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Conserved domains on  [gi|1073931601|gb|AOU74539|]
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Histag-putative ferredoxin:NAD+ oxidoreductase [Cloning vector pTOPO-0705]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
sulfite_red_B super family cl31266
sulfite reductase, subunit B; Members of this protein family include the B subunit, one of ...
13-273 1.14e-132

sulfite reductase, subunit B; Members of this protein family include the B subunit, one of three subunits, of the anaerobic sulfite reductase of Salmonella, and close homologs from various Clostridum species, where the three-gene neighborhood is preserved. Two such gene clusters are found in Clostridium perfringens, but it may be that these sets of genes correspond to the distinct assimilatory and dissimilatory forms as seen in Clostridium pasteurianum. [Central intermediary metabolism, Sulfur metabolism]


The actual alignment was detected with superfamily member TIGR02911:

Pssm-ID: 131957 [Multi-domain]  Cd Length: 261  Bit Score: 375.67  E-value: 1.14e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  13 NVYMPKKVEILSIIPQTDIDYTFRLKSDILPRHGQFLQVSIPKIGEAPISISDYTDEYIELTIRKVGTVTDAIHELKPGD 92
Cdd:TIGR02911   1 NSYLPFKSEILEIIKHTDIEYTFRMSYDGPVKPGQFFEVSLPKYGEAPISVSGIGEGYIDLTIRRVGKVTDEVFTLKEGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  93 FLFIRGPYGHGFPVEDFKDKNVVIAAGGTGLAPVKSIINRYYRNPKEIKNLNILMGFKSPKDILFEDEIKKWKEKFDVLL 172
Cdd:TIGR02911  81 NLFLRGPYGNGFDVDNYKHKELVVVAGGTGVAPVKGVVEYFVKNPKEIKSLNLILGFKTPDDILFKEDIAEWKGNINLTL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 173 TVDNGDETWTGNTGLITKFIPELKIENPNDTIVIVVGPPMMMKFTCLEFLKRNIPDENIWVSFERKMSCGIGKCGHCKIN 252
Cdd:TIGR02911 161 TLDEAEEDYKGNIGLVTKYIPELTLKDIEEVQAIVVGPPIMMKFTVQELLKKGIKEENIWVSYERKMCCGVGKCGHCKID 240
                         250       260
                  ....*....|....*....|.
gi 1073931601 253 ETYVCLEGPVFNYTKSKQLLD 273
Cdd:TIGR02911 241 DVYVCLDGPVFNYTKAKRLID 261
 
Name Accession Description Interval E-value
sulfite_red_B TIGR02911
sulfite reductase, subunit B; Members of this protein family include the B subunit, one of ...
13-273 1.14e-132

sulfite reductase, subunit B; Members of this protein family include the B subunit, one of three subunits, of the anaerobic sulfite reductase of Salmonella, and close homologs from various Clostridum species, where the three-gene neighborhood is preserved. Two such gene clusters are found in Clostridium perfringens, but it may be that these sets of genes correspond to the distinct assimilatory and dissimilatory forms as seen in Clostridium pasteurianum. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 131957 [Multi-domain]  Cd Length: 261  Bit Score: 375.67  E-value: 1.14e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  13 NVYMPKKVEILSIIPQTDIDYTFRLKSDILPRHGQFLQVSIPKIGEAPISISDYTDEYIELTIRKVGTVTDAIHELKPGD 92
Cdd:TIGR02911   1 NSYLPFKSEILEIIKHTDIEYTFRMSYDGPVKPGQFFEVSLPKYGEAPISVSGIGEGYIDLTIRRVGKVTDEVFTLKEGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  93 FLFIRGPYGHGFPVEDFKDKNVVIAAGGTGLAPVKSIINRYYRNPKEIKNLNILMGFKSPKDILFEDEIKKWKEKFDVLL 172
Cdd:TIGR02911  81 NLFLRGPYGNGFDVDNYKHKELVVVAGGTGVAPVKGVVEYFVKNPKEIKSLNLILGFKTPDDILFKEDIAEWKGNINLTL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 173 TVDNGDETWTGNTGLITKFIPELKIENPNDTIVIVVGPPMMMKFTCLEFLKRNIPDENIWVSFERKMSCGIGKCGHCKIN 252
Cdd:TIGR02911 161 TLDEAEEDYKGNIGLVTKYIPELTLKDIEEVQAIVVGPPIMMKFTVQELLKKGIKEENIWVSYERKMCCGVGKCGHCKID 240
                         250       260
                  ....*....|....*....|.
gi 1073931601 253 ETYVCLEGPVFNYTKSKQLLD 273
Cdd:TIGR02911 241 DVYVCLDGPVFNYTKAKRLID 261
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
22-265 1.26e-126

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: 360.00  E-value: 1.26e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  22 ILSIIPQTDIDYTFRLKSDIL------PRHGQFLQVSIPKIGEAPISISDYT--DEYIELTIRKVGTVTDAIHELKPGDF 93
Cdd:cd06221     1 IVEVVDETEDIKTFTLRLEDDdeelftFKPGQFVMLSLPGVGEAPISISSDPtrRGPLELTIRRVGRVTEALHELKPGDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  94 LFIRGPYGHGFPVEDFKDKNVVIAAGGTGLAPVKSIINRYYRNPKEIKNLNILMGFKSPKDILFEDEIKKWKEKFD--VL 171
Cdd:cd06221    81 VGLRGPFGNGFPVEEMKGKDLLLVAGGLGLAPLRSLINYILDNREDYGKVTLLYGARTPEDLLFKEELKEWAKRSDveVI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 172 LTVDNGDETWTGNTGLITKFIPELKIeNPNDTIVIVVGPPMMMKFTCLEFLKRNIPDENIWVSFERKMSCGIGKCGHCKI 251
Cdd:cd06221   161 LTVDRAEEGWTGNVGLVTDLLPELTL-DPDNTVAIVCGPPIMMRFVAKELLKLGVPEEQIWVSLERRMKCGVGKCGHCQI 239
                         250
                  ....*....|....
gi 1073931601 252 NETYVCLEGPVFNY 265
Cdd:cd06221   240 GPKYVCKDGPVFSY 253
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
21-267 5.70e-87

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 259.41  E-value: 5.70e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  21 EILSIIPQTDIDYTFRLKSDILPRH---GQFLQVSIP-KIGEAPISISDY--TDEYIELTIRKVGTVTDAIHELKPGDFL 94
Cdd:COG0543     1 KVVSVERLAPDVYLLRLEAPLIALKfkpGQFVMLRVPgDGLRRPFSIASAprEDGTIELHIRVVGKGTRALAELKPGDEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  95 FIRGPYGHGFPVEDFkDKNVVIAAGGTGLAPVKSIINRYYRNPKEIKnlnILMGFKSPKDILFEDEIKKWKEkFDVLLTV 174
Cdd:COG0543    81 DVRGPLGNGFPLEDS-GRPVLLVAGGTGLAPLRSLAEALLARGRRVT---LYLGARTPEDLYLLDELEALAD-FRVVVTT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 175 DNGdetWTGNTGLITKFIPELkIENPNDTIVIVVGPPMMMKFTCLEFLKRNIPDENIWVSFERKMSCGIGKCGHCKINET 254
Cdd:COG0543   156 DDG---WYGRKGFVTDALKEL-LAEDSGDDVYACGPPPMMKAVAELLLERGVPPERIYVSLERRMACGIGMCGGCVVPVG 231
                         250
                  ....*....|...
gi 1073931601 255 YVCLEGPVFNYTK 267
Cdd:COG0543   232 GGCKDGPVFDAAE 244
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
13-265 4.19e-70

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 217.75  E-value: 4.19e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  13 NVYMPKKVEILSIIPQTDID--YTFRLKSDILPRH-----GQFLQVSIPKIGEAPISI--SDYTDEYIELTIRKVGTVTD 83
Cdd:PRK08345    1 NPYALHDAKILEVYDLTEREklFLLRFEDPELAESftfkpGQFVQVTIPGVGEVPISIcsSPTRKGFFELCIRRAGRVTT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  84 AIHELKPGDFLFIRGPYGHGFPVEDFKDKNVVIAAGGTGLAPVKSIINRYYRNPKEIKNLNILMGFKSPKDILFEDEIK- 162
Cdd:PRK08345   81 VIHRLKEGDIVGVRGPYGNGFPVDEMEGMDLLLIAGGLGMAPLRSVLLYAMDNRWKYGNITLIYGAKYYEDLLFYDELIk 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 163 --KWKEKFDVLLTVDNGDEtWTGNTGLITKFIPELKIE-----------NPNDTIVIVVGPPMMMKFTCLEFLKRNIPDE 229
Cdd:PRK08345  161 dlAEAENVKIIQSVTRDPE-WPGCHGLPQGFIERVCKGvvtdlfreantDPKNTYAAICGPPVMYKFVFKELINRGYRPE 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1073931601 230 NIWVSFERKMSCGIGKCGHCKINET----YVCLEGPVFNY 265
Cdd:PRK08345  240 RIYVTLERRMRCGIGKCGHCIVGTStsikYVCKDGPVFTY 279
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
118-218 4.64e-18

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: 77.30  E-value: 4.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 118 AGGTGLAPVKSIINRYYRNPKEIKNLNILMGFKSPKDILFEDEIKKWKEK----FDVLLTVDNGDETWTGNTGLITKFIP 193
Cdd:pfam00175   3 AGGTGIAPVRSMLRAILEDPKDPTQVVLVFGNRNEDDILYREELDELAEKhpgrLTVVYVVSRPEAGWTGGKGRVQDALL 82
                          90       100
                  ....*....|....*....|....*.
gi 1073931601 194 ELKIENPND-TIVIVVGPPMMMKFTC 218
Cdd:pfam00175  83 EDHLSLPDEeTHVYVCGPPGMIKAVR 108
 
Name Accession Description Interval E-value
sulfite_red_B TIGR02911
sulfite reductase, subunit B; Members of this protein family include the B subunit, one of ...
13-273 1.14e-132

sulfite reductase, subunit B; Members of this protein family include the B subunit, one of three subunits, of the anaerobic sulfite reductase of Salmonella, and close homologs from various Clostridum species, where the three-gene neighborhood is preserved. Two such gene clusters are found in Clostridium perfringens, but it may be that these sets of genes correspond to the distinct assimilatory and dissimilatory forms as seen in Clostridium pasteurianum. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 131957 [Multi-domain]  Cd Length: 261  Bit Score: 375.67  E-value: 1.14e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  13 NVYMPKKVEILSIIPQTDIDYTFRLKSDILPRHGQFLQVSIPKIGEAPISISDYTDEYIELTIRKVGTVTDAIHELKPGD 92
Cdd:TIGR02911   1 NSYLPFKSEILEIIKHTDIEYTFRMSYDGPVKPGQFFEVSLPKYGEAPISVSGIGEGYIDLTIRRVGKVTDEVFTLKEGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  93 FLFIRGPYGHGFPVEDFKDKNVVIAAGGTGLAPVKSIINRYYRNPKEIKNLNILMGFKSPKDILFEDEIKKWKEKFDVLL 172
Cdd:TIGR02911  81 NLFLRGPYGNGFDVDNYKHKELVVVAGGTGVAPVKGVVEYFVKNPKEIKSLNLILGFKTPDDILFKEDIAEWKGNINLTL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 173 TVDNGDETWTGNTGLITKFIPELKIENPNDTIVIVVGPPMMMKFTCLEFLKRNIPDENIWVSFERKMSCGIGKCGHCKIN 252
Cdd:TIGR02911 161 TLDEAEEDYKGNIGLVTKYIPELTLKDIEEVQAIVVGPPIMMKFTVQELLKKGIKEENIWVSYERKMCCGVGKCGHCKID 240
                         250       260
                  ....*....|....*....|.
gi 1073931601 253 ETYVCLEGPVFNYTKSKQLLD 273
Cdd:TIGR02911 241 DVYVCLDGPVFNYTKAKRLID 261
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
22-265 1.26e-126

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: 360.00  E-value: 1.26e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  22 ILSIIPQTDIDYTFRLKSDIL------PRHGQFLQVSIPKIGEAPISISDYT--DEYIELTIRKVGTVTDAIHELKPGDF 93
Cdd:cd06221     1 IVEVVDETEDIKTFTLRLEDDdeelftFKPGQFVMLSLPGVGEAPISISSDPtrRGPLELTIRRVGRVTEALHELKPGDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  94 LFIRGPYGHGFPVEDFKDKNVVIAAGGTGLAPVKSIINRYYRNPKEIKNLNILMGFKSPKDILFEDEIKKWKEKFD--VL 171
Cdd:cd06221    81 VGLRGPFGNGFPVEEMKGKDLLLVAGGLGLAPLRSLINYILDNREDYGKVTLLYGARTPEDLLFKEELKEWAKRSDveVI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 172 LTVDNGDETWTGNTGLITKFIPELKIeNPNDTIVIVVGPPMMMKFTCLEFLKRNIPDENIWVSFERKMSCGIGKCGHCKI 251
Cdd:cd06221   161 LTVDRAEEGWTGNVGLVTDLLPELTL-DPDNTVAIVCGPPIMMRFVAKELLKLGVPEEQIWVSLERRMKCGVGKCGHCQI 239
                         250
                  ....*....|....
gi 1073931601 252 NETYVCLEGPVFNY 265
Cdd:cd06221   240 GPKYVCKDGPVFSY 253
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
21-267 5.70e-87

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 259.41  E-value: 5.70e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  21 EILSIIPQTDIDYTFRLKSDILPRH---GQFLQVSIP-KIGEAPISISDY--TDEYIELTIRKVGTVTDAIHELKPGDFL 94
Cdd:COG0543     1 KVVSVERLAPDVYLLRLEAPLIALKfkpGQFVMLRVPgDGLRRPFSIASAprEDGTIELHIRVVGKGTRALAELKPGDEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  95 FIRGPYGHGFPVEDFkDKNVVIAAGGTGLAPVKSIINRYYRNPKEIKnlnILMGFKSPKDILFEDEIKKWKEkFDVLLTV 174
Cdd:COG0543    81 DVRGPLGNGFPLEDS-GRPVLLVAGGTGLAPLRSLAEALLARGRRVT---LYLGARTPEDLYLLDELEALAD-FRVVVTT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 175 DNGdetWTGNTGLITKFIPELkIENPNDTIVIVVGPPMMMKFTCLEFLKRNIPDENIWVSFERKMSCGIGKCGHCKINET 254
Cdd:COG0543   156 DDG---WYGRKGFVTDALKEL-LAEDSGDDVYACGPPPMMKAVAELLLERGVPPERIYVSLERRMACGIGMCGGCVVPVG 231
                         250
                  ....*....|...
gi 1073931601 255 YVCLEGPVFNYTK 267
Cdd:COG0543   232 GGCKDGPVFDAAE 244
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
13-265 4.19e-70

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 217.75  E-value: 4.19e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  13 NVYMPKKVEILSIIPQTDID--YTFRLKSDILPRH-----GQFLQVSIPKIGEAPISI--SDYTDEYIELTIRKVGTVTD 83
Cdd:PRK08345    1 NPYALHDAKILEVYDLTEREklFLLRFEDPELAESftfkpGQFVQVTIPGVGEVPISIcsSPTRKGFFELCIRRAGRVTT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  84 AIHELKPGDFLFIRGPYGHGFPVEDFKDKNVVIAAGGTGLAPVKSIINRYYRNPKEIKNLNILMGFKSPKDILFEDEIK- 162
Cdd:PRK08345   81 VIHRLKEGDIVGVRGPYGNGFPVDEMEGMDLLLIAGGLGMAPLRSVLLYAMDNRWKYGNITLIYGAKYYEDLLFYDELIk 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 163 --KWKEKFDVLLTVDNGDEtWTGNTGLITKFIPELKIE-----------NPNDTIVIVVGPPMMMKFTCLEFLKRNIPDE 229
Cdd:PRK08345  161 dlAEAENVKIIQSVTRDPE-WPGCHGLPQGFIERVCKGvvtdlfreantDPKNTYAAICGPPVMYKFVFKELINRGYRPE 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1073931601 230 NIWVSFERKMSCGIGKCGHCKINET----YVCLEGPVFNY 265
Cdd:PRK08345  240 RIYVTLERRMRCGIGKCGHCIVGTStsikYVCKDGPVFTY 279
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
20-264 2.27e-51

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


Pssm-ID: 99816 [Multi-domain]  Cd Length: 233  Bit Score: 167.81  E-value: 2.27e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  20 VEILSIIPQTDIDYTFRLKSDILPRHGQFLQVSIPKIGEAPISISdYTDEYIELTIRKVGTVTDAIHELKPGDFLFIRGP 99
Cdd:cd06220     1 VTIKEVIDETPTVKTFVFDWDFDFKPGQFVMVWVPGVDEIPMSLS-YIDGPNSITVKKVGEATSALHDLKEGDKLGIRGP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 100 YGHGFpveDFKDKNVVIAAGGTGLAPVKSIINRYyrnpKEIKNLNILMGFKSPKDILFEDEIKKWKEkfdVLLTVDNGDE 179
Cdd:cd06220    80 YGNGF---ELVGGKVLLIGGGIGIAPLAPLAERL----KKAADVTVLLGARTKEELLFLDRLRKSDE---LIVTTDDGSY 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 180 twtGNTGLITKFIPELKIENPnDTIViVVGPPMMMKFTcLEFLK-RNIPDEniwVSFERKMSCGIGKCGHCKINET--YV 256
Cdd:cd06220   150 ---GFKGFVTDLLKELDLEEY-DAIY-VCGPEIMMYKV-LEILDeRGVRAQ---FSLERYMKCGIGICGSCCIDPTglRV 220

                  ....*...
gi 1073931601 257 CLEGPVFN 264
Cdd:cd06220   221 CRDGPVFD 228
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
15-264 9.76e-51

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 166.97  E-value: 9.76e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  15 YMPKKVEILSIIPQTDIDYTFRLKSD--ILPRHGQFLQVSIP---KIGEAPISISDYTDEYIELTIRKVGTVTDAIHELK 89
Cdd:PRK00054    2 MKPENMKIVENKEIAPNIYTLVLDGEkvFDMKPGQFVMVWVPgvePLLERPISISDIDKNEITILYRKVGEGTKKLSKLK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  90 PGDFLFIRGPYGHGFPVEDFKDKnVVIAAGGTGLAPVKSIINRYYRNPKEIKnlnILMGFKSPKDILFEDEIKKWKEkfd 169
Cdd:PRK00054   82 EGDELDIRGPLGNGFDLEEIGGK-VLLVGGGIGVAPLYELAKELKKKGVEVT---TVLGARTKDEVIFEEEFAKVGD--- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 170 VLLTVDNGDEtwtGNTGLITKFIPELKIENpndTIVIVVGPPMMMKfTCLEFLK-RNIPdenIWVSFERKMSCGIGKCGH 248
Cdd:PRK00054  155 VYVTTDDGSY---GFKGFVTDVLDELDSEY---DAIYSCGPEIMMK-KVVEILKeKKVP---AYVSLERRMKCGIGACGA 224
                         250       260
                  ....*....|....*....|
gi 1073931601 249 C--KINETY--VCLEGPVFN 264
Cdd:PRK00054  225 CvcDTETGGkrVCKDGPVFS 244
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
22-264 3.89e-41

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: 141.91  E-value: 3.89e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  22 ILSIIPQTDIDYTFRLKSDILPRH---GQFLQVSIPKIGEA----PISISDY--TDEYIELTIRKVGTVTDAIHELKPGD 92
Cdd:cd06218     1 VLSNREIADDIYRLVLEAPEIAAAakpGQFVMLRVPDGSDPllrrPISIHDVdpEEGTITLLYKVVGKGTRLLSELKAGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  93 FLFIRGPYGHGFPVEDfKDKNVVIAAGGTGLAPVKSIINRYYRNPKEIknlNILMGFKSPKDILFEDEIKKWKEkfDVLL 172
Cdd:cd06218    81 ELDVLGPLGNGFDLPD-DDGKVLLVGGGIGIAPLLFLAKQLAERGIKV---TVLLGFRSADDLFLVEEFEALGA--EVYV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 173 TVDNGDetwTGNTGLITKFIPELKIENPNDTiVIVVGPPMMMKFTCLEFLKRNIPdenIWVSFERKMSCGIGKCGHC--- 249
Cdd:cd06218   155 ATDDGS---AGTKGFVTDLLKELLAEARPDV-VYACGPEPMLKAVAELAAERGVP---CQVSLEERMACGIGACLGCvvk 227
                         250
                  ....*....|....*....
gi 1073931601 250 -KINETY---VCLEGPVFN 264
Cdd:cd06218   228 tKDDEGGykrVCKDGPVFD 246
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
42-264 8.76e-41

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: 140.92  E-value: 8.76e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  42 LPRHGQF--LQVSI-PKIGEAPISISDYTDE--YIELTIRKVGTVTDAIHELKPGDFLFIRGPYGHGFPVEDfKDKNVVI 116
Cdd:cd06192    24 LFRPGQFvfLRNFEsPGLERIPLSLAGVDPEegTISLLVEIRGPKTKLIAELKPGEKLDVMGPLGNGFEGPK-KGGTVLL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 117 AAGGTGLAPVKSIINRYYRNPKEIKnlnILMGFKSPKDILFEDEIKkwKEKFDVLLTVDNGDETWTGNTGLITKFIPELK 196
Cdd:cd06192   103 VAGGIGLAPLLPIAKKLAANGNKVT---VLAGAKKAKEEFLDEYFE--LPADVEIWTTDDGELGLEGKVTDSDKPIPLED 177
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1073931601 197 IenpndTIVIVVGPPMMMKFtCLEFLKRNIPDENIWVSFERKMSCGIGKCGHCKInET-----YVCLEGPVFN 264
Cdd:cd06192   178 V-----DRIIVAGSDIMMKA-VVEALDEWLQLIKASVSNNSPMCCGIGICGACTI-ETkhgvkRLCKDGPVFR 243
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
33-233 1.35e-35

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: 127.30  E-value: 1.35e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  33 YTFRLKSDI----LPRhGQFLQVSIPKIGEA------PISiSDYTDEYIELTIRKV--GTVTDAIHELKPGDFLFIRGPY 100
Cdd:cd06183    16 FRFELPSPDqvlgLPV-GQHVELKAPDDGEQvvrpytPIS-PDDDKGYFDLLIKIYpgGKMSQYLHSLKPGDTVEIRGPF 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 101 GHgFPVEDF-KDKNVVIAAGGTGLAPVKSIINRYYRNPKEIKNLNILMGFKSPKDILFEDEI----KKWKEKFDVLLTVD 175
Cdd:cd06183    94 GK-FEYKPNgKVKHIGMIAGGTGITPMLQLIRAILKDPEDKTKISLLYANRTEEDILLREELdelaKKHPDRFKVHYVLS 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1073931601 176 NGDETWTGNTGLITKFIPELKIENPN--DTIVIVVGPPMMMKFTCLEFLKR-NIPDENIWV 233
Cdd:cd06183   173 RPPEGWKGGVGFITKEMIKEHLPPPPseDTLVLVCGPPPMIEGAVKGLLKElGYKKDNVFK 233
DHOD_e_trans_like1 cd06219
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
21-264 3.09e-31

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


Pssm-ID: 99815 [Multi-domain]  Cd Length: 248  Bit Score: 116.14  E-value: 3.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  21 EILSIIPQTDIDYTFRLKSDILPRH---GQFLQVSIPKIGE-APISISDYTDE--YIELTIRKVGTVTDAIHELKPGD-F 93
Cdd:cd06219     2 KILEKEELAPNVKLFEIEAPLIAKKakpGQFVIVRADEKGErIPLTIADWDPEkgTITIVVQVVGKSTRELATLEEGDkI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  94 LFIRGPYGHGFPVEDFKdkNVVIAAGGTGLAPVKSIInryyRNPKEIKNLNIL-MGFKSPKDILFEDEIKKWKEkfDVLL 172
Cdd:cd06219    82 HDVVGPLGKPSEIENYG--TVVFVGGGVGIAPIYPIA----KALKEAGNRVITiIGARTKDLVILEDEFRAVSD--ELII 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 173 TVDNGDEtwtGNTGLITKFIPELKIENPNDTIVIVVGPPMMMKFTCLEFLKRNIPdenIWVSFERKMSCGIGKCGHCKIN 252
Cdd:cd06219   154 TTDDGSY---GEKGFVTDPLKELIESGEKVDLVIAIGPPIMMKAVSELTRPYGIP---TVVSLNPIMVDGTGMCGACRVT 227
                         250
                  ....*....|....*.
gi 1073931601 253 ---ET-YVCLEGPVFN 264
Cdd:cd06219   228 vggETkFACVDGPEFD 243
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
23-233 5.62e-30

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: 112.16  E-value: 5.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  23 LSIIPQTDIDYTFRLKSDILPRH--GQFLQVSIPKIGE---APISISDYTDE--YIELTIRKV--GTVTDAIHELKPGDF 93
Cdd:cd00322     1 VATEDVTDDVRLFRLQLPNGFSFkpGQYVDLHLPGDGRglrRAYSIASSPDEegELELTVKIVpgGPFSAWLHDLKPGDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  94 LFIRGPYGHgFPVEDFKDKNVVIAAGGTGLAPVKSIIN--RYYRNPKEIKnlnILMGFKSPKDILFEDEIKKWKEK---F 168
Cdd:cd00322    81 VEVSGPGGD-FFLPLEESGPVVLIAGGIGITPFRSMLRhlAADKPGGEIT---LLYGARTPADLLFLDELEELAKEgpnF 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1073931601 169 DVLLTVDNG-DETWTGNTGLITKFIPELKIENPNDTIVIVVGPPMMMKFTCLEFLKRNIPDENIWV 233
Cdd:cd00322   157 RLVLALSREsEAKLGPGGRIDREAEILALLPDDSGALVYICGPPAMAKAVREALVSLGVPEERIHT 222
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
19-237 2.83e-29

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 110.65  E-value: 2.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  19 KVEILSIIPQTDIDYTFRLKSD---ILPRH--GQFLQVSIPkIGEAPI----SI-SDYTDEYIELTIRKV--GTVTDAIH 86
Cdd:COG1018     5 PLRVVEVRRETPDVVSFTLEPPdgaPLPRFrpGQFVTLRLP-IDGKPLrraySLsSAPGDGRLEITVKRVpgGGGSNWLH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  87 E-LKPGDFLFIRGPYGHgFPVEDFKDKNVVIAAGGTGLAPVKSIINRYYRNPKEiKNLNILMGFKSPKDILFEDEIKKWK 165
Cdd:COG1018    84 DhLKVGDTLEVSGPRGD-FVLDPEPARPLLLIAGGIGITPFLSMLRTLLARGPF-RPVTLVYGARSPADLAFRDELEALA 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1073931601 166 E---KFDVLLTVDNGDEtwtGNTGLITKFIPELKIENPNDTIVIVVGPPMMMKFTCLEFLKRNIPDENIwvSFER 237
Cdd:COG1018   162 ArhpRLRLHPVLSREPA---GLQGRLDAELLAALLPDPADAHVYLCGPPPMMEAVRAALAELGVPEERI--HFER 231
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
46-231 9.50e-27

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: 103.83  E-value: 9.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  46 GQFLQVSIPKIGEA--PISISDYTDEY--IELTIRKV--GTVTDAIH-ELKPGDFLFIRGPYGHgFPVEDFKDKNVVIAA 118
Cdd:cd06187    27 GQYVNVTVPGRPRTwrAYSPANPPNEDgeIEFHVRAVpgGRVSNALHdELKVGDRVRLSGPYGT-FYLRRDHDRPVLCIA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 119 GGTGLAPVKSIIN---RYYRNPKeiknLNILMGFKSPKDILFEDEIKKWKEK---FDVLLTVDNGDETWTGNTGLITKFI 192
Cdd:cd06187   106 GGTGLAPLRAIVEdalRRGEPRP----VHLFFGARTERDLYDLEGLLALAARhpwLRVVPVVSHEEGAWTGRRGLVTDVV 181
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1073931601 193 PELkIENPNDTIVIVVGPPMMMKFTCLEFLKRNIPDENI 231
Cdd:cd06187   182 GRD-GPDWADHDIYICGPPAMVDATVDALLARGAPPERI 219
PRK06222 PRK06222
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;
46-263 2.29e-25

sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;


Pssm-ID: 235747 [Multi-domain]  Cd Length: 281  Bit Score: 101.42  E-value: 2.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  46 GQFLQVSIPKIGE-APISISDYTDE--YIELTIRKVGTVTDAIHELKPGDFLF-IRGPYGHGFPVEDFKdkNVVIAAGGT 121
Cdd:PRK06222   31 GQFVIVRIDEKGErIPLTIADYDREkgTITIVFQAVGKSTRKLAELKEGDSILdVVGPLGKPSEIEKFG--TVVCVGGGV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 122 GLAPVKSIInryyRNPKEIKNLNI-LMGFKSPKDILFEDEIKKWKEKfdVLLTVDNGDEtwtGNTGLITKFIPELkIENP 200
Cdd:PRK06222  109 GIAPVYPIA----KALKEAGNKVItIIGARNKDLLILEDEMKAVSDE--LYVTTDDGSY---GRKGFVTDVLKEL-LESG 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1073931601 201 ND-TIVIVVGPPMMMKFTCLEFLKRNIPdenIWVSFERKMSCGIGKCGHCKI---NET-YVCLEGPVF 263
Cdd:PRK06222  179 KKvDRVVAIGPVIMMKFVAELTKPYGIK---TIVSLNPIMVDGTGMCGACRVtvgGETkFACVDGPEF 243
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
46-264 5.97e-25

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 104.05  E-value: 5.97e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  46 GQFLQVSIPKIGE-APISISDYTDE--YIELTIRKVGTVTDAIHELKPGDFLF-IRGPYGHGFPVEDFKdkNVVIAAGGT 121
Cdd:PRK12778   31 GQFVIVRVGEKGErIPLTIADADPEkgTITLVIQEVGLSTTKLCELNEGDYITdVVGPLGNPSEIENYG--TVVCAGGGV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 122 GLAPVKSIInryyrnpKEIK----NLNILMGFKSPKDILFEDEIKKWKEkfDVLLTVDNGDetwTGNTGLITKFIPELKI 197
Cdd:PRK12778  109 GVAPMLPIV-------KALKaagnRVITILGGRSKELIILEDEMRESSD--EVIIMTDDGS---YGRKGLVTDGLEEVIK 176
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1073931601 198 ENPNDTIVIVVGPPMMMKFTCLEFLKRNIPDEniwVSFERKMSCGIGKCGHCKI---NET-YVCLEGPVFN 264
Cdd:PRK12778  177 RETKVDKVFAIGPAIMMKFVCLLTKKYGIPTI---VSLNTIMVDGTGMCGACRVtvgGKTkFACVDGPEFD 244
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
21-231 4.84e-22

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: 91.56  E-value: 4.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  21 EILSIIPQTDIDYTFRLKSD--ILPRH--GQFLQVSIPKIG----EAPISISDYTDE--YIELTIRKV--GTVTDAIH-E 87
Cdd:cd06217     5 RVTEIIQETPTVKTFRLAVPdgVPPPFlaGQHVDLRLTAIDgytaQRSYSIASSPTQrgRVELTVKRVpgGEVSPYLHdE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  88 LKPGDFLFIRGPYGHgFPVEDFKDKNVVIAAGGTGLAPVKSIInRYYRNPKEIKNLNILMGFKSPKDILFEDEIKKWKEK 167
Cdd:cd06217    85 VKVGDLLEVRGPIGT-FTWNPLHGDPVVLLAGGSGIVPLMSMI-RYRRDLGWPVPFRLLYSARTAEDVIFRDELEQLARR 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1073931601 168 FDVLLTV----DNGDETWTGNTGLITKFIPELKIENPNDTIVIVVGPPMMMKFTCLEFLKRNIPDENI 231
Cdd:cd06217   163 HPNLHVTealtRAAPADWLGPAGRITADLIAELVPPLAGRRVYVCGPPAFVEAATRLLLELGVPRDRI 230
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
46-231 1.08e-21

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: 93.00  E-value: 1.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  46 GQFLQVSIP---------------------KIGEAPI---SISDYTDE--YIELTIRKV--------GTVTDAIHELKPG 91
Cdd:COG2871   164 GQYIQIEVPpyevdfkdfdipeeekfglfdKNDEEVTraySMANYPAEkgIIELNIRIAtppmdvppGIGSSYIFSLKPG 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  92 DFLFIRGPYGHGFPVEDfkDKNVVIAAGGTGLAPVKSIINRYYRNPKEIKNLNILMGFKSPKDILFEDEIKKWKEKFD-- 169
Cdd:COG2871   244 DKVTISGPYGEFFLRDS--DREMVFIGGGAGMAPLRSHIFDLLERGKTDRKITFWYGARSLRELFYLEEFRELEKEHPnf 321
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 170 ----VLLTVDNGDEtWTGNTGLITKFIPE--LKI-ENPNDTIVIVVGPPMMMKfTCLEFLKR-NIPDENI 231
Cdd:COG2871   322 kfhpALSEPLPEDN-WDGETGFIHEVLYEnyLKDhPAPEDCEAYLCGPPPMID-AVIKMLDDlGVEEENI 389
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
31-213 4.77e-20

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: 86.15  E-value: 4.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  31 IDYTFRLKSDILPRHGQFLQVSIPKI-GEAPISISDYTDE--YIELTIRKV--GTVTDAI-HELKPGDFLFIRGPYGHGF 104
Cdd:cd06190    12 AEFRFALDGPADFLPGQYALLALPGVeGARAYSMANLANAsgEWEFIIKRKpgGAASNALfDNLEPGDELELDGPYGLAY 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 105 PVEDfKDKNVVIAAGGTGLAPVKSIINRYYRNPKEI-KNLNILMGFKSPKDILFEDEIKKWKE---KFDVLLTVDNGDET 180
Cdd:cd06190    92 LRPD-EDRDIVCIAGGSGLAPMLSILRGAARSPYLSdRPVDLFYGGRTPSDLCALDELSALVAlgaRLRVTPAVSDAGSG 170
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1073931601 181 ----WTGNTGLITKFIPELKIENPNDTIVIVVGPPMM 213
Cdd:cd06190   171 saagWDGPTGFVHEVVEATLGDRLAEFEFYFAGPPPM 207
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
46-231 2.17e-19

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate while mono-oxygenases add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate.


Pssm-ID: 99809  Cd Length: 227  Bit Score: 84.29  E-value: 2.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  46 GQFLQVSIPKIGEA-PISISDYTDE--YIELTIRKV--GTVTDAIHE-LKPGDFLFIRGPYGhgfpveDF----KDKNVV 115
Cdd:cd06213    31 GQYAELTLPGLPAArSYSFANAPQGdgQLSFHIRKVpgGAFSGWLFGaDRTGERLTVRGPFG------DFwlrpGDAPIL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 116 IAAGGTGLAPVKSIINRYYRNpKEIKNLNILMGFKSPKDILFEDEI----KKWKEKFDVL--LTVDNGDETWTGNTGLIT 189
Cdd:cd06213   105 CIAGGSGLAPILAILEQARAA-GTKRDVTLLFGARTQRDLYALDEIaaiaARWRGRFRFIpvLSEEPADSSWKGARGLVT 183
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1073931601 190 KFIPELKienPNDTIVIVVGPPMMMKFTCLEFLKRNIPDENI 231
Cdd:cd06213   184 EHIAEVL---LAATEAYLCGPPAMIDAAIAVLRALGIAREHI 222
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
22-231 2.44e-19

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: 83.75  E-value: 2.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  22 ILSIIPQTDIDYTFRLKSDILPRH--GQFLQVSIPKIGEAPISI--SDYTDEYIELTIRKV--GTVTDAIHE-LKPGDFL 94
Cdd:cd06189     3 VESIEPLNDDVYRVRLKPPAPLDFlaGQYLDLLLDDGDKRPFSIasAPHEDGEIELHIRAVpgGSFSDYVFEeLKENGLV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  95 FIRGPYGHGFPVEDfKDKNVVIAAGGTGLAPVKSI----INRYYRNPkeiknLNILMGFKSPKDILFEDEIKKWKEK--- 167
Cdd:cd06189    83 RIEGPLGDFFLRED-SDRPLILIAGGTGFAPIKSIlehlLAQGSKRP-----IHLYWGARTEEDLYLDELLEAWAEAhpn 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1073931601 168 FDVLLTVDNGDETWTGNTGLITKFIPElKIENPNDTIVIVVGPPMMMKFTCLEFLKRNIPDENI 231
Cdd:cd06189   157 FTYVPVLSEPEEGWQGRTGLVHEAVLE-DFPDLSDFDVYACGSPEMVYAARDDFVEKGLPEENF 219
PRK12779 PRK12779
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ...
22-261 1.80e-18

putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional


Pssm-ID: 183740 [Multi-domain]  Cd Length: 944  Bit Score: 84.88  E-value: 1.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  22 ILSIIPQTDIDYTFRLKSDILPRH---GQFLQVSIPKIGE-APISISDYTDE--YIELTIRKVGTVTDAIHELKPGD-FL 94
Cdd:PRK12779  653 IVGKVQLAGGIVEFTVRAPMVARSaqaGQFVRVLPWEKGElIPLTLADWDAEkgTIDLVVQGMGTSSLEINRMAIGDaFS 732
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  95 FIRGPYGHGFPVEDFK-DKNVVIAAGGTGLAPVKSIInryyRNPKEIKN-LNILMGFKSpKDILF---EDE-----IKKW 164
Cdd:PRK12779  733 GIAGPLGRASELHRYEgNQTVVFCAGGVGLPPVYPIM----RAHLRLGNhVTLISGFRA-KEFLFwtgDDErvgklKAEF 807
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 165 KEKFDVLLTVDNGDetwTGNTGLITKFIPELKIENPN---DTI--VIVVGPPMMMKFTCLEFLKRNIPDEniwVSFERKM 239
Cdd:PRK12779  808 GDQLDVIYTTNDGS---FGVKGFVTGPLEEMLKANQQgkgRTIaeVIAIGPPLMMRAVSDLTKPYGVKTV---ASLNSIM 881
                         250       260       270
                  ....*....|....*....|....*....|
gi 1073931601 240 SCGIGKCGHC--------KINETYVCLEGP 261
Cdd:PRK12779  882 VDATGMCGACmvpvtidgKMVRKHACIDGP 911
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
46-232 2.90e-18

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: 81.22  E-value: 2.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  46 GQFLQVSIPKIgEAP----ISISDYTDEYIELTIRKV--GTVTDAIHE-LKPGDFLFIRGPYGHgFPVEDFKDKNVVIAA 118
Cdd:cd06211    39 GQYVNLQAPGY-EGTrafsIASSPSDAGEIELHIRLVpgGIATTYVHKqLKEGDELEISGPYGD-FFVRDSDQRPIIFIA 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 119 GGTGLAPVKSIINRyYRNPKEIKNLNILMGFKSPKDILFEDEIKKWKEKFD------VLLTVDNGDEtWTGNTGLITKFI 192
Cdd:cd06211   117 GGSGLSSPRSMILD-LLERGDTRKITLFFGARTRAELYYLDEFEALEKDHPnfkyvpALSREPPESN-WKGFTGFVHDAA 194
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1073931601 193 PELKIENPNDTIVIVVGPPMMMKFTCLEFLKRNIPDENIW 232
Cdd:cd06211   195 KKHFKNDFRGHKAYLCGPPPMIDACIKTLMQGRLFERDIY 234
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
118-218 4.64e-18

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: 77.30  E-value: 4.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 118 AGGTGLAPVKSIINRYYRNPKEIKNLNILMGFKSPKDILFEDEIKKWKEK----FDVLLTVDNGDETWTGNTGLITKFIP 193
Cdd:pfam00175   3 AGGTGIAPVRSMLRAILEDPKDPTQVVLVFGNRNEDDILYREELDELAEKhpgrLTVVYVVSRPEAGWTGGKGRVQDALL 82
                          90       100
                  ....*....|....*....|....*.
gi 1073931601 194 ELKIENPND-TIVIVVGPPMMMKFTC 218
Cdd:pfam00175  83 EDHLSLPDEeTHVYVCGPPGMIKAVR 108
PLN02252 PLN02252
nitrate reductase [NADPH]
60-235 9.95e-18

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 82.80  E-value: 9.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  60 PISiSDYTDEYIELTIrKV------------GTVTDAIHELKPGDFLFIRGPYGH-------GFPVED---FKDKNVVIA 117
Cdd:PLN02252  688 PTS-SDDEVGHFELVI-KVyfknvhpkfpngGLMSQYLDSLPIGDTIDVKGPLGHieyagrgSFLVNGkpkFAKKLAMLA 765
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 118 aGGTGLAPVKSIINRYYRNPKEIKNLNILMGFKSPKDILFEDEIKKW----KEKFDVLLTVDNGD-ETWTGNTGLITKFI 192
Cdd:PLN02252  766 -GGTGITPMYQVIQAILRDPEDKTEMSLVYANRTEDDILLREELDRWaaehPDRLKVWYVVSQVKrEGWKYSVGRVTEAM 844
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1073931601 193 PELKI-ENPNDTIVIVVGPPMMMKFTCLEFLKRNIPDENIWVSF 235
Cdd:PLN02252  845 LREHLpEGGDETLALMCGPPPMIEFACQPNLEKMGYDKDSILVF 888
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
22-225 3.20e-16

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: 75.68  E-value: 3.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  22 ILSIIPQTDIDYTFRLKSDILPRH--GQFLQVSIPKIGEAPI----SI-SDYTDEYIELTIRKV--GTVTDAIHELKPGD 92
Cdd:cd06195     2 VLKRRDWTDDLFSFRVTRDIPFRFqaGQFTKLGLPNDDGKLVrraySIaSAPYEENLEFYIILVpdGPLTPRLFKLKPGD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  93 FLFI-RGPYGHgFPVEDFKD-KNVVIAAGGTGLAPVKSIIN---RYYRNpkeiKNLNILMGFKSPKDILFEDEIKKWKE- 166
Cdd:cd06195    82 TIYVgKKPTGF-LTLDEVPPgKRLWLLATGTGIAPFLSMLRdleIWERF----DKIVLVHGVRYAEELAYQDEIEALAKq 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1073931601 167 ---KFDVLLTVDNGDETWtGNTGLITKFIPELKIEN-------PNDTIVIVVGPPMMMKFTClEFLKRN 225
Cdd:cd06195   157 yngKFRYVPIVSREKENG-ALTGRIPDLIESGELEEhaglpldPETSHVMLCGNPQMIDDTQ-ELLKEK 223
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
23-231 1.31e-15

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: 73.78  E-value: 1.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  23 LSIIPQTDIDYTFRLKS------DILPrhGQFLQVSIPKIGEAP-----ISISDYTDEYIELTIRKV--GTVTDAIHE-L 88
Cdd:cd06215     4 VKIIQETPDVKTFRFAApdgslfAYKP--GQFLTLELEIDGETVyraytLSSSPSRPDSLSITVKRVpgGLVSNWLHDnL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  89 KPGDFLFIRGPYGHgFPVEDFKDKNVVIAAGGTGLAPVKSIInRYYRNPKEIKNLNILMGFKSPKDILFEDEIKKWKEKF 168
Cdd:cd06215    82 KVGDELWASGPAGE-FTLIDHPADKLLLLSAGSGITPMMSMA-RWLLDTRPDADIVFIHSARSPADIIFADELEELARRH 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1073931601 169 D----VLLTVDNGDETWTGNTGLITKFIPELKIENPNDTIVIVVGPPMMMKFTCLEFLKRNIPDENI 231
Cdd:cd06215   160 PnfrlHLILEQPAPGAWGGYRGRLNAELLALLVPDLKERTVFVCGPAGFMKAVKSLLAELGFPMSRF 226
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
85-231 1.28e-14

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: 71.95  E-value: 1.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  85 IHELKPGDFLFIRGPYGHGFPVEDfkDKNVVIAAGGTGLAPVKSIINRYYRNPKEIKNLNILMGFKSPKDILFEDEIKKW 164
Cdd:cd06188   126 IFNLKPGDKVTASGPFGEFFIKDT--DREMVFIGGGAGMAPLRSHIFHLLKTLKSKRKISFWYGARSLKELFYQEEFEAL 203
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1073931601 165 KEKFD-----VLLTVDNGDETWTGNTGLITK-FIPEL--KIENPNDTIVIVVGPPMMMKfTCLEFLK-RNIPDENI 231
Cdd:cd06188   204 EKEFPnfkyhPVLSEPQPEDNWDGYTGFIHQvLLENYlkKHPAPEDIEFYLCGPPPMNS-AVIKMLDdLGVPRENI 278
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
19-215 8.88e-14

Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which varies in orientation with respect to the NAD(P) binding domain. The N-terminal region may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99793 [Multi-domain]  Cd Length: 218  Bit Score: 68.42  E-value: 8.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  19 KVEILSIIPQT-DI---------DYTFRlksdilPrhGQFLQVSIPKIG----EAPISI-SDYTDEYIELTIrKV----G 79
Cdd:cd06196     2 TVTLLSIEPVThDVkrlrfdkpeGYDFT------P--GQATEVAIDKPGwrdeKRPFTFtSLPEDDVLEFVI-KSypdhD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  80 TVTDAIHELKPGDFLFIRGPYGhgfpVEDFKDKNVVIaAGGTGLAPVKSIINRYYRNpKEIKNLNILMGFKSPKDILFED 159
Cdd:cd06196    73 GVTEQLGRLQPGDTLLIEDPWG----AIEYKGPGVFI-AGGAGITPFIAILRDLAAK-GKLEGNTLIFANKTEKDIILKD 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1073931601 160 EIKKWK-EKFDVLLTvDNGDETWTgnTGLITKFIPELKIENPNDTiVIVVGPPMMMK 215
Cdd:cd06196   147 ELEKMLgLKFINVVT-DEKDPGYA--HGRIDKAFLKQHVTDFNQH-FYVCGPPPMEE 199
nqrF TIGR01941
NADH:ubiquinone oxidoreductase, Na(+)-translocating, F subunit; This model represents the NqrF ...
62-231 1.62e-13

NADH:ubiquinone oxidoreductase, Na(+)-translocating, F subunit; This model represents the NqrF subunit of the six-protein, Na(+)-pumping NADH-quinone reductase of a number of marine and pathogenic Gram-negative bacteria. This oxidoreductase complex functions primarily as a sodium ion pump. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130996 [Multi-domain]  Cd Length: 405  Bit Score: 69.82  E-value: 1.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  62 SISDYTDEY--IELTIR-----------KVGTVTDAIHELKPGDFLFIRGPYGHGFPVEDfkDKNVVIAAGGTGLAPVKS 128
Cdd:TIGR01941 210 SMANYPAEKgiIKLNVRiatppfinsdiPPGIMSSYIFSLKPGDKVTISGPFGEFFAKDT--DAEMVFIGGGAGMAPMRS 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 129 IINRYYRNPKEIKNLNILMGFKSPKDILFEDEIKKWKEKFD-----VLLTVDNGDETWTGNTGLITKFIPE--LK-IENP 200
Cdd:TIGR01941 288 HIFDQLKRLKSKRKISFWYGARSLREMFYQEDFDQLEAENPnfvwhVALSDPQPEDNWTGYTGFIHNVLYEnyLKdHDAP 367
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1073931601 201 NDTIVIVVGPPMMMKfTCLEFLKR-NIPDENI 231
Cdd:TIGR01941 368 EDCEFYMCGPPMMNA-AVIKMLEDlGVERENI 398
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
22-231 3.25e-13

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: 66.90  E-value: 3.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  22 ILSIIPQTDIdyTFRLKSDILP-RHGQFLQVSIP---KIGEAPISISDYTDEY--IELTIRKVGTVTDAI-HELKPGDFL 94
Cdd:cd06198     3 VTEVRPTTTL--TLEPRGPALGhRAGQFAFLRFDasgWEEPHPFTISSAPDPDgrLRFTIKALGDYTRRLaERLKPGTRV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  95 FIRGPYGHgFPVEDFKDKNVVIaAGGTGLAPVKSIInRYYRNPKEIKNLNILMGFKSPKDILFEDEIKKWKEKFDVLLTV 174
Cdd:cd06198    81 TVEGPYGR-FTFDDRRARQIWI-AGGIGITPFLALL-EALAARGDARPVTLFYCVRDPEDAVFLDELRALAAAAGVVLHV 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1073931601 175 -DNGDETWTGNTGLITKFIPELKienpnDTIVIVVGPPMMMKFTCLEFLKRNIPDENI 231
Cdd:cd06198   158 iDSPSDGRLTLEQLVRALVPDLA-----DADVWFCGPPGMADALEKGLRALGVPARRF 210
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
34-231 1.10e-12

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 67.23  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  34 TFRLKSDILPRH--GQFLQVSIP----KIGEAPISISDY--TDEYIELTIRKVGTVTDAIHELKPGDFLFIRGPYGHGFP 105
Cdd:COG4097   233 TLRPEGGRWLGHraGQFAFLRFDgspfWEEAHPFSISSApgGDGRLRFTIKALGDFTRRLGRLKPGTRVYVEGPYGRFTF 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 106 VEDFKDKNVVIAAGGTGLAPVKSIINRYYRNPKEIKNLNILMGFKSPKDILFEDEIKKWKEK---FDVLLTVDNGDETWT 182
Cdd:COG4097   313 DRRDTAPRQVWIAGGIGITPFLALLRALAARPGDQRPVDLFYCVRDEEDAPFLEELRALAARlagLRLHLVVSDEDGRLT 392
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1073931601 183 GntGLITKFIPELKienpnDTIVIVVGPPMMMKFTCLEFLKRNIPDENI 231
Cdd:COG4097   393 A--ERLRRLVPDLA-----EADVFFCGPPGMMDALRRDLRALGVPARRI 434
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
46-230 2.61e-12

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 65.66  E-value: 2.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  46 GQFLQVSIPKIGEAPISI--SDYTDEYIELTIRKV--GTVTDAI-HELKPGDFLFIRGPYGHGFPVEDfKDKNVVIAAGG 120
Cdd:PRK07609  135 GQYIEFILKDGKRRSYSIanAPHSGGPLELHIRHMpgGVFTDHVfGALKERDILRIEGPLGTFFLRED-SDKPIVLLASG 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 121 TGLAPVKSIINrYYRNPKEIKNLNILMGFKSPKDiLFEDEI-KKWKE-----KFDVLLTVDNGDETWTGNTGLITKF--- 191
Cdd:PRK07609  214 TGFAPIKSIVE-HLRAKGIQRPVTLYWGARRPED-LYLSALaEQWAEelpnfRYVPVVSDALDDDAWTGRTGFVHQAvle 291
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1073931601 192 -IPELkienpNDTIVIVVGPPMMMKFTCLEFLKRNIPDEN 230
Cdd:PRK07609  292 dFPDL-----SGHQVYACGSPVMVYAARDDFVAAGLPAEE 326
PRK12775 PRK12775
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ...
46-264 3.02e-12

putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional


Pssm-ID: 183738 [Multi-domain]  Cd Length: 1006  Bit Score: 66.50  E-value: 3.02e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601   46 GQFLQVSIPKIGE-APISISDYTDE--YIELTIRKVGTVT-DAIHELKPGD-FLFIRGPYGhgFPVEDFKDKNVVIAAGG 120
Cdd:PRK12775    31 GHFVMLRLYEGAErIPLTVADFDRKkgTITMVVQALGKTTrEMMTKFKAGDtFEDFVGPLG--LPQHIDKAGHVVLVGGG 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  121 TGLAPVKSIInryyRNPKEIKNLNI-LMGFKSpKDILFedeikkWKEKF-----DVLLTVDNGDetwTGNTGLITKFIPE 194
Cdd:PRK12775   109 LGVAPVYPQL----RAFKEAGARTTgIIGFRN-KDLVF------WEDKFgkycdDLIVCTDDGS---YGKPGFVTAALKE 174
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1073931601  195 LkIENPNDTIVIVVGP-PMMMkfTCLEFLKrniP-DENIWVSFERKMSCGIGKCGHCKI----NETYVCLEGPVFN 264
Cdd:PRK12775   175 V-CEKDKPDLVVAIGPlPMMN--ACVETTR---PfGVKTMVSLNAIMVDGTGMCGSCRVtvggEVKFACVDGPDFD 244
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
68-213 1.17e-11

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: 62.67  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  68 DEYIELTIRKV--GTVTDAIH-ELKPGDFLFIRGPYGHGFPVEDFKDKNVVIAAGGTGLAPVKSIInR--YYRNPK-EIK 141
Cdd:cd06194    51 DNELEFHIRRKpnGAFSGWLGeEARPGHALRLQGPFGQAFYRPEYGEGPLLLVGAGTGLAPLWGIA-RaaLRQGHQgEIR 129
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1073931601 142 nlnILMGFKSPKDILFEDEIKKWKEK---FDVLLTVD-NGDETWTGNTGLITKFIPELkienPNDTIVIVVGPPMM 213
Cdd:cd06194   130 ---LVHGARDPDDLYLHPALLWLAREhpnFRYIPCVSeGSQGDPRVRAGRIAAHLPPL----TRDDVVYLCGAPSM 198
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
22-231 1.41e-11

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: 62.56  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  22 ILSIIPQTD--IDYTF----RLKSDILPRHGQFLQVSIPKIGEAPI---SI-SDYTDEYIELTIRKV--GTV-TDAIHEL 88
Cdd:cd06214     6 VAEVVRETAdaVSITFdvpeELRDAFRYRPGQFLTLRVPIDGEEVRrsySIcSSPGDDELRITVKRVpgGRFsNWANDEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  89 KPGDFLFIRGPYGHGFPVEDFKDKNVVIAAGGTGLAPVKSIINRYYRNPKEiKNLNILMGFKSPKDILFEDEIKKWKEK- 167
Cdd:cd06214    86 KAGDTLEVMPPAGRFTLPPLPGARHYVLFAAGSGITPVLSILKTALAREPA-SRVTLVYGNRTEASVIFREELADLKARy 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1073931601 168 ---FDVLLTVDNGDETWTGNTGLITK----FIPELKIENPNDTIVIVVGPPMMMKfTCLEFLK-RNIPDENI 231
Cdd:cd06214   165 pdrLTVIHVLSREQGDPDLLRGRLDAaklnALLKNLLDATEFDEAFLCGPEPMMD-AVEAALLeLGVPAERI 235
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
46-213 1.97e-11

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: 62.35  E-value: 1.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  46 GQFLQVSIPKIGEA---PISISDYTDEYIELTIRK-----VGTVTDaiHELKPGDFLFIRGPYGhGFPVEDFKDKNVVIA 117
Cdd:cd06212    33 GQYVDITVPGTEETrsfSMANTPADPGRLEFIIKKypgglFSSFLD--DGLAVGDPVTVTGPYG-TCTLRESRDRPIVLI 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 118 AGGTGLAPVKSIInRYYRNPKEIKNLNILMGFKSPKDILFEDEIKKWKEKFDVLLTV----DNGDET-WTGNTGLITKFI 192
Cdd:cd06212   110 GGGSGMAPLLSLL-RDMAASGSDRPVRFFYGARTARDLFYLEEIAALGEKIPDFTFIpalsESPDDEgWSGETGLVTEVV 188
                         170       180
                  ....*....|....*....|.
gi 1073931601 193 PElKIENPNDTIVIVVGPPMM 213
Cdd:cd06212   189 QR-NEATLAGCDVYLCGPPPM 208
PRK05802 PRK05802
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;
58-252 2.16e-11

sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;


Pssm-ID: 235613 [Multi-domain]  Cd Length: 320  Bit Score: 63.07  E-value: 2.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  58 EAPISI--SDYTDEYIELTIRKVGTVTDAIHELKPGDFLFIRGPYGHGF----PVEDFKDKNVVIAAGGTGLAPVKSIIN 131
Cdd:PRK05802  113 DVPISImeADTEENIIKVAIEIRGVKTKKIAKLNKGDEILLRGPYWNGIlglkNIKSTKNGKSLVIARGIGQAPGVPVIK 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 132 RYYRNPKEIKnlnILMGFKSPKDILFEDEIKKWKEKFDVLLTVDNGDETWTGNtglitKFIPELkIENpNDTIVIVVGPP 211
Cdd:PRK05802  193 KLYSNGNKII---VIIDKGPFKNNFIKEYLELYNIEIIELNLLDDGELSEEGK-----DILKEI-IKK-EDINLIHCGGS 262
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1073931601 212 MMMKFTCLEFLKRNIPDENIWVSFERKMSCGIGKCGHCKIN 252
Cdd:PRK05802  263 DILHYKIIEYLDKLNEKIKLSCSNNAKMCCGEGICGACTVR 303
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
27-237 4.46e-11

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: 61.20  E-value: 4.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  27 PQTDIDYTFRLKSDILPrhGQFLQVSIPKIGEA-PISISDYT--DEYIELTIRKV--GTVTDAI-HELKPGDFLFIRGPY 100
Cdd:cd06210    21 LQPDDAEGAGIAAEFVP--GQFVEIEIPGTDTRrSYSLANTPnwDGRLEFLIRLLpgGAFSTYLeTRAKVGQRLNLRGPL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 101 GhGFPVEDFKDKNVVIAAGGTGLAPVKSIINRY--YRNPKEIKnlnILMGFKSPKDILFEDEIKKWKEK---FDVLLTVD 175
Cdd:cd06210    99 G-AFGLRENGLRPRWFVAGGTGLAPLLSMLRRMaeWGEPQEAR---LFFGVNTEAELFYLDELKRLADSlpnLTVRICVW 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1073931601 176 NGDETWTGNTG----LITKFIPELKIeNPNdtiVIVVGPPMMMKFTCLEFLKRNIPDENiwVSFER 237
Cdd:cd06210   175 RPGGEWEGYRGtvvdALREDLASSDA-KPD---IYLCGPPGMVDAAFAAAREAGVPDEQ--VYLEK 234
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
40-213 9.97e-11

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: 60.30  E-value: 9.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  40 DILPrhGQFLQVSIPKIGEA-PISISDYTDE-YIELTIRKV--GTVTDAIHEL-KPGDFLFIRGPYGHGF--PVEdfkdK 112
Cdd:cd06209    30 AFLP--GQYVNLQVPGTDETrSYSFSSAPGDpRLEFLIRLLpgGAMSSYLRDRaQPGDRLTLTGPLGSFYlrEVK----R 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 113 NVVIAAGGTGLAPVKSIINRYYRNPKEIKnLNILMGFKSPKDiLFE----DEIKKWKEKFDVLLTVDNgDETWTGNTGLI 188
Cdd:cd06209   104 PLLMLAGGTGLAPFLSMLDVLAEDGSAHP-VHLVYGVTRDAD-LVEldrlEALAERLPGFSFRTVVAD-PDSWHPRKGYV 180
                         170       180
                  ....*....|....*....|....*
gi 1073931601 189 TKFIPELKIENPnDTIVIVVGPPMM 213
Cdd:cd06209   181 TDHLEAEDLNDG-DVDVYLCGPPPM 204
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
18-231 3.28e-10

FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain containing a B-type heme fused with a ferredoxin reductase-like FAD/NAD-binding domain. Flavohemoglobins detoxify nitric oxide (NO) via an NO dioxygenase reaction. The hemoglobin domain adopts a globin fold with an embedded heme molecule. Flavohemoglobins also have a C-terminal reductase domain with bindiing sites for FAD and NAD(P)H. This domain catalyzes the conversion of NO + O2 + NAD(P)H to NO3- + NAD(P)+. Instead of the oxygen transport function of hemoglobins, flavohemoglobins seem to act in NO dioxygenation and NO signalling.


Pssm-ID: 99781  Cd Length: 247  Bit Score: 58.72  E-value: 3.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  18 KKVEILSIIPQTDIDYTFRLKSD---ILPRH--GQFL--QVSIPKIGEAPI---SISDY-TDEYIELTIRKV--GTVTDA 84
Cdd:cd06184     7 RPFVVARKVAESEDITSFYLEPAdggPLPPFlpGQYLsvRVKLPGLGYRQIrqySLSDApNGDYYRISVKREpgGLVSNY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  85 IH-ELKPGDFLFIRGPYGHgFPVEDFKDKNVVIAAGGTGLAPVKSIINR--YYRNPKEIknlNILMGFKSPKDILFEDEI 161
Cdd:cd06184    87 LHdNVKVGDVLEVSAPAGD-FVLDEASDRPLVLISAGVGITPMLSMLEAlaAEGPGRPV---TFIHAARNSAVHAFRDEL 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1073931601 162 KKWKEK---FDVLLTVDNGDETWTGN----TGLITK-FIPELKIenPNDTIVIVVGPPMMMKFTCLEFLKRNIPDENI 231
Cdd:cd06184   163 EELAARlpnLKLHVFYSEPEAGDREEdydhAGRIDLaLLRELLL--PADADFYLCGPVPFMQAVREGLKALGVPAERI 238
PTZ00319 PTZ00319
NADH-cytochrome B5 reductase; Provisional
60-224 1.80e-09

NADH-cytochrome B5 reductase; Provisional


Pssm-ID: 173521 [Multi-domain]  Cd Length: 300  Bit Score: 57.15  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  60 PISISD---YTDEYIELTIRKV-------GTVTDAIHELKPGDFLFIRGPYGH-----------GFPVEDFKDKNV---V 115
Cdd:PTZ00319   91 PISSDDekgYVDFLIKVYFKGVhpsfpngGRLSQHLYHMKLGDKIEMRGPVGKfeylgngtytvHKGKGGLKTMHVdafA 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 116 IAAGGTGLAPVKSIINRYYRNPKEIKNLNILMGFKSPKDILFEDEIKKWKE--KFDVLLTVD-NGDETWTGNTGLIT--- 189
Cdd:PTZ00319  171 MIAGGTGITPMLQIIHAIKKNKEDRTKVFLVYANQTEDDILLRKELDEAAKdpRFHVWYTLDrEATPEWKYGTGYVDeem 250
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1073931601 190 --KFIPELKIENP--NDTIVIVVGPPMMMKFTCLEFLKR 224
Cdd:PTZ00319  251 lrAHLPVPDPQNSgiKKVMALMCGPPPMLQMAVKPNLEK 289
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
19-214 1.02e-08

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


Pssm-ID: 99812 [Multi-domain]  Cd Length: 243  Bit Score: 54.54  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  19 KVEILSIIPQTDIDYTFRLKSDILPRH---GQFLQVSIPKIGE------APISISDYTDEYIELTIRKV--GTVTDAIHE 87
Cdd:cd06216    19 RARVVAVRPETADMVTLTLRPNRGWPGhraGQHVRLGVEIDGVrhwrsySLSSSPTQEDGTITLTVKAQpdGLVSNWLVN 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  88 -LKPGDFLFIRGPYGhGFPVEDFKDKNVVIAAGGTGLAPVKSIINRYYRNPkEIKNLNILMGFKSPKDILFEDEIKKWKE 166
Cdd:cd06216    99 hLAPGDVVELSQPQG-DFVLPDPLPPRLLLIAAGSGITPVMSMLRTLLARG-PTADVVLLYYARTREDVIFADELRALAA 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1073931601 167 KFDVL-LTVDNGDETWTG--NTGLITKFIPELkienpNDTIVIVVGPPMMM 214
Cdd:cd06216   177 QHPNLrLHLLYTREELDGrlSAAHLDAVVPDL-----ADRQVYACGPPGFL 222
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
44-215 1.34e-07

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: 50.99  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  44 RHGQFLQVSIPKIGEA-----PISISDYTDEyIELTIRKV--GTVTDAIHE-LKPGDFLFIRGPYGHgFPVEDFKDKNVV 115
Cdd:cd06191    29 RPGQHVTLKLDFDGEElrrcySLCSSPAPDE-ISITVKRVpgGRVSNYLREhIQPGMTVEVMGPQGH-FVYQPQPPGRYL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 116 IAAGGTGLAPVKSIInRYYRNPKEIKNLNILMGFKSPKDILFEDEIKKWKEK---FDVL--LTVDNGDETWTGNTGLITK 190
Cdd:cd06191   107 LVAAGSGITPLMAMI-RATLQTAPESDFTLIHSARTPADMIFAQELRELADKpqrLRLLciFTRETLDSDLLHGRIDGEQ 185
                         170       180
                  ....*....|....*....|....*
gi 1073931601 191 FIPELKIENPNDTIVIVVGPPMMMK 215
Cdd:cd06191   186 SLGAALIPDRLEREAFICGPAGMMD 210
DHODB_Fe-S_bind pfam10418
Iron-sulfur cluster binding domain of dihydroorotate dehydrogenase B; Lactococcus lactis is ...
236-267 1.76e-07

Iron-sulfur cluster binding domain of dihydroorotate dehydrogenase B; Lactococcus lactis is one of the few organizms with two dihydroorotate dehydrogenases, DHODs, A and B. The B enzyme is a prototype for DHODs in Gram-positive bacteria that use NAD+ as the second substrate. DHODB is a hetero-tetramer composed of a central homodimer of PyrDB subunits resembling the DHODA structure and two PyrK subunits along with three different cofactors: FMN, FAD, and a [2Fe-2S] cluster. The [2Fe-2S] iron-sulfur cluster binds to this C-terminal domain of the PyrK subunit, which is at the interface between the flavin and NAD binding domains and contains three beta-strands. The four cysteine residues at the N-terminal part of this domain are the ones that bind, in pairs, to the iron-sulfur cluster. The conformation of the whole molecule means that the iron-sulfur cluster is localized in a well-ordered part of this domain close to the FAD binding site. The FAD and and NAD binding domains are FAD_binding_6, pfam00970 and NAD_binding_1, pfam00175.


Pssm-ID: 463084 [Multi-domain]  Cd Length: 40  Bit Score: 46.44  E-value: 1.76e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1073931601 236 ERKMSCGIGKCGHCKI-------NETYVCLEGPVFNYTK 267
Cdd:pfam10418   1 EERMACGVGACGGCVVktkggdgEYKRVCVDGPVFDADE 39
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
66-168 1.21e-06

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: 48.86  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  66 YTDEyiELTIRKVGTVTDAIHELKPGDFLFIRGPYGHGFPVEDFKDKNVVIAAGGTGLAPVKSIINRYYR----NPKEIK 141
Cdd:cd06208    92 YTDP--ETDETKKGVCSNYLCDLKPGDDVQITGPVGKTMLLPEDPNATLIMIATGTGIAPFRSFLRRLFRekhaDYKFTG 169
                          90       100
                  ....*....|....*....|....*..
gi 1073931601 142 NLNILMGFKSPKDILFEDEIKKWKEKF 168
Cdd:cd06208   170 LAWLFFGVPNSDSLLYDDELEKYPKQY 196
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
19-102 1.57e-06

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 45.65  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  19 KVEILSiiPQTDIdYTFRLKSDI----LPRhGQFLQVSIPKIGEA------PISiSDYTDEYIELTIRKV--GTVTDAIH 86
Cdd:pfam00970   6 EKELVS--HDTRI-FRFALPHPDqvlgLPV-GQHLFLRLPIDGELvirsytPIS-SDDDKGYLELLVKVYpgGKMSQYLD 80
                          90
                  ....*....|....*.
gi 1073931601  87 ELKPGDFLFIRGPYGH 102
Cdd:pfam00970  81 ELKIGDTIDFKGPLGR 96
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
17-166 2.15e-06

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 48.17  E-value: 2.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  17 PKKVEILSIIPQTDIDYTFRLKS-DILP-RHGQFLQVSI---PKIGEA-PISISDYTDEYIELTIRK----VGTvTDAIH 86
Cdd:PRK10684    9 PNRMQVHSIVQETPDVWTISLIChDFYPyRAGQYALVSIrnsAETLRAyTLSSTPGVSEFITLTVRRiddgVGS-QWLTR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  87 ELKPGDFLFIRGPYGHgFPVEDFKDKNVVIAAGGTGLAPVKSiINRYYRNPKEIKNLNILMGFKSPKDILFEDEikkWKE 166
Cdd:PRK10684   88 DVKRGDYLWLSDAMGE-FTCDDKAEDKYLLLAAGCGVTPIMS-MRRWLLKNRPQADVQVIFNVRTPQDVIFADE---WRQ 162
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
79-215 4.09e-06

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 47.85  E-value: 4.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601   79 GTVTDAIHELKPGDFLFIRGpyGHGFPVE-DFKDKNVV----------IAAGGTGLAPVKSIINRYYRNP--KEIKNLNI 145
Cdd:PTZ00306   990 GTLKEWISALRPGDSVEMKA--CGGLRIErRPADKQFVfrghvirklaLIAGGTGVAPMLQIIRAALKKPyvDSIESIRL 1067
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1073931601  146 LMGFKSPKDI----LFEDEIKKWKEKFDVLLTVDNGDETWTGNTGLITKFIPELKIENP-NDTIVIVVGPPMMMK 215
Cdd:PTZ00306  1068 IYAAEDVSELtyreLLESYRKENPGKFKCHFVLNNPPEGWTDGVGFVDRALLQSALQPPsKDLLVAICGPPVMQR 1142
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
66-175 4.57e-06

ferredoxin--NADP(+) reductase; Provisional


Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 47.30  E-value: 4.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  66 YTDEYIELTirkVGTVTDAIHELKPGDFLFIRGPYGHGFPVEDFKDKNVVIAAGGTGLAPVKSIINRYYRNPKEIKNLN- 144
Cdd:PLN03115  173 YTNDQGEIV---KGVCSNFLCDLKPGAEVKITGPVGKEMLMPKDPNATIIMLATGTGIAPFRSFLWKMFFEKHDDYKFNg 249
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1073931601 145 ---ILMGFKSPKDILFEDEIKKWKEKFDVLLTVD 175
Cdd:PLN03115  250 lawLFLGVPTSSSLLYKEEFEKMKEKAPENFRLD 283
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
46-166 1.95e-05

NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 44.60  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  46 GQFLQVSIPKIG---EA----PISISDYTDEYIELTIRKVGTVT-----DAIHELKPGDFL--FIRGPYGHgfPVEDFKD 111
Cdd:cd06186    28 GQHVYLNFPSLLsfwQShpftIASSPEDEQDTLSLIIRAKKGFTtrllrKALKSPGGGVSLkvLVEGPYGS--SSEDLLS 105
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1073931601 112 -KNVVIAAGGTGLAPV----KSIINRYYRNPKeIKNLNILMGFKSPKDIL-FEDEIKKWKE 166
Cdd:cd06186   106 yDNVLLVAGGSGITFVlpilRDLLRRSSKTSR-TRRVKLVWVVRDREDLEwFLDELRAAQE 165
PTZ00274 PTZ00274
cytochrome b5 reductase; Provisional
64-214 3.35e-05

cytochrome b5 reductase; Provisional


Pssm-ID: 140300  Cd Length: 325  Bit Score: 44.53  E-value: 3.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  64 SDYTDEYIELTIR--KVGTVTDAIHELKPGDFLFIRGPyghGFPVE--DFKDKNVVIAAGGTGLAPVKSIINRYYRNP-- 137
Cdd:PTZ00274  111 ANHTKGYFDIIVKrkKDGLMTNHLFGMHVGDKLLFRSV---TFKIQyrPNRWKHVGMIAGGTGFTPMLQIIRHSLTEPwd 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601 138 -KEIKN--LNILMGFKSPKDIL----FEDEIKKWKEKFDVLLTVDNG--DETWTGNTGLITKFIPELKIENPND--TIVI 206
Cdd:PTZ00274  188 sGEVDRtkLSFLFCNRTERHILlkglFDDLARRYSNRFKVYYTIDQAvePDKWNHFLGYVTKEMVRRTMPAPEEkkKIIM 267

                  ....*...
gi 1073931601 207 VVGPPMMM 214
Cdd:PTZ00274  268 LCGPDQLL 275
fre PRK08051
FMN reductase; Validated
19-188 6.66e-05

FMN reductase; Validated


Pssm-ID: 236142 [Multi-domain]  Cd Length: 232  Bit Score: 42.92  E-value: 6.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  19 KVEilSIIPQTDIDYTFRLK--SDILPRHGQFLQVSIPKIGEAPISI--SDYTDEYIELTI------RKVGTVTDAIHEl 88
Cdd:PRK08051    6 KVT--SVEAITDTVYRVRLVpeAPFSFRAGQYLMVVMGEKDKRPFSIasTPREKGFIELHIgaselnLYAMAVMERILK- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  89 kpGDFLFIRGPYGHGFPVEDfKDKNVVIAAGGTGLAPVKSII-NRYYRNPKeiKNLNILMGFKSPKDILFEDEIKKWKEK 167
Cdd:PRK08051   83 --DGEIEVDIPHGDAWLREE-SERPLLLIAGGTGFSYARSILlTALAQGPN--RPITLYWGGREEDHLYDLDELEALALK 157
                         170       180
                  ....*....|....*....|....
gi 1073931601 168 ---FDVLLTVDNGDETWTGNTGLI 188
Cdd:PRK08051  158 hpnLHFVPVVEQPEEGWQGKTGTV 181
PLN02631 PLN02631
ferric-chelate reductase
25-161 7.57e-03

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 37.71  E-value: 7.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073931601  25 IIPQTDIDYTFRLKSDI--LPRHGQFLQV-SIPKIGEAPISI---SDYTDEYIELTIRKVGTVTDAI--HELKPGDFLFI 96
Cdd:PLN02631  317 ILPSDNLELTFSKTPGLhyTPTSILFLHVpSISKLQWHPFTItssSNLEKDTLSVVIRRQGSWTQKLytHLSSSIDSLEV 396
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1073931601  97 --RGPYG-HGFPVEdfKDKNVVIAAGGTGLAPVKSIINRYY---RNPK-EIKNLNILMGFKSPKDILFEDEI 161
Cdd:PLN02631  397 stEGPYGpNSFDVS--RHNSLILVSGGSGITPFISVIRELIfqsQNPStKLPDVLLVCSFKHYHDLAFLDLI 466
 
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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