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Conserved domains on  [gi|488256378|ref|WP_002327586|]
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MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Enterococcus]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 11441299)

NAD(P)/FAD-dependent oxidoreductase catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant; similar to sulfide:quinone oxidoreductase which catalyzes the oxidation of hydrogen sulfide using quinone as the electron acceptor

EC:  1.6.-.-
Gene Ontology:  GO:0003954|GO:0006116
PubMed:  15590775|28181562

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
3-392 2.19e-139

NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];


:

Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 411.83  E-value: 2.19e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378   3 KQNIVVVGAGYAGVSATKYLAKKLKKeDVAITLIDRHSYHTMMTELHEVAGGRVEPEAIQYDLQHLFARQkNVQLVTDTV 82
Cdd:COG1252    1 MKRIVIVGGGFAGLEAARRLRKKLGG-DAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRA-GVRFIQGEV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378  83 IGIDKEQKIVKTKLG-SYPFDQLILGMGGEPNDFGTPGVKAHGFTLWSFEDSVRIREHIEKTVAKAAlepddelRKAMLT 161
Cdd:COG1252   79 TGIDPEARTVTLADGrTLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERAE-------RRRLLT 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 162 FVVCGSGFTGIEMIGELIDWKNRLAKDYKLDPNEITLMVVEAMPTILNMLDRNDAAKAERYLRKHNVELLLNAPIVEVAA 241
Cdd:COG1252  152 IVVVGGGPTGVELAGELAELLRKLLRYPGIDPDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDA 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 242 DHIKLKDGRNIPTHTLIWTAGVKGTSDAADFGLESARGQRLIANEYMQAKGYEdkNIYIIGDLVFYEEFPGTPTPQIVQA 321
Cdd:COG1252  232 DGVTLEDGEEIPADTVIWAAGVKAPPLLADLGLPTDRRGRVLVDPTLQVPGHP--NVFAIGDCAAVPDPDGKPVPKTAQA 309

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488256378 322 AEQTGHTAAANIVASIKGGEKHKFKGNYQGFMVSIGAKWGVANLFdKIHLSGFLAIVMKHIVNLKYFFDIR 392
Cdd:COG1252  310 AVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVG-GLKLSGFLAWLLKRAIHLYFLPGFR 379
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
3-392 2.19e-139

NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 411.83  E-value: 2.19e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378   3 KQNIVVVGAGYAGVSATKYLAKKLKKeDVAITLIDRHSYHTMMTELHEVAGGRVEPEAIQYDLQHLFARQkNVQLVTDTV 82
Cdd:COG1252    1 MKRIVIVGGGFAGLEAARRLRKKLGG-DAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRA-GVRFIQGEV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378  83 IGIDKEQKIVKTKLG-SYPFDQLILGMGGEPNDFGTPGVKAHGFTLWSFEDSVRIREHIEKTVAKAAlepddelRKAMLT 161
Cdd:COG1252   79 TGIDPEARTVTLADGrTLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERAE-------RRRLLT 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 162 FVVCGSGFTGIEMIGELIDWKNRLAKDYKLDPNEITLMVVEAMPTILNMLDRNDAAKAERYLRKHNVELLLNAPIVEVAA 241
Cdd:COG1252  152 IVVVGGGPTGVELAGELAELLRKLLRYPGIDPDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDA 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 242 DHIKLKDGRNIPTHTLIWTAGVKGTSDAADFGLESARGQRLIANEYMQAKGYEdkNIYIIGDLVFYEEFPGTPTPQIVQA 321
Cdd:COG1252  232 DGVTLEDGEEIPADTVIWAAGVKAPPLLADLGLPTDRRGRVLVDPTLQVPGHP--NVFAIGDCAAVPDPDGKPVPKTAQA 309

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488256378 322 AEQTGHTAAANIVASIKGGEKHKFKGNYQGFMVSIGAKWGVANLFdKIHLSGFLAIVMKHIVNLKYFFDIR 392
Cdd:COG1252  310 AVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVG-GLKLSGFLAWLLKRAIHLYFLPGFR 379
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 1-395 6.11e-43

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 159.93  E-value: 6.11e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378   1 MAKQNIVVVGAGYAGVsatkYLAKKLKKEDVAITLIDRHSYHTMMTELHEVAGGRVEPEAIQYDLQHLFARQKNvQLVTD 80
Cdd:PTZ00318   8 LKKPNVVVLGTGWAGA----YFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRPALAKLPN-RYLRA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378  81 TVIGIDKEQKIVKTKLGS-----------YPFDQLILGMGGEPNDFGTPGVKAHGFTLWSFEDSVRIREHIEKTVAKAAL 149
Cdd:PTZ00318  83 VVYDVDFEEKRVKCGVVSksnnanvntfsVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIERASL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 150 EPDD-ELRKAMLTFVVCGSGFTGIEMIGELIDWKNRLAKdyKLDP---NEITLMVVEAMPTILNMLDRNDAAKAERYLRK 225
Cdd:PTZ00318 163 PTTSvEERKRLLHFVVVGGGPTGVEFAAELADFFRDDVR--NLNPelvEECKVTVLEAGSEVLGSFDQALRKYGQRRLRR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 226 HNVELLLNAPIVEVAADHIKLKDGRNIPTHTLIWTAGVKGTSDAADFGLESARGQRLIANEYMQAKGYEdkNIYIIGDLV 305
Cdd:PTZ00318 241 LGVDIRTKTAVKEVLDKEVVLKDGEVIPTGLVVWSTGVGPGPLTKQLKVDKTSRGRISVDDHLRVKPIP--NVFALGDCA 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 306 FYEEfpgTPTPQIVQAAEQTGHTAAANIVASIKGGEKHK-FKGNYQGFMVSIGAKWGVANLfDKIHLSGFLAivmkhivn 384
Cdd:PTZ00318 319 ANEE---RPLPTLAQVASQQGVYLAKEFNNELKGKPMSKpFVYRSLGSLAYLGNYSAIVQL-GAFDLSGFKA-------- 386

                        410
                 ....*....|.
gi 488256378 385 lkyFFDIRSGY 395
Cdd:PTZ00318 387 ---LLFWRSAY 394
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 5-326 3.60e-36

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 137.83  E-value: 3.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378    5 NIVVVGAGYAGVSAtkylAKKLKKEDVAITLIDR----HSYHTMMTELHEVAGGRVEPEAIQYDLQ-----HLFARQKNV 75
Cdd:pfam07992   2 DVVVIGGGPAGLAA----ALTLAQLGGKVTLIEDegtcPYGGCVLSKALLGAAEAPEIASLWADLYkrkeeVVKKLNNGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378   76 QLVTDT-VIGIDKEQKIVKT------KLGSYPFDQLILGMGGEPNDFGTPGVKAHGFTLWSFEDSVrirehiektvakaa 148
Cdd:pfam07992  78 EVLLGTeVVSIDPGAKKVVLeelvdgDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSA-------------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378  149 lepdDELRKAML--TFVVCGSGFTGIEMIGELidwkNRLAKdykldpnEITLmvVEAMPTILNMLDRNDAAKAERYLRKH 226
Cdd:pfam07992 144 ----EALRLKLLpkRVVVVGGGYIGVELAAAL----AKLGK-------EVTL--IEALDRLLRAFDEEISAALEKALEKN 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378  227 NVELLLNAPIVEVAAD----HIKLKDGRNIPTHTLIWTAGVKGTSDAADF-GLESARGQRLIANEYMQAKgyeDKNIYII 301
Cdd:pfam07992 207 GVEVRLGTSVKEIIGDgdgvEVILKDGTEIDADLVVVAIGRRPNTELLEAaGLELDERGGIVVDEYLRTS---VPGIYAA 283

                         330       340
                  ....*....|....*....|....*
gi 488256378  302 GDLvfyeefpGTPTPQIVQAAEQTG 326
Cdd:pfam07992 284 GDC-------RVGGPELAQNAVAQG 301
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 5-333 3.93e-09

dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.


Pssm-ID: 273568 [Multi-domain]  Cd Length: 460  Bit Score: 59.19  E-value: 3.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378    5 NIVVVGAGYAGVSATKYLAK-KLK-----KEDVAITLIDR---------HSYHTMmTELHEVAGGRVEPEAIQYDLQHLF 69
Cdd:TIGR01350   3 DVIVIGGGPGGYVAAIRAAQlGLKvalveKEYLGGTCLNVgciptkallHSAEVY-DEIKHAKDLGIEVENVSVDWEKMQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378   70 AR-QKNVQLVTDTVIGIDKEQKI----------------VKTKLG--SYPFDQLILGMGGEPNDFGTPgVKAHGFTLWSF 130
Cdd:TIGR01350  82 KRkNKVVKKLVGGVSGLLKKNKVtvikgeakfldpgtvsVTGENGeeTLEAKNIIIATGSRPRSLPGP-FDFDGKVVITS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378  131 EDSVRIREHIEKtvakaalepddelrkamltFVVCGSGFTGIEmIGELIdwkNRLAKDykldpneitLMVVEAMPTILNM 210
Cdd:TIGR01350 161 TGALNLEEVPES-------------------LVIIGGGVIGIE-FASIF---ASLGSK---------VTVIEMLDRILPG 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378  211 LDRNDAAKAERYLRKHNVELLLNAPI--VEVAADHIKLK-DGRNIPTHT----LIwTAGVKGTSDAADF---GLESARGQ 280
Cdd:TIGR01350 209 EDAEVSKVLQKALKKKGVKILTNTKVtaVEKNDDQVTYEnKGGETETLTgekvLV-AVGRKPNTEGLGLeklGVELDERG 287

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 488256378  281 RLIANEYMQAKgyeDKNIYIIGDLvfyeefpgTPTPQIVQAAEQTGHTAAANI 333
Cdd:TIGR01350 288 RIVVDEYMRTN---VPGIYAIGDV--------IGGPMLAHVASHEGIVAAENI 329
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
3-392 2.19e-139

NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 411.83  E-value: 2.19e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378   3 KQNIVVVGAGYAGVSATKYLAKKLKKeDVAITLIDRHSYHTMMTELHEVAGGRVEPEAIQYDLQHLFARQkNVQLVTDTV 82
Cdd:COG1252    1 MKRIVIVGGGFAGLEAARRLRKKLGG-DAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRA-GVRFIQGEV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378  83 IGIDKEQKIVKTKLG-SYPFDQLILGMGGEPNDFGTPGVKAHGFTLWSFEDSVRIREHIEKTVAKAAlepddelRKAMLT 161
Cdd:COG1252   79 TGIDPEARTVTLADGrTLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERAE-------RRRLLT 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 162 FVVCGSGFTGIEMIGELIDWKNRLAKDYKLDPNEITLMVVEAMPTILNMLDRNDAAKAERYLRKHNVELLLNAPIVEVAA 241
Cdd:COG1252  152 IVVVGGGPTGVELAGELAELLRKLLRYPGIDPDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDA 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 242 DHIKLKDGRNIPTHTLIWTAGVKGTSDAADFGLESARGQRLIANEYMQAKGYEdkNIYIIGDLVFYEEFPGTPTPQIVQA 321
Cdd:COG1252  232 DGVTLEDGEEIPADTVIWAAGVKAPPLLADLGLPTDRRGRVLVDPTLQVPGHP--NVFAIGDCAAVPDPDGKPVPKTAQA 309

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488256378 322 AEQTGHTAAANIVASIKGGEKHKFKGNYQGFMVSIGAKWGVANLFdKIHLSGFLAIVMKHIVNLKYFFDIR 392
Cdd:COG1252  310 AVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVG-GLKLSGFLAWLLKRAIHLYFLPGFR 379
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
3-347 2.05e-43

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 160.69  E-value: 2.05e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378   3 KQNIVVVGAGYAGVSAtkylAKKLKKED--VAITLI---DRHSYHTMMteLHEVAGGRVEPEAIQYDLQHlFARQKNVQL 77
Cdd:COG1251    1 KMRIVIIGAGMAGVRA----AEELRKLDpdGEITVIgaePHPPYNRPP--LSKVLAGETDEEDLLLRPAD-FYEENGIDL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378  78 VTDT-VIGIDKEQKIVKTKLGS-YPFDQLILGMGGEPNDFGTPGVKAHG-FTLWSFEDSVRIREHIEKTvakaalepdde 154
Cdd:COG1251   74 RLGTrVTAIDRAARTVTLADGEtLPYDKLVLATGSRPRVPPIPGADLPGvFTLRTLDDADALRAALAPG----------- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 155 lRKAmltfVVCGSGFTGIEmigelidwknrLAKDYKLDPNEITlmVVEAMPTILN-MLDRNDAAKAERYLRKHNVELLLN 233
Cdd:COG1251  143 -KRV----VVIGGGLIGLE-----------AAAALRKRGLEVT--VVERAPRLLPrQLDEEAGALLQRLLEALGVEVRLG 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 234 APIVEVAADH----IKLKDGRNIPTHTLIWTAGVK-GTSDAADFGLESARGqrLIANEYMQAkgyEDKNIYIIGDLV-FY 307
Cdd:COG1251  205 TGVTEIEGDDrvtgVRLADGEELPADLVVVAIGVRpNTELARAAGLAVDRG--IVVDDYLRT---SDPDIYAAGDCAeHP 279

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 488256378 308 EEFPGTPTPQIVQAAEQTGHTAAANIVasikgGEKHKFKG 347
Cdd:COG1251  280 GPVYGRRVLELVAPAYEQARVAAANLA-----GGPAAYEG 314
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 1-395 6.11e-43

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 159.93  E-value: 6.11e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378   1 MAKQNIVVVGAGYAGVsatkYLAKKLKKEDVAITLIDRHSYHTMMTELHEVAGGRVEPEAIQYDLQHLFARQKNvQLVTD 80
Cdd:PTZ00318   8 LKKPNVVVLGTGWAGA----YFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRPALAKLPN-RYLRA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378  81 TVIGIDKEQKIVKTKLGS-----------YPFDQLILGMGGEPNDFGTPGVKAHGFTLWSFEDSVRIREHIEKTVAKAAL 149
Cdd:PTZ00318  83 VVYDVDFEEKRVKCGVVSksnnanvntfsVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIERASL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 150 EPDD-ELRKAMLTFVVCGSGFTGIEMIGELIDWKNRLAKdyKLDP---NEITLMVVEAMPTILNMLDRNDAAKAERYLRK 225
Cdd:PTZ00318 163 PTTSvEERKRLLHFVVVGGGPTGVEFAAELADFFRDDVR--NLNPelvEECKVTVLEAGSEVLGSFDQALRKYGQRRLRR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 226 HNVELLLNAPIVEVAADHIKLKDGRNIPTHTLIWTAGVKGTSDAADFGLESARGQRLIANEYMQAKGYEdkNIYIIGDLV 305
Cdd:PTZ00318 241 LGVDIRTKTAVKEVLDKEVVLKDGEVIPTGLVVWSTGVGPGPLTKQLKVDKTSRGRISVDDHLRVKPIP--NVFALGDCA 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 306 FYEEfpgTPTPQIVQAAEQTGHTAAANIVASIKGGEKHK-FKGNYQGFMVSIGAKWGVANLfDKIHLSGFLAivmkhivn 384
Cdd:PTZ00318 319 ANEE---RPLPTLAQVASQQGVYLAKEFNNELKGKPMSKpFVYRSLGSLAYLGNYSAIVQL-GAFDLSGFKA-------- 386

                        410
                 ....*....|.
gi 488256378 385 lkyFFDIRSGY 395
Cdd:PTZ00318 387 ---LLFWRSAY 394
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 5-326 3.60e-36

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 137.83  E-value: 3.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378    5 NIVVVGAGYAGVSAtkylAKKLKKEDVAITLIDR----HSYHTMMTELHEVAGGRVEPEAIQYDLQ-----HLFARQKNV 75
Cdd:pfam07992   2 DVVVIGGGPAGLAA----ALTLAQLGGKVTLIEDegtcPYGGCVLSKALLGAAEAPEIASLWADLYkrkeeVVKKLNNGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378   76 QLVTDT-VIGIDKEQKIVKT------KLGSYPFDQLILGMGGEPNDFGTPGVKAHGFTLWSFEDSVrirehiektvakaa 148
Cdd:pfam07992  78 EVLLGTeVVSIDPGAKKVVLeelvdgDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSA-------------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378  149 lepdDELRKAML--TFVVCGSGFTGIEMIGELidwkNRLAKdykldpnEITLmvVEAMPTILNMLDRNDAAKAERYLRKH 226
Cdd:pfam07992 144 ----EALRLKLLpkRVVVVGGGYIGVELAAAL----AKLGK-------EVTL--IEALDRLLRAFDEEISAALEKALEKN 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378  227 NVELLLNAPIVEVAAD----HIKLKDGRNIPTHTLIWTAGVKGTSDAADF-GLESARGQRLIANEYMQAKgyeDKNIYII 301
Cdd:pfam07992 207 GVEVRLGTSVKEIIGDgdgvEVILKDGTEIDADLVVVAIGRRPNTELLEAaGLELDERGGIVVDEYLRTS---VPGIYAA 283

                         330       340
                  ....*....|....*....|....*
gi 488256378  302 GDLvfyeefpGTPTPQIVQAAEQTG 326
Cdd:pfam07992 284 GDC-------RVGGPELAQNAVAQG 301
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 27-367 1.28e-35

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 136.86  E-value: 1.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378  27 KKEDVAITLIDR---HSYHTMMTELHeVAGGRVEPEAIQYDLQHLFARqKNVQLVT-DTVIGIDKEQKIVKTKLG-SYPF 101
Cdd:COG0446    2 LGPDAEITVIEKgphHSYQPCGLPYY-VGGGIKDPEDLLVRTPESFER-KGIDVRTgTEVTAIDPEAKTVTLRDGeTLSY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 102 DQLILGMGGEPNDFGTPGVKAHG-FTLWSFEDSVRIREHIEKTVAKaalepddelrkamlTFVVCGSGFTGIEMIGELID 180
Cdd:COG0446   80 DKLVLATGARPRPPPIPGLDLPGvFTLRTLDDADALREALKEFKGK--------------RAVVIGGGPIGLELAEALRK 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 181 WKnrlakdykldpneITLMVVEAMPTILNMLDRNDAAKAERYLRKHNVELLLNAPIVEVAADH---IKLKDGRNIPTHTL 257
Cdd:COG0446  146 RG-------------LKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDDkvaVTLTDGEEIPADLV 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 258 IWTAGVKGTSD-AADFGLESARGQRLIANEYMQAKgyeDKNIYIIGDLVfyeEFPGTPTPQIV-----QAAEQTGHTAAA 331
Cdd:COG0446  213 VVAPGVRPNTElAKDAGLALGERGWIKVDETLQTS---DPDVYAAGDCA---EVPHPVTGKTVyiplaSAANKQGRVAAE 286

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 488256378 332 NIVasikgGEKHKFKgnyqgfmvsiGAKWGVANLFD 367
Cdd:COG0446  287 NIL-----GGPAPFP----------GLGTFISKVFD 307
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 6-333 6.09e-14

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 74.41  E-value: 6.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378   6 IVVVGAGYAGVSATKYLAK-KLK-----KEDVAITLIDR------------HSYHTMMTELH---EVAGGRVEPEAIQY- 63
Cdd:PRK06416   7 VIVIGAGPGGYVAAIRAAQlGLKvaiveKEKLGGTCLNRgcipskallhaaERADEARHSEDfgiKAENVGIDFKKVQEw 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378  64 ----------DLQHLFARQKnvqlvTDTVIG---IDKEQKI-VKTKLGS--YPFDQLILGMGGEPndFGTPGVKAHGFTL 127
Cdd:PRK06416  87 kngvvnrltgGVEGLLKKNK-----VDIIRGeakLVDPNTVrVMTEDGEqtYTAKNIILATGSRP--RELPGIEIDGRVI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 128 W-SFEdsvrirehiektvakaALEPDdELRKAMltfVVCGSGFTGIEmigelidwknrLAKDYKLDPNEITlmVVEAMPT 206
Cdd:PRK06416 160 WtSDE----------------ALNLD-EVPKSL---VVIGGGYIGVE-----------FASAYASLGAEVT--IVEALPR 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 207 ILNMLDRNDAAKAERYLRKHNVELLLNAPI--VEVAADHIKLKDGRNIPTHT-----LIWTAGVKGTSDaaDFGLESA-- 277
Cdd:PRK06416 207 ILPGEDKEISKLAERALKKRGIKIKTGAKAkkVEQTDDGVTVTLEDGGKEETleadyVLVAVGRRPNTE--NLGLEELgv 284

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488256378 278 ---RGQrLIANEYMQAkgyEDKNIYIIGDLVfyeefpgtPTPQIVQAAEQTGHTAAANI 333
Cdd:PRK06416 285 ktdRGF-IEVDEQLRT---NVPNIYAIGDIV--------GGPMLAHKASAEGIIAAEAI 331
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 1-345 7.28e-13

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 70.89  E-value: 7.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378   1 MAKQNIVVVGAGYAGVSATKYLAKKLKKedVAitLIDRHSY----------------HT--MMTELHEVAGGRVEPEAIQ 62
Cdd:COG1249    1 MKDYDLVVIGAGPGGYVAAIRAAQLGLK--VA--LVEKGRLggtclnvgcipskallHAaeVAHEARHAAEFGISAGAPS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378  63 YDLQHLFARQKNV------------------------QLVTDTVIGIDKEQKIVktklgsypFDQLILGMGGEPNDFGTP 118
Cdd:COG1249   77 VDWAALMARKDKVvdrlrggveellkkngvdvirgraRFVDPHTVEVTGGETLT--------ADHIVIATGSRPRVPPIP 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 119 GVkahgftlwsfeDSVRI---REhiektvakaALEPDdELRKAMltfVVCGSGFTGIEMIGELidwkNRLAKdykldpnE 195
Cdd:COG1249  149 GL-----------DEVRVltsDE---------ALELE-ELPKSL---VVIGGGYIGLEFAQIF----ARLGS-------E 193

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 196 ITlmVVEAMPTILNMLDRnDAAKA-ERYLRKHNVELLLNAPIVEVAAD----HIKLKDGRNIPTHT---LIWTAGVKGTS 267
Cdd:COG1249  194 VT--LVERGDRLLPGEDP-EISEAlEKALEKEGIDILTGAKVTSVEKTgdgvTVTLEDGGGEEAVEadkVLVATGRRPNT 270

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 268 DaaDFGLESA------RGqRLIANEYMQAKgyeDKNIYIIGDLvfyeefpgTPTPQIVQAAEQTGHTAAANIVasikGGE 341
Cdd:COG1249  271 D--GLGLEAAgveldeRG-GIKVDEYLRTS---VPGIYAIGDV--------TGGPQLAHVASAEGRVAAENIL----GKK 332


                 ....
gi 488256378 342 KHKF 345
Cdd:COG1249  333 PRPV 336
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
5-303 7.75e-13

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 70.33  E-value: 7.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378   5 NIVVVGAGYagvsATKYLAKKLKKED--VAITLIDRHSYHtmmtelhevaggrvepeaiQY---DLQHL----------- 68
Cdd:PRK04965   4 GIVIIGSGF----AARQLVKNIRKQDahIPITLITADSGD-------------------EYnkpDLSHVfsqgqraddlt 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378  69 ------FARQKNVQLVTDT-VIGIDKEQKIVKTKLGSYPFDQLILGMGGEPndFgTPGVKAHG--FTLWSFEdsvrireh 139
Cdd:PRK04965  61 rqsageFAEQFNLRLFPHTwVTDIDAEAQVVKSQGNQWQYDKLVLATGASA--F-VPPIPGRElmLTLNSQQ-------- 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 140 iEKTVAKAalepddELRKAMLTFVVcGSGFTGIEmigelidwknrLAKDYKLDPNEITLmvVEAMPTIL-NMLDRNDAAK 218
Cdd:PRK04965 130 -EYRAAET------QLRDAQRVLVV-GGGLIGTE-----------LAMDLCRAGKAVTL--VDNAASLLaSLMPPEVSSR 188

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 219 AERYLRKHNVELLLNAPI--VEVAADHIK--LKDGRNIPTHTLIWTAGVK-GTSDAADFGLESARGqrLIANEYMQAkgy 293
Cdd:PRK04965 189 LQHRLTEMGVHLLLKSQLqgLEKTDSGIRatLDSGRSIEVDAVIAAAGLRpNTALARRAGLAVNRG--IVVDSYLQT--- 263

                        330
                 ....*....|
gi 488256378 294 EDKNIYIIGD 303
Cdd:PRK04965 264 SAPDIYALGD 273
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 5-333 3.93e-09

dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.


Pssm-ID: 273568 [Multi-domain]  Cd Length: 460  Bit Score: 59.19  E-value: 3.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378    5 NIVVVGAGYAGVSATKYLAK-KLK-----KEDVAITLIDR---------HSYHTMmTELHEVAGGRVEPEAIQYDLQHLF 69
Cdd:TIGR01350   3 DVIVIGGGPGGYVAAIRAAQlGLKvalveKEYLGGTCLNVgciptkallHSAEVY-DEIKHAKDLGIEVENVSVDWEKMQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378   70 AR-QKNVQLVTDTVIGIDKEQKI----------------VKTKLG--SYPFDQLILGMGGEPNDFGTPgVKAHGFTLWSF 130
Cdd:TIGR01350  82 KRkNKVVKKLVGGVSGLLKKNKVtvikgeakfldpgtvsVTGENGeeTLEAKNIIIATGSRPRSLPGP-FDFDGKVVITS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378  131 EDSVRIREHIEKtvakaalepddelrkamltFVVCGSGFTGIEmIGELIdwkNRLAKDykldpneitLMVVEAMPTILNM 210
Cdd:TIGR01350 161 TGALNLEEVPES-------------------LVIIGGGVIGIE-FASIF---ASLGSK---------VTVIEMLDRILPG 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378  211 LDRNDAAKAERYLRKHNVELLLNAPI--VEVAADHIKLK-DGRNIPTHT----LIwTAGVKGTSDAADF---GLESARGQ 280
Cdd:TIGR01350 209 EDAEVSKVLQKALKKKGVKILTNTKVtaVEKNDDQVTYEnKGGETETLTgekvLV-AVGRKPNTEGLGLeklGVELDERG 287

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 488256378  281 RLIANEYMQAKgyeDKNIYIIGDLvfyeefpgTPTPQIVQAAEQTGHTAAANI 333
Cdd:TIGR01350 288 RIVVDEYMRTN---VPGIYAIGDV--------IGGPMLAHVASHEGIVAAENI 329
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 6-347 1.59e-08

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 57.36  E-value: 1.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378   6 IVVVGAGYAGVSATKYlAKKLKKEDVaITLIDRHSYHTMMT-ELHEVAGGRVEpeaiqyDLQHLFAR------QKNVQLV 78
Cdd:PRK09564   3 IIIIGGTAAGMSAAAK-AKRLNKELE-ITVYEKTDIVSFGAcGLPYFVGGFFD------DPNTMIARtpeefiKSGIDVK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378  79 TDT-VIGIDKEQKIVKTK------LGSYPFDQLILGMGGEPNDFGTPGVKAHGF-TLWSFEDSVRIREHIEKTVAKAAle 150
Cdd:PRK09564  75 TEHeVVKVDAKNKTITVKnlktgsIFNDTYDKLMIATGARPIIPPIKNINLENVyTLKSMEDGLALKELLKDEEIKNI-- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 151 pddelrkamltfVVCGSGFTGIEMIGE---------LIDWKNRLAKDyKLDPnEITLMVVEAmptilnmldrndaakaer 221
Cdd:PRK09564 153 ------------VIIGAGFIGLEAVEAakhlgknvrIIQLEDRILPD-SFDK-EITDVMEEE------------------ 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 222 yLRKHNVELLLNAPIVEVAAD---HIKLKDGRNIPTHTLIWTAGVKGTSD-AADFGLESARGQRLIANEYMQAkgyEDKN 297
Cdd:PRK09564 201 -LRENGVELHLNEFVKSLIGEdkvEGVVTDKGEYEADVVIVATGVKPNTEfLEDTGLKTLKNGAIIVDEYGET---SIEN 276

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488256378 298 IYIIGDL-VFYEEFPGTPtpqiVQAAEQTGHTAAANIVASIKGGEKHKFKG 347
Cdd:PRK09564 277 IYAAGDCaTIYNIVSNKN----VYVPLATTANKLGRMVGENLAGRHVSFKG 323
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 163-249 5.50e-08

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 50.28  E-value: 5.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378  163 VVCGSGFTGIEMIGELidwkNRLAKdykldpnEITlmVVEAMPTILNMLDRNDAAKAERYLRKHNVELLLNAPIVEVAAD 242
Cdd:pfam00070   3 VVVGGGYIGLELAGAL----ARLGS-------KVT--VVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGN 69

                          90
                  ....*....|.
gi 488256378  243 ----HIKLKDG 249
Cdd:pfam00070  70 gdgvVVVLTDG 80
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
6-339 1.96e-07

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 53.20  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378   6 IVVVGAGYAGVSATKYLAkklkKEDVAITLIDRHSYH---TMMTELHEVAGgrvEPEAIQ-YDL-----QHlfARQKNVQ 76
Cdd:COG0492    3 VVIIGAGPAGLTAAIYAA----RAGLKTLVIEGGEPGgqlATTKEIENYPG---FPEGISgPELaerlrEQ--AERFGAE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378  77 LVTDTVIGIDKEQ--KIVKT-KLGSYPFDQLILGMGGEPNDFGTPG------------VKAHGFtlwSFEDsvrirehie 141
Cdd:COG0492   74 ILLEEVTSVDKDDgpFRVTTdDGTEYEAKAVIIATGAGPRKLGLPGeeefegrgvsycATCDGF---FFRG--------- 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 142 KTVakaalepddelrkamltfVVCGSGFTGIEMIGELidwkNRLAKdykldpnEITLMVveamptilnmldRNDAAKAER 221
Cdd:COG0492  142 KDV------------------VVVGGGDSALEEALYL----TKFAS-------KVTLIH------------RRDELRASK 180

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 222 YLRKH-----NVELLLNAPIVEVAAD----HIKLKDGRN-----IPTHTLIWTAGVKGTSD-AADFGLESARGQRLIANE 286
Cdd:COG0492  181 ILVERlranpKIEVLWNTEVTEIEGDgrveGVTLKNVKTgeekeLEVDGVFVAIGLKPNTElLKGLGLELDEDGYIVVDE 260

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488256378 287 YMQAKgyeDKNIYIIGDLVfyeefpGTPTPQIVQAAEQtGHTAAANIVASIKG 339
Cdd:COG0492  261 DMETS---VPGVFAAGDVR------DYKYRQAATAAGE-GAIAALSAARYLEP 303
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 4-116 4.99e-06

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 48.85  E-value: 4.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378    4 QNIVVVGAGYAGVSATKYLAKKLKKedvaITLIDRhsyhtmMTELhevagGRVEPEAIQYDLQHLFaRQKNVQLVTDTVI 83
Cdd:pfam07992 153 KRVVVVGGGYIGVELAAALAKLGKE----VTLIEA------LDRL-----LRAFDEEISAALEKAL-EKNGVEVRLGTSV 216

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 488256378   84 -GIDKEQKIVKTKLG---SYPFDQLILGMGGEPNDFG 116
Cdd:pfam07992 217 kEIIGDGDGVEVILKdgtEIDADLVVVAIGRRPNTEL 253
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 4-113 1.81e-05

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 47.11  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378   4 QNIVVVGAGYAGVSATKYLAKKlkkeDVAITLIDRHSYhtMMtelhevagGRVEPEAIQYDLQHLfaRQKNVQLVT-DTV 82
Cdd:COG0446  125 KRAVVIGGGPIGLELAEALRKR----GLKVTLVERAPR--LL--------GVLDPEMAALLEEEL--REHGVELRLgETV 188

                         90       100       110
                 ....*....|....*....|....*....|...
gi 488256378  83 IGIDKEQK--IVKTKLGSYPFDQLILGMGGEPN 113
Cdd:COG0446  189 VAIDGDDKvaVTLTDGEEIPADLVVVAPGVRPN 221
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 69-347 5.67e-05

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 45.93  E-value: 5.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378  69 FARQKNVQLVT-DTVIGIDKEQKIV--------KTKLGSYpfDQLILGMGGEPNDFGTPgvKAHGFTLWSFEDSVRIREH 139
Cdd:PRK13512  67 FYDRKQITVKTyHEVIAINDERQTVtvlnrktnEQFEESY--DKLILSPGASANSLGFE--SDITFTLRNLEDTDAIDQF 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 140 IEKTVAKAALepddelrkamltfvVCGSGFTGIEMIGELidwKNRlakdyKLDPNEI-------TLMVVEAMPTILNMLD 212
Cdd:PRK13512 143 IKANQVDKAL--------------VVGAGYISLEVLENL---YER-----GLHPTLIhrsdkinKLMDADMNQPILDELD 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 213 rndaakaerylrKHNVELLLNAPIVEVAADHIKLKDGrNIPTHTLIWTA-GVKGTSD-AADFGLESARGQRLIANEYMQA 290
Cdd:PRK13512 201 ------------KREIPYRLNEEIDAINGNEVTFKSG-KVEHYDMIIEGvGTHPNSKfIESSNIKLDDKGFIPVNDKFET 267

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488256378 291 KgyeDKNIYIIGDLV--FYEEfpgTPTPQIVQAAEQTgHTAAANIVASIKGGEKHKFKG 347
Cdd:PRK13512 268 N---VPNIYAIGDIItsHYRH---VDLPASVPLAWGA-HRAASIVAEQIAGNDTIEFKG 319
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 3-113 2.46e-04

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 43.88  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378   3 KQNIVVVGAGYAGVSATKyLAKKLKKEDVAITLIDRhsyhtmmtelheVAGGRVEPEAIQYDLQHLfaRQKNVQLVTD-T 81
Cdd:PRK09564 149 IKNIVIIGAGFIGLEAVE-AAKHLGKNVRIIQLEDR------------ILPDSFDKEITDVMEEEL--RENGVELHLNeF 213

                         90       100       110
                 ....*....|....*....|....*....|....
gi 488256378  82 VIGIDKEQK--IVKTKLGSYPFDQLILGMGGEPN 113
Cdd:PRK09564 214 VKSLIGEDKveGVVTDKGEYEADVVIVATGVKPN 247
NAD_binding_9 pfam13454
FAD-NAD(P)-binding;
7-109 4.30e-04

FAD-NAD(P)-binding;


Pssm-ID: 433222 [Multi-domain]  Cd Length: 155  Bit Score: 41.11  E-value: 4.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378    7 VVVGAGYAGVSATKYLAKKLKKEDVAITLIDRHS-------------YHTM------MT--------------------E 47
Cdd:pfam13454   1 AIVGGGPSGLALLERLLARAPKRPLEITLFDPSPpgaggvyrtdqspEHLLnvpasrMSlfpddpphflewlrargaldE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488256378   48 LHEVAGGRVEPEAI--QYdLQHLFAR-------QKNVQLVTDTVIGIDK---EQKIVKTKLGSYPFDQLILGMG 109
Cdd:pfam13454  81 APGLDPDDFPPRALygRY-LRDRFEEalarapaGVTVRVHRARVTDLRPrgdGYRVLLADGRTLAADAVVLATG 153
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
 1-303 9.48e-03

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 39.33  E-value: 9.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378   1 MAKQNIVVVGAGYAGVSATKYLAKKLKKEDVAITLI--------DR-H-----SYHTmMTELHEVAGGRVEPEAIqydlq 66
Cdd:PRK14989   1 MSKVRLAIIGNGMVGHRFIEDLLDKADAANFDITVFceepriayDRvHlssyfSHHT-AEELSLVREGFYEKHGI----- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378  67 hlfarqkNVqLVTDTVIGIDKEQKIVKTKLG-SYPFDQLILGMGGEPndfGTPGVKAHG----FTLWSFEDsvriREHIE 141
Cdd:PRK14989  75 -------KV-LVGERAITINRQEKVIHSSAGrTVFYDKLIMATGSYP---WIPPIKGSEtqdcFVYRTIED----LNAIE 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 142 KTVAKAAlepddelrkamlTFVVCGSGFTGIEMIGELidwKNRlakdykldpnEITLMVVEAMPTIL-NMLDRNDAAKAE 220
Cdd:PRK14989 140 ACARRSK------------RGAVVGGGLLGLEAAGAL---KNL----------GVETHVIEFAPMLMaEQLDQMGGEQLR 194

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488256378 221 RYLRKHNVELLLNAPIVEVAAD------HIKLKDGRNIPTHTLIWTAGVKGTSD-AADFGLESARGQRLIANEYMQAkgy 293
Cdd:PRK14989 195 RKIESMGVRVHTSKNTLEIVQEgvearkTMRFADGSELEVDFIVFSTGIRPQDKlATQCGLAVAPRGGIVINDSCQT--- 271

                        330
                 ....*....|
gi 488256378 294 EDKNIYIIGD 303
Cdd:PRK14989 272 SDPDIYAIGE 281
 
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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