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Conserved domains on  [gi|47169163]
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Chain A, chloroplast ferredoxin-NADP+ oxidoreductase

Protein Classification

PLN03115 family protein( domain architecture ID 11477437)

PLN03115 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
 1-296 0e+00

ferredoxin--NADP(+) reductase; Provisional


:

Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 645.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163    1 ISKKQDEGVVVNKFRPKEPYIGRCLLNTKITGDDAPGETWHMVFSTEGEIPYREGQSIGVIADGVDANGKPHKLRLYSIA 80
Cdd:PLN03115  72 VSKKNEEGVVVNKFRPKEPYTGRCLLNTKITGDDAPGETWHMVFSTEGEIPYREGQSIGVIPDGIDKNGKPHKLRLYSIA 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163   81 SSALGDFGDSKTVSLCVKRLVYTNDKGEEVKGVCSNFLCDLKPGADVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPFR 160
Cdd:PLN03115 152 SSALGDFGDSKTVSLCVKRLVYTNDQGEIVKGVCSNFLCDLKPGAEVKITGPVGKEMLMPKDPNATIIMLATGTGIAPFR 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  161 SFLWKMFFEKHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQTNEKGEKMYIQTRMAQYAEEL 240
Cdd:PLN03115 232 SFLWKMFFEKHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQTNAKGEKMYIQTRMAEYAEEL 311

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 47169163  241 WTLLKKDNTFVYMCGLKGMEQGIDDIMSSLAAKEGIDWADYKKQLKKAEQWNVEVY 296
Cdd:PLN03115 312 WELLKKDNTYVYMCGLKGMEKGIDDIMVSLAAKDGIDWFEYKKQLKKAEQWNVEVY 367
 
Name Accession Description Interval E-value
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
 1-296 0e+00

ferredoxin--NADP(+) reductase; Provisional


Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 645.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163    1 ISKKQDEGVVVNKFRPKEPYIGRCLLNTKITGDDAPGETWHMVFSTEGEIPYREGQSIGVIADGVDANGKPHKLRLYSIA 80
Cdd:PLN03115  72 VSKKNEEGVVVNKFRPKEPYTGRCLLNTKITGDDAPGETWHMVFSTEGEIPYREGQSIGVIPDGIDKNGKPHKLRLYSIA 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163   81 SSALGDFGDSKTVSLCVKRLVYTNDKGEEVKGVCSNFLCDLKPGADVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPFR 160
Cdd:PLN03115 152 SSALGDFGDSKTVSLCVKRLVYTNDQGEIVKGVCSNFLCDLKPGAEVKITGPVGKEMLMPKDPNATIIMLATGTGIAPFR 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  161 SFLWKMFFEKHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQTNEKGEKMYIQTRMAQYAEEL 240
Cdd:PLN03115 232 SFLWKMFFEKHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQTNAKGEKMYIQTRMAEYAEEL 311

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 47169163  241 WTLLKKDNTFVYMCGLKGMEQGIDDIMSSLAAKEGIDWADYKKQLKKAEQWNVEVY 296
Cdd:PLN03115 312 WELLKKDNTYVYMCGLKGMEKGIDDIMVSLAAKDGIDWFEYKKQLKKAEQWNVEVY 367
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
 12-296 3.72e-175

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: 485.29  E-value: 3.72e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  12 NKFRPKEPYIGRCLLNTKITGDDAPGETWHMVFSTEGEIPYREGQSIGVIADGVDA-NGKPHKLRLYSIASSALGDFGDS 90
Cdd:cd06208   1 NLYKPKNPLIGKVVSNTRLTGPDAPGEVCHIVIDHGGKLPYLEGQSIGIIPPGTDAkNGKPHKLRLYSIASSRYGDDGDG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  91 KTVSLCVKRLVYTNDKG-EEVKGVCSNFLCDLKPGADVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPFRSFLWKMFFE 169
Cdd:cd06208  81 KTLSLCVKRLVYTDPETdETKKGVCSNYLCDLKPGDDVQITGPVGKTMLLPEDPNATLIMIATGTGIAPFRSFLRRLFRE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 170 KHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQTNEKGEKMYIQTRMAQYAEELWTLLKKDNT 249
Cdd:cd06208 161 KHADYKFTGLAWLFFGVPNSDSLLYDDELEKYPKQYPDNFRIDYAFSREQKNADGGKMYVQDRIAEYAEEIWNLLDKDNT 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 47169163 250 FVYMCGLKGMEQGIDDIMSSLaAKEGIDWADYKKQLKKAEQWNVEVY 296
Cdd:cd06208 241 HVYICGLKGMEPGVDDALTSV-AEGGLAWEEFWESLKKKGRWHVEVY 286
PetH COG5675
Ferredoxin-NADP+ oxidoreductase PetH, often fused with N-terminal CpcD domain [Energy ...
 3-296 2.72e-167

Ferredoxin-NADP+ oxidoreductase PetH, often fused with N-terminal CpcD domain [Energy production and conversion];


Pssm-ID: 444389 [Multi-domain]  Cd Length: 405  Bit Score: 469.91  E-value: 2.72e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163   3 KKQDEGVVVNKFRPKEPYIGRCLLNTKITGDDAPGETWHMVFS-TEGEIPYREGQSIGVIADGVDANGKPHKLRLYSIAS 81
Cdd:COG5675 108 KKKKADVPVNIYRPKNPFIGKCISNYELVAEGGIGTVRHLTFDiSGGDLRYLEGQSIGIIPPGTDKKGKPHKLRLYSIAS 187

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  82 SALGDFGDSKTVSLCVKRLVYTNDK-GEEVKGVCSNFLCDLKPGADVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPFR 160
Cdd:COG5675 188 TRHGDNVDDKTVSLCVRQLEYKHPEtGETVYGVCSTYLCNLEPGADVKITGPVGKEMLLPDDEDANIIMMATGTGIAPFR 267

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 161 SFLWKMFFEKH--DDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQTNEKGEKMYIQTRMAQYAE 238
Cdd:COG5675 268 AYLWRMFKEQEenPDYQFKGLAWLIFGIPTTPNILYKEELEELQAEYPDNFRLTYAISREQKNPEGGRMYIQDRVAEHAD 347

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 47169163 239 ELWTLLKKDNTFVYMCGLKGMEQGIDDIMSSLAAKEGIDWADYKKQLKKAEQWNVEVY 296
Cdd:COG5675 348 ELWKLIQKPKTHTYICGLKGMEDGIDEALTAAAAKNGVNWSDYQKQLKKAGRWHVETY 405
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 149-265 1.93e-28

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: 105.42  E-value: 1.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163   149 MLGTGTGIAPFRSFLWKMFFEKHDdykfNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQTNEKGEKMY 228
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILEDPKD----PTQVVLVFGNRNEDDILYREELDELAEKHPGRLTVVYVVSRPEAGWTGGKGR 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 47169163   229 IQTRMAQYAEElwtlLKKDNTFVYMCGLKGMEQGIDD 265
Cdd:pfam00175  77 VQDALLEDHLS----LPDEETHVYVCGPPGMIKAVRK 109
 
Name Accession Description Interval E-value
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
 1-296 0e+00

ferredoxin--NADP(+) reductase; Provisional


Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 645.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163    1 ISKKQDEGVVVNKFRPKEPYIGRCLLNTKITGDDAPGETWHMVFSTEGEIPYREGQSIGVIADGVDANGKPHKLRLYSIA 80
Cdd:PLN03115  72 VSKKNEEGVVVNKFRPKEPYTGRCLLNTKITGDDAPGETWHMVFSTEGEIPYREGQSIGVIPDGIDKNGKPHKLRLYSIA 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163   81 SSALGDFGDSKTVSLCVKRLVYTNDKGEEVKGVCSNFLCDLKPGADVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPFR 160
Cdd:PLN03115 152 SSALGDFGDSKTVSLCVKRLVYTNDQGEIVKGVCSNFLCDLKPGAEVKITGPVGKEMLMPKDPNATIIMLATGTGIAPFR 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  161 SFLWKMFFEKHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQTNEKGEKMYIQTRMAQYAEEL 240
Cdd:PLN03115 232 SFLWKMFFEKHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQTNAKGEKMYIQTRMAEYAEEL 311

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 47169163  241 WTLLKKDNTFVYMCGLKGMEQGIDDIMSSLAAKEGIDWADYKKQLKKAEQWNVEVY 296
Cdd:PLN03115 312 WELLKKDNTYVYMCGLKGMEKGIDDIMVSLAAKDGIDWFEYKKQLKKAEQWNVEVY 367
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
 12-296 3.72e-175

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: 485.29  E-value: 3.72e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  12 NKFRPKEPYIGRCLLNTKITGDDAPGETWHMVFSTEGEIPYREGQSIGVIADGVDA-NGKPHKLRLYSIASSALGDFGDS 90
Cdd:cd06208   1 NLYKPKNPLIGKVVSNTRLTGPDAPGEVCHIVIDHGGKLPYLEGQSIGIIPPGTDAkNGKPHKLRLYSIASSRYGDDGDG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  91 KTVSLCVKRLVYTNDKG-EEVKGVCSNFLCDLKPGADVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPFRSFLWKMFFE 169
Cdd:cd06208  81 KTLSLCVKRLVYTDPETdETKKGVCSNYLCDLKPGDDVQITGPVGKTMLLPEDPNATLIMIATGTGIAPFRSFLRRLFRE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 170 KHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQTNEKGEKMYIQTRMAQYAEELWTLLKKDNT 249
Cdd:cd06208 161 KHADYKFTGLAWLFFGVPNSDSLLYDDELEKYPKQYPDNFRIDYAFSREQKNADGGKMYVQDRIAEYAEEIWNLLDKDNT 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 47169163 250 FVYMCGLKGMEQGIDDIMSSLaAKEGIDWADYKKQLKKAEQWNVEVY 296
Cdd:cd06208 241 HVYICGLKGMEPGVDDALTSV-AEGGLAWEEFWESLKKKGRWHVEVY 286
PetH COG5675
Ferredoxin-NADP+ oxidoreductase PetH, often fused with N-terminal CpcD domain [Energy ...
 3-296 2.72e-167

Ferredoxin-NADP+ oxidoreductase PetH, often fused with N-terminal CpcD domain [Energy production and conversion];


Pssm-ID: 444389 [Multi-domain]  Cd Length: 405  Bit Score: 469.91  E-value: 2.72e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163   3 KKQDEGVVVNKFRPKEPYIGRCLLNTKITGDDAPGETWHMVFS-TEGEIPYREGQSIGVIADGVDANGKPHKLRLYSIAS 81
Cdd:COG5675 108 KKKKADVPVNIYRPKNPFIGKCISNYELVAEGGIGTVRHLTFDiSGGDLRYLEGQSIGIIPPGTDKKGKPHKLRLYSIAS 187

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  82 SALGDFGDSKTVSLCVKRLVYTNDK-GEEVKGVCSNFLCDLKPGADVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPFR 160
Cdd:COG5675 188 TRHGDNVDDKTVSLCVRQLEYKHPEtGETVYGVCSTYLCNLEPGADVKITGPVGKEMLLPDDEDANIIMMATGTGIAPFR 267

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 161 SFLWKMFFEKH--DDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQTNEKGEKMYIQTRMAQYAE 238
Cdd:COG5675 268 AYLWRMFKEQEenPDYQFKGLAWLIFGIPTTPNILYKEELEELQAEYPDNFRLTYAISREQKNPEGGRMYIQDRVAEHAD 347

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 47169163 239 ELWTLLKKDNTFVYMCGLKGMEQGIDDIMSSLAAKEGIDWADYKKQLKKAEQWNVEVY 296
Cdd:COG5675 348 ELWKLIQKPKTHTYICGLKGMEDGIDEALTAAAAKNGVNWSDYQKQLKKAGRWHVETY 405
PLN03116 PLN03116
ferredoxin--NADP+ reductase; Provisional
 11-296 1.20e-132

ferredoxin--NADP+ reductase; Provisional


Pssm-ID: 215586 [Multi-domain]  Cd Length: 307  Bit Score: 378.29  E-value: 1.20e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163   11 VNKFRPKEPYIGRCLLNTKITGDDAPGETWHMVFSTEGEIPYREGQSIGVIADGVDAN--GKPHKLRLYSIASSALGDFG 88
Cdd:PLN03116  16 LNLYKPKAPYTATIVSVERIVGPKAPGETCHIVIDHGGNVPYWEGQSYGVIPPGTNPKkpGAPHNVRLYSIASTRYGDDF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163   89 DSKTVSLCVKRLVY----TNDKGEEVKGVCSNFLCDLKPGADVKITGPVGKEMLMP-KDPNATVIMLGTGTGIAPFRSFL 163
Cdd:PLN03116  96 DGKTASLCVRRAVYydpeTGKEDPAKKGVCSNFLCDAKPGDKVQITGPSGKVMLLPeEDPNATHIMVATGTGIAPFRGFL 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  164 WKMFFEKHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQTNEKGEKMYIQTRMAQYAEELWTL 243
Cdd:PLN03116 176 RRMFMEDVPAFKFGGLAWLFLGVANSDSLLYDDEFERYLKDYPDNFRYDYALSREQKNKKGGKMYVQDKIEEYSDEIFKL 255

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 47169163  244 LkKDNTFVYMCGLKGMEQGIDDIMSSLAAKEGIDWADYKKQLKKAEQWNVEVY 296
Cdd:PLN03116 256 L-DNGAHIYFCGLKGMMPGIQDTLKRVAEERGESWEEKLSGLKKNKQWHVEVY 307
CYPOR_like cd06182
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 23-296 2.36e-93

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: 277.30  E-value: 2.36e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  23 RCLLNTKITGDDAPGETWHMVFST--EGEIPYREGQSIGVIADGvdangkPHKLRLYSIASSALGDfgdSKTVSLCVKRL 100
Cdd:cd06182   1 AITVNRKLTPPDSPRSTRHLEFDLsgNSVLKYQPGDHLGVIPPN------PLQPRYYSIASSPDVD---PGEVHLCVRVV 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 101 VYTNDKGEEVKGVCSNFLCDLKPGADVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPFRSFLWKMFFEKHdDYKFNGLA 180
Cdd:cd06182  72 SYEAPAGRIRKGVCSNFLAGLQLGAKVTVFIRPAPSFRLPKDPTTPIIMVGPGTGIAPFRGFLQERAALRA-NGKARGPA 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 181 WLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQTNekgEKMYIQTRMAQYAEELWTLLKKDNtFVYMCG-LKGM 259
Cdd:cd06182 151 WLFFGCRNFASDYLYREELQEALKDGALTRLDVAFSREQAE---PKVYVQDKLKEHAEELRRLLNEGA-HIYVCGdAKSM 226

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 47169163 260 EQGIDDIMSSLAAKEG----IDWADYKKQLKKAEQWNVEVY 296
Cdd:cd06182 227 AKDVEDALVKIIAKAGgvdeSDAEEYLKELEDEGRYVEDVW 267
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 38-275 3.46e-36

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: 129.10  E-value: 3.46e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  38 ETWHMVFSTEGEIPYREGQSIGVIADgvdaNGKPHKLRLYSIASSAlgdfGDSKTVSLCVKRlvytndkgeEVKGVCSNF 117
Cdd:cd00322   9 DVRLFRLQLPNGFSFKPGQYVDLHLP----GDGRGLRRAYSIASSP----DEEGELELTVKI---------VPGGPFSAW 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 118 LCDLKPGADVKITGPVGKEMLmPKDPNATVIMLGTGTGIAPFRSFLWKMFFEKHddykfNGLAWLFLGVPTSSSLLYKEE 197
Cdd:cd00322  72 LHDLKPGDEVEVSGPGGDFFL-PLEESGPVVLIAGGIGITPFRSMLRHLAADKP-----GGEITLLYGARTPADLLFLDE 145

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47169163 198 FEKMKEKAPeNFRLDFAVSREQTNEKGEkmyiQTRMAQYAEELWTLLKKDNTFVYMCGLKGMEQGIDDIMSSLAAKEG 275
Cdd:cd00322 146 LEELAKEGP-NFRLVLALSRESEAKLGP----GGRIDREAEILALLPDDSGALVYICGPPAMAKAVREALVSLGVPEE 218
CyPoR_like cd06207
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 75-296 9.73e-34

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


Pssm-ID: 99803 [Multi-domain]  Cd Length: 382  Bit Score: 126.62  E-value: 9.73e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  75 RLYSIASSALGDfgdSKTVSLCVKRLVYTNDKGEEVKGVCSNFLCDLKPGadVKITGPVGK-EMLMPKDPNATVIMLGTG 153
Cdd:cd06207 165 RYYSISSSPLKN---PNEVHLLVSLVSWKTPSGRSRYGLCSSYLAGLKVG--QRVTVFIKKsSFKLPKDPKKPIIMVGPG 239

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 154 TGIAPFRSFL-WKMFFEKHDdyKFNGLAWLFLGVPT-SSSLLYKEEFEKMKEKAPENfRLDFAVSREQtnekGEKMYIQT 231
Cdd:cd06207 240 TGLAPFRAFLqERAALLAQG--PEIGPVLLYFGCRHeDKDYLYKEELEEYEKSGVLT-TLGTAFSRDQ----PKKVYVQD 312

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47169163 232 RMAQYAEELWTLLKKDNTFVYMCG-----LKGMEQGIDDImssLAAKEGIDWAD---YKKQLKKAEQWNVEVY 296
Cdd:cd06207 313 LIRENSDLVYQLLEEGAGVIYVCGstwkmPPDVQEAFEEI---LKKHGGGDEELaekKIEELEERGRYVVEAW 382
SiR cd06199
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 75-296 1.85e-33

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


Pssm-ID: 99796 [Multi-domain]  Cd Length: 360  Bit Score: 125.42  E-value: 1.85e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  75 RLYSIASSALGDfGDSktVSLCVKRLVYTNDkGEEVKGVCSNFLCD-LKPGADVKITGPVGKEMLMPKDPNATVIMLGTG 153
Cdd:cd06199 147 RLYSIASSPKAV-PDE--VHLTVAVVRYESH-GRERKGVASTFLADrLKEGDTVPVFVQPNPHFRLPEDPDAPIIMVGPG 222

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 154 TGIAPFRSFLWKMFFEKHddykfNGLAWLFLGVPTS-SSLLYKEEFEKMKEKAPENfRLDFAVSREQTnekgEKMYIQTR 232
Cdd:cd06199 223 TGIAPFRAFLQEREATGA-----KGKNWLFFGERHFaTDFLYQDELQQWLKDGVLT-RLDTAFSRDQA----EKVYVQDR 292

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47169163 233 MAQYAEELWTLLKKDNTFvYMCG-LKGMEQGIDDIMSSLAAKEG-IDWA---DYKKQLKKAEQWNVEVY 296
Cdd:cd06199 293 MREQGAELWAWLEEGAHF-YVCGdAKRMAKDVDAALLDIIATEGgMDEEeaeAYLKELKKEKRYQRDVY 360
PRK06214 PRK06214
sulfite reductase subunit alpha;
17-296 2.88e-32

sulfite reductase subunit alpha;


Pssm-ID: 235745 [Multi-domain]  Cd Length: 530  Bit Score: 124.80  E-value: 2.88e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163   17 KEPYIGRCLLNTKITGDDAPGETWHMVFSTEGE-IPYREGQSIGV----------------------------------- 60
Cdd:PRK06214 166 DNPVEATFLSRRRLNKPGSEKETWHVEIDLAGSgLDYEVGDSLGLfpandpalvdaviaalgappefpiggktlrealle 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163   61 -----------------------------IADGVDANGKPHKL----------------------------RLYSIASSA 83
Cdd:PRK06214 246 dvslgpapdglfellsyitggaarkkaraLAAGEDPDGDAATLdvlaalekfpgirpdpeafvealdplqpRLYSISSSP 325

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163   84 LGDFGdskTVSLCVKRLVYTNdKGEEVKGVCSNFLCD-LKPGADVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPFRSF 162
Cdd:PRK06214 326 KATPG---RVSLTVDAVRYEI-GSRLRLGVASTFLGErLAPGTRVRVYVQKAHGFALPADPNTPIIMVGPGTGIAPFRAF 401

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  163 LWkmffeKHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQtnekGEKMYIQTRMAQYAEELWT 242
Cdd:PRK06214 402 LH-----ERAATKAPGRNWLFFGHQRSATDFFYEDELNGLKAAGVLTRLSLAWSRDG----EEKTYVQDRMRENGAELWK 472

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 47169163  243 LLKKDNTFvYMCG-----LKGMEQGIDDIMSSLAAKEGIDWADYKKQLKKAEQWNVEVY 296
Cdd:PRK06214 473 WLEEGAHF-YVCGdakrmAKDVERALVDIVAQFGGRSPDEAVAFVAELKKAGRYQADVY 530
CysJ COG0369
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ...
 9-288 2.21e-31

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


Pssm-ID: 440138 [Multi-domain]  Cd Length: 561  Bit Score: 122.56  E-value: 2.21e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163   9 VVVNKFRPKEPYIGRCLLNTKITGDDAPGETWHMVFSTEG-EIPYREGQSIGVIA----------------DG---VDAN 68
Cdd:COG0369 186 AAAPAYSRKNPFPATVLENRELTGRGSAKETRHIEIDLPGsGLSYEPGDALGVWPendpalvdellarlglDGdepVTLD 265

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  69 GKPHKL-------------------------------------------------------------------------- 74
Cdd:COG0369 266 GEPLSLrealtehleltrltppllekyaeltgnaelaalladedkaalreylagrqlldllrefpaaelsaeellellrp 345

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  75 ---RLYSIASSALGDfGDskTVSLCVKRLVYTNDkGEEVKGVCSNFLCDLKPGADVKI---TGPVGKemlMPKDPNATVI 148
Cdd:COG0369 346 ltpRLYSISSSPKAH-PD--EVHLTVGVVRYEAS-GRERKGVASTYLADLEEGDTVPVfvePNPNFR---LPADPDTPII 418

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 149 MLGTGTGIAPFRSFLWkmffEKHDDyKFNGLAWLFLGVPTSSS-LLYKEEFekmkekapENF-------RLDFAVSREQt 220
Cdd:COG0369 419 MIGPGTGIAPFRAFLQ----EREAR-GASGKNWLFFGDRHFTTdFLYQTEL--------QAWlkdgvltRLDLAFSRDQ- 484

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47169163 221 nekGEKMYIQTRMAQYAEELWTLLkKDNTFVYMCG-LKGMEQGIDDIMSSLAAKEG---IDWA-DYKKQLKKA 288
Cdd:COG0369 485 ---AEKIYVQHRLLEQGAELWAWL-EEGAHVYVCGdASRMAKDVDAALLDIIAEHGglsEEEAeEYLAELRAE 553
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 149-265 1.93e-28

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: 105.42  E-value: 1.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163   149 MLGTGTGIAPFRSFLWKMFFEKHDdykfNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQTNEKGEKMY 228
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILEDPKD----PTQVVLVFGNRNEDDILYREELDELAEKHPGRLTVVYVVSRPEAGWTGGKGR 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 47169163   229 IQTRMAQYAEElwtlLKKDNTFVYMCGLKGMEQGIDD 265
Cdd:pfam00175  77 VQDALLEDHLS----LPDEETHVYVCGPPGMIKAVRK 109
CYPOR cd06204
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 75-291 4.41e-23

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


Pssm-ID: 99801 [Multi-domain]  Cd Length: 416  Bit Score: 97.71  E-value: 4.41e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  75 RLYSIASSALGDfgdSKTVSLCVKRLVYTNDKGEEVKGVCSNFLCDLKP-GADVKITGPVGKEML--------------- 138
Cdd:cd06204 179 RYYSISSSSKVH---PNRIHITAVVVKYPTPTGRIIKGVATNWLLALKPaLNGEKPPTPYYLSGPrkkgggskvpvfvrr 255

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 139 ----MPKDPNATVIMLGTGTGIAPFRSFL-----WKmffEKHDDYkfnGLAWLFLGVPTSSS-LLYKEEFEKMKEKApEN 208
Cdd:cd06204 256 snfrLPTKPSTPVIMIGPGTGVAPFRGFIqeraaLK---ESGKKV---GPTLLFFGCRHPDEdFIYKDELEEYAKLG-GL 328

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 209 FRLDFAVSREQtnekGEKMYIQTRMAQYAEELWTLLKKDnTFVYMCG-LKGMEQGIDDIMSSLAAKEGiDWAD-----YK 282
Cdd:cd06204 329 LELVTAFSREQ----PKKVYVQHRLAEHAEQVWELINEG-AYIYVCGdAKNMARDVEKTLLEILAEQG-GMTEteaeeYV 402


                ....*....
gi 47169163 283 KQLKKAEQW 291
Cdd:cd06204 403 KKLKTRGRY 411
bifunctional_CYPOR cd06206
These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase ...
 71-291 1.65e-21

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


Pssm-ID: 99802 [Multi-domain]  Cd Length: 384  Bit Score: 93.09  E-value: 1.65e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  71 PHKLRLYSIASSALGDfgdSKTVSLCVKRLVYTNDKGE-EVKGVCSNFLCDLKPGADVKIT-GPVGKEMLMPKDPNATVI 148
Cdd:cd06206 158 PMRPRQYSISSSPLVD---PGHATLTVSVLDAPALSGQgRYRGVASSYLSSLRPGDSIHVSvRPSHSAFRPPSDPSTPLI 234

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 149 MLGTGTGIAPFRSFLWKMFFEKHDDYKFnGLAWLFLGV--PTSSSlLYKeefekmkekapENFR---------LDFAVSR 217
Cdd:cd06206 235 MIAAGTGLAPFRGFLQERAALLAQGRKL-APALLFFGCrhPDHDD-LYR-----------DELEeweaagvvsVRRAYSR 301

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47169163 218 eqTNEKGEKmYIQTRMAQYAEELWTLLKKDNTfVYMCGLKGMEQGIDDIMSSLAAKEgiDWADYKKQLKKAEQW 291
Cdd:cd06206 302 --PPGGGCR-YVQDRLWAEREEVWELWEQGAR-VYVCGDGRMAPGVREVLKRIYAEK--DERGGGSDDEEAEEW 369
methionine_synthase_red cd06203
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ...
 75-296 1.64e-20

Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for the regeneration of methionine from homocysteine, as well as the coversion of methyltetrahydrofolate to tetrahydrofolate. In MSR, electrons are transferred from NADPH to FAD to FMN to cob(II)alamin. MSR resembles proteins of the cytochrome p450 family including nitric oxide synthase, the alpha subunit of sulfite reductase, but contains an extended hinge region. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPORs resemble ferredoxin reductase (FNR) but have a connecting subdomain inserted within the flavin binding region, which helps orient the FMN binding doamin with the FNR module. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99800 [Multi-domain]  Cd Length: 398  Bit Score: 90.46  E-value: 1.64e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  75 RLYSIASSALGDFGdskTVSLCVKRLVYTndkgeeVKGVCSNFLCDLKPGADvKITGPVGKEM-------LMPKDPNATV 147
Cdd:cd06203 175 RPYSIASSPLEGPG---KLRFIFSVVEFP------AKGLCTSWLESLCLSAS-SHGVKVPFYLrsssrfrLPPDDLRRPI 244

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 148 IMLGTGTGIAPFRSFL--WKMFFEKHDDYKFnGLAWLFLGVPTSS-SLLYKEEFEKMKEKAPENfRLDFAVSREqTNEKG 224
Cdd:cd06203 245 IMVGPGTGVAPFLGFLqhREKLKESHTETVF-GEAWLFFGCRHRDrDYLFRDELEEFLEEGILT-RLIVAFSRD-ENDGS 321

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47169163 225 EKMYIQTRMAQYAEELWTLLKKDNTFVYMCG-----LKGMEQGIDDIMSSLAAKEGIDWADYKKQLKKAEQWNVEVY 296
Cdd:cd06203 322 TPKYVQDKLEERGKKLVDLLLNSNAKIYVCGdakgmAKDVRDTFVDILSKELGLDKLEAKKLLARLRKEDRYLEDVW 398
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
51-272 5.47e-20

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 86.38  E-value: 5.47e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  51 PYREGQSIGViadGVDANGKPHkLRLYSIASSAlgdfgDSKTVSLCVKRlvytndkgeEVKGVCSNFLCD-LKPGADVKI 129
Cdd:COG1018  33 RFRPGQFVTL---RLPIDGKPL-RRAYSLSSAP-----GDGRLEITVKR---------VPGGGGSNWLHDhLKVGDTLEV 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 130 TGPVGkEMLMPKDPNATVIMLGTGTGIAPFRSFLwkmffEKHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPeNF 209
Cdd:COG1018  95 SGPRG-DFVLDPEPARPLLLIAGGIGITPFLSML-----RTLLARGPFRPVTLVYGARSPADLAFRDELEALAARHP-RL 167

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47169163 210 RLDFAVSREQTNEKGekmYIQtrmaqyAEELWTLLK-KDNTFVYMCGLKGMeqgIDDIMSSLAA 272
Cdd:COG1018 168 RLHPVLSREPAGLQG---RLD------AELLAALLPdPADAHVYLCGPPPM---MEAVRAALAE 219
cysJ PRK10953
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;
75-296 8.98e-18

NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;


Pssm-ID: 182862 [Multi-domain]  Cd Length: 600  Bit Score: 83.23  E-value: 8.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163   75 RLYSIASSAlGDFGDSKTVSLCVKRlvYTNDkGEEVKGVCSNFLCD-LKPGADVKITGPVGKEMLMPKDPNATVIMLGTG 153
Cdd:PRK10953 387 RLYSIASSQ-AEVENEVHITVGVVR--YDIE-GRARAGGASSFLADrLEEEGEVRVFIEHNDNFRLPANPETPVIMIGPG 462

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  154 TGIAPFRSFLwkmffEKHDDYKFNGLAWLFLGVPT-SSSLLYKEEFEKMKEKAPENfRLDFAVSREQTnekgEKMYIQTR 232
Cdd:PRK10953 463 TGIAPFRAFM-----QQRAADGAPGKNWLFFGNPHfTEDFLYQVEWQRYVKEGLLT-RIDLAWSRDQK----EKIYVQDK 532

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  233 MAQYAEELWTLLkKDNTFVYMCG-----LKGMEQGIDDIMSSLAAKEgIDWAD-YKKQLKKAEQWNVEVY 296
Cdd:PRK10953 533 LREQGAELWRWI-NDGAHIYVCGdanrmAKDVEQALLEVIAEFGGMD-TEAADeFLSELRVERRYQRDVY 600
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 41-270 2.42e-17

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: 79.15  E-value: 2.42e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  41 HMVFSTEGEI--PYREGQ--SIGViadgVDANGKPhKLRLYSIASSALGD---FGdsktvslcvkrLVYTNDkgeevkGV 113
Cdd:cd06195  12 LFSFRVTRDIpfRFQAGQftKLGL----PNDDGKL-VRRAYSIASAPYEEnleFY-----------IILVPD------GP 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 114 CSNFLCDLKPGADVKIT-GPVGKEMLMPKDPNATVIMLGTGTGIAPFRSFLWKMFFEKHDDyKFNglawLFLGVPTSSSL 192
Cdd:cd06195  70 LTPRLFKLKPGDTIYVGkKPTGFLTLDEVPPGKRLWLLATGTGIAPFLSMLRDLEIWERFD-KIV----LVHGVRYAEEL 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 193 LYKEEFEKMKEKAPENFRLDFAVSREQtNEKGEKMYIQTRMAQ-YAEELWTL-LKKDNTFVYMCGLKGMeqgIDDIMSSL 270
Cdd:cd06195 145 AYQDEIEALAKQYNGKFRYVPIVSREK-ENGALTGRIPDLIESgELEEHAGLpLDPETSHVMLCGNPQM---IDDTQELL 220
Nitric_oxide_synthase cd06202
The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses ...
 75-255 6.81e-16

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


Pssm-ID: 99799 [Multi-domain]  Cd Length: 406  Bit Score: 76.99  E-value: 6.81e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  75 RLYSIASSAlgDFgDSKTVSLCVKRLVY-TND-KGEEVKGVCSNFLCDLKPGADVKITGPVGKEMLMPKDPNATVIMLGT 152
Cdd:cd06202 178 RYYSISSSP--DM-YPGEIHLTVAVVSYrTRDgQGPVHHGVCSTWLNGLTPGDTVPCFVRSAPSFHLPEDPSVPVIMVGP 254

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 153 GTGIAPFRSFlWK-----MFFEKHDDYKFnGLAWLFLGVPTSSSL-LYKEEFEKMKEKapENF-RLDFAVSREQTNekgE 225
Cdd:cd06202 255 GTGIAPFRSF-WQqrqydLRMSEDPGKKF-GDMTLFFGCRNSTIDdIYKEETEEAKNK--GVLtEVYTALSREPGK---P 327

                       170       180       190
                ....*....|....*....|....*....|
gi 47169163 226 KMYIQTRMAQYAEELWTLLKKDNTFVYMCG 255
Cdd:cd06202 328 KTYVQDLLKEQAESVYDALVREGGHIYVCG 357
SiR_like1 cd06200
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 22-277 1.75e-13

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


Pssm-ID: 99797  Cd Length: 245  Bit Score: 68.46  E-value: 1.75e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  22 GRCLLNTKITGddapGETWHMVFSTEGEIPyreGQSIGVIADGVDANGKPHklRLYSIASsaLGDFGDsktVSLCVkRLV 101
Cdd:cd06200   5 ARVLLNPGSQG----APLWRLRLTPPDAGA---QWQAGDIAEIGPRHPLPH--REYSIAS--LPADGA---LELLV-RQV 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 102 YTNDKGeevKGVCSNFLCDLKP-GADVKITgPVGKEMLMPKDPNATVIMLGTGTGIAPFRSFL-----------WKMFFE 169
Cdd:cd06200  70 RHADGG---LGLGSGWLTRHAPiGASVALR-LRENPGFHLPDDGRPLILIGNGTGLAGLRSHLrararagrhrnWLLFGE 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 170 KHDDYKF----NGLAWLFLGVPTsssllykeefekmkekapenfRLDFAVSREQtnekGEKMYIQTRMAQYAEEL--WTl 243
Cdd:cd06200 146 RQAAHDFfcreELEAWQAAGHLA---------------------RLDLAFSRDQ----AQKRYVQDRLRAAADELraWV- 199

                       250       260       270
                ....*....|....*....|....*....|....*
gi 47169163 244 lkKDNTFVYMCG-LKGMEQGIDDIMSSLAAKEGID 277
Cdd:cd06200 200 --AEGAAIYVCGsLQGMAPGVDAVLDEILGEEAVE 232
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 49-270 3.34e-13

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: 67.73  E-value: 3.34e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  49 EIPYREGQSIGVIADGVDANgkphklRLYSIASSAlgdfGDSKTVSLCVkRLVytndkgeeVKGVCSNFLCD-LKPGADV 127
Cdd:cd06211  33 EIEFQAGQYVNLQAPGYEGT------RAFSIASSP----SDAGEIELHI-RLV--------PGGIATTYVHKqLKEGDEL 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 128 KITGPVGkEMLMPKDPNATVIMLGTGTGIAPFRSFLWKMfFEKHDDYKfnglAWLFLGVPTSSSLLYKEEFEKMKEKAPe 207
Cdd:cd06211  94 EISGPYG-DFFVRDSDQRPIIFIAGGSGLSSPRSMILDL-LERGDTRK----ITLFFGARTRAELYYLDEFEALEKDHP- 166

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47169163 208 NFRLDFAVSR--EQTNEKGEKMYIQTRMAQYAEElwtllKKDNTFVYMCGLKGMeqgIDDIMSSL 270
Cdd:cd06211 167 NFKYVPALSRepPESNWKGFTGFVHDAAKKHFKN-----DFRGHKAYLCGPPPM---IDACIKTL 223
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 51-284 5.99e-13

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: 67.74  E-value: 5.99e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  51 PYREGQSIGVIADGVDAngkPhklRLYSIASSALGDFgdsktVSLCVKRlvytndkgeEVKGVCSNFLCDLKPGADVKIT 130
Cdd:cd06201  83 SFEAGDLLGILPPGSDV---P---RFYSLASSSSDGF-----LEICVRK---------HPGGLCSGYLHGLKPGDTIKAF 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 131 GPVGKEMLMPKDpNATVIMLGTGTGIAPFRSFLwkmffeKHDDYKFNglAWLFLGVPT-SSSLLYKEEFEKMKEKAP-EN 208
Cdd:cd06201 143 IRPNPSFRPAKG-AAPVILIGAGTGIAPLAGFI------RANAARRP--MHLYWGGRDpASDFLYEDELDQYLADGRlTQ 213

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47169163 209 FRLDFavSREQtnekgEKMYIQTRMAQYAEELWTLLkKDNTFVYMCGLKGMEQGIDDIMSSLAAKEGIDWADYKKQ 284
Cdd:cd06201 214 LHTAF--SRTP-----DGAYVQDRLRADAERLRRLI-EDGAQIMVCGSRAMAQGVAAVLEEILAPQPLSLDELKLQ 281
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 111-262 7.20e-12

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: 63.74  E-value: 7.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 111 KGVCSNFLCDLKPGADVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPFRSFLWKMFFEKHDDYKFnglaWLFLGVPTSS 190
Cdd:cd06183  71 GGKMSQYLHSLKPGDTVEIRGPFGKFEYKPNGKVKHIGMIAGGTGITPMLQLIRAILKDPEDKTKI----SLLYANRTEE 146

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47169163 191 SLLYKEEFEKMKEKAPENFRLDFAVSREQTNEKGEKMYIQtrmAQYAEELWTLLKKDNTFVYMCGLKGMEQG 262
Cdd:cd06183 147 DILLREELDELAKKHPDRFKVHYVLSRPPEGWKGGVGFIT---KEMIKEHLPPPPSEDTLVLVCGPPPMIEG 215
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
 75-255 7.38e-12

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: 64.25  E-value: 7.38e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  75 RLYSIASSAlgdfGDSKTVSLCVKRLVYTNDKGEEVKGVCSNFLCDLKPGADVKITGPVGkEMLMpKDPNATVIMLGTGT 154
Cdd:cd06188  87 RAYSLANYP----AEEGELKLNVRIATPPPGNSDIPPGIGSSYIFNLKPGDKVTASGPFG-EFFI-KDTDREMVFIGGGA 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 155 GIAPFRSFLWKMFFEKHDDYKfnglAWLFLGVPTSSSLLYKEEFEKMKEKAPeNFRLDFAVSR--EQTNEKGEKMYIQTR 232
Cdd:cd06188 161 GMAPLRSHIFHLLKTLKSKRK----ISFWYGARSLKELFYQEEFEALEKEFP-NFKYHPVLSEpqPEDNWDGYTGFIHQV 235

                       170       180
                ....*....|....*....|....*...
gi 47169163 233 MAQYaeelwtLLKK-----DNTFvYMCG 255
Cdd:cd06188 236 LLEN------YLKKhpapeDIEF-YLCG 256
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 75-270 1.09e-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: 64.50  E-value: 1.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  75 RLYSIASSalgdFGDSKTVSLCVKRLVytndKGEEV-KGVCSNFLCDLKPGADVKITGPVGKEMLmpKDPNATVIMLGTG 153
Cdd:COG2871 201 RAYSMANY----PAEKGIIELNIRIAT----PPMDVpPGIGSSYIFSLKPGDKVTISGPYGEFFL--RDSDREMVFIGGG 270

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 154 TGIAPFRSFLWKMFFEKHDDYKfnglAWLFLGVPTSSSLLYKEEFEKMKEKAPeNFRLDFAVSREQ--TNEKGEKMYIQt 231
Cdd:COG2871 271 AGMAPLRSHIFDLLERGKTDRK----ITFWYGARSLRELFYLEEFRELEKEHP-NFKFHPALSEPLpeDNWDGETGFIH- 344

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 47169163 232 rmaQYAEElwTLLKKDNTF----VYMCGLKGMeqgIDDIMSSL 270
Cdd:COG2871 345 ---EVLYE--NYLKDHPAPedceAYLCGPPPM---IDAVIKML 379
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 52-272 1.72e-09

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: 56.77  E-value: 1.72e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  52 YREGQSIGViadGVDANGKPHKlRLYSIASSALGDfgdskTVSLCVKRLvytndKGEEVkgvcSNFLCD-LKPGADVKIT 130
Cdd:cd06191  28 FRPGQHVTL---KLDFDGEELR-RCYSLCSSPAPD-----EISITVKRV-----PGGRV----SNYLREhIQPGMTVEVM 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 131 GPVGKEMLMPKDPnATVIMLGTGTGIAPfrsfLWKMFFEKHD---DYKFNglawLFLGVPTSSSLLYkEEFEKMKEKAPE 207
Cdd:cd06191  90 GPQGHFVYQPQPP-GRYLLVAAGSGITP----LMAMIRATLQtapESDFT----LIHSARTPADMIF-AQELRELADKPQ 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47169163 208 NFRLDFAVSRE--QTNEKGEKMYiqtRMAQYAEELWTLLKKDNTFVymCGLKGMeqgIDDIMSSLAA 272
Cdd:cd06191 160 RLRLLCIFTREtlDSDLLHGRID---GEQSLGAALIPDRLEREAFI--CGPAGM---MDAVETALKE 218
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 52-163 3.37e-09

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap 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: 56.08  E-value: 3.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  52 YREGQSIGViadGVDANGKPHKlRLYSIASSALGDFGdskTVSLCVKRLVytndkgeevKGVCSNFLCD-LKPGADVKIT 130
Cdd:cd06216  46 HRAGQHVRL---GVEIDGVRHW-RSYSLSSSPTQEDG---TITLTVKAQP---------DGLVSNWLVNhLAPGDVVELS 109

                        90       100       110
                ....*....|....*....|....*....|...
gi 47169163 131 GPVGkEMLMPKDPNATVIMLGTGTGIAPFRSFL 163
Cdd:cd06216 110 QPQG-DFVLPDPLPPRLLLIAAGSGITPVMSML 141
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 50-158 4.23e-08

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal 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: 52.98  E-value: 4.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  50 IPYREGQSIGViadGVDANGKPHkLRLYSIASSAlgdfGDSKTVSLCVKRLvytndKGeevkGVCSNFLCD-LKPGADVK 128
Cdd:cd06215  26 FAYKPGQFLTL---ELEIDGETV-YRAYTLSSSP----SRPDSLSITVKRV-----PG----GLVSNWLHDnLKVGDELW 88

                        90       100       110
                ....*....|....*....|....*....|
gi 47169163 129 ITGPVGkEMLMPKDPNATVIMLGTGTGIAP 158
Cdd:cd06215  89 ASGPAG-EFTLIDHPADKLLLLSAGSGITP 117
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 46-259 6.54e-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: 52.27  E-value: 6.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  46 TEGEIPYREGQSIGVI-ADGVdangkphkLRLYSIASsalgDFGDSKTVSLCVKRlvYTNdkgeevkGVCSNFLCDL-KP 123
Cdd:cd06194  18 PDRPLPYLPGQYVNLRrAGGL--------ARSYSPTS----LPDGDNELEFHIRR--KPN-------GAFSGWLGEEaRP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 124 GADVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPfrsfLWKM----FFEKHddykfNGLAWLFLGVPTSSSlLYKEEFE 199
Cdd:cd06194  77 GHALRLQGPFGQAFYRPEYGEGPLLLVGAGTGLAP----LWGIaraaLRQGH-----QGEIRLVHGARDPDD-LYLHPAL 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 200 KMKEKAPENFRLDFAVSREQTNEKGekmyiqTRMAQYAEELWTLLKkdNTFVYMCGLKGM 259
Cdd:cd06194 147 LWLAREHPNFRYIPCVSEGSQGDPR------VRAGRIAAHLPPLTR--DDVVYLCGAPSM 198
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 27-270 9.84e-08

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 51.79  E-value: 9.84e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  27 NTKITGDdapgeTWHMVFSTEGE-IPYREGQSIGVIADGvdaNGKPhklRLYSIASSAlgdfGDSKTVSLCVKrlvytnd 105
Cdd:COG0543   5 VERLAPD-----VYLLRLEAPLIaLKFKPGQFVMLRVPG---DGLR---RPFSIASAP----REDGTIELHIR------- 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 106 kgeeVKGVCSNFLCDLKPGADVKITGPVGKeMLMPKDPNATVIMLGTGTGIAPFRSFLWKMFFEKHDdykfnglAWLFLG 185
Cdd:COG0543  63 ----VVGKGTRALAELKPGDELDVRGPLGN-GFPLEDSGRPVLLVAGGTGLAPLRSLAEALLARGRR-------VTLYLG 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 186 VPTSSSLLYKeefekmkekapENFR----LDFAVSREQtNEKGEKMYIQTRMAQYAEElwtllkKDNTFVYMCGLKGM-- 259
Cdd:COG0543 131 ARTPEDLYLL-----------DELEaladFRVVVTTDD-GWYGRKGFVTDALKELLAE------DSGDDVYACGPPPMmk 192

                       250       260
                ....*....|....*....|
gi 47169163 260 -------EQGI--DDIMSSL 270
Cdd:COG0543 193 avaelllERGVppERIYVSL 212
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 39-270 1.55e-07

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: 51.11  E-value: 1.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  39 TWHMVFSTEGEIPYREGQSIGVIADGVDANgkpHKLRLYSIASSALGDFGdsktVSLCVKRlvytndkgeEVKGVCSNFL 118
Cdd:cd06217  18 TFRLAVPDGVPPPFLAGQHVDLRLTAIDGY---TAQRSYSIASSPTQRGR----VELTVKR---------VPGGEVSPYL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 119 CD-LKPGADVKITGPVGKEMLMPKDPNaTVIMLGTGTGIAPFRSflwkMFFEKHDdykfngLAW-----LFLGVPTSSSL 192
Cdd:cd06217  82 HDeVKVGDLLEVRGPIGTFTWNPLHGD-PVVLLAGGSGIVPLMS----MIRYRRD------LGWpvpfrLLYSARTAEDV 150

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47169163 193 LYKEEFEKMKEKAPeNFRLDFAVSREQTNE-KGEKMYIQTRMAQyaeELWTLLkkDNTFVYMCGLKGMEQGIDDIMSSL 270
Cdd:cd06217 151 IFRDELEQLARRHP-NLHVTEALTRAAPADwLGPAGRITADLIA---ELVPPL--AGRRVYVCGPPAFVEAATRLLLEL 223
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 78-255 2.49e-07

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: 50.68  E-value: 2.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  78 SIASSAlgdfGDSKTVSLCVKRLvytndkgeevkGVCSNFLCDLKPGADVKITGPVGKEMLMPKDPNATVIMLGTGTGIA 157
Cdd:cd06221  47 SISSDP----TRRGPLELTIRRV-----------GRVTEALHELKPGDTVGLRGPFGNGFPVEEMKGKDLLLVAGGLGLA 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 158 PFRSFLWKmFFEKHDDYkfnGLAWLFLGVPTSSSLLYKEEFEKMKEKapENFRLDFAVSREQTNEKGEKMYIQTRMAQya 237
Cdd:cd06221 112 PLRSLINY-ILDNREDY---GKVTLLYGARTPEDLLFKEELKEWAKR--SDVEVILTVDRAEEGWTGNVGLVTDLLPE-- 183

                       170
                ....*....|....*...
gi 47169163 238 eelwTLLKKDNTFVYMCG 255
Cdd:cd06221 184 ----LTLDPDNTVAIVCG 197
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 36-163 4.48e-07

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: 49.56  E-value: 4.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  36 PGETWHMVFSTEG-EIPYREGQSIGVIADGVDANGkPHKlrlYSIASSAlgdfGDSKTVSLCVKRL-VYTNDKGEevkgv 113
Cdd:cd06198   6 VRPTTTLTLEPRGpALGHRAGQFAFLRFDASGWEE-PHP---FTISSAP----DPDGRLRFTIKALgDYTRRLAE----- 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 47169163 114 csnflcDLKPGADVKITGPVGKemLMPKDPNATVIMLGTGTGIAPFRSFL 163
Cdd:cd06198  73 ------RLKPGTRVTVEGPYGR--FTFDDRRARQIWIAGGIGITPFLALL 114
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 44-270 5.80e-07

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: 49.56  E-value: 5.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  44 FSTEGEIPYREGQSIGVIADGVDANgkphklRLYSIASSAlgdfGDSKTVSLCVKRlvYTNDKGeevkgvcSNFLCD-LK 122
Cdd:cd06190  16 FALDGPADFLPGQYALLALPGVEGA------RAYSMANLA----NASGEWEFIIKR--KPGGAA-------SNALFDnLE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 123 PGADVKITGPVGKEMLMPKDPNaTVIMLGTGTGIAPFRSFL-----WKMFFEKHDDykfnglawLFLGVPTSSSlLYKEE 197
Cdd:cd06190  77 PGDELELDGPYGLAYLRPDEDR-DIVCIAGGSGLAPMLSILrgaarSPYLSDRPVD--------LFYGGRTPSD-LCALD 146

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47169163 198 FEKMKEKAPENFRLDFAVSREQTNEK----GEKMYIQTRMAQYAEELWtllkkDNTFVYMCGLKGMeqgIDDIMSSL 270
Cdd:cd06190 147 ELSALVALGARLRVTPAVSDAGSGSAagwdGPTGFVHEVVEATLGDRL-----AEFEFYFAGPPPM---VDAVQRML 215
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 37-255 1.89e-06

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: 47.93  E-value: 1.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  37 GETWHMVFSTEGEIPYREGQSIGVIADGVDAngkphklRLYSIASSAlgdfGDSKTVSLCVKRlvytndkgeEVKGVCSN 116
Cdd:cd06189  11 DDVYRVRLKPPAPLDFLAGQYLDLLLDDGDK-------RPFSIASAP----HEDGEIELHIRA---------VPGGSFSD 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 117 FLCD-LKPGADVKITGPVGKEMLMPkDPNATVIMLGTGTGIAPFRSFLwkmffEKHDDYKFNGLAWLFLGVPTSSSlLYK 195
Cdd:cd06189  71 YVFEeLKENGLVRIEGPLGDFFLRE-DSDRPLILIAGGTGFAPIKSIL-----EHLLAQGSKRPIHLYWGARTEED-LYL 143

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 196 EEFEKMKEKAPENFRLDFAVSREQTNEKGEKMYIQTRMAQYAEELwtllkkDNTFVYMCG 255
Cdd:cd06189 144 DELLEAWAEAHPNFTYVPVLSEPEEGWQGRTGLVHEAVLEDFPDL------SDFDVYACG 197
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
77-272 4.85e-06

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 47.58  E-value: 4.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  77 YSIASSALGDfgdsKTVSLCVKRLvytndkgeevkGVCSNFLCDLKPGADVKITGPVGKEMLMPKDPNATVIMLGTGTGI 156
Cdd:COG4097 266 FSISSAPGGD----GRLRFTIKAL-----------GDFTRRLGRLKPGTRVYVEGPYGRFTFDRRDTAPRQVWIAGGIGI 330

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 157 APFRSFLWKMFFEKHDDYKfnglAWLFLGVPTSSSLLYKEEFEKMKEKAPeNFRLDFAVSREQTnekgekmYI-QTRMAQ 235
Cdd:COG4097 331 TPFLALLRALAARPGDQRP----VDLFYCVRDEEDAPFLEELRALAARLA-GLRLHLVVSDEDG-------RLtAERLRR 398

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 47169163 236 YAEELwtllkkDNTFVYMCGLKGMeqgIDDIMSSLAA 272
Cdd:COG4097 399 LVPDL------AEADVFFCGPPGM---MDALRRDLRA 426
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 112-255 3.51e-05

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: 44.12  E-value: 3.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 112 GVCSNFLCDL-KPGADVKITGPVGKEMLmpKDPNATVIMLGTGTGIAPFRSFLWKMffekhddyKFNGLAW---LFLGVP 187
Cdd:cd06209  71 GAMSSYLRDRaQPGDRLTLTGPLGSFYL--REVKRPLLMLAGGTGLAPFLSMLDVL--------AEDGSAHpvhLVYGVT 140

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47169163 188 TSSSLLYKEEFEKMKEKAPeNFRLDFAVSREQTNEkGEKMYIqtrmAQYAEELWtlLKKDNTFVYMCG 255
Cdd:cd06209 141 RDADLVELDRLEALAERLP-GFSFRTVVADPDSWH-PRKGYV----TDHLEAED--LNDGDVDVYLCG 200
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 47-161 3.81e-05

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: 44.12  E-value: 3.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  47 EGEIPYREGQSIGVIADGvdangKPHKLRLYSIASSAlgdfGDSKTVSLCVKRLvytndkgEEvkGVCSNFLCD-LKPGA 125
Cdd:cd06187  19 DQPLPFWAGQYVNVTVPG-----RPRTWRAYSPANPP----NEDGEIEFHVRAV-------PG--GRVSNALHDeLKVGD 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 47169163 126 DVKITGPVGkEMLMPKDPNATVIMLGTGTGIAPFRS 161
Cdd:cd06187  81 RVRLSGPYG-TFYLRRDHDRPVLCIAGGTGLAPLRA 115
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 52-277 5.34e-05

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: 43.69  E-value: 5.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  52 YREGQSIGVIadgVDANGKPHkLRLYSIASSAlgdfgDSKTVSLCVKRlvytndkgeEVKGVCSNFLCD-LKPGADVKIT 130
Cdd:cd06214  33 YRPGQFLTLR---VPIDGEEV-RRSYSICSSP-----GDDELRITVKR---------VPGGRFSNWANDeLKAGDTLEVM 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 131 GPVGKEMLMPKDPNATVIMLGTGTGIAPFRSFLwKMFFEKHDDYKFNglawLFLGVPTSSSLLYKEEFEKMKEKAPENFR 210
Cdd:cd06214  95 PPAGRFTLPPLPGARHYVLFAAGSGITPVLSIL-KTALAREPASRVT----LVYGNRTEASVIFREELADLKARYPDRLT 169

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 211 LDFAVSREQtnekGEKMYIQTRMAQ-YAEELWTLLKKDNTF--VYMCGLKGMeqgIDDIMSSLAAKeGID 277
Cdd:cd06214 170 VIHVLSREQ----GDPDLLRGRLDAaKLNALLKNLLDATEFdeAFLCGPEPM---MDAVEAALLEL-GVP 231
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 95-255 9.49e-05

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 43.26  E-value: 9.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163   95 LCVKRLvytndkgeevkGVCSNFLCDLKPGADVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPFRSFLWkmfFEKHDDY 174
Cdd:PRK08345  70 LCIRRA-----------GRVTTVIHRLKEGDIVGVRGPYGNGFPVDEMEGMDLLLIAGGLGMAPLRSVLL---YAMDNRW 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  175 KFnGLAWLFLGVPTSSSLLYKEEFEKMKEKApENFRLDFAVSREQtnekgEKMYIQTRMAQYAEELWTLLKKD------- 247
Cdd:PRK08345 136 KY-GNITLIYGAKYYEDLLFYDELIKDLAEA-ENVKIIQSVTRDP-----EWPGCHGLPQGFIERVCKGVVTDlfreant 208

                        170
                 ....*....|.
gi 47169163  248 ---NTFVYMCG 255
Cdd:PRK08345 209 dpkNTYAAICG 219
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 112-259 1.14e-04

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: 42.71  E-value: 1.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 112 GVCSNFL-CDLKPGADVKITGPVGKEMLMPKDPnATVIMLGTGTGIAPFRSFLWKMffekhDDYKFNGLAWLFLGVPTSS 190
Cdd:cd06210  76 GAFSTYLeTRAKVGQRLNLRGPLGAFGLRENGL-RPRWFVAGGTGLAPLLSMLRRM-----AEWGEPQEARLFFGVNTEA 149

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47169163 191 SLLYKEEFEKMKEKAPeNFRLDFAVSREQTNEKGEKmyiQTRMAQYAEELWTLLKKDNtfVYMCGLKGM 259
Cdd:cd06210 150 ELFYLDELKRLADSLP-NLTVRICVWRPGGEWEGYR---GTVVDALREDLASSDAKPD--IYLCGPPGM 212
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 118-259 1.45e-04

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: 42.53  E-value: 1.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 118 LCDLKPGADVKITGPVGKEmLMPKDPNATVIMLGTGTGIAPFRsFLWKMFFEKHDDykfnglAWLFLGVPTSSSLLYKee 197
Cdd:cd06218  73 LSELKAGDELDVLGPLGNG-FDLPDDDGKVLLVGGGIGIAPLL-FLAKQLAERGIK------VTVLLGFRSADDLFLV-- 142

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47169163 198 fekmkekapENFRLDFAVSREQTN--EKGEKMYIQTRMAQYAEELwtllkkDNTFVYMCGLKGM 259
Cdd:cd06218 143 ---------EEFEALGAEVYVATDdgSAGTKGFVTDLLKELLAEA------RPDVVYACGPEPM 191
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 71-158 1.40e-03

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: 39.23  E-value: 1.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  71 PHKLRLYSIASSALGDFGDSKTVSLCVkrlvytndkgeEVKGVCSNFLCDLKPGADVKITGPVGKEMLMPKDpNATVIML 150
Cdd:cd06192  36 FESPGLERIPLSLAGVDPEEGTISLLV-----------EIRGPKTKLIAELKPGEKLDVMGPLGNGFEGPKK-GGTVLLV 103


                ....*...
gi 47169163 151 GTGTGIAP 158
Cdd:cd06192 104 AGGIGLAP 111
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 49-270 1.59e-03

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: 39.24  E-value: 1.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163  49 EIPYREGQSIGVIADGVDangkphKLRLYSIASSAlgdfGDSKTVSLCVKrlVYTNdkgeevkGVCSNFLCD-LKPGADV 127
Cdd:cd06212  27 PIKFFAGQYVDITVPGTE------ETRSFSMANTP----ADPGRLEFIIK--KYPG-------GLFSSFLDDgLAVGDPV 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47169163 128 KITGPVGKEMLMPKDPNAtVIMLGTGTGIAPFRSFLwkmffEKHDDYKFNGLAWLFLGVPTSSSLLYkEEFEKMKEKAPE 207
Cdd:cd06212  88 TVTGPYGTCTLRESRDRP-IVLIGGGSGMAPLLSLL-----RDMAASGSDRPVRFFYGARTARDLFY-LEEIAALGEKIP 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47169163 208 NFRLDFAVSREQTNE--KGEKMYIQTRMAQYAEELwtllkkDNTFVYMCGLKGMeqgIDDIMSSL 270
Cdd:cd06212 161 DFTFIPALSESPDDEgwSGETGLVTEVVQRNEATL------AGCDVYLCGPPPM---IDAALPVL 216
 
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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