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Conserved domains on  [gi|2790412202|ref|WP_371127001|]
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2Fe-2S iron-sulfur cluster-binding protein [Variovorax sp. YR216]

Protein Classification

PDR/VanB family oxidoreductase( domain architecture ID 18977663)

PDR/VanB family oxidoreductase containing a 2Fe-2S iron-sulfur cluster binding domain, similar to phthalate dioxygenase reductase (PDR), which is involved in the pyridine nucleotide-dependent dihydroxylation of phthalate, and to vanillate O-demethylase oxidoreductase, which plays a role in the degradation of aromatic compounds

CATH:  3.10.20.30|3.40.50.80|2.40.30.10
EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0051537|GO:0046872|GO:0010181
PubMed:  11192725|11734195
SCOP:  4000241|4003789|4002840

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 2-212 4.23e-90

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: 267.43  E-value: 4.23e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202   2 SRLTHEAEGVLGIELRAAADGTLPAFTAGSHIDLHLPGGLCRQYSLTNAPSEQERYCLGVGLAPESRGGSRHVHQQLRAG 81
Cdd:cd06185     1 VRIRDEAPDIRSFELEAPDGAPLPAFEPGAHIDVHLPNGLVRQYSLCGDPADRDRYRIAVLREPASRGGSRYMHELLRVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  82 DQIQISAPRSLFSLNAEADEHVFIAGGIGITPIMSMIEACRSKGERWRLLYCVRTRARAAYLWRLAEHHA-QVQLHVDEE 160
Cdd:cd06185    81 DELEVSAPRNLFPLDEAARRHLLIAGGIGITPILSMARALAARGADFELHYAGRSREDAAFLDELAALPGdRVHLHFDDE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2790412202 161 qGGPADVSGFIRSVSRTAHIYCCGPAPLMNAVEAAASAAEHPSKAVHFERFS 212
Cdd:cd06185   161 -GGRLDLAALLAAPPAGTHVYVCGPEGMMDAVRAAAAALGWPEARLHFERFA 211
Fdx COG0633
Ferredoxin [Energy production and conversion];
227-311 1.71e-22

Ferredoxin [Energy production and conversion];


:

Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 89.14  E-value: 1.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202 227 RVTLKRTGGTFMVPGGRSILQTLEDNGIALPCSCREGLCRTCETPLIGGRADHRD-FVLSDEERAGNsSIIPCVSRALDD 305
Cdd:COG0633     3 KVTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREeDALSDEERAAG-SRLACQARPTSD 81


                  ....*.
gi 2790412202 306 eLVLDI 311
Cdd:COG0633    82 -LVVEL 86
 
Name Accession Description Interval E-value
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 2-212 4.23e-90

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: 267.43  E-value: 4.23e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202   2 SRLTHEAEGVLGIELRAAADGTLPAFTAGSHIDLHLPGGLCRQYSLTNAPSEQERYCLGVGLAPESRGGSRHVHQQLRAG 81
Cdd:cd06185     1 VRIRDEAPDIRSFELEAPDGAPLPAFEPGAHIDVHLPNGLVRQYSLCGDPADRDRYRIAVLREPASRGGSRYMHELLRVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  82 DQIQISAPRSLFSLNAEADEHVFIAGGIGITPIMSMIEACRSKGERWRLLYCVRTRARAAYLWRLAEHHA-QVQLHVDEE 160
Cdd:cd06185    81 DELEVSAPRNLFPLDEAARRHLLIAGGIGITPILSMARALAARGADFELHYAGRSREDAAFLDELAALPGdRVHLHFDDE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2790412202 161 qGGPADVSGFIRSVSRTAHIYCCGPAPLMNAVEAAASAAEHPSKAVHFERFS 212
Cdd:cd06185   161 -GGRLDLAALLAAPPAGTHVYVCGPEGMMDAVRAAAAALGWPEARLHFERFA 211
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
3-210 1.63e-54

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 177.29  E-value: 1.63e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202   3 RLTHEAEGVLGIELRAAADGTLPAFTAGSHIDLHLPGG---LCRQYSLTNAPSEqERYCLGVGLAPEsRGGSRHVHQQLR 79
Cdd:COG1018    10 EVRRETPDVVSFTLEPPDGAPLPRFRPGQFVTLRLPIDgkpLRRAYSLSSAPGD-GRLEITVKRVPG-GGGSNWLHDHLK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  80 AGDQIQISAPRSLFSLNAEADEH-VFIAGGIGITPIMSMIEACRSKG--ERWRLLYCVRTRARAAY---LWRLAEHHAQV 153
Cdd:COG1018    88 VGDTLEVSGPRGDFVLDPEPARPlLLIAGGIGITPFLSMLRTLLARGpfRPVTLVYGARSPADLAFrdeLEALAARHPRL 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790412202 154 QLHV-----DEEQGGPADVSgFIRSV---SRTAHIYCCGPAPLMNAVEAAASAAEHPSKAVHFER 210
Cdd:COG1018   168 RLHPvlsrePAGLQGRLDAE-LLAALlpdPADAHVYLCGPPPMMEAVRAALAELGVPEERIHFER 231
Fdx COG0633
Ferredoxin [Energy production and conversion];
227-311 1.71e-22

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 89.14  E-value: 1.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202 227 RVTLKRTGGTFMVPGGRSILQTLEDNGIALPCSCREGLCRTCETPLIGGRADHRD-FVLSDEERAGNsSIIPCVSRALDD 305
Cdd:COG0633     3 KVTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREeDALSDEERAAG-SRLACQARPTSD 81


                  ....*.
gi 2790412202 306 eLVLDI 311
Cdd:COG0633    82 -LVVEL 86
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 43-275 1.37e-21

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 92.85  E-value: 1.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  43 RQYSLTNAPSEQERYCLGVGLAPESRGgSRHVHQQLRAGDQIQISAPRSLFSL-NAEADEHVFIAGGIGITPIMSMieac 121
Cdd:PRK10684   55 RAYTLSSTPGVSEFITLTVRRIDDGVG-SQWLTRDVKRGDYLWLSDAMGEFTCdDKAEDKYLLLAAGCGVTPIMSM---- 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202 122 rskgERW----------RLLYCVRTRARA--AYLWR-LAEHHAQVQLHVDEEQGG-PADVSGFI-RSV---------SRT 177
Cdd:PRK10684  130 ----RRWllknrpqadvQVIFNVRTPQDVifADEWRqLKQRYPQLNLTLVAENNAtEGFIAGRLtRELlqqavpdlaSRT 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202 178 ahIYCCGPAPLMNAVEAAASAAEHPSKAVHFERFSAEGARAnanADGAFRVTLKRTGGTFMVPGGRSILQTLEDNGIALP 257
Cdd:PRK10684  206 --VMTCGPAPYMDWVEQEVKALGVTADRFFKEKFFTPVAEA---ATSGLTFTKLQPAREFYAPVGTTLLEALESNKVPVV 280

                         250
                  ....*....|....*...
gi 2790412202 258 CSCREGLCRTCETPLIGG 275
Cdd:PRK10684  281 AACRAGVCGCCKTKVVSG 298
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 227-305 7.42e-16

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: 71.27  E-value: 7.42e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790412202 227 RVTLKRTGGTFMVPGGRSILQTLEDNGIALPCSCREGLCRTCETPLIGGRADHRDFVLSDEERAGNSSIIPCVSRALDD 305
Cdd:cd00207     2 TINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYVLACQTRVTDG 80
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
228-302 3.87e-10

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 55.22  E-value: 3.87e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790412202 228 VTLKRTGGTFMVP-GGRSILQTLEDNGIALPCSCREGLCRTCETPLIGGRADHRDFVLSDEERAGNSSIIPCVSRA 302
Cdd:pfam00111   1 VTINGKGVTIEVPdGETTLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSDQSFLEDDELAAGYVVLACQTYP 76
PRK10713 PRK10713
2Fe-2S ferredoxin-like protein;
227-305 2.58e-09

2Fe-2S ferredoxin-like protein;


Pssm-ID: 182668 [Multi-domain]  Cd Length: 84  Bit Score: 53.19  E-value: 2.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202 227 RVTLKRTGGTFMVPG-GRSILQTLEDNGIALPCSCREGLCRTCETPLIGGRADHRD----FVLSDEeragnssIIPCVSR 301
Cdd:PRK10713    3 RVTLRITGTQLLCQDeHPSLLAALESHNVAVEYQCREGYCGSCRTRLVAGQVDWIAeplaFIQPGE-------ILPCCCR 75


                  ....
gi 2790412202 302 ALDD 305
Cdd:PRK10713   76 AKGD 79
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 104-190 9.14e-09

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: 52.26  E-value: 9.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202 104 FIAGGIGITPIMSMIEAC----RSKGERWrLLYCVRTRARAAY------LWRLAEHHAQVQLHVDEEQGGPADVSGFIR- 172
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAIledpKDPTQVV-LVFGNRNEDDILYreeldeLAEKHPGRLTVVYVVSRPEAGWTGGKGRVQd 79

                          90       100
                  ....*....|....*....|....*.
gi 2790412202 173 --------SVSRTAHIYCCGPAPLMN 190
Cdd:pfam00175  80 alledhlsLPDEETHVYVCGPPGMIK 105
 
Name Accession Description Interval E-value
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 2-212 4.23e-90

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: 267.43  E-value: 4.23e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202   2 SRLTHEAEGVLGIELRAAADGTLPAFTAGSHIDLHLPGGLCRQYSLTNAPSEQERYCLGVGLAPESRGGSRHVHQQLRAG 81
Cdd:cd06185     1 VRIRDEAPDIRSFELEAPDGAPLPAFEPGAHIDVHLPNGLVRQYSLCGDPADRDRYRIAVLREPASRGGSRYMHELLRVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  82 DQIQISAPRSLFSLNAEADEHVFIAGGIGITPIMSMIEACRSKGERWRLLYCVRTRARAAYLWRLAEHHA-QVQLHVDEE 160
Cdd:cd06185    81 DELEVSAPRNLFPLDEAARRHLLIAGGIGITPILSMARALAARGADFELHYAGRSREDAAFLDELAALPGdRVHLHFDDE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2790412202 161 qGGPADVSGFIRSVSRTAHIYCCGPAPLMNAVEAAASAAEHPSKAVHFERFS 212
Cdd:cd06185   161 -GGRLDLAALLAAPPAGTHVYVCGPEGMMDAVRAAAAALGWPEARLHFERFA 211
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
3-210 1.63e-54

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 177.29  E-value: 1.63e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202   3 RLTHEAEGVLGIELRAAADGTLPAFTAGSHIDLHLPGG---LCRQYSLTNAPSEqERYCLGVGLAPEsRGGSRHVHQQLR 79
Cdd:COG1018    10 EVRRETPDVVSFTLEPPDGAPLPRFRPGQFVTLRLPIDgkpLRRAYSLSSAPGD-GRLEITVKRVPG-GGGSNWLHDHLK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  80 AGDQIQISAPRSLFSLNAEADEH-VFIAGGIGITPIMSMIEACRSKG--ERWRLLYCVRTRARAAY---LWRLAEHHAQV 153
Cdd:COG1018    88 VGDTLEVSGPRGDFVLDPEPARPlLLIAGGIGITPFLSMLRTLLARGpfRPVTLVYGARSPADLAFrdeLEALAARHPRL 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790412202 154 QLHV-----DEEQGGPADVSgFIRSV---SRTAHIYCCGPAPLMNAVEAAASAAEHPSKAVHFER 210
Cdd:COG1018   168 RLHPvlsrePAGLQGRLDAE-LLAALlpdPADAHVYLCGPPPMMEAVRAALAELGVPEERIHFER 231
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 3-211 4.84e-33

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: 121.90  E-value: 4.84e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202   3 RLTHEAEGVLGIELRAAADGTLPAFTAGSHI--DLHLPGG---LCRQYSLTNAPSEqERYCLGV-----GLApesrggSR 72
Cdd:cd06184    13 RKVAESEDITSFYLEPADGGPLPPFLPGQYLsvRVKLPGLgyrQIRQYSLSDAPNG-DYYRISVkrepgGLV------SN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  73 HVHQQLRAGDQIQISAPRSLFSLNAEADEH-VFIAGGIGITPIMSMIEAC--RSKGERWRLLYCVR---TRARAAYLWRL 146
Cdd:cd06184    86 YLHDNVKVGDVLEVSAPAGDFVLDEASDRPlVLISAGVGITPMLSMLEALaaEGPGRPVTFIHAARnsaVHAFRDELEEL 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790412202 147 AEHHAQVQLHV------DEEQGGPADVSGFI-------RSVSRTAHIYCCGPAPLMNAVEAAASAAEHPSKAVHFERF 211
Cdd:cd06184   166 AARLPNLKLHVfysepeAGDREEDYDHAGRIdlallreLLLPADADFYLCGPVPFMQAVREGLKALGVPAERIHYEVF 243
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 5-189 3.54e-30

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: 113.84  E-value: 3.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202   5 THEAEGVLGIELRAAaDGTLPAFTAGSHIDLHL--PGGLC-RQYSLTNAPSEQERYCLGVGLAPESRGgSRHVHQQLRAG 81
Cdd:cd06215     7 IQETPDVKTFRFAAP-DGSLFAYKPGQFLTLELeiDGETVyRAYTLSSSPSRPDSLSITVKRVPGGLV-SNWLHDNLKVG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  82 DQIQISAPRSLFSL-NAEADEHVFIAGGIGITPIMSMIeacrskgeRW----------RLLYCVRTRARAAY---LWRLA 147
Cdd:cd06215    85 DELWASGPAGEFTLiDHPADKLLLLSAGSGITPMMSMA--------RWlldtrpdadiVFIHSARSPADIIFadeLEELA 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2790412202 148 EHHAQVQLHVDEEQGGPADVSGF-----------IRSVSRTAHIYCCGPAPLM 189
Cdd:cd06215   157 RRHPNFRLHLILEQPAPGAWGGYrgrlnaellalLVPDLKERTVFVCGPAGFM 209
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 24-209 1.59e-28

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: 109.46  E-value: 1.59e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  24 LPAFTAGSHIDLHLPGGLC---RQYSLTNAPSEQERYCLGVGLAPESRGgSRHVHQqLRAGDQIQISAPRSLFSLNAEAD 100
Cdd:cd00322    20 GFSFKPGQYVDLHLPGDGRglrRAYSIASSPDEEGELELTVKIVPGGPF-SAWLHD-LKPGDEVEVSGPGGDFFLPLEES 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202 101 EH-VFIAGGIGITPIMSMIEACRSKGER--WRLLYCVRTRARAAY---LWRLAEHHAQVQLHVDEEQGGPADVSGFIRSV 174
Cdd:cd00322    98 GPvVLIAGGIGITPFRSMLRHLAADKPGgeITLLYGARTPADLLFldeLEELAKEGPNFRLVLALSRESEAKLGPGGRID 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2790412202 175 SR-----------TAHIYCCGPAPLMNAVEAAASAAEHPSKAVHFE 209
Cdd:cd00322   178 REaeilallpddsGALVYICGPPAMAKAVREALVSLGVPEERIHTE 223
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 3-211 3.31e-26

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal 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: 103.50  E-value: 3.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202   3 RLTHEAEGVLGIELRAAaDGTLPAFTAGSHIDLHLPGG----LCRQYSLTNAPSEQERYCLGVGLAPesrGG--SRHVHQ 76
Cdd:cd06217     8 EIIQETPTVKTFRLAVP-DGVPPPFLAGQHVDLRLTAIdgytAQRSYSIASSPTQRGRVELTVKRVP---GGevSPYLHD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  77 QLRAGDQIQISAPRSLFSLN-AEADEHVFIAGGIGITPIMSMIEACRSKGE--RWRLLYCVRTRAR---AAYLWRLAEHH 150
Cdd:cd06217    84 EVKVGDLLEVRGPIGTFTWNpLHGDPVVLLAGGSGIVPLMSMIRYRRDLGWpvPFRLLYSARTAEDvifRDELEQLARRH 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790412202 151 AQVQLHVDEEQGGPADVSGF-----------IRSVSRTAHIYCCGPAPLMNAVEAAASAAEHPSKAVHFERF 211
Cdd:cd06217   164 PNLHVTEALTRAAPADWLGPagritadliaeLVPPLAGRRVYVCGPPAFVEAATRLLLELGVPRDRIRTEAF 235
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 15-211 1.17e-25

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: 102.24  E-value: 1.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  15 ELRAAadgtlPAFTAGSHIDLHLP---GGLCRQYSLTNAPSEQErycLGVGLAPEsRGG--SRHVHQQLRAGDQIQISAP 89
Cdd:cd06214    26 ELRDA-----FRYRPGQFLTLRVPidgEEVRRSYSICSSPGDDE---LRITVKRV-PGGrfSNWANDELKAGDTLEVMPP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  90 RSLFSL--NAEADEHVFIAGGIGITPIMSMIEAC--RSKGERWRLLYCVRTRA-----------RAAYLWRLAEHHaqvq 154
Cdd:cd06214    97 AGRFTLppLPGARHYVLFAAGSGITPVLSILKTAlaREPASRVTLVYGNRTEAsvifreeladlKARYPDRLTVIH---- 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790412202 155 lHVDEEQGGPADVSGFI------------RSVSRTAHIYCCGPAPLMNAVEAAASAAEHPSKAVHFERF 211
Cdd:cd06214   173 -VLSREQGDPDLLRGRLdaaklnallknlLDATEFDEAFLCGPEPMMDAVEAALLELGVPAERIHRELF 240
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 7-211 1.35e-24

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: 99.61  E-value: 1.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202   7 EAEGVLGIELRAAADgtLPAFTAGSHIDLHLP-GG--LCRQYSLTNAP-SEQERYCLGVGLAPESRGgSRHVHQQLRAGD 82
Cdd:cd06216    28 ETADMVTLTLRPNRG--WPGHRAGQHVRLGVEiDGvrHWRSYSLSSSPtQEDGTITLTVKAQPDGLV-SNWLVNHLAPGD 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  83 QIQISAPRSLFSL-NAEADEHVFIAGGIGITPIMSMIEACRSKGERWR--LLYCVRTRARAAY---LWRLAEHHAQVQLH 156
Cdd:cd06216   105 VVELSQPQGDFVLpDPLPPRLLLIAAGSGITPVMSMLRTLLARGPTADvvLLYYARTREDVIFadeLRALAAQHPNLRLH 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202 157 V---DEEQGGPADVSGFIRSVS--RTAHIYCCGPAPLMNAVEAAASAAEHPSkAVHFERF 211
Cdd:cd06216   185 LlytREELDGRLSAAHLDAVVPdlADRQVYACGPPGFLDAAEELLEAAGLAD-RLHTERF 243
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 70-212 3.10e-23

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: 95.02  E-value: 3.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  70 GSRHVHQQLRAGDQIQISAPRSLFSLNAEADEHVFIAGGIGITPIMSMIEACRSKGERWR--LLYCVRTRARAAYLWRLA 147
Cdd:cd06198    66 YTRRLAERLKPGTRVTVEGPYGRFTFDDRRARQIWIAGGIGITPFLALLEALAARGDARPvtLFYCVRDPEDAVFLDELR 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790412202 148 E--HHAQVQLHV-DEEQGGPADVSGFIRSV---SRTAHIYCCGPAPLMNAVEAAASAAEHPSKAVHFERFS 212
Cdd:cd06198   146 AlaAAAGVVLHViDSPSDGRLTLEQLVRALvpdLADADVWFCGPPGMADALEKGLRALGVPARRFHYERFE 216
Fdx COG0633
Ferredoxin [Energy production and conversion];
227-311 1.71e-22

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 89.14  E-value: 1.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202 227 RVTLKRTGGTFMVPGGRSILQTLEDNGIALPCSCREGLCRTCETPLIGGRADHRD-FVLSDEERAGNsSIIPCVSRALDD 305
Cdd:COG0633     3 KVTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREeDALSDEERAAG-SRLACQARPTSD 81


                  ....*.
gi 2790412202 306 eLVLDI 311
Cdd:COG0633    82 -LVVEL 86
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
76-212 3.07e-22

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 96.12  E-value: 3.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  76 QQLRAGDQIQISAPRSLFSLNAEADEH--VFIAGGIGITPIMSMIEACRSKGERWR---LLYCVRTRARAAY---LWRLA 147
Cdd:COG4097   293 GRLKPGTRVYVEGPYGRFTFDRRDTAPrqVWIAGGIGITPFLALLRALAARPGDQRpvdLFYCVRDEEDAPFleeLRALA 372

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790412202 148 EHHAQVQLH-VDEEQGGPADVSGFIRSVS--RTAHIYCCGPAPLMNAVEAAASAAEHPSKAVHFERFS 212
Cdd:COG4097   373 ARLAGLRLHlVVSDEDGRLTAERLRRLVPdlAEADVFFCGPPGMMDALRRDLRALGVPARRIHQERFE 440
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 43-275 1.37e-21

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 92.85  E-value: 1.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  43 RQYSLTNAPSEQERYCLGVGLAPESRGgSRHVHQQLRAGDQIQISAPRSLFSL-NAEADEHVFIAGGIGITPIMSMieac 121
Cdd:PRK10684   55 RAYTLSSTPGVSEFITLTVRRIDDGVG-SQWLTRDVKRGDYLWLSDAMGEFTCdDKAEDKYLLLAAGCGVTPIMSM---- 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202 122 rskgERW----------RLLYCVRTRARA--AYLWR-LAEHHAQVQLHVDEEQGG-PADVSGFI-RSV---------SRT 177
Cdd:PRK10684  130 ----RRWllknrpqadvQVIFNVRTPQDVifADEWRqLKQRYPQLNLTLVAENNAtEGFIAGRLtRELlqqavpdlaSRT 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202 178 ahIYCCGPAPLMNAVEAAASAAEHPSKAVHFERFSAEGARAnanADGAFRVTLKRTGGTFMVPGGRSILQTLEDNGIALP 257
Cdd:PRK10684  206 --VMTCGPAPYMDWVEQEVKALGVTADRFFKEKFFTPVAEA---ATSGLTFTKLQPAREFYAPVGTTLLEALESNKVPVV 280

                         250
                  ....*....|....*...
gi 2790412202 258 CSCREGLCRTCETPLIGG 275
Cdd:PRK10684  281 AACRAGVCGCCKTKVVSG 298
PRK13289 PRK13289
NO-inducible flavohemoprotein;
15-211 4.29e-20

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 89.47  E-value: 4.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  15 ELRAAADGTLPAFTAGSHIDLHL-PGGL----CRQYSLTNAPSEQErYCLGV-----GLApesrggSRHVHQQLRAGDQI 84
Cdd:PRK13289  173 YLEPVDGGPVADFKPGQYLGVRLdPEGEeyqeIRQYSLSDAPNGKY-YRISVkreagGKV------SNYLHDHVNVGDVL 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  85 QISAPRSLFSLNAEADEH-VFIAGGIGITPIMSMIE--ACRSKGERWRLLYCVR---TRARAAYLWRLAEHHAQVQLHV- 157
Cdd:PRK13289  246 ELAAPAGDFFLDVASDTPvVLISGGVGITPMLSMLEtlAAQQPKRPVHFIHAARnggVHAFRDEVEALAARHPNLKAHTw 325

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790412202 158 ------DEEQGGPADVSGFI-----RSV--SRTAHIYCCGPAPLMNAVEAAASAAEHPSKAVHFERF 211
Cdd:PRK13289  326 yrepteQDRAGEDFDSEGLMdlewlEAWlpDPDADFYFCGPVPFMQFVAKQLLELGVPEERIHYEFF 392
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 14-211 8.22e-20

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: 86.11  E-value: 8.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  14 IELRAAADGTLPaFTAGSHIDLHLPG--GLCRQYSLTNAPSEQERYCLGVGLAPESRGgSRHVHQQLRAGDQIQISAPRS 91
Cdd:cd06187    12 AVVRLQLDQPLP-FWAGQYVNVTVPGrpRTWRAYSPANPPNEDGEIEFHVRAVPGGRV-SNALHDELKVGDRVRLSGPYG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  92 LFSLNAEAD-EHVFIAGGIGITPIMSMIEACRSKGE--RWRLLYCVRTRAR---AAYLWRLAEHHAQVQLH--VDEEQGG 163
Cdd:cd06187    90 TFYLRRDHDrPVLCIAGGTGLAPLRAIVEDALRRGEprPVHLFFGARTERDlydLEGLLALAARHPWLRVVpvVSHEEGA 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2790412202 164 PADVSGFIRSVSRTAH-------IYCCGPAPLMNAVEAAASAAEHPSKAVHFERF 211
Cdd:cd06187   170 WTGRRGLVTDVVGRDGpdwadhdIYICGPPAMVDATVDALLARGAPPERIHFDKF 224
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 3-189 1.28e-18

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 83.37  E-value: 1.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202   3 RLTHEAEGVLGIELRAAADGtlPAFTAGSHIDLHLPG-GLCRQYSLTNAPSEQERYCL---GVGLapesrgGSRHVHQqL 78
Cdd:COG0543     4 SVERLAPDVYLLRLEAPLIA--LKFKPGQFVMLRVPGdGLRRPFSIASAPREDGTIELhirVVGK------GTRALAE-L 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  79 RAGDQIQISAPR-SLFSLNAEADEHVFIAGGIGITPIMSMIEACRSKGERWRLLYCVRTRARAAYLWRLAEhHAQVQLHV 157
Cdd:COG0543    75 KPGDELDVRGPLgNGFPLEDSGRPVLLVAGGTGLAPLRSLAEALLARGRRVTLYLGARTPEDLYLLDELEA-LADFRVVV 153

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2790412202 158 DEEQgGPADVSGFIRSV-------SRTAHIYCCGPAPLM 189
Cdd:COG0543   154 TTDD-GWYGRKGFVTDAlkellaeDSGDDVYACGPPPMM 191
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 2-189 1.02e-16

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: 77.59  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202   2 SRLTHEAEGVLGIELRAAADgtlPAFTAGSHIDLHLPGGLCRQYSLTNAPSEQERYCLGVGLAPESRgGSRHVHQQLRAG 81
Cdd:cd06189     4 ESIEPLNDDVYRVRLKPPAP---LDFLAGQYLDLLLDDGDKRPFSIASAPHEDGEIELHIRAVPGGS-FSDYVFEELKEN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  82 DQIQISAPRSLFSLNAEADE-HVFIAGGIGITPIMSMIEACRSKG-ERWRLLY-CVRTRA---RAAYLWRLAEHHAQVQL 155
Cdd:cd06189    80 GLVRIEGPLGDFFLREDSDRpLILIAGGTGFAPIKSILEHLLAQGsKRPIHLYwGARTEEdlyLDELLEAWAEAHPNFTY 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2790412202 156 H--VDEEQGGPADVSGFIRSVSRTAH-------IYCCGPaPLM 189
Cdd:cd06189   160 VpvLSEPEEGWQGRTGLVHEAVLEDFpdlsdfdVYACGS-PEM 201
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 26-211 1.92e-16

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: 76.99  E-value: 1.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  26 AFTAGSHIDLHLPG-GLCRQYSLTNAPSEQERYCLGVGLAPesrGG--SRHVHQQLRAGDQIQISAPRSLFSLNAEADEH 102
Cdd:cd06212    29 KFFAGQYVDITVPGtEETRSFSMANTPADPGRLEFIIKKYP---GGlfSSFLDDGLAVGDPVTVTGPYGTCTLRESRDRP 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202 103 -VFIAGGIGITPIMSMIEACRSKGERW--RLLYCVRTRARAAYLWRLAEHHAQVQ-------LHVDEEQGGPADVSGFIR 172
Cdd:cd06212   106 iVLIGGGSGMAPLLSLLRDMAASGSDRpvRFFYGARTARDLFYLEEIAALGEKIPdftfipaLSESPDDEGWSGETGLVT 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2790412202 173 SV-------SRTAHIYCCGPAPLMNAVEAAASAAEHPSKAVHFERF 211
Cdd:cd06212   186 EVvqrneatLAGCDVYLCGPPPMIDAALPVLEMSGVPPDQIFYDKF 231
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 4-211 3.14e-16

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: 76.59  E-value: 3.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202   4 LTHEAEGVLgIELRaaaDGTLPAFTAGSHIDLHLPGG-LCRQYSLTNAPSEQERYCLGVGLAPESRGgSRHVHQQLRAGD 82
Cdd:cd06211    17 LTPTIKGVR-LKLD---EPEEIEFQAGQYVNLQAPGYeGTRAFSIASSPSDAGEIELHIRLVPGGIA-TTYVHKQLKEGD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  83 QIQISAPRSLFSLNAEADEH-VFIAGGIGITPIMSMIEACRSKGE--RWRLLYCVRTRARaayLWRLAEHHAQVQLHVD- 158
Cdd:cd06211    92 ELEISGPYGDFFVRDSDQRPiIFIAGGSGLSSPRSMILDLLERGDtrKITLFFGARTRAE---LYYLDEFEALEKDHPNf 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790412202 159 -------EEQGGPaDVSGFIRSVSRTAHIYC-----------CGPAPLMNAVEAAASAAEHPSKAVHFERF 211
Cdd:cd06211   169 kyvpalsREPPES-NWKGFTGFVHDAAKKHFkndfrghkaylCGPPPMIDACIKTLMQGRLFERDIYYEKF 238
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 227-305 7.42e-16

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: 71.27  E-value: 7.42e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790412202 227 RVTLKRTGGTFMVPGGRSILQTLEDNGIALPCSCREGLCRTCETPLIGGRADHRDFVLSDEERAGNSSIIPCVSRALDD 305
Cdd:cd00207     2 TINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYVLACQTRVTDG 80
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 1-212 2.58e-15

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: 73.78  E-value: 2.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202   1 MSRLTHEAEGVLGIELRAAADGTLpAFTAGSHIDLHLPG-GLCRQYSLTNAPSEQERYCLgVGLAPesrGG--SRHVHQQ 77
Cdd:cd06209     6 VTEVERLSDSTIGLTLELDEAGAL-AFLPGQYVNLQVPGtDETRSYSFSSAPGDPRLEFL-IRLLP---GGamSSYLRDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  78 LRAGDQIQISAPRSLFSLNAEADEHVFIAGGIGITPIMSMIEACRSKGERW--RLLYCVRTRARAAYLWRLAEHHAQV-- 153
Cdd:cd06209    81 AQPGDRLTLTGPLGSFYLREVKRPLLMLAGGTGLAPFLSMLDVLAEDGSAHpvHLVYGVTRDADLVELDRLEALAERLpg 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202 154 -QLHV---DEEQGGPAdvSGFIRSVSRTAH-------IYCCGPAPLMNAVEAAASAAEHPSKAVHFERFS 212
Cdd:cd06209   161 fSFRTvvaDPDSWHPR--KGYVTDHLEAEDlndgdvdVYLCGPPPMVDAVRSWLDEQGIEPANFYYEKFT 228
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 27-211 6.62e-15

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: 72.56  E-value: 6.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  27 FTAGSHIDLHLPGG---LCRQYSLTNAPSeQERYCLGVGLAPesrGG--SRHVHQQLRAGDQIQISAPRSLFSLNAEADE 101
Cdd:cd06191    28 FRPGQHVTLKLDFDgeeLRRCYSLCSSPA-PDEISITVKRVP---GGrvSNYLREHIQPGMTVEVMGPQGHFVYQPQPPG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202 102 HV-FIAGGIGITPIMSMIEACRSKGER--WRLLYCVRTR------------ARAAYLWRLAEHHAQVQLHVDEEQG---G 163
Cdd:cd06191   104 RYlLVAAGSGITPLMAMIRATLQTAPEsdFTLIHSARTPadmifaqelrelADKPQRLRLLCIFTRETLDSDLLHGridG 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2790412202 164 PADVSGFIRSVSRTAHIYCCGPAPLMNAVEAAASAAEHPSKAVHFERF 211
Cdd:cd06191   184 EQSLGAALIPDRLEREAFICGPAGMMDAVETALKELGMPPERIHTERF 231
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 29-190 1.41e-13

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: 68.75  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  29 AGSHIDLHLPGG---LCRQYSLTNAPSEQERYCLgvgLAPESRGG--SRHVHQqLRAGDQIQISAPRSLFSL--NAEADE 101
Cdd:cd06183    31 VGQHVELKAPDDgeqVVRPYTPISPDDDKGYFDL---LIKIYPGGkmSQYLHS-LKPGDTVEIRGPFGKFEYkpNGKVKH 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202 102 HVFIAGGIGITPIMSMIEA---CRSKGERWRLLYCVRTRA-----------RAAYLWRLaehhaQVQLHVDEEQGGPADV 167
Cdd:cd06183   107 IGMIAGGTGITPMLQLIRAilkDPEDKTKISLLYANRTEEdillreeldelAKKHPDRF-----KVHYVLSRPPEGWKGG 181

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2790412202 168 SGFI----------RSVSRTAHIYCCGPAPLMN 190
Cdd:cd06183   182 VGFItkemikehlpPPPSEDTLVLVCGPPPMIE 214
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 3-211 4.17e-13

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: 67.34  E-value: 4.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202   3 RLTHEAegvlgIELRAAADGTLPaFTAGSHIDLHLPGGLC-RQYSLTNAPSEQERYCLGVGLAPesrGG--SRHVHQQLR 79
Cdd:cd06213    10 RLTHDI-----VRLTVQLDRPIA-YKAGQYAELTLPGLPAaRSYSFANAPQGDGQLSFHIRKVP---GGafSGWLFGADR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  80 AGDQIQISAPRSLFSLNaEADEH-VFIAGGIGITPIMSMIEACRSKGERwR---LLYCVRTR---------ARAAYLWRL 146
Cdd:cd06213    81 TGERLTVRGPFGDFWLR-PGDAPiLCIAGGSGLAPILAILEQARAAGTK-RdvtLLFGARTQrdlyaldeiAAIAARWRG 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790412202 147 AEHHAQVQLHVDEE---QGGPADVSGFIRSVSRTAH-IYCCGPAPLMNAVEAAASAAEHPSKAVHFERF 211
Cdd:cd06213   159 RFRFIPVLSEEPADsswKGARGLVTEHIAEVLLAATeAYLCGPPAMIDAAIAVLRALGIAREHIHADRF 227
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 2-189 8.44e-13

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 67.97  E-value: 8.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202   2 SRLTHEAEGVLGIELRAAAdGTLPAFTAGSHIDLHLPGGLCRQYSLTNAPSEQERYCLGVGLAPESRGgSRHVHQQLRAG 81
Cdd:PRK07609  108 ASLERVAGDVMRLKLRLPA-TERLQYLAGQYIEFILKDGKRRSYSIANAPHSGGPLELHIRHMPGGVF-TDHVFGALKER 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  82 DQIQISAPRSLFSLNAEADEH-VFIAGGIGITPIMSMIEACRSKGERW--RLLYCVRTRAR--AAYLWRL-AEHHAQVQL 155
Cdd:PRK07609  186 DILRIEGPLGTFFLREDSDKPiVLLASGTGFAPIKSIVEHLRAKGIQRpvTLYWGARRPEDlyLSALAEQwAEELPNFRY 265

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2790412202 156 H--VDEEQGGP-----------------ADVSGFirsvsrtaHIYCCGpAPLM 189
Cdd:PRK07609  266 VpvVSDALDDDawtgrtgfvhqavledfPDLSGH--------QVYACG-SPVM 309
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 16-211 5.93e-12

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: 64.29  E-value: 5.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  16 LRAAADGTLPAFTAGSHIDLHLPG-GLCRQYSLTNAPSEQERYCLGVGLAPesrGG--SRHVHQQLRAGDQIQISAPRSL 92
Cdd:cd06210    24 DDAEGAGIAAEFVPGQFVEIEIPGtDTRRSYSLANTPNWDGRLEFLIRLLP---GGafSTYLETRAKVGQRLNLRGPLGA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  93 FSLnaeaDEH-----VFIAGGIGITPIMSMIeacRSKGERW-----RLLYCVRTRARAAY---LWRLAEHHAQVQLHV-- 157
Cdd:cd06210   101 FGL----RENglrprWFVAGGTGLAPLLSML---RRMAEWGepqeaRLFFGVNTEAELFYldeLKRLADSLPNLTVRIcv 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790412202 158 -------DEEQGGPADVsgFIRSVSRTA---HIYCCGPAPLMNAVEAAASAAEHPSKAVHFERF 211
Cdd:cd06210   174 wrpggewEGYRGTVVDA--LREDLASSDakpDIYLCGPPGMVDAAFAAAREAGVPDEQVYLEKF 235
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 3-211 7.35e-12

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: 63.81  E-value: 7.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202   3 RLTHEAegvlgIELRAAADGtlPA-FTAGSHIDLHLPGG-LCRQYSLTNAPSEQERYCLGVGLAPESRGgSRHVHQQLRA 80
Cdd:cd06190     6 ELTHDV-----AEFRFALDG--PAdFLPGQYALLALPGVeGARAYSMANLANASGEWEFIIKRKPGGAA-SNALFDNLEP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  81 GDQIQISAPRSLFSLNAEAD-EHVFIAGGIGITPIMSMIE-ACRSKGERWR---LLYCVRTRARAAYLWRLAEH-HAQVQ 154
Cdd:cd06190    78 GDELELDGPYGLAYLRPDEDrDIVCIAGGSGLAPMLSILRgAARSPYLSDRpvdLFYGGRTPSDLCALDELSALvALGAR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790412202 155 LHV-----DEEQGGPADV---SGFIRSV------SRTAH--IYCCGPAPLMNAVEAA-ASAAEHPSKAVHFERF 211
Cdd:cd06190   158 LRVtpavsDAGSGSAAGWdgpTGFVHEVveatlgDRLAEfeFYFAGPPPMVDAVQRMlMIEGVVPFDQIHFDRF 231
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 77-189 3.01e-11

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: 62.18  E-value: 3.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  77 QLRAGDQIQISAP--RSlFSLNAEADEHVFIAGGIGITPimsMIEACRS---KGERWRLLYCVRTRARAAYLWRLAEHHA 151
Cdd:cd06218    75 ELKAGDELDVLGPlgNG-FDLPDDDGKVLLVGGGIGIAP---LLFLAKQlaeRGIKVTVLLGFRSADDLFLVEEFEALGA 150

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2790412202 152 QVQLHV-DEEQGGPADVSGFIRSVSRTAH---IYCCGPAPLM 189
Cdd:cd06218   151 EVYVATdDGSAGTKGFVTDLLKELLAEARpdvVYACGPEPML 192
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 21-190 3.84e-11

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: 63.34  E-value: 3.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  21 DGTLPAFTAGSHIDLHLPGGLC------------------------RQYSLTNAPSEQERYCLGVGLAPESRG-----GS 71
Cdd:COG2871   155 EGEEIDFKAGQYIQIEVPPYEVdfkdfdipeeekfglfdkndeevtRAYSMANYPAEKGIIELNIRIATPPMDvppgiGS 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  72 RHVHQqLRAGDQIQISAPRSLFSLNAEADEHVFIAGGIGITPIMSMIE--ACRSKGER-WRLLYCVRTRARAAYL---WR 145
Cdd:COG2871   235 SYIFS-LKPGDKVTISGPYGEFFLRDSDREMVFIGGGAGMAPLRSHIFdlLERGKTDRkITFWYGARSLRELFYLeefRE 313

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790412202 146 LAEHHAQVQLHV--DEEQggPADV----SGFIRSVSRTAHI-----------YCCGPaPLMN 190
Cdd:COG2871   314 LEKEHPNFKFHPalSEPL--PEDNwdgeTGFIHEVLYENYLkdhpapedceaYLCGP-PPMI 372
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
228-302 3.87e-10

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 55.22  E-value: 3.87e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790412202 228 VTLKRTGGTFMVP-GGRSILQTLEDNGIALPCSCREGLCRTCETPLIGGRADHRDFVLSDEERAGNSSIIPCVSRA 302
Cdd:pfam00111   1 VTINGKGVTIEVPdGETTLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSDQSFLEDDELAAGYVVLACQTYP 76
PRK10713 PRK10713
2Fe-2S ferredoxin-like protein;
227-305 2.58e-09

2Fe-2S ferredoxin-like protein;


Pssm-ID: 182668 [Multi-domain]  Cd Length: 84  Bit Score: 53.19  E-value: 2.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202 227 RVTLKRTGGTFMVPG-GRSILQTLEDNGIALPCSCREGLCRTCETPLIGGRADHRD----FVLSDEeragnssIIPCVSR 301
Cdd:PRK10713    3 RVTLRITGTQLLCQDeHPSLLAALESHNVAVEYQCREGYCGSCRTRLVAGQVDWIAeplaFIQPGE-------ILPCCCR 75


                  ....
gi 2790412202 302 ALDD 305
Cdd:PRK10713   76 AKGD 79
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
 43-190 3.77e-09

Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) provides a means of storing redox reaction energy via the transmembrane translocation of Na2+ ions. The C-terminal domain resembles ferredoxin:NADP+ oxidoreductase, and has NADH and FAD binding sites. (Na+-NQR) is distinct from H+-translocating NADH:quinone oxidoreductases and noncoupled NADH:quinone oxidoreductases. The NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain of this group typically contains an iron-sulfur cluster binding domain.


Pssm-ID: 99785 [Multi-domain]  Cd Length: 283  Bit Score: 56.54  E-value: 3.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  43 RQYSLTNAPSEQERYCLGVGLA---PESRG-----GSRHVHQqLRAGDQIQISAPRSLFSLNAEADEHVFIAGGIGITPI 114
Cdd:cd06188    87 RAYSLANYPAEEGELKLNVRIAtppPGNSDippgiGSSYIFN-LKPGDKVTASGPFGEFFIKDTDREMVFIGGGAGMAPL 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202 115 MSMIE---ACRSKGERWRLLYCVRTRARAAY---LWRLAEHHAQVQLHV--------DEEQGgpadVSGFIRSV------ 174
Cdd:cd06188   166 RSHIFhllKTLKSKRKISFWYGARSLKELFYqeeFEALEKEFPNFKYHPvlsepqpeDNWDG----YTGFIHQVllenyl 241

                         170       180
                  ....*....|....*....|.
gi 2790412202 175 -----SRTAHIYCCGPAPLMN 190
Cdd:cd06188   242 kkhpaPEDIEFYLCGPPPMNS 262
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 104-190 9.14e-09

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: 52.26  E-value: 9.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202 104 FIAGGIGITPIMSMIEAC----RSKGERWrLLYCVRTRARAAY------LWRLAEHHAQVQLHVDEEQGGPADVSGFIR- 172
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAIledpKDPTQVV-LVFGNRNEDDILYreeldeLAEKHPGRLTVVYVVSRPEAGWTGGKGRVQd 79

                          90       100
                  ....*....|....*....|....*.
gi 2790412202 173 --------SVSRTAHIYCCGPAPLMN 190
Cdd:pfam00175  80 alledhlsLPDEETHVYVCGPPGMIK 105
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 225-311 2.80e-08

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 54.11  E-value: 2.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202 225 AFRVTLKRTGGTFMVPGGRSILQTLEDNGIALPCSCREGLCRTCETPLIGGRADHRDF---VLSDEERAgNSSIIPCVSR 301
Cdd:PRK07609    2 SFQVTLQPSGRQFTAEPDETILDAALRQGIHLPYGCKNGACGSCKGRLLEGEVEQGPHqasALSGEERA-AGEALTCCAK 80

                          90
                  ....*....|
gi 2790412202 302 ALDDeLVLDI 311
Cdd:PRK07609   81 PLSD-LVLEA 89
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 14-190 3.60e-08

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: 53.04  E-value: 3.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  14 IELRAAADGTLPaFTAGSHIDLHLPGGLCRQYSLTNAPSEQERYCLGVGLAPESRgGSRHVHQQLRAGDQIQISAPRSLF 93
Cdd:cd06194    12 LRVRLEPDRPLP-YLPGQYVNLRRAGGLARSYSPTSLPDGDNELEFHIRRKPNGA-FSGWLGEEARPGHALRLQGPFGQA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  94 SLNAE--ADEHVFIAGGIGITPIMSMIEACRSKGER--WRLLYCVRTRA----RAAYLWrLAEHHAQ--VQLHVDEEQGG 163
Cdd:cd06194    90 FYRPEygEGPLLLVGAGTGLAPLWGIARAALRQGHQgeIRLVHGARDPDdlylHPALLW-LAREHPNfrYIPCVSEGSQG 168

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2790412202 164 PADVSGF-----IRSVSRTAHIYCCGPAPLMN 190
Cdd:cd06194   169 DPRVRAGriaahLPPLTRDDVVYLCGAPSMVN 200
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
14-189 6.68e-08

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 53.21  E-value: 6.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  14 IELRAAADGTLPAFTAGSHIDLHLPGGLC-RQYSLTNAPSEQERYCLGVGLAPesrGG--SRHVHQQLRAGDQIQISAPR 90
Cdd:PRK11872  124 LHLDASAHGRQLDFLPGQYARLQIPGTDDwRSYSFANRPNATNQLQFLIRLLP---DGvmSNYLRERCQVGDEILFEAPL 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  91 SLFSLNAEADEHVFIAGGIGITPIMSMIEACRSKGERW--RLLYCVRTRARAAYLWRLAEHHAQ--------VQLHVDEE 160
Cdd:PRK11872  201 GAFYLREVERPLVFVAGGTGLSAFLGMLDELAEQGCSPpvHLYYGVRHAADLCELQRLAAYAERlpnfryhpVVSKASAD 280

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2790412202 161 QGGPadvSGFI-------RSVSRTAHIYCCGPAPLM 189
Cdd:PRK11872  281 WQGK---RGYIhehfdkaQLRDQAFDMYLCGPPPMV 313
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 16-184 9.32e-08

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: 52.18  E-value: 9.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  16 LRAAADGTLPaFTAGSHIDLHLPGG----LCRQYSLTNAPSEQ--ERYclgVGLAPESRGGSRHvhQQLRAGDQIQISA- 88
Cdd:cd06195    15 FRVTRDIPFR-FQAGQFTKLGLPNDdgklVRRAYSIASAPYEEnlEFY---IILVPDGPLTPRL--FKLKPGDTIYVGKk 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  89 PRSLFSLNA--EADEHVFIAGGIGITPIMSMIEAcrskGERWR------LLYCVRTRARAAYLWRLAEHHAQV--QLHV- 157
Cdd:cd06195    89 PTGFLTLDEvpPGKRLWLLATGTGIAPFLSMLRD----LEIWErfdkivLVHGVRYAEELAYQDEIEALAKQYngKFRYv 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2790412202 158 ------DEEQGGPADVSGFIRS-----------VSRTAHIYCCG 184
Cdd:cd06195   165 pivsreKENGALTGRIPDLIESgeleehaglplDPETSHVMLCG 208
petF CHL00134
ferredoxin; Validated
 236-300 1.52e-07

ferredoxin; Validated


Pssm-ID: 177056 [Multi-domain]  Cd Length: 99  Bit Score: 48.56  E-value: 1.52e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790412202 236 TFMVPGGRSILQTLEDNGIALPCSCREGLCRTCETPLIGGRADHRDFVLSDEERAGNSSIIPCVS 300
Cdd:CHL00134   18 TIDCPDDVYILDAAEEQGIDLPYSCRAGACSTCAGKVTEGTVDQSDQSFLDDDQLEAGFVLTCVA 82
FNR_like_2 cd06197
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) ...
 93-211 2.68e-07

FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and have a variety of physiological functions in a variety of organisms including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which varies in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one-electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99794  Cd Length: 220  Bit Score: 50.47  E-value: 2.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  93 FSLNAEADEH--VFIAGGIGITPIMSMIEAcrskgerwrLLYCVRTRARAAYLWRLAEHHAQ-VQLHVDEEQGGPADVSG 169
Cdd:cd06197   117 LSLPGEGAERkmVWIAGGVGITPFLAMLRA---------ILSSRNTTWDITLLWSLREDDLPlVMDTLVRFPGLPVSTTL 187

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2790412202 170 FIrsvsrTAHIYCCGPAPLMNAVEAAASaaehpSKAVHFERF 211
Cdd:cd06197   188 FI-----TSEVYLCGPPALEKAVLEWLE-----GKKVHRESF 219
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 6-211 3.16e-07

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: 50.00  E-value: 3.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202   6 HEAEGVLGIELRAAADGTlpaFTAGSHIDLHLPGGLCR-Q---YSLTNAPSEQERYcLGVGLAPESrGGSRHVHQQLRAG 81
Cdd:cd06186     7 LPDSDVIRLTIPKPKPFK---WKPGQHVYLNFPSLLSFwQshpFTIASSPEDEQDT-LSLIIRAKK-GFTTRLLRKALKS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  82 DQIQISAP-------RSLFSLNAEADEHVFIAGGIGITPIMSMIEACRSKGERWRLLYCVR----TRARAAYLWRLAEhh 150
Cdd:cd06186    82 PGGGVSLKvlvegpyGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSSKTSRTRRVKlvwvVRDREDLEWFLDE-- 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790412202 151 aqvqLHVDEEQGGPADVSGFIRSVsrtahiYCCGPAPLMNAVEAAASAAEHPSKAVHFERF 211
Cdd:cd06186   160 ----LRAAQELEVDGEIEIYVTRV------VVCGPPGLVDDVRNAVAKKGGTGVEFHEESF 210
PTZ00038 PTZ00038
ferredoxin; Provisional
 245-305 2.20e-06

ferredoxin; Provisional


Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 47.52  E-value: 2.20e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790412202 245 ILQTLEDNGIALPCSCREGLCRTCETPLIGGRADHRDFVLSDEERAGNSSIIPCVSRALDD 305
Cdd:PTZ00038  117 ILDAAERQGVELPYSCRGGSCSTCAAKLLEGEVDNEDQSYLDDEQLKKGYCLLCTCYPKSD 177
PLN03136 PLN03136
Ferredoxin; Provisional
 245-305 3.26e-06

Ferredoxin; Provisional


Pssm-ID: 178681 [Multi-domain]  Cd Length: 148  Bit Score: 46.28  E-value: 3.26e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790412202 245 ILQTLEDNGIALPCSCREGLCRTCETPLIGGRADHRDFVLSDEERAGNSSIIPCVSRALDD 305
Cdd:PLN03136   76 VLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSIDQSDQSFLDDEQISEGYVLTCVAYPTSD 136
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 77-189 6.10e-06

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 46.79  E-value: 6.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  77 QLRAGDQIQISAPrsL---FSLNAEADEHVFIAGGIGITPIMSMIEACRSKGERWRLLYCVRTRARAAYLWRLAEHhaqV 153
Cdd:PRK00054   79 KLKEGDELDIRGP--LgngFDLEEIGGKVLLVGGGIGVAPLYELAKELKKKGVEVTTVLGARTKDEVIFEEEFAKV---G 153

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2790412202 154 QLHVDEEQGGpADVSGFIRSV-----SRTAHIYCCGPAPLM 189
Cdd:PRK00054  154 DVYVTTDDGS-YGFKGFVTDVldeldSEYDAIYSCGPEIMM 193
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 76-189 3.29e-05

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


Pssm-ID: 99817 [Multi-domain]  Cd Length: 253  Bit Score: 44.52  E-value: 3.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  76 QQLRAGDQIQISAP--RSlFSLNAEADEHV-FIAGGIGITPIMSMIEAC---RSKGERWRLLYCVRTRARAAYL-----W 144
Cdd:cd06221    73 HELKPGDTVGLRGPfgNG-FPVEEMKGKDLlLVAGGLGLAPLRSLINYIldnREDYGKVTLLYGARTPEDLLFKeelkeW 151

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2790412202 145 RlAEHHAQVQLHVDEEQGGPADVSGFIRSVSRTAHI-------YCCGPAPLM 189
Cdd:cd06221   152 A-KRSDVEVILTVDRAEEGWTGNVGLVTDLLPELTLdpdntvaIVCGPPIMM 202
CYPOR_like cd06182
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 14-189 2.58e-04

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


Pssm-ID: 99779 [Multi-domain]  Cd Length: 267  Bit Score: 41.94  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  14 IELRAAaDGTLPAFTAGSHIDLHLPGGL-CRQYSLTNAPSEQE---RYCLGV--GLAPESR---GGSRHVHQQLRAGDQI 84
Cdd:cd06182    20 LEFDLS-GNSVLKYQPGDHLGVIPPNPLqPRYYSIASSPDVDPgevHLCVRVvsYEAPAGRirkGVCSNFLAGLQLGAKV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  85 QISAPRSL-FSLNAEADEHVF-IAGGIGITPIMSMIEA-------CRSKGERWrLLYCVRTRARAaYLWR-------LAE 148
Cdd:cd06182    99 TVFIRPAPsFRLPKDPTTPIImVGPGTGIAPFRGFLQEraalranGKARGPAW-LFFGCRNFASD-YLYReelqealKDG 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2790412202 149 HHAQVQLHVDEEQGGPA---------DVSGFIRSVSRTAHIYCCGPAPLM 189
Cdd:cd06182   177 ALTRLDVAFSREQAEPKvyvqdklkeHAEELRRLLNEGAHIYVCGDAKSM 226
PLN02252 PLN02252
nitrate reductase [NADPH]
 69-190 3.28e-04

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 42.36  E-value: 3.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  69 GG--SRHVHQqLRAGDQIQISAP--------RSLFSLNAE---ADEHVFIAGGIGITPIMSMIEACRSKGE---RWRLLY 132
Cdd:PLN02252  716 GGlmSQYLDS-LPIGDTIDVKGPlghieyagRGSFLVNGKpkfAKKLAMLAGGTGITPMYQVIQAILRDPEdktEMSLVY 794

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790412202 133 CVRT------RARaayLWRLA-EHHAQVQLHVDEEQGGPADVS---GFIRSVSRTAHIY---------CCGPAPLMN 190
Cdd:PLN02252  795 ANRTeddillREE---LDRWAaEHPDRLKVWYVVSQVKREGWKysvGRVTEAMLREHLPeggdetlalMCGPPPMIE 868
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 78-189 3.71e-04

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: 41.08  E-value: 3.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790412202  78 LRAGDQIQISAPR-SLFSLnaEADEHVFIAGGIGITPIMSMIEACRSKGERwRLLYCVRTRARAAYLWRLAEHHaqvQLH 156
Cdd:cd06220    68 LKEGDKLGIRGPYgNGFEL--VGGKVLLIGGGIGIAPLAPLAERLKKAADV-TVLLGARTKEELLFLDRLRKSD---ELI 141

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2790412202 157 VDEE------QGGPADVSGFIRSVSRTAhIYCCGPAPLM 189
Cdd:cd06220   142 VTTDdgsygfKGFVTDLLKELDLEEYDA-IYVCGPEIMM 179
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 77-126 6.77e-04

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: 40.30  E-value: 6.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2790412202  77 QLRAGDQIQISAPRSLFSLNAEAdehVFIAGGIGITPIMSMIEACRSKGE 126
Cdd:cd06196    80 RLQPGDTLLIEDPWGAIEYKGPG---VFIAGGAGITPFIAILRDLAAKGK 126
 
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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