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Conserved domains on  [gi|1314859353|gb|AUG16167|]
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1,2-phenylacetyl-CoA epoxidase subunit E [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

PA_CoA_Oxy5 family protein( domain architecture ID 11493792)

PA_CoA_Oxy5 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PA_CoA_Oxy5 TIGR02160
phenylacetate-CoA oxygenase/reductase, PaaK subunit; Phenylacetate-CoA oxygenase is comprised ...
4-351 0e+00

phenylacetate-CoA oxygenase/reductase, PaaK subunit; Phenylacetate-CoA oxygenase is comprised of a five gene complex responsible for the hydroxylation of phenylacetate-CoA (PA-CoA) as the second catabolic step in phenylacetic acid (PA) degradation. Although the exact function of this enzyme has not been determined, it has been shown to be required for phenylacetic acid degradation and has been proposed to function in a multicomponent oxygenase acting on phenylacetate-CoA. [Energy metabolism, Other]


:

Pssm-ID: 131215 [Multi-domain]  Cd Length: 352  Bit Score: 629.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   4 FHSLTVAKVESETRDAVTITFAVPQPLQEAYRFRPGQHLTLKASFDGEELRRCYSICRSYLPGEISVAVKAIEGGRFSRY 83
Cdd:TIGR02160   1 FHRLTVAEVERLTADAVAISFEIPDELAEDYRFAPGQHLTLRREVDGEELRRSYSICSAPAPGEIRVAVKKIPGGLFSTW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  84 AREHIRQGMTLEVMVPQGHFGYQPQAERQGRYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALAD 163
Cdd:TIGR02160  81 ANDEIRPGDTLEVMAPQGLFTPDLSTPHAGHYVAVAAGSGITPMLSIAETVLAAEPRSTFTLVYGNRRTASVMFAEELAD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 164 LKDKYPQRLQLLCIFSQETLDSDLLHGRIDGEKLQSLGASLINFRLYDEAFICGPAAMMDDAETALKALGMPDKTIHLER 243
Cdd:TIGR02160 161 LKDKHPQRFHLAHVLSREPREAPLLSGRLDGERLAALLDSLIDVDRADEWFLCGPQAMVDDAEQALTGLGVPAGRVHLEL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 244 FNT---PGTRVKRSVN-VQSDGQKVTVRQDGRDREIVLNADDESILDAALRQGADLPYACKGGVCATCKCKVLRGKVAME 319
Cdd:TIGR02160 241 FYTddePGREVRHEVSgPEGDVSKVTVTLDGRSTETSSLSRDESVLDAALRARPDLPFACKGGVCGTCRAKVLEGKVDME 320
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1314859353 320 TNYSLEPDELAAGYVLSCQALPLTSDVVVDFD 351
Cdd:TIGR02160 321 RNYALEPDEVDAGYVLTCQAYPLSDKLVVDYD 352
 
Name Accession Description Interval E-value
PA_CoA_Oxy5 TIGR02160
phenylacetate-CoA oxygenase/reductase, PaaK subunit; Phenylacetate-CoA oxygenase is comprised ...
4-351 0e+00

phenylacetate-CoA oxygenase/reductase, PaaK subunit; Phenylacetate-CoA oxygenase is comprised of a five gene complex responsible for the hydroxylation of phenylacetate-CoA (PA-CoA) as the second catabolic step in phenylacetic acid (PA) degradation. Although the exact function of this enzyme has not been determined, it has been shown to be required for phenylacetic acid degradation and has been proposed to function in a multicomponent oxygenase acting on phenylacetate-CoA. [Energy metabolism, Other]


Pssm-ID: 131215 [Multi-domain]  Cd Length: 352  Bit Score: 629.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   4 FHSLTVAKVESETRDAVTITFAVPQPLQEAYRFRPGQHLTLKASFDGEELRRCYSICRSYLPGEISVAVKAIEGGRFSRY 83
Cdd:TIGR02160   1 FHRLTVAEVERLTADAVAISFEIPDELAEDYRFAPGQHLTLRREVDGEELRRSYSICSAPAPGEIRVAVKKIPGGLFSTW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  84 AREHIRQGMTLEVMVPQGHFGYQPQAERQGRYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALAD 163
Cdd:TIGR02160  81 ANDEIRPGDTLEVMAPQGLFTPDLSTPHAGHYVAVAAGSGITPMLSIAETVLAAEPRSTFTLVYGNRRTASVMFAEELAD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 164 LKDKYPQRLQLLCIFSQETLDSDLLHGRIDGEKLQSLGASLINFRLYDEAFICGPAAMMDDAETALKALGMPDKTIHLER 243
Cdd:TIGR02160 161 LKDKHPQRFHLAHVLSREPREAPLLSGRLDGERLAALLDSLIDVDRADEWFLCGPQAMVDDAEQALTGLGVPAGRVHLEL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 244 FNT---PGTRVKRSVN-VQSDGQKVTVRQDGRDREIVLNADDESILDAALRQGADLPYACKGGVCATCKCKVLRGKVAME 319
Cdd:TIGR02160 241 FYTddePGREVRHEVSgPEGDVSKVTVTLDGRSTETSSLSRDESVLDAALRARPDLPFACKGGVCGTCRAKVLEGKVDME 320
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1314859353 320 TNYSLEPDELAAGYVLSCQALPLTSDVVVDFD 351
Cdd:TIGR02160 321 RNYALEPDEVDAGYVLTCQAYPLSDKLVVDYD 352
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
4-244 5.62e-136

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: 386.51  E-value: 5.62e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   4 FHSLTVAKVESETRDAVTITFAVPQPLQEAYRFRPGQHLTLKASFDGEELRRCYSICRSYLPGEISVAVKAIEGGRFSRY 83
Cdd:cd06214     1 FHPLTVAEVVRETADAVSITFDVPEELRDAFRYRPGQFLTLRVPIDGEEVRRSYSICSSPGDDELRITVKRVPGGRFSNW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  84 AREHIRQGMTLEVMVPQGHFGYQPQAeRQGRYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALAD 163
Cdd:cd06214    81 ANDELKAGDTLEVMPPAGRFTLPPLP-GARHYVLFAAGSGITPVLSILKTALAREPASRVTLVYGNRTEASVIFREELAD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 164 LKDKYPQRLQLLCIFSQETLDSDLLHGRIDGEKLQSLGASLINFRLYDEAFICGPAAMMDDAETALKALGMPDKTIHLER 243
Cdd:cd06214   160 LKARYPDRLTVIHVLSREQGDPDLLRGRLDAAKLNALLKNLLDATEFDEAFLCGPEPMMDAVEAALLELGVPAERIHREL 239

                  .
gi 1314859353 244 F 244
Cdd:cd06214   240 F 240
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
2-243 3.72e-86

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 259.72  E-value: 3.72e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   2 TTFHSLTVAKVESETRDAVTITFAVPQPLqEAYRFRPGQHLTLKASFDGEELRRCYSICRSYLPGEISVAVKAIEGGRFS 81
Cdd:COG1018     1 AGFRPLRVVEVRRETPDVVSFTLEPPDGA-PLPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVKRVPGGGGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  82 RYAREHIRQGMTLEVMVPQGHFGYQPQAERqgRYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQAL 161
Cdd:COG1018    80 NWLHDHLKVGDTLEVSGPRGDFVLDPEPAR--PLLLIAGGIGITPFLSMLRTLLARGPFRPVTLVYGARSPADLAFRDEL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 162 ADLKDKYPqRLQLLCIFSQETldsDLLHGRIDGEKLQSLGASLINfrlyDEAFICGPAAMMDDAETALKALGMPDKTIHL 241
Cdd:COG1018   158 EALAARHP-RLRLHPVLSREP---AGLQGRLDAELLAALLPDPAD----AHVYLCGPPPMMEAVRAALAELGVPEERIHF 229

                  ..
gi 1314859353 242 ER 243
Cdd:COG1018   230 ER 231
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
7-348 4.11e-44

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 154.87  E-value: 4.11e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   7 LTVAKVESETRDAVTITFAVpqplQEAYRFRPGQHlTLKASFDGEELRRCYSIcrSYLPGE---ISVAVKAIEGGRFSRY 83
Cdd:PRK10684   12 MQVHSIVQETPDVWTISLIC----HDFYPYRAGQY-ALVSIRNSAETLRAYTL--SSTPGVsefITLTVRRIDDGVGSQW 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  84 AREHIRQGMTLEVMVPQGHFGYQPQAErqGRYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALAD 163
Cdd:PRK10684   85 LTRDVKRGDYLWLSDAMGEFTCDDKAE--DKYLLLAAGCGVTPIMSMRRWLLKNRPQADVQVIFNVRTPQDVIFADEWRQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 164 LKDKYPQrLQLLCIFSQETLDSdLLHGRIDGEKLQSLGASLINFRLydeaFICGPAAMMDDAETALKALGMPDKTIHLER 243
Cdd:PRK10684  163 LKQRYPQ-LNLTLVAENNATEG-FIAGRLTRELLQQAVPDLASRTV----MTCGPAPYMDWVEQEVKALGVTADRFFKEK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 244 FNTPgtrvkrSVNVQSDGQKVTVRQDGRDreivLNADDESILDAALRQGaDLPY--ACKGGVCATCKCKVLRGKVAMETN 321
Cdd:PRK10684  237 FFTP------VAEAATSGLTFTKLQPARE----FYAPVGTTLLEALESN-KVPVvaACRAGVCGCCKTKVVSGEYTVSST 305
                         330       340
                  ....*....|....*....|....*....
gi 1314859353 322 YSLEPDELAAGYVL--SCQalpLTSDVVV 348
Cdd:PRK10684  306 MTLTPAEIAQGYVLacSCH---PQGDLVL 331
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
266-341 4.11e-18

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 77.95  E-value: 4.11e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314859353 266 VRQDGRDREIVLNADDESILDAALRQGADLPYACKGGVCATCKCKVLRGKVAMETNYsLEPDELAAGYV-LSCQALP 341
Cdd:pfam00111   1 VTINGKGVTIEVPDGETTLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSDQSF-LEDDELAAGYVvLACQTYP 76
 
Name Accession Description Interval E-value
PA_CoA_Oxy5 TIGR02160
phenylacetate-CoA oxygenase/reductase, PaaK subunit; Phenylacetate-CoA oxygenase is comprised ...
4-351 0e+00

phenylacetate-CoA oxygenase/reductase, PaaK subunit; Phenylacetate-CoA oxygenase is comprised of a five gene complex responsible for the hydroxylation of phenylacetate-CoA (PA-CoA) as the second catabolic step in phenylacetic acid (PA) degradation. Although the exact function of this enzyme has not been determined, it has been shown to be required for phenylacetic acid degradation and has been proposed to function in a multicomponent oxygenase acting on phenylacetate-CoA. [Energy metabolism, Other]


Pssm-ID: 131215 [Multi-domain]  Cd Length: 352  Bit Score: 629.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   4 FHSLTVAKVESETRDAVTITFAVPQPLQEAYRFRPGQHLTLKASFDGEELRRCYSICRSYLPGEISVAVKAIEGGRFSRY 83
Cdd:TIGR02160   1 FHRLTVAEVERLTADAVAISFEIPDELAEDYRFAPGQHLTLRREVDGEELRRSYSICSAPAPGEIRVAVKKIPGGLFSTW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  84 AREHIRQGMTLEVMVPQGHFGYQPQAERQGRYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALAD 163
Cdd:TIGR02160  81 ANDEIRPGDTLEVMAPQGLFTPDLSTPHAGHYVAVAAGSGITPMLSIAETVLAAEPRSTFTLVYGNRRTASVMFAEELAD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 164 LKDKYPQRLQLLCIFSQETLDSDLLHGRIDGEKLQSLGASLINFRLYDEAFICGPAAMMDDAETALKALGMPDKTIHLER 243
Cdd:TIGR02160 161 LKDKHPQRFHLAHVLSREPREAPLLSGRLDGERLAALLDSLIDVDRADEWFLCGPQAMVDDAEQALTGLGVPAGRVHLEL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 244 FNT---PGTRVKRSVN-VQSDGQKVTVRQDGRDREIVLNADDESILDAALRQGADLPYACKGGVCATCKCKVLRGKVAME 319
Cdd:TIGR02160 241 FYTddePGREVRHEVSgPEGDVSKVTVTLDGRSTETSSLSRDESVLDAALRARPDLPFACKGGVCGTCRAKVLEGKVDME 320
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1314859353 320 TNYSLEPDELAAGYVLSCQALPLTSDVVVDFD 351
Cdd:TIGR02160 321 RNYALEPDEVDAGYVLTCQAYPLSDKLVVDYD 352
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
4-244 5.62e-136

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: 386.51  E-value: 5.62e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   4 FHSLTVAKVESETRDAVTITFAVPQPLQEAYRFRPGQHLTLKASFDGEELRRCYSICRSYLPGEISVAVKAIEGGRFSRY 83
Cdd:cd06214     1 FHPLTVAEVVRETADAVSITFDVPEELRDAFRYRPGQFLTLRVPIDGEEVRRSYSICSSPGDDELRITVKRVPGGRFSNW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  84 AREHIRQGMTLEVMVPQGHFGYQPQAeRQGRYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALAD 163
Cdd:cd06214    81 ANDELKAGDTLEVMPPAGRFTLPPLP-GARHYVLFAAGSGITPVLSILKTALAREPASRVTLVYGNRTEASVIFREELAD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 164 LKDKYPQRLQLLCIFSQETLDSDLLHGRIDGEKLQSLGASLINFRLYDEAFICGPAAMMDDAETALKALGMPDKTIHLER 243
Cdd:cd06214   160 LKARYPDRLTVIHVLSREQGDPDLLRGRLDAAKLNALLKNLLDATEFDEAFLCGPEPMMDAVEAALLELGVPAERIHREL 239

                  .
gi 1314859353 244 F 244
Cdd:cd06214   240 F 240
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
7-244 6.11e-125

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: 358.38  E-value: 6.11e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   7 LTVAKVESETRDAVTITFAVPQPLQeaYRFRPGQHLTLKASFDGEELRRCYSICRSYLPGEISVAVKAIEGGRFSRYARE 86
Cdd:cd06191     1 LRVAEVRSETPDAVTIVFAVPGPLQ--YGFRPGQHVTLKLDFDGEELRRCYSLCSSPAPDEISITVKRVPGGRVSNYLRE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  87 HIRQGMTLEVMVPQGHFGYQPQaeRQGRYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALADLKD 166
Cdd:cd06191    79 HIQPGMTVEVMGPQGHFVYQPQ--PPGRYLLVAAGSGITPLMAMIRATLQTAPESDFTLIHSARTPADMIFAQELRELAD 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314859353 167 KyPQRLQLLCIFSQETLDSDLLHGRIDGEklQSLGASLINFRLYDEAFICGPAAMMDDAETALKALGMPDKTIHLERF 244
Cdd:cd06191   157 K-PQRLRLLCIFTRETLDSDLLHGRIDGE--QSLGAALIPDRLEREAFICGPAGMMDAVETALKELGMPPERIHTERF 231
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
2-243 3.72e-86

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 259.72  E-value: 3.72e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   2 TTFHSLTVAKVESETRDAVTITFAVPQPLqEAYRFRPGQHLTLKASFDGEELRRCYSICRSYLPGEISVAVKAIEGGRFS 81
Cdd:COG1018     1 AGFRPLRVVEVRRETPDVVSFTLEPPDGA-PLPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVKRVPGGGGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  82 RYAREHIRQGMTLEVMVPQGHFGYQPQAERqgRYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQAL 161
Cdd:COG1018    80 NWLHDHLKVGDTLEVSGPRGDFVLDPEPAR--PLLLIAGGIGITPFLSMLRTLLARGPFRPVTLVYGARSPADLAFRDEL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 162 ADLKDKYPqRLQLLCIFSQETldsDLLHGRIDGEKLQSLGASLINfrlyDEAFICGPAAMMDDAETALKALGMPDKTIHL 241
Cdd:COG1018   158 EALAARHP-RLRLHPVLSREP---AGLQGRLDAELLAALLPDPAD----AHVYLCGPPPMMEAVRAALAELGVPEERIHF 229

                  ..
gi 1314859353 242 ER 243
Cdd:COG1018   230 ER 231
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
7-244 2.93e-53

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: 175.47  E-value: 2.93e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   7 LTVAKVESETRDAVTITFAVPQPlqEAYRFRPGQHLTLKASFDGEELRRCYSICRSylPGE---ISVAVKAIEGGRFSRY 83
Cdd:cd06215     1 LRCVKIIQETPDVKTFRFAAPDG--SLFAYKPGQFLTLELEIDGETVYRAYTLSSS--PSRpdsLSITVKRVPGGLVSNW 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  84 AREHIRQGMTLEVMVPQGHFGYQPQAERqgRYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALAD 163
Cdd:cd06215    77 LHDNLKVGDELWASGPAGEFTLIDHPAD--KLLLLSAGSGITPMMSMARWLLDTRPDADIVFIHSARSPADIIFADELEE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 164 LKDKYPQ-RLQLLCIfSQETLDSDLLHGRIDGEKLQSLgASLINFRlydEAFICGPAAMMDDAETALKALGMPDKTIHLE 242
Cdd:cd06215   155 LARRHPNfRLHLILE-QPAPGAWGGYRGRLNAELLALL-VPDLKER---TVFVCGPAGFMKAVKSLLAELGFPMSRFHQE 229

                  ..
gi 1314859353 243 RF 244
Cdd:cd06215   230 SF 231
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
9-244 2.20e-52

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: 173.56  E-value: 2.20e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   9 VAKVESETRDAVTITFavpQPLQEAYRFRPGQHLTLKASFDGEELRRCYSICRS--YLPGEISVAVKAIEGGRFSRYARE 86
Cdd:cd06216    22 VVAVRPETADMVTLTL---RPNRGWPGHRAGQHVRLGVEIDGVRHWRSYSLSSSptQEDGTITLTVKAQPDGLVSNWLVN 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  87 HIRQGMTLEVMVPQGHFgyQPQAERQGRYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALADLKD 166
Cdd:cd06216    99 HLAPGDVVELSQPQGDF--VLPDPLPPRLLLIAAGSGITPVMSMLRTLLARGPTADVVLLYYARTREDVIFADELRALAA 176
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314859353 167 KYPQ-RLQLLcifsqetLDSDLLHGRIDGEKLQSLgASLINFRlydEAFICGPAAMMDDAETALKALGMPDKtIHLERF 244
Cdd:cd06216   177 QHPNlRLHLL-------YTREELDGRLSAAHLDAV-VPDLADR---QVYACGPPGFLDAAEELLEAAGLADR-LHTERF 243
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
14-242 4.33e-52

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: 172.25  E-value: 4.33e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  14 SETRDAVTITFAVPQPLQEAYRFRPGQHLTLKASFDGEELRRCYSICRS-YLPGEISVAVKAIEGGRFSRYAREHiRQGM 92
Cdd:cd00322     1 VATEDVTDDVRLFRLQLPNGFSFKPGQYVDLHLPGDGRGLRRAYSIASSpDEEGELELTVKIVPGGPFSAWLHDL-KPGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  93 TLEVMVPQGHFGYQPqaERQGRYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALADLKdKYPQRL 172
Cdd:cd00322    80 EVEVSGPGGDFFLPL--EESGPVVLIAGGIGITPFRSMLRHLAADKPGGEITLLYGARTPADLLFLDELEELA-KEGPNF 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 173 QLLCIFSQetlDSDLLHGRIDGEKLQSLGASLINFRLYDEAFICGPAAMMDDAETALKALGMPDKTIHLE 242
Cdd:cd00322   157 RLVLALSR---ESEAKLGPGGRIDREAEILALLPDDSGALVYICGPPAMAKAVREALVSLGVPEERIHTE 223
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
6-244 4.04e-46

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: 157.04  E-value: 4.04e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   6 SLTVAKVESETRDAVTITFAVPQPlqEAYRFRPGQHLTLKASF-DGEELRRCYSICRSylPGE---ISVAVKAIEGGRFS 81
Cdd:cd06217     3 VLRVTEIIQETPTVKTFRLAVPDG--VPPPFLAGQHVDLRLTAiDGYTAQRSYSIASS--PTQrgrVELTVKRVPGGEVS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  82 RYAREHIRQGMTLEVMVPQGHFgYQPQAERQgRYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQAL 161
Cdd:cd06217    79 PYLHDEVKVGDLLEVRGPIGTF-TWNPLHGD-PVVLLAGGSGIVPLMSMIRYRRDLGWPVPFRLLYSARTAEDVIFRDEL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 162 ADLKDKYPqRLQLLCIFSQETLDSDL-LHGRIDGEKLQSLGASLINFRlydeAFICGPAAMMDDAETALKALGMPDKTIH 240
Cdd:cd06217   157 EQLARRHP-NLHVTEALTRAAPADWLgPAGRITADLIAELVPPLAGRR----VYVCGPPAFVEAATRLLLELGVPRDRIR 231

                  ....
gi 1314859353 241 LERF 244
Cdd:cd06217   232 TEAF 235
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
4-244 2.74e-45

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: 155.41  E-value: 2.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   4 FHSLTVAKVESETRDAVTITFaVPQPLQEAYRFRPGQHLTLKASFDGEELR--RCYSICRSYLPGEISVAVKAIEGGRFS 81
Cdd:cd06184     6 FRPFVVARKVAESEDITSFYL-EPADGGPLPPFLPGQYLSVRVKLPGLGYRqiRQYSLSDAPNGDYYRISVKREPGGLVS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  82 RYAREHIRQGMTLEVMVPQGHFGYQPQAERqgRYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQAL 161
Cdd:cd06184    85 NYLHDNVKVGDVLEVSAPAGDFVLDEASDR--PLVLISAGVGITPMLSMLEALAAEGPGRPVTFIHAARNSAVHAFRDEL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 162 ADLKDKYPQrLQLLCIFSQETLDSDLLH----GRIDGEKLQSLGASlinfrlyDEA--FICGPAAMMDDAETALKALGMP 235
Cdd:cd06184   163 EELAARLPN-LKLHVFYSEPEAGDREEDydhaGRIDLALLRELLLP-------ADAdfYLCGPVPFMQAVREGLKALGVP 234

                  ....*....
gi 1314859353 236 DKTIHLERF 244
Cdd:cd06184   235 AERIHYEVF 243
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
7-348 4.11e-44

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 154.87  E-value: 4.11e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   7 LTVAKVESETRDAVTITFAVpqplQEAYRFRPGQHlTLKASFDGEELRRCYSIcrSYLPGE---ISVAVKAIEGGRFSRY 83
Cdd:PRK10684   12 MQVHSIVQETPDVWTISLIC----HDFYPYRAGQY-ALVSIRNSAETLRAYTL--SSTPGVsefITLTVRRIDDGVGSQW 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  84 AREHIRQGMTLEVMVPQGHFGYQPQAErqGRYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALAD 163
Cdd:PRK10684   85 LTRDVKRGDYLWLSDAMGEFTCDDKAE--DKYLLLAAGCGVTPIMSMRRWLLKNRPQADVQVIFNVRTPQDVIFADEWRQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 164 LKDKYPQrLQLLCIFSQETLDSdLLHGRIDGEKLQSLGASLINFRLydeaFICGPAAMMDDAETALKALGMPDKTIHLER 243
Cdd:PRK10684  163 LKQRYPQ-LNLTLVAENNATEG-FIAGRLTRELLQQAVPDLASRTV----MTCGPAPYMDWVEQEVKALGVTADRFFKEK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 244 FNTPgtrvkrSVNVQSDGQKVTVRQDGRDreivLNADDESILDAALRQGaDLPY--ACKGGVCATCKCKVLRGKVAMETN 321
Cdd:PRK10684  237 FFTP------VAEAATSGLTFTKLQPARE----FYAPVGTTLLEALESN-KVPVvaACRAGVCGCCKTKVVSGEYTVSST 305
                         330       340
                  ....*....|....*....|....*....
gi 1314859353 322 YSLEPDELAAGYVL--SCQalpLTSDVVV 348
Cdd:PRK10684  306 MTLTPAEIAQGYVLacSCH---PQGDLVL 331
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
7-240 1.46e-33

Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor. Like ferredoxin reductases, these proteins have an N-terminal FAD binding subdomain and a C-terminal NADH binding subdomain, separated by a cleft, which accepts FAD. The NADH-binding moiety interacts with part of the FAD and resembles a Rossmann fold. However, NAD is bound differently than in canonical Rossmann fold proteins. Nitrate reductases, flavoproteins similar to pyridine nucleotide cytochrome reductases, catalyze the reduction of nitrate to nitrite. The enzyme can be divided into three functional fragments that bind the cofactors molybdopterin, heme-iron, and FAD/NADH.


Pssm-ID: 99780 [Multi-domain]  Cd Length: 234  Bit Score: 124.22  E-value: 1.46e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   7 LTVAKVESETRDAVTITFAVPQPLQEaYRFRPGQHLTLKASFDGEELRRCYS-ICRSYLPGEISVAVKAIEGGRFSRYAr 85
Cdd:cd06183     1 FKLVSKEDISHDTRIFRFELPSPDQV-LGLPVGQHVELKAPDDGEQVVRPYTpISPDDDKGYFDLLIKIYPGGKMSQYL- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  86 EHIRQGMTLEVMVPQGHFGYQPQaERQGRYLAIAAGSGITPMLAIIATTLQT-EPESQFTLIYGNRTSQSMMFRQALADL 164
Cdd:cd06183    79 HSLKPGDTVEIRGPFGKFEYKPN-GKVKHIGMIAGGTGITPMLQLIRAILKDpEDKTKISLLYANRTEEDILLREELDEL 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314859353 165 KDKYPQRLQLLCIFSQETLDSDLLHGRIDGEKLQSLGASLINFRLYdeAFICGPAAMMDDA-ETALKALGMPDKTIH 240
Cdd:cd06183   158 AKKHPDRFKVHYVLSRPPEGWKGGVGFITKEMIKEHLPPPPSEDTL--VLVCGPPPMIEGAvKGLLKELGYKKDNVF 232
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
9-244 1.88e-31

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: 118.08  E-value: 1.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   9 VAKVESETRDAVTITFAVPQPLqeayRFRPGQHLTLKASfDGEELRRCYSIcrSYLP---GEISVAVKAIEGGRFSRYAR 85
Cdd:cd06187     1 VVSVERLTHDIAVVRLQLDQPL----PFWAGQYVNVTVP-GRPRTWRAYSP--ANPPnedGEIEFHVRAVPGGRVSNALH 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  86 EHIRQGMTLEVMVPQGHFGYQPQAERQgrYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALADLK 165
Cdd:cd06187    74 DELKVGDRVRLSGPYGTFYLRRDHDRP--VLCIAGGTGLAPLRAIVEDALRRGEPRPVHLFFGARTERDLYDLEGLLALA 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314859353 166 DKYPqRLQLLCIFSQETLDSDLLHGRIdGEKLQSLGASLINFRLYdeafICGPAAMMDDAETALKALGMPDKTIHLERF 244
Cdd:cd06187   152 ARHP-WLRVVPVVSHEEGAWTGRRGLV-TDVVGRDGPDWADHDIY----ICGPPAMVDATVDALLARGAPPERIHFDKF 224
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
10-244 7.10e-31

Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron transfer from NADH to FMN to an iron sulfur cluster. PDR has an an N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding domain and a C-terminal iron-sulfur [2Fe-2S] cluster domain. Although structurally homologous to FNR, PDR binds FMN rather than FAD in it's FNR-like domain. Electron transfer between pyrimidines and iron-sulfur clusters (Rieske center [2Fe-2S]) or heme groups is mediated by flavins in respiration, photosynthesis, and oxygenase systems. Type I dioxygenase systems, including the hydroxylate phthalate system, have 2 components, a monomeric reductase consisting of a flavin and a 2Fe-2S center and a multimeric oxygenase. In contrast to other Rieske dioxygenases the ferredoxin like domain is C-, not N-terminal.


Pssm-ID: 99782 [Multi-domain]  Cd Length: 211  Bit Score: 116.43  E-value: 7.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  10 AKVESETRDAVTITFAVPQPLQEAyRFRPGQHLTLKAsfdGEELRRCYSICRSylPGEIS---VAVKAIEGGR-FSRYAR 85
Cdd:cd06185     1 VRIRDEAPDIRSFELEAPDGAPLP-AFEPGAHIDVHL---PNGLVRQYSLCGD--PADRDryrIAVLREPASRgGSRYMH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  86 EHIRQGMTLEVMVPQGHFgyqPQAERQGRYLAIAAGSGITPMLAIiATTLQTEPESqFTLIYGNRTSQSMMFRQALADLk 165
Cdd:cd06185    75 ELLRVGDELEVSAPRNLF---PLDEAARRHLLIAGGIGITPILSM-ARALAARGAD-FELHYAGRSREDAAFLDELAAL- 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314859353 166 dkYPQRLQLLCifsqetldsDLLHGRIDGEKLqsLGASLINFRLYdeafICGPAAMMDDAETALKALGMPDKTIHLERF 244
Cdd:cd06185   149 --PGDRVHLHF---------DDEGGRLDLAAL--LAAPPAGTHVY----VCGPEGMMDAVRAAAAALGWPEARLHFERF 210
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
5-245 1.06e-30

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 121.15  E-value: 1.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   5 HSLTVAKVESETRDAVTITFAVPQPlqEAYRFRPGQHLTLKasFDGEELRRC---YSICRSYL-PGEISVAVKAIegGRF 80
Cdd:COG4097   215 HPYRVESVEPEAGDVVELTLRPEGG--RWLGHRAGQFAFLR--FDGSPFWEEahpFSISSAPGgDGRLRFTIKAL--GDF 288
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  81 SRyAREHIRQGMTLEVMVPQGHFGYqPQAERQGRYLAIAAGSGITPMLAIIaTTLQTEPESQ--FTLIYGNRTSQSMMFR 158
Cdd:COG4097   289 TR-RLGRLKPGTRVYVEGPYGRFTF-DRRDTAPRQVWIAGGIGITPFLALL-RALAARPGDQrpVDLFYCVRDEEDAPFL 365
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 159 QALADLKDKYPQ-RLQLLCifSQETldsdllhGRIDGEKLQSLGASLINFrlydEAFICGPAAMMDDAETALKALGMPDK 237
Cdd:COG4097   366 EELRALAARLAGlRLHLVV--SDED-------GRLTAERLRRLVPDLAEA----DVFFCGPPGMMDALRRDLRALGVPAR 432

                  ....*...
gi 1314859353 238 TIHLERFN 245
Cdd:COG4097   433 RIHQERFE 440
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
15-245 1.18e-30

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: 115.82  E-value: 1.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  15 ETRDAVTITFAVPQPlqeAYRFRPGQHLTLKasFDGEELRRC--YSICRSYLP-GEISVAVKAIegGRFSRYAREHIRQG 91
Cdd:cd06198     5 EVRPTTTLTLEPRGP---ALGHRAGQFAFLR--FDASGWEEPhpFTISSAPDPdGRLRFTIKAL--GDYTRRLAERLKPG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  92 MTLEVMVPQGHFGYQPQAERQgryLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALADLKDKYPQR 171
Cdd:cd06198    78 TRVTVEGPYGRFTFDDRRARQ---IWIAGGIGITPFLALLEALAARGDARPVTLFYCVRDPEDAVFLDELRALAAAAGVV 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314859353 172 LQLLCIFSQETLDSDLLHGRIDGEKLQSlgaslinfrlydEAFICGPAAMMDDAETALKALGMPDKTIHLERFN 245
Cdd:cd06198   155 LHVIDSPSDGRLTLEQLVRALVPDLADA------------DVWFCGPPGMADALEKGLRALGVPARRFHYERFE 216
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
8-244 3.85e-29

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: 112.02  E-value: 3.85e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   8 TVAKVESETRDAVTITFAVPQPLqeayRFRPGQHLTLkaSFDGEELRRCYSICRSYLP-GEISVAVKAIEGGRFSRYARE 86
Cdd:cd06213     4 TIVAQERLTHDIVRLTVQLDRPI----AYKAGQYAEL--TLPGLPAARSYSFANAPQGdGQLSFHIRKVPGGAFSGWLFG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  87 HIRQGMTLEVMVPQGHFGYQPQAERqgrYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALADLKD 166
Cdd:cd06213    78 ADRTGERLTVRGPFGDFWLRPGDAP---ILCIAGGSGLAPILAILEQARAAGTKRDVTLLFGARTQRDLYALDEIAAIAA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 167 KYPQRLQLLCIFSQETLDSD------LLHGRIDGEKLQSLgaslinfrlydEAFICGPAAMMDDAETALKALGMPDKTIH 240
Cdd:cd06213   155 RWRGRFRFIPVLSEEPADSSwkgargLVTEHIAEVLLAAT-----------EAYLCGPPAMIDAAIAVLRALGIAREHIH 223

                  ....
gi 1314859353 241 LERF 244
Cdd:cd06213   224 ADRF 227
PRK13289 PRK13289
NO-inducible flavohemoprotein;
9-244 4.71e-28

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 112.97  E-value: 4.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   9 VAKV-ESETrdavtIT-FA-VPQPLQEAYRFRPGQHLTLKASFDGEELR--RCYSIcrSYLPGE----ISVavKAIEGGR 79
Cdd:PRK13289  160 VKKVpESEV-----ITsFYlEPVDGGPVADFKPGQYLGVRLDPEGEEYQeiRQYSL--SDAPNGkyyrISV--KREAGGK 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  80 FSRYAREHIRQGMTLEVMVPQGHFGYQPQAERQgryLA-IAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFR 158
Cdd:PRK13289  231 VSNYLHDHVNVGDVLELAAPAGDFFLDVASDTP---VVlISGGVGITPMLSMLETLAAQQPKRPVHFIHAARNGGVHAFR 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 159 QALADLKDKYPQrLQLLcIFSQETLDSDLLH------GRIDgekLQSLGASLINFRLydEAFICGPAAMMDDAETALKAL 232
Cdd:PRK13289  308 DEVEALAARHPN-LKAH-TWYREPTEQDRAGedfdseGLMD---LEWLEAWLPDPDA--DFYFCGPVPFMQFVAKQLLEL 380
                         250
                  ....*....|..
gi 1314859353 233 GMPDKTIHLERF 244
Cdd:PRK13289  381 GVPEERIHYEFF 392
Fdx COG0633
Ferredoxin [Energy production and conversion];
263-351 5.72e-28

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 104.55  E-value: 5.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 263 KVTVRQDGRDREIvlnADDESILDAALRQGADLPYACKGGVCATCKCKVLRGKVAMETNYSLEPDELAAGYVLSCQALPl 342
Cdd:COG0633     3 KVTFIPEGHTVEV---PAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQARP- 78

                  ....*....
gi 1314859353 343 TSDVVVDFD 351
Cdd:COG0633    79 TSDLVVELP 87
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
8-242 2.48e-25

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 102.25  E-value: 2.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   8 TVAKVESETRDAVTITFAVPQplqEAYRFRPGQHLTLKAsfDGEELRRCYSICRS-YLPGEISVAVKAIegGRFSRYARE 86
Cdd:COG0543     1 KVVSVERLAPDVYLLRLEAPL---IALKFKPGQFVMLRV--PGDGLRRPFSIASApREDGTIELHIRVV--GKGTRALAE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  87 hIRQGMTLEVMVPQGHFGyqPQAERQGRYLAIAAGSGITPMLAIIATTLQTEPEsqFTLIYGNRTSQSMMFRQALADLKD 166
Cdd:COG0543    74 -LKPGDELDVRGPLGNGF--PLEDSGRPVLLVAGGTGLAPLRSLAEALLARGRR--VTLYLGARTPEDLYLLDELEALAD 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1314859353 167 kypqrLQLLCIfSQEtlDSDLLHGRIdGEKLqslgASLINFRLYDEAFICGPAAMMDDAETALKALGMPDKTIHLE 242
Cdd:COG0543   149 -----FRVVVT-TDD--GWYGRKGFV-TDAL----KELLAEDSGDDVYACGPPPMMKAVAELLLERGVPPERIYVS 211
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
264-349 5.83e-24

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 94.00  E-value: 5.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 264 VTVRQDGRDREIVLNaDDESILDAALRQGADLPYACKGGVCATCKCKVLRGKVAMETNYSLEPDELAAGYVLSCQALPlT 343
Cdd:cd00207     1 VTINVPGSGVEVEVP-EGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYVLACQTRV-T 78

                  ....*.
gi 1314859353 344 SDVVVD 349
Cdd:cd00207    79 DGLVIE 84
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
18-240 9.55e-24

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


Pssm-ID: 99791 [Multi-domain]  Cd Length: 222  Bit Score: 97.34  E-value: 9.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  18 DAVTITFAVPQPLqeayRFRPGQHLTLKaSFDGeeLRRCYSIcrSYLPGE---ISVAVKAIEGGRFSRYAREHIRQGMTL 94
Cdd:cd06194    10 DVLRVRLEPDRPL----PYLPGQYVNLR-RAGG--LARSYSP--TSLPDGdneLEFHIRRKPNGAFSGWLGEEARPGHAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  95 EVMVPQGHFGYQPqAERQGRYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALADLKDKYPQRLQL 174
Cdd:cd06194    81 RLQGPFGQAFYRP-EYGEGPLLLVGAGTGLAPLWGIARAALRQGHQGEIRLVHGARDPDDLYLHPALLWLAREHPNFRYI 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1314859353 175 LCIFSQETLDSDLLHGRIDGEKLQSLGAslinfrlyDEAFICGPAAMMDDAETALKALGMPDKTIH 240
Cdd:cd06194   160 PCVSEGSQGDPRVRAGRIAAHLPPLTRD--------DVVYLCGAPSMVNAVRRRAFLAGAPMKRIY 217
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
8-244 4.52e-23

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: 96.24  E-value: 4.52e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   8 TVAKVESETRDAVTITFAVPQPlqEAYRFRPGQHLTLKASfdGEELRRCYSICRSylP---GEISVAVKAIEGGRFSRYA 84
Cdd:cd06211    10 TVVEIEDLTPTIKGVRLKLDEP--EEIEFQAGQYVNLQAP--GYEGTRAFSIASS--PsdaGEIELHIRLVPGGIATTYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  85 REHIRQGMTLEVMVPQGHFGYQPQAERQgrYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALADL 164
Cdd:cd06211    84 HKQLKEGDELEISGPYGDFFVRDSDQRP--IIFIAGGSGLSSPRSMILDLLERGDTRKITLFFGARTRAELYYLDEFEAL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 165 KDKYPqRLQLLCIFSQETLDSD--LLHGRIDgeklQSLGASLINFRLYDEAFICGPAAMMDDAETALKALGMPDKTIHLE 242
Cdd:cd06211   162 EKDHP-NFKYVPALSREPPESNwkGFTGFVH----DAAKKHFKNDFRGHKAYLCGPPPMIDACIKTLMQGRLFERDIYYE 236

                  ..
gi 1314859353 243 RF 244
Cdd:cd06211   237 KF 238
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
9-240 5.63e-23

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: 95.31  E-value: 5.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   9 VAKVESETRDAVTITFAVPQPLQeayrFRPGQHLTLKasFDGEElRRCYSIC-RSYLPGEISVAVKAIEGGRFSRYAREH 87
Cdd:cd06189     3 VESIEPLNDDVYRVRLKPPAPLD----FLAGQYLDLL--LDDGD-KRPFSIAsAPHEDGEIELHIRAVPGGSFSDYVFEE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  88 IRQGMTLEVMVPQGHFGYQPQAERQgrYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALADLKDK 167
Cdd:cd06189    76 LKENGLVRIEGPLGDFFLREDSDRP--LILIAGGTGFAPIKSILEHLLAQGSKRPIHLYWGARTEEDLYLDELLEAWAEA 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314859353 168 YPQrLQLLCIFSQETLDSDllhGRIdGEKLQSLGASLINFRLYDeAFICGPAAMMDDAETALKALGMPDKTIH 240
Cdd:cd06189   154 HPN-FTYVPVLSEPEEGWQ---GRT-GLVHEAVLEDFPDLSDFD-VYACGSPEMVYAARDDFVEKGLPEENFF 220
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
5-242 7.45e-21

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: 89.61  E-value: 7.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   5 HSLTVAKVESETRDAVTITFAVPqplqEAYRFRPGQ--HLTLKAsfDG-EELRRCYSIcrSYLPG----EISVAVKAIEG 77
Cdd:cd06196     1 HTVTLLSIEPVTHDVKRLRFDKP----EGYDFTPGQatEVAIDK--PGwRDEKRPFTF--TSLPEddvlEFVIKSYPDHD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  78 GRFSRYARehIRQGMTLEVMVPQGHFGYQpqaerqGRYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMF 157
Cdd:cd06196    73 GVTEQLGR--LQPGDTLLIEDPWGAIEYK------GPGVFIAGGAGITPFIAILRDLAAKGKLEGNTLIFANKTEKDIIL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 158 RQALadlkDKYPQrLQLLCIFSQETlDSDLLHGRIDGEKLQSLgasLINFRlyDEAFICGPAAMMDDAETALKALGMPDK 237
Cdd:cd06196   145 KDEL----EKMLG-LKFINVVTDEK-DPGYAHGRIDKAFLKQH---VTDFN--QHFYVCGPPPMEEAINGALKELGVPED 213

                  ....*
gi 1314859353 238 TIHLE 242
Cdd:cd06196   214 SIVFE 218
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
263-349 6.85e-20

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 89.16  E-value: 6.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 263 KVTVRQDGRDREIvlnADDESILDAALRQGADLPYACKGGVCATCKCKVLRGKVAMETNYS--LEPDELAAGYVLSCQAL 340
Cdd:PRK07609    4 QVTLQPSGRQFTA---EPDETILDAALRQGIHLPYGCKNGACGSCKGRLLEGEVEQGPHQAsaLSGEERAAGEALTCCAK 80

                  ....*....
gi 1314859353 341 PLtSDVVVD 349
Cdd:PRK07609   81 PL-SDLVLE 88
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
32-244 7.30e-20

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: 87.24  E-value: 7.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  32 EAYRFRPGQHLTLK-ASFDGEELRRCYSICRSYLPGEISVAVKAIEGGRFSryAR-EHIRQGMTLEVMV-PQGHF--GYQ 106
Cdd:cd06195    21 IPFRFQAGQFTKLGlPNDDGKLVRRAYSIASAPYEENLEFYIILVPDGPLT--PRlFKLKPGDTIYVGKkPTGFLtlDEV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 107 PQAERqgrYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALADLKDKYPQRLQLLCIFSQETLDSD 186
Cdd:cd06195    99 PPGKR---LWLLATGTGIAPFLSMLRDLEIWERFDKIVLVHGVRYAEELAYQDEIEALAKQYNGKFRYVPIVSREKENGA 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314859353 187 lLHGRI-----DGEKLQSLGASLINFRlyDEAFICGPAAMMDDAETALKALG-MPD-----KTIHLERF 244
Cdd:cd06195   176 -LTGRIpdlieSGELEEHAGLPLDPET--SHVMLCGNPQMIDDTQELLKEKGfSKNhrrkpGNITVEKY 241
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
16-244 2.12e-19

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: 85.77  E-value: 2.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  16 TRDAVTITFAVPQPLqeayRFRPGQHLTLkaSFDGEELRRCYSICRsyLP---GEISVAVKAIEGGRFSRYAREHIRQGM 92
Cdd:cd06190     8 THDVAEFRFALDGPA----DFLPGQYALL--ALPGVEGARAYSMAN--LAnasGEWEFIIKRKPGGAASNALFDNLEPGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  93 TLEVMVPQGHFGYQPQAERQgrYLAIAAGSGITPMLAIIATTLQT--EPESQFTLIYGNRTSQSMMFRQALADLKDkYPQ 170
Cdd:cd06190    80 ELELDGPYGLAYLRPDEDRD--IVCIAGGSGLAPMLSILRGAARSpyLSDRPVDLFYGGRTPSDLCALDELSALVA-LGA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 171 RLQLLCIFSQETLDSDLLhgrIDGEK-------LQSLGASLINFrlydEAFICGPAAMMDDA-ETALKALGMPDKTIHLE 242
Cdd:cd06190   157 RLRVTPAVSDAGSGSAAG---WDGPTgfvhevvEATLGDRLAEF----EFYFAGPPPMVDAVqRMLMIEGVVPFDQIHFD 229

                  ..
gi 1314859353 243 RF 244
Cdd:cd06190   230 RF 231
petF CHL00134
ferredoxin; Validated
263-348 2.27e-19

ferredoxin; Validated


Pssm-ID: 177056 [Multi-domain]  Cd Length: 99  Bit Score: 82.08  E-value: 2.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 263 KVTVRQDGRDREIVLN-ADDESILDAALRQGADLPYACKGGVCATCKCKVLRGKVAMETNYSLEPDELAAGYVLSCQALP 341
Cdd:CHL00134    5 KVTLLSEEEGIDVTIDcPDDVYILDAAEEQGIDLPYSCRAGACSTCAGKVTEGTVDQSDQSFLDDDQLEAGFVLTCVAYP 84

                  ....*..
gi 1314859353 342 lTSDVVV 348
Cdd:CHL00134   85 -TSDCTI 90
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
8-244 2.55e-19

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: 85.46  E-value: 2.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   8 TVAKVESETRDAVTITFAVPQPlqEAYRFRPGQHLTLkaSFDGEELRRCYSI-CRSYLPGEISVAVKAIEGGRFSRYARE 86
Cdd:cd06212     4 TVVAVEALTHDIRRLRLRLEEP--EPIKFFAGQYVDI--TVPGTEETRSFSMaNTPADPGRLEFIIKKYPGGLFSSFLDD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  87 HIRQGMTLEVMVPQGHFGYQpqAERQGRYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALADLKD 166
Cdd:cd06212    80 GLAVGDPVTVTGPYGTCTLR--ESRDRPIVLIGGGSGMAPLLSLLRDMAASGSDRPVRFFYGARTARDLFYLEEIAALGE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 167 KYPQrLQLLCIFSQETlDSDLLHGR------IDGEKLQSLGASlinfrlydEAFICGPAAMMDDAETALKALGMPDKTIH 240
Cdd:cd06212   158 KIPD-FTFIPALSESP-DDEGWSGEtglvteVVQRNEATLAGC--------DVYLCGPPPMIDAALPVLEMSGVPPDQIF 227

                  ....
gi 1314859353 241 LERF 244
Cdd:cd06212   228 YDKF 231
PTZ00038 PTZ00038
ferredoxin; Provisional
230-348 1.47e-18

ferredoxin; Provisional


Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 82.58  E-value: 1.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 230 KALGMPDKTIHLERFN------TPGTRVKR---SVNVQSDGQKVTVRQDgrDREIVLNAD-DESILDAALRQGADLPYAC 299
Cdd:PTZ00038   55 RASCYSLGNSKGNTSRpssngvTPGSSPVRsllSLRRNPLFYNITLQTP--DGEKVIECDeDEYILDAAERQGVELPYSC 132
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1314859353 300 KGGVCATCKCKVLRGKVAMETNYSLEPDELAAGYVLSCQALPlTSDVVV 348
Cdd:PTZ00038  133 RGGSCSTCAAKLLEGEVDNEDQSYLDDEQLKKGYCLLCTCYP-KSDCTI 180
fdx_plant TIGR02008
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ...
263-348 1.69e-18

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


Pssm-ID: 273926 [Multi-domain]  Cd Length: 97  Bit Score: 79.42  E-value: 1.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 263 KVT-VRQDGRDREIVLNaDDESILDAALRQGADLPYACKGGVCATCKCKVLRGKVAMETNYSLEPDELAAGYVLSCQALP 341
Cdd:TIGR02008   4 KVTlVNPDGGEETIECP-DDQYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQSDQSFLDDDQMEAGYVLTCVAYP 82

                  ....*..
gi 1314859353 342 lTSDVVV 348
Cdd:TIGR02008  83 -TSDCTI 88
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
5-245 3.99e-18

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: 82.26  E-value: 3.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   5 HSLTVAKVESETRDAVTITFAVPQplQEAYRFRPGQHLTLKASfdGEELRRCYSIcrSYLPG--EISVAVKAIEGGRFSR 82
Cdd:cd06209     2 FEATVTEVERLSDSTIGLTLELDE--AGALAFLPGQYVNLQVP--GTDETRSYSF--SSAPGdpRLEFLIRLLPGGAMSS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  83 YAREHIRQGMTLEVMVPQGHFGYQpqaERQGRYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALA 162
Cdd:cd06209    76 YLRDRAQPGDRLTLTGPLGSFYLR---EVKRPLLMLAGGTGLAPFLSMLDVLAEDGSAHPVHLVYGVTRDADLVELDRLE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 163 DLKDKYPQRLQLLCIFSQETldsdlLHGR-------IDGEKLQSLGAslinfrlydEAFICGPAAMMDDAETALKALGMP 235
Cdd:cd06209   153 ALAERLPGFSFRTVVADPDS-----WHPRkgyvtdhLEAEDLNDGDV---------DVYLCGPPPMVDAVRSWLDEQGIE 218
                         250
                  ....*....|
gi 1314859353 236 DKTIHLERFN 245
Cdd:cd06209   219 PANFYYEKFT 228
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
266-341 4.11e-18

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 77.95  E-value: 4.11e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314859353 266 VRQDGRDREIVLNADDESILDAALRQGADLPYACKGGVCATCKCKVLRGKVAMETNYsLEPDELAAGYV-LSCQALP 341
Cdd:pfam00111   1 VTINGKGVTIEVPDGETTLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSDQSF-LEDDELAAGYVvLACQTYP 76
PLN02252 PLN02252
nitrate reductase [NADPH]
39-239 4.33e-18

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 85.50  E-value: 4.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  39 GQHLTLKASFDGEELRRCYS-ICRSYLPGEISVAVKAI---------EGGRFSRYArEHIRQGMTLEVMVPQGHFGYqpq 108
Cdd:PLN02252  668 GKHVFLCATINGKLCMRAYTpTSSDDEVGHFELVIKVYfknvhpkfpNGGLMSQYL-DSLPIGDTIDVKGPLGHIEY--- 743
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 109 aERQGRYLA------------IAAGSGITPMLAIIATTLQT-EPESQFTLIYGNRTSQSMMFRQALADLKDKYPQRLQLL 175
Cdd:PLN02252  744 -AGRGSFLVngkpkfakklamLAGGTGITPMYQVIQAILRDpEDKTEMSLVYANRTEDDILLREELDRWAAEHPDRLKVW 822
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314859353 176 CIFSQeTLDSDLLH--GRIDGEKLQSLGaslinFRLYDE--AFICGPAAMMDDAET-ALKALGMPDKTI 239
Cdd:PLN02252  823 YVVSQ-VKREGWKYsvGRVTEAMLREHL-----PEGGDEtlALMCGPPPMIEFACQpNLEKMGYDKDSI 885
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
10-244 1.22e-16

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: 78.15  E-value: 1.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  10 AKVESETRDAVTITFAVPQPLQE-----AYRFRPGQHLTLkaSFDGEELRRCYSIcrSYLP---GEISVAVKAIEGGRFS 81
Cdd:cd06210     4 AEIVAVDRVSSNVVRLRLQPDDAegagiAAEFVPGQFVEI--EIPGTDTRRSYSL--ANTPnwdGRLEFLIRLLPGGAFS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  82 RYAREHIRQGMTLEVMVPQGHFGYQPQAERQgRYLaIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQAL 161
Cdd:cd06210    80 TYLETRAKVGQRLNLRGPLGAFGLRENGLRP-RWF-VAGGTGLAPLLSMLRRMAEWGEPQEARLFFGVNTEAELFYLDEL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 162 ADLKDKYPQrLQLLCIFSQETLDSDLLHGRIDGEKLQSLGASLINFRLYdeafICGPAAMMDDAETALKALGMPDKTIHL 241
Cdd:cd06210   158 KRLADSLPN-LTVRICVWRPGGEWEGYRGTVVDALREDLASSDAKPDIY----LCGPPGMVDAAFAAAREAGVPDEQVYL 232

                  ...
gi 1314859353 242 ERF 244
Cdd:cd06210   233 EKF 235
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
253-348 1.73e-16

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: 79.91  E-value: 1.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 253 RSVNVQSDGQKVTVRQDGRDREIvlnADDESILDAALRQGADLPYAC-KGGVCATCKCKVLRGKVAM---ETNYsLEPDE 328
Cdd:COG2871    26 KSKLVPSGEVKITINGDGKEIEV---EEGQTLLDALLRQGIFLPSACgGGGTCGQCKVKVLEGGGDIlptETFH-LSDRE 101
                          90       100
                  ....*....|....*....|
gi 1314859353 329 LAAGYVLSCQALPlTSDVVV 348
Cdd:COG2871   102 RKEGYRLACQVKV-KSDMEI 120
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
9-243 1.21e-15

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: 75.72  E-value: 1.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   9 VAKVESETRDAVTITFAVPQPLQEAYRFRPGQHLTLKASFDGEelrRCYSICRS-YLPGEISVAVKAIegGRFSRyAREH 87
Cdd:cd06221     1 IVEVVDETEDIKTFTLRLEDDDEELFTFKPGQFVMLSLPGVGE---APISISSDpTRRGPLELTIRRV--GRVTE-ALHE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  88 IRQGMTLEVMVPQG-HFgyqPQAERQGR-YLAIAAGSGITPMLAIIATTL-QTEPESQFTLIYGNRTSQSMMFRQALADL 164
Cdd:cd06221    75 LKPGDTVGLRGPFGnGF---PVEEMKGKdLLLVAGGLGLAPLRSLINYILdNREDYGKVTLLYGARTPEDLLFKEELKEW 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 165 KDKypQRLQLLCIFSQETLDSDLLHGRIdGEKLQSLGASLINFRlydeAFICGPAAMMDDAETALKALGMPDKTIH--LE 242
Cdd:cd06221   152 AKR--SDVEVILTVDRAEEGWTGNVGLV-TDLLPELTLDPDNTV----AIVCGPPIMMRFVAKELLKLGVPEEQIWvsLE 224

                  .
gi 1314859353 243 R 243
Cdd:cd06221   225 R 225
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
118-225 2.66e-14

Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity.


Pssm-ID: 425503 [Multi-domain]  Cd Length: 109  Bit Score: 68.44  E-value: 2.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 118 IAAGSGITPMLAIIATTLQ-TEPESQFTLIYGNRTSQSMMFRQALADLKDKYPQRLQLLCIFSQETLDSDLLHGRIDGEK 196
Cdd:pfam00175   2 IAGGTGIAPVRSMLRAILEdPKDPTQVVLVFGNRNEDDILYREELDELAEKHPGRLTVVYVVSRPEAGWTGGKGRVQDAL 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 1314859353 197 L-QSLGASLINFRLYdeafICGPAAMMDDA 225
Cdd:pfam00175  82 LeDHLSLPDEETHVY----VCGPPGMIKAV 107
PLN03136 PLN03136
Ferredoxin; Provisional
280-349 2.24e-13

Ferredoxin; Provisional


Pssm-ID: 178681 [Multi-domain]  Cd Length: 148  Bit Score: 67.08  E-value: 2.24e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 280 DDESILDAALRQGADLPYACKGGVCATCKCKVLRGKVAMETNYSLEPDELAAGYVLSCQALPlTSDVVVD 349
Cdd:PLN03136   72 EDVYVLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSIDQSDQSFLDDEQISEGYVLTCVAYP-TSDVVIE 140
COG3894 COG3894
Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain ...
263-349 1.33e-12

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


Pssm-ID: 443101 [Multi-domain]  Cd Length: 621  Bit Score: 68.68  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 263 KVTVRQDGRDREIVLNADdESILDAALRQGADLPYACKG-GVCATCKCKVLRGKVAM----ETNYsLEPDELAAGYVLSC 337
Cdd:COG3894     3 KVKVTFLPSGKRVEVEAG-TTLLDAAREAGVDIDAPCGGrGTCGKCKVKVEEGEFSPvteeERRL-LSPEELAEGYRLAC 80
                          90
                  ....*....|..
gi 1314859353 338 QALPLtSDVVVD 349
Cdd:COG3894    81 QARVL-GDLVVE 91
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
6-105 2.28e-12

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 62.60  E-value: 2.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   6 SLTVAKVESETRDAVTITFAVPQPLQEaYRFRPGQHLTLKASFDGEELRRCYS-ICRSYLPGEISVAVKAIEGGRFSRYA 84
Cdd:pfam00970   1 PLTLVEKELVSHDTRIFRFALPHPDQV-LGLPVGQHLFLRLPIDGELVIRSYTpISSDDDKGYLELLVKVYPGGKMSQYL 79
                          90       100
                  ....*....|....*....|.
gi 1314859353  85 REhIRQGMTLEVMVPQGHFGY 105
Cdd:pfam00970  80 DE-LKIGDTIDFKGPLGRFEY 99
PTZ00319 PTZ00319
NADH-cytochrome B5 reductase; Provisional
2-225 6.37e-12

NADH-cytochrome B5 reductase; Provisional


Pssm-ID: 173521 [Multi-domain]  Cd Length: 300  Bit Score: 65.62  E-value: 6.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   2 TTFHSLTVAKVESETRDAVTITFAVPQPLQeAYRFRPGQHLTLKASFDGEElrRCYSICRSYLP-------GEISVAVKA 74
Cdd:PTZ00319   31 DMFQHFKLIKKTEVTHDTFIFRFALHSPTQ-RLGLPIGQHIVFRCDCTTPG--KPETVQHSYTPissddekGYVDFLIKV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  75 I---------EGGRFSRYArEHIRQGMTLEVMVPQGHFGY-------------QPQAERQGRYLAIAAGSGITPMLAIIA 132
Cdd:PTZ00319  108 YfkgvhpsfpNGGRLSQHL-YHMKLGDKIEMRGPVGKFEYlgngtytvhkgkgGLKTMHVDAFAMIAGGTGITPMLQIIH 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 133 TTLQT-EPESQFTLIYGNRTSQSMMFRQALADL-KDKypqRLQLLCIFSQE-TLDSDLLHGRIDGEKLQSLGASLINFRL 209
Cdd:PTZ00319  187 AIKKNkEDRTKVFLVYANQTEDDILLRKELDEAaKDP---RFHVWYTLDREaTPEWKYGTGYVDEEMLRAHLPVPDPQNS 263
                         250
                  ....*....|....*....
gi 1314859353 210 YDE---AFICGPAAMMDDA 225
Cdd:PTZ00319  264 GIKkvmALMCGPPPMLQMA 282
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
87-244 1.02e-08

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: 55.77  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  87 HIRQGMTLEVMVPQGHFgYQPQAERQGRYlaIAAGSGITPMLAIIATTLQTE-PESQFTLIYGNRTSQSMMFRQALADLK 165
Cdd:cd06188   128 NLKPGDKVTASGPFGEF-FIKDTDREMVF--IGGGAGMAPLRSHIFHLLKTLkSKRKISFWYGARSLKELFYQEEFEALE 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 166 DKYPqRLQLLCIFS--QETLDSDLLHGRIDGEKLQSLGAslINFRLYD-EAFICGPAAMMDDAETALKALGMPDKTIHLE 242
Cdd:cd06188   205 KEFP-NFKYHPVLSepQPEDNWDGYTGFIHQVLLENYLK--KHPAPEDiEFYLCGPPPMNSAVIKMLDDLGVPRENIAFD 281

                  ..
gi 1314859353 243 RF 244
Cdd:cd06188   282 DF 283
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
36-222 9.00e-08

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 52.57  E-value: 9.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  36 FRPGQHLTLKASFDGEELRRCYSICrsYL-PGEISVAVKAIegGRFSRYAREhIRQGMTLEVMVPQGHfGYQPQaERQGR 114
Cdd:PRK00054   32 MKPGQFVMVWVPGVEPLLERPISIS--DIdKNEITILYRKV--GEGTKKLSK-LKEGDELDIRGPLGN-GFDLE-EIGGK 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 115 YLAIAAGSGITPMLAiIATTLqTEPESQFTLIYGNRTSQSMMFRQALADLKDKYPQrlqllcifsqeTLD-SDLLHGRID 193
Cdd:PRK00054  105 VLLVGGGIGVAPLYE-LAKEL-KKKGVEVTTVLGARTKDEVIFEEEFAKVGDVYVT-----------TDDgSYGFKGFVT 171
                         170       180
                  ....*....|....*....|....*....
gi 1314859353 194 gEKLQSLGASlinfrlYDEAFICGPAAMM 222
Cdd:PRK00054  172 -DVLDELDSE------YDAIYSCGPEIMM 193
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
281-351 3.12e-07

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 51.67  E-value: 3.12e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314859353 281 DESILDAALRQGADLPYACKGGVCATCKCKVLRGKVAME--TNYSLEPDELAAGYVLSCQAlPLTSDVVVDFD 351
Cdd:PRK11872   22 DELLLDAALRNGINLPLDCREGVCGTCQGRCESGIYSQDyvDEDALSERDLAQRKMLACQT-RVKSDAAFYFD 93
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
7-222 5.32e-07

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


Pssm-ID: 99816 [Multi-domain]  Cd Length: 233  Bit Score: 49.94  E-value: 5.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   7 LTVAKVESETRDAVTITFavpqplQEAYRFRPGQHLTLKASFDGEelrRCYSIcrSYLPGEISVAVKAIegGRFSRYARE 86
Cdd:cd06220     1 VTIKEVIDETPTVKTFVF------DWDFDFKPGQFVMVWVPGVDE---IPMSL--SYIDGPNSITVKKV--GEATSALHD 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  87 hIRQGMTLEVMVPQGHfGYQPqaeRQGRYLAIAAGSGITPMLAIIAttlQTEPESQFTLIYGNRTSQSMMFRQALADLKD 166
Cdd:cd06220    68 -LKEGDKLGIRGPYGN-GFEL---VGGKVLLIGGGIGIAPLAPLAE---RLKKAADVTVLLGARTKEELLFLDRLRKSDE 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 167 KYpqrlqlLCI----FSQETLDSDLLHgRIDGEKlqslgaslinfrlYDEAFICGPAAMM 222
Cdd:cd06220   140 LI------VTTddgsYGFKGFVTDLLK-ELDLEE-------------YDAIYVCGPEIMM 179
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
36-244 8.67e-07

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 50.13  E-value: 8.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  36 FRPGQHLTLKASfdGEELRRCYSICRSYLPG-EISVAVKAIEGGRFSRYAREHIRQGMTLEVMVPQGHFgYQPQAERQgr 114
Cdd:PRK11872  137 FLPGQYARLQIP--GTDDWRSYSFANRPNATnQLQFLIRLLPDGVMSNYLRERCQVGDEILFEAPLGAF-YLREVERP-- 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 115 YLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALAdlkdKYPQRLQllcIFSQETLDSD-------- 186
Cdd:PRK11872  212 LVFVAGGTGLSAFLGMLDELAEQGCSPPVHLYYGVRHAADLCELQRLA----AYAERLP---NFRYHPVVSKasadwqgk 284
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 187 --LLHGRIDGEKLQSLGASLinfrlydeaFICGPAAMMDDAETALKALGMPDKTIHLERF 244
Cdd:PRK11872  285 rgYIHEHFDKAQLRDQAFDM---------YLCGPPPMVEAVKQWLDEQALENYRLYYEKF 335
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
9-244 1.03e-06

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: 48.84  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   9 VAKVES-ETRDAVTITFAVPQPLqeayRFRPGQHLTLkasfdgeelrRCYSICRSY-------------LPGEISVAVKA 74
Cdd:cd06186     1 IATVELlPDSDVIRLTIPKPKPF----KWKPGQHVYL----------NFPSLLSFWqshpftiasspedEQDTLSLIIRA 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  75 IEGG--RFSRYAREHIRQGMTLEVMVpQGHFGYQPQ-AERQGRYLAIAAGSGITPMLAIIAttlqtepesqfTLIYGNRT 151
Cdd:cd06186    67 KKGFttRLLRKALKSPGGGVSLKVLV-EGPYGSSSEdLLSYDNVLLVAGGSGITFVLPILR-----------DLLRRSSK 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 152 SQSmmfrqaladlkdkyPQRLQLLCI---FSQETLDSDLLHgridgeKLQSLGAsLINFRLY-DEAFICGPAAMMDDAET 227
Cdd:cd06186   135 TSR--------------TRRVKLVWVvrdREDLEWFLDELR------AAQELEV-DGEIEIYvTRVVVCGPPGLVDDVRN 193
                         250
                  ....*....|....*..
gi 1314859353 228 ALKALGMPDKTIHLERF 244
Cdd:cd06186   194 AVAKKGGTGVEFHEESF 210
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
9-235 2.63e-06

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 48.71  E-value: 2.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   9 VAKVESETRDAVTITFAVPQplQEAYRFRPGQHLTLKASfDGEelRRCYSICRS-YLPGEISVAVKAIEGGRFSRYAREH 87
Cdd:PRK07609  107 VASLERVAGDVMRLKLRLPA--TERLQYLAGQYIEFILK-DGK--RRSYSIANApHSGGPLELHIRHMPGGVFTDHVFGA 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  88 IRQGMTLEVMVPQGHFGYQpqAERQGRYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSmMFRQALADLKDK 167
Cdd:PRK07609  182 LKERDILRIEGPLGTFFLR--EDSDKPIVLLASGTGFAPIKSIVEHLRAKGIQRPVTLYWGARRPED-LYLSALAEQWAE 258
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314859353 168 YPQRLQLLCIFSQETLDSD------LLHGRIdgekLQSLgASLINFRLYdeafICGPAAMMDDAETALKALGMP 235
Cdd:PRK07609  259 ELPNFRYVPVVSDALDDDAwtgrtgFVHQAV----LEDF-PDLSGHQVY----ACGSPVMVYAARDDFVAAGLP 323
PTZ00274 PTZ00274
cytochrome b5 reductase; Provisional
118-174 1.69e-04

cytochrome b5 reductase; Provisional


Pssm-ID: 140300  Cd Length: 325  Bit Score: 42.98  E-value: 1.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314859353 118 IAAGSGITPMLAIIATTLQTEPES------QFTLIYGNRTSQSMMFRQALADLKDKYPQRLQL 174
Cdd:PTZ00274  165 IAGGTGFTPMLQIIRHSLTEPWDSgevdrtKLSFLFCNRTERHILLKGLFDDLARRYSNRFKV 227
PRK10713 PRK10713
2Fe-2S ferredoxin-like protein;
264-343 3.04e-04

2Fe-2S ferredoxin-like protein;


Pssm-ID: 182668 [Multi-domain]  Cd Length: 84  Bit Score: 38.94  E-value: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 264 VTVRQDGRDreivLNADDE--SILDAALRQGADLPYACKGGVCATCKCKVLRGKVAmetnYSLEPdeLA---AGYVLSCQ 338
Cdd:PRK10713    4 VTLRITGTQ----LLCQDEhpSLLAALESHNVAVEYQCREGYCGSCRTRLVAGQVD----WIAEP--LAfiqPGEILPCC 73

                  ....*
gi 1314859353 339 ALPLT 343
Cdd:PRK10713   74 CRAKG 78
PRK05713 PRK05713
iron-sulfur-binding ferredoxin reductase;
279-338 3.72e-04

iron-sulfur-binding ferredoxin reductase;


Pssm-ID: 235575 [Multi-domain]  Cd Length: 312  Bit Score: 42.02  E-value: 3.72e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 279 ADDESILDAALRQGADLPYACKGGVCATCKCKVLRGKVAMETNYSLEPDELAAGYVLSCQ 338
Cdd:PRK05713   14 PAGSNLLDALNAAGVAVPYSCRAGSCHACLVRCLQGEPEDALPEALAAEKREQGWRLACQ 73
fre PRK08051
FMN reductase; Validated
8-170 8.06e-04

FMN reductase; Validated


Pssm-ID: 236142 [Multi-domain]  Cd Length: 232  Bit Score: 40.22  E-value: 8.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353   8 TVAKVESETrDAVTITFAVPQplqEAYRFRPGQHLTLKAsfdGEELRRCYSICRSylP---GEISVAVKAIEGgrfSRYA 84
Cdd:PRK08051    6 KVTSVEAIT-DTVYRVRLVPE---APFSFRAGQYLMVVM---GEKDKRPFSIAST--PrekGFIELHIGASEL---NLYA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  85 R---EHIRQGMTLEVMVPQGHFGYQPQAERQgrYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQAL 161
Cdd:PRK08051   74 MavmERILKDGEIEVDIPHGDAWLREESERP--LLLIAGGTGFSYARSILLTALAQGPNRPITLYWGGREEDHLYDLDEL 151

                  ....*....
gi 1314859353 162 ADLKDKYPQ 170
Cdd:PRK08051  152 EALALKHPN 160
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
50-229 2.65e-03

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


Pssm-ID: 99798 [Multi-domain]  Cd Length: 289  Bit Score: 39.23  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353  50 GEELRRCYSICRSYLPGEISVAVKAIEGGRFSRYAREhIRQGMTLEVMVpQGHFGYQPQAERQGRYLaIAAGSGITPMLA 129
Cdd:cd06201    96 GSDVPRFYSLASSSSDGFLEICVRKHPGGLCSGYLHG-LKPGDTIKAFI-RPNPSFRPAKGAAPVIL-IGAGTGIAPLAG 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314859353 130 IIATTLQTEPesqFTLIYGNRTSQS-MMFRQALAD-LKDKypqRL-QLLCIFSQETLDS---DLLhgRIDGEKLQSL--- 200
Cdd:cd06201   173 FIRANAARRP---MHLYWGGRDPASdFLYEDELDQyLADG---RLtQLHTAFSRTPDGAyvqDRL--RADAERLRRLied 244
                         170       180
                  ....*....|....*....|....*....
gi 1314859353 201 GASLInfrlydeafICGPAAMMDDAETAL 229
Cdd:cd06201   245 GAQIM---------VCGSRAMAQGVAAVL 264
 
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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