYfkgvhpsfPNGgRLS 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 182 SRLDgDLAVGTEVGIKGPYGTC----------------FRRENKTG-AMIlvGGGSGMSPLWSILHDHISSGEVRP-VRF 243
Cdd:PTZ00319  124 QHLY-HMKLGDKIEMRGPVGKFeylgngtytvhkgkggLKTMHVDAfAMI--AGGTGITPMLQIIHAIKKNKEDRTkVFL 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 244 FYGARTQNDLFYLDHFAElAAKHPEFTfvpvLSHAADDTA---WGGAKGFVHEAV-GEHL-----RGADYgEDVDVYACG 314
Cdd:PTZ00319  201 VYANQTEDDILLRKELDE-AAKDPRFH----VWYTLDREAtpeWKYGTGYVDEEMlRAHLpvpdpQNSGI-KKVMALMCG 274

                         250       260
                  ....*....|....*....|....
gi 2022570156 315 PSPMIE-ALTPVLQMSDVESDRIF 337
Cdd:PTZ00319  275 PPPMLQmAVKPNLEKIGYTADNMF 298
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 114-342 3.40e-16

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: 76.37  E-value: 3.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 114 TSVSALTHDIRRLEITLE--QPLKFW-AGQYVDITLPGPetITRSFSMANSPGESQNLAFIIKKYPNGRFSSR-LDGDLA 189
Cdd:cd06185     1 VRIRDEAPDIRSFELEAPdgAPLPAFePGAHIDVHLPNG--LVRQYSLCGDPADRDRYRIAVLREPASRGGSRyMHELLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 190 VGTEVGIKGPYGTcFRRENKTGAMILVGGGSGMSPLWSILHDHISSGevRPVRFFYGARTQNDLFYLDHFAELAAKHpef 269
Cdd:cd06185    79 VGDELEVSAPRNL-FPLDEAARRHLLIAGGIGITPILSMARALAARG--ADFELHYAGRSREDAAFLDELAALPGDR--- 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2022570156 270 tfvpVLSHAADdtawggakgfvhEAVGEHLRG--ADYGEDVDVYACGPSPMIEALTPVLQMSDVESDRIFFDKFT 342
Cdd:cd06185   153 ----VHLHFDD------------EGGRLDLAAllAAPPAGTHVYVCGPEGMMDAVRAAAAALGWPEARLHFERFA 211
PLN02252 PLN02252
nitrate reductase [NADPH]
 119-337 1.81e-15

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 77.41  E-value: 1.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 119 LTHDIRRLEITLEQP---LKFWAGQ--YVDITLPGpETITRSFSMANSPGESQNLAFIIK--------KYPNG-RFSSRL 184
Cdd:PLN02252  645 LSHDVRLFRFALPSEdhvLGLPVGKhvFLCATING-KLCMRAYTPTSSDDEVGHFELVIKvyfknvhpKFPNGgLMSQYL 723

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 185 DGdLAVGTEVGIKGPYG---------------TCFRREnktgaMILVGGGSGMSPLW----SILHDHISSGEVRpvrFFY 245
Cdd:PLN02252  724 DS-LPIGDTIDVKGPLGhieyagrgsflvngkPKFAKK-----LAMLAGGTGITPMYqviqAILRDPEDKTEMS---LVY 794

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 246 GARTQNDLFYLDHFAELAAKHPE-FTFVPVLSHAADDTaWGGAKGFVHEAV-GEHLrgADYGEDVDVYACGPSPMIE-AL 322
Cdd:PLN02252  795 ANRTEDDILLREELDRWAAEHPDrLKVWYVVSQVKREG-WKYSVGRVTEAMlREHL--PEGGDETLALMCGPPPMIEfAC 871

                         250
                  ....*....|....*
gi 2022570156 323 TPVLQMSDVESDRIF 337
Cdd:PLN02252  872 QPNLEKMGYDKDSIL 886
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
8-84 1.99e-15

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 70.25  E-value: 1.99e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2022570156   8 VRLQPVGIEFEVEENET-VLDAAFRQGIALPHGCKEGQCSACKCVLTGGDVELKkySTFALNEMERGQDYILLCRTLA 84
Cdd:pfam00111   1 VTINGKGVTIEVPDGETtLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSD--QSFLEDDELAAGYVVLACQTYP 76
PRK13289 PRK13289
NO-inducible flavohemoprotein;
134-344 5.11e-15

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 75.22  E-value: 5.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 134 LKFWAGQYVDITL-PGPETIT--RSFSMANSPGESQnlaFII--KKYPNGRFSSRLDGDLAVGTEVGIKGPYGTCFRREN 208
Cdd:PRK13289  183 ADFKPGQYLGVRLdPEGEEYQeiRQYSLSDAPNGKY---YRIsvKREAGGKVSNYLHDHVNVGDVLELAAPAGDFFLDVA 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 209 KTGAMILVGGGSGMSPLWSILHDHISSGEVRPVRFFYGARTQNDLFYLDHFAELAAKHPEFTFVPVLSHAADDTAWGG-- 286
Cdd:PRK13289  260 SDTPVVLISGGVGITPMLSMLETLAAQQPKRPVHFIHAARNGGVHAFRDEVEALAARHPNLKAHTWYREPTEQDRAGEdf 339

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2022570156 287 -AKGFVHEavgEHLRGADYGEDVDVYACGPSPMIEALTPVLQMSDVESDRIFFDKFTPA 344
Cdd:PRK13289  340 dSEGLMDL---EWLEAWLPDPDADFYFCGPVPFMQFVAKQLLELGVPEERIHYEFFGPA 395
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
 105-314 9.36e-15

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: 73.51  E-value: 9.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 105 PVKDFTGTVTSVSALT-----HDIRRLEITLEQPLKFWAGQYVDITLPGPETIT------RSFSMANS----PGESQNLA 169
Cdd:cd06208     5 PKNPLIGKVVSNTRLTgpdapGEVCHIVIDHGGKLPYLEGQSIGIIPPGTDAKNgkphklRLYSIASSrygdDGDGKTLS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 170 FIIKK--YPNGRFSSRLDG-------DLAVGTEVGIKGPYGTCFRRENKTGA-MILVGGGSGMSP----LWSILH-DHIS 234
Cdd:cd06208    85 LCVKRlvYTDPETDETKKGvcsnylcDLKPGDDVQITGPVGKTMLLPEDPNAtLIMIATGTGIAPfrsfLRRLFReKHAD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 235 SGEVRPVRFFYGARTQNDLFYLDHFAELAAKHPE-FTFVPVLSHaADDTAWGGaKGFVHEAVGEH---LRGADYGEDVDV 310
Cdd:cd06208   165 YKFTGLAWLFFGVPNSDSLLYDDELEKYPKQYPDnFRIDYAFSR-EQKNADGG-KMYVQDRIAEYaeeIWNLLDKDNTHV 242


                  ....
gi 2022570156 311 YACG 314
Cdd:cd06208   243 YICG 246
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 110-258 2.08e-13

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: 68.49  E-value: 2.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 110 TGTVTSVSAltHDIRRLEITLEQPLKFWAGQYVDITLPGPETITRS--FSMANSPGESQN-LAFIIKKYpNGRFSSRLDG 186
Cdd:cd06186     1 IATVELLPD--SDVIRLTIPKPKPFKWKPGQHVYLNFPSLLSFWQShpFTIASSPEDEQDtLSLIIRAK-KGFTTRLLRK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 187 DLAVGTE-----VGIKGPYGTCFRRENKTGAMILVGGGSGMSPLWSILHDHI----SSGEVRPVRFFYGARTQNDLFYLD 257
Cdd:cd06186    78 ALKSPGGgvslkVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLrrssKTSRTRRVKLVWVVRDREDLEWFL 157


                  .
gi 2022570156 258 H 258
Cdd:cd06186   158 D 158
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 138-344 2.32e-13

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 70.12  E-value: 2.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 138 AGQYVDITLPGPETITRSFSMANSPGESQNLAFIIKKYPNGRFSSRLDGDLAVGTEVGIKGPYG--TCfrrENKTG-AMI 214
Cdd:PRK10684   39 AGQYALVSIRNSAETLRAYTLSSTPGVSEFITLTVRRIDDGVGSQWLTRDVKRGDYLWLSDAMGefTC---DDKAEdKYL 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 215 LVGGGSGMSPLWSI---LHDHissgevRP---VRFFYGARTQNDLFYLDHFAELAAKHPEFTFVPVLSHAADDtawggak 288
Cdd:PRK10684  116 LLAAGCGVTPIMSMrrwLLKN------RPqadVQVIFNVRTPQDVIFADEWRQLKQRYPQLNLTLVAENNATE------- 182

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2022570156 289 GFVHEAV-GEHLRG-----ADYgedvDVYACGPSPMIEALTPVLQMSDVESDRIFFDKFTPA 344
Cdd:PRK10684  183 GFIAGRLtRELLQQavpdlASR----TVMTCGPAPYMDWVEQEVKALGVTADRFFKEKFFTP 240
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 121-322 4.00e-13

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: 68.12  E-value: 4.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 121 HDIRRL-----EITLEQPLK---FWAGQYVDITLPGPETITRS-FSMANSPGESQNLAFIIKkyPNGRfSSRLDGDLAVG 191
Cdd:cd06192     2 VKKEQLepnlvLLTIKAPLAarlFRPGQFVFLRNFESPGLERIpLSLAGVDPEEGTISLLVE--IRGP-KTKLIAELKPG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 192 TEVGIKGPYGTCFRRENKTGAMILVGGGSGMSPLWSILHDHISSGevRPVRFFYGARTQNDLFYLDHFAELAAkhpeftf 271
Cdd:cd06192    79 EKLDVMGPLGNGFEGPKKGGTVLLVAGGIGLAPLLPIAKKLAANG--NKVTVLAGAKKAKEEFLDEYFELPAD------- 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2022570156 272 vpVLSHAADDtAWGGAKGFVHEA-VGEHLRGADYgedvdVYACGPSPMIEAL 322
Cdd:cd06192   150 --VEIWTTDD-GELGLEGKVTDSdKPIPLEDVDR-----IIVAGSDIMMKAV 193
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 123-337 5.93e-12

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 65.21  E-value: 5.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 123 IRRLEITLEQPLKFWAGQYVDITLPGPETITrsFSMANSPGESQNLAFIIKKYpnGRFSSRLDgDLAVGTEVGIKGPYGT 202
Cdd:PRK08345   25 LRFEDPELAESFTFKPGQFVQVTIPGVGEVP--ISICSSPTRKGFFELCIRRA--GRVTTVIH-RLKEGDIVGVRGPYGN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 203 CFRRENKTGA-MILVGGGSGMSPLWSILHDHISSG-EVRPVRFFYGARTQNDLFYLDHFAELaAKHPEftFVPVLSHAAD 280
Cdd:PRK08345  100 GFPVDEMEGMdLLLIAGGLGMAPLRSVLLYAMDNRwKYGNITLIYGAKYYEDLLFYDELIKD-LAEAE--NVKIIQSVTR 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2022570156 281 DTAWGG----AKGFVHEAVGEHLRGADYGEDVDV---YA--CGPSPMIEALTPVLQMSDVESDRIF 337
Cdd:PRK08345  177 DPEWPGchglPQGFIERVCKGVVTDLFREANTDPkntYAaiCGPPVMYKFVFKELINRGYRPERIY 242
PTZ00038 PTZ00038
ferredoxin; Provisional
 16-91 4.27e-11

ferredoxin; Provisional


Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 61.39  E-value: 4.27e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2022570156  16 EFEVEENETVLDAAFRQGIALPHGCKEGQCSACKCVLTGGDVELKKYSTFALNEMERGqdYILLCRTLAYSDLEVE 91
Cdd:PTZ00038  108 VIECDEDEYILDAAERQGVELPYSCRGGSCSTCAAKLLEGEVDNEDQSYLDDEQLKKG--YCLLCTCYPKSDCTIE 181
COG3894 COG3894
Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain ...
 8-133 7.51e-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: 63.29  E-value: 7.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156   8 VRLQPVGIEFEVEENETVLDAAFRQGIALPHGC-KEGQCSACKCVLTGGDVEL-----KKYstfaLNEMERGQDYILLCR 81
Cdd:COG3894     6 VTFLPSGKRVEVEAGTTLLDAAREAGVDIDAPCgGRGTCGKCKVKVEEGEFSPvteeeRRL----LSPEELAEGYRLACQ 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2022570156  82 TLAYSDLEVELLnyDEEVLSKSIPVKDFTGTVTSVSALthdIRRLEITLEQP 133
Cdd:COG3894    82 ARVLGDLVVEVP--PESRLDKQKILKEGLEREIELDPA---VRKYYVELPEP 128
PLN03136 PLN03136
Ferredoxin; Provisional
 10-91 1.24e-08

Ferredoxin; Provisional


Pssm-ID: 178681 [Multi-domain]  Cd Length: 148  Bit Score: 53.21  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156  10 LQPVG-IEFEVEENETVLDAAFRQGIALPHGCKEGQCSACKCVLTGGDVELKKYSTfaLNEMERGQDYILLCRTLAYSDL 88
Cdd:PLN03136   60 ITPEGeQEVECEEDVYVLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSIDQSDQSF--LDDEQISEGYVLTCVAYPTSDV 137


                  ...
gi 2022570156  89 EVE 91
Cdd:PLN03136  138 VIE 140
petF CHL00134
ferredoxin; Validated
 10-100 1.38e-08

ferredoxin; Validated


Pssm-ID: 177056 [Multi-domain]  Cd Length: 99  Bit Score: 51.65  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156  10 LQPVGIEFEVEENETV--LDAAFRQGIALPHGCKEGQCSACKCVLTGGDVELKKYSTFALNEMERGqdYILLCrtLAYSD 87
Cdd:CHL00134   10 SEEEGIDVTIDCPDDVyiLDAAEEQGIDLPYSCRAGACSTCAGKVTEGTVDQSDQSFLDDDQLEAG--FVLTC--VAYPT 85

                          90
                  ....*....|...
gi 2022570156  88 LEVELLNYDEEVL 100
Cdd:CHL00134   86 SDCTILTHQEEEL 98
DHOD_e_trans_like1 cd06219
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 127-323 2.25e-07

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


Pssm-ID: 99815 [Multi-domain]  Cd Length: 248  Bit Score: 51.04  E-value: 2.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 127 EITLEQPL---KFWAGQYVDITL-PGPETITRSFSMANSpgESQNLAFIIKKYpnGRfSSRLDGDLAVGTEV-GIKGPYG 201
Cdd:cd06219    15 LFEIEAPLiakKAKPGQFVIVRAdEKGERIPLTIADWDP--EKGTITIVVQVV--GK-STRELATLEEGDKIhDVVGPLG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 202 TCFRRENKtGAMILVGGGSGMSPLWSILHDHISSGEvrPVRFFYGARTQNDLFYLDHFAELAAKHPEFTfvpvlshaaDD 281
Cdd:cd06219    90 KPSEIENY-GTVVFVGGGVGIAPIYPIAKALKEAGN--RVITIIGARTKDLVILEDEFRAVSDELIITT---------DD 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2022570156 282 TAWgGAKGFVHEAVGEHLrgaDYGEDVD-VYACGPSPMIEALT 323
Cdd:cd06219   158 GSY-GEKGFVTDPLKELI---ESGEKVDlVIAIGPPIMMKAVS 196
PRK10713 PRK10713
2Fe-2S ferredoxin-like protein;
8-92 1.66e-06

2Fe-2S ferredoxin-like protein;


Pssm-ID: 182668 [Multi-domain]  Cd Length: 84  Bit Score: 45.49  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156   8 VRLQPVGIEFEV-EENETVLDAAFRQGIALPHGCKEGQCSACKCVLTGGDVelkKYSTFALNEMERGQdyILLCRTLAYS 86
Cdd:PRK10713    4 VTLRITGTQLLCqDEHPSLLAALESHNVAVEYQCREGYCGSCRTRLVAGQV---DWIAEPLAFIQPGE--ILPCCCRAKG 78


                  ....*.
gi 2022570156  87 DLEVEL 92
Cdd:PRK10713   79 DIEIEM 84
CYPOR_like cd06182
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 126-315 1.16e-05

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


Pssm-ID: 99779 [Multi-domain]  Cd Length: 267  Bit Score: 46.18  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 126 LEITL--EQPLKFWAGQYVDITLPGPETiTRSFSMANSPGESQN---LAFIIKKY--PNGRF-----SSRLDgDLAVGTE 193
Cdd:cd06182    20 LEFDLsgNSVLKYQPGDHLGVIPPNPLQ-PRYYSIASSPDVDPGevhLCVRVVSYeaPAGRIrkgvcSNFLA-GLQLGAK 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 194 VGIKGPYGTCFRRENKTGA-MILVGGGSGMSPLWSIL----HDHISSGEVRPVRFFYGARTQN-DLFYLDHFAElAAKHP 267
Cdd:cd06182    98 VTVFIRPAPSFRLPKDPTTpIIMVGPGTGIAPFRGFLqeraALRANGKARGPAWLFFGCRNFAsDYLYREELQE-ALKDG 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2022570156 268 EFTFVpvlshaadDTAW----GGAKGFVHEAV---GEHLRGAdYGEDVDVYACGP 315
Cdd:cd06182   177 ALTRL--------DVAFsreqAEPKVYVQDKLkehAEELRRL-LNEGAHIYVCGD 222
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
 89-318 8.86e-05

ferredoxin--NADP(+) reductase; Provisional


Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 43.84  E-value: 8.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156  89 EVELLNYDEE--VLSKSIPVKDFTGTVTSVSALTHD-----IRRLEITLEQPLKFWAGQYVDITLPG------PETItRS 155
Cdd:PLN03115   69 VVKVSKKNEEgvVVNKFRPKEPYTGRCLLNTKITGDdapgeTWHMVFSTEGEIPYREGQSIGVIPDGidkngkPHKL-RL 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 156 FSMANSP----GESQNLAFIIKK--YPNGR------FSSRLDGDLAVGTEVGIKGPYGT-CFRRENKTGAMILVGGGSGM 222
Cdd:PLN03115  148 YSIASSAlgdfGDSKTVSLCVKRlvYTNDQgeivkgVCSNFLCDLKPGAEVKITGPVGKeMLMPKDPNATIIMLATGTGI 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 223 SP----LWSILHDHISSGEVRPVRF-FYGARTQNDLFYLDHFAELAAKHPEfTFVPVLSHAADDTAWGGAKGFVHEavge 297
Cdd:PLN03115  228 APfrsfLWKMFFEKHDDYKFNGLAWlFLGVPTSSSLLYKEEFEKMKEKAPE-NFRLDFAVSREQTNAKGEKMYIQT---- 302

                         250       260       270
                  ....*....|....*....|....*....|
gi 2022570156 298 hlRGADYGEDV---------DVYACGPSPM 318
Cdd:PLN03115  303 --RMAEYAEELwellkkdntYVYMCGLKGM 330
PLN02631 PLN02631
ferric-chelate reductase
 149-257 9.18e-05

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 44.26  E-value: 9.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 149 PETITRSFSManspgESQNLAFIIKKypNGRFSSRLDGDLAVGT---EVGIKGPYGTCFRRENKTGAMILVGGGSGMSPL 225
Cdd:PLN02631  355 PFTITSSSNL-----EKDTLSVVIRR--QGSWTQKLYTHLSSSIdslEVSTEGPYGPNSFDVSRHNSLILVSGGSGITPF 427

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2022570156 226 WSILHDHIS-----SGEVRPVRFFYGARTQNDLFYLD 257
Cdd:PLN02631  428 ISVIRELIFqsqnpSTKLPDVLLVCSFKHYHDLAFLD 464
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 136-326 1.51e-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: 43.09  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 136 FWAGQYVDITLPGpETITRSFSMANSpgeSQN--LAFIIKKYPNGRFSSRLDGdLAVGTEvgIKGpygtcFRREN----- 208
Cdd:cd06201    84 FEAGDLLGILPPG-SDVPRFYSLASS---SSDgfLEICVRKHPGGLCSGYLHG-LKPGDT--IKA-----FIRPNpsfrp 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 209 --KTGAMILVGGGSGMSPLWSILHDHISSgevRPVRFFYGARTQN-DLFYLDHFAELAAKHPEFTFVPVLSHAADdtawg 285
Cdd:cd06201   152 akGAAPVILIGAGTGIAPLAGFIRANAAR---RPMHLYWGGRDPAsDFLYEDELDQYLADGRLTQLHTAFSRTPD----- 223

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2022570156 286 gaKGFVHEAV---GEHLR-----GAdygedvDVYACGPSPMIEALTPVL 326
Cdd:cd06201   224 --GAYVQDRLradAERLRrliedGA------QIMVCGSRAMAQGVAAVL 264
PTZ00274 PTZ00274
cytochrome b5 reductase; Provisional
 171-333 2.71e-04

cytochrome b5 reductase; Provisional


Pssm-ID: 140300  Cd Length: 325  Bit Score: 42.21  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 171 IIKKYPNGRFSSRL----DGDLAVGTEVGIKGPYgtcfrRENKTGAMILVGGGSGMSPLWSI----LHDHISSGEVRPVR 242
Cdd:PTZ00274  121 IVKRKKDGLMTNHLfgmhVGDKLLFRSVTFKIQY-----RPNRWKHVGMIAGGTGFTPMLQIirhsLTEPWDSGEVDRTK 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156 243 --FFYGARTQNDLFYLDHFAELAAKHPE-FTFVPVLSHAADDTAWGGAKGFVHEAVGEHLRGADYGEDVDVYACGPSPMI 319
Cdd:PTZ00274  196 lsFLFCNRTERHILLKGLFDDLARRYSNrFKVYYTIDQAVEPDKWNHFLGYVTKEMVRRTMPAPEEKKKIIMLCGPDQLL 275

                         170
                  ....*....|....*.
gi 2022570156 320 E--ALTPVLQMSDVES 333
Cdd:PTZ00274  276 NhvAGTPMGTMSSMSS 291
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 12-91 4.59e-03

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 38.54  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022570156  12 PVGIefeveeneTVLDAAFRQGIALPHGCKEGQCSACKCVLTGGDVELKkySTFALNEMERGQDYILLCRTLAYSDLEVE 91
Cdd:PRK10684  263 PVGT--------TLLEALESNKVPVVAACRAGVCGCCKTKVVSGEYTVS--STMTLTPAEIAQGYVLACSCHPQGDLVLA 332
 
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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