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Conserved domains on  [gi|6323794|ref|NP_013865|]
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NADH-ubiquinone reductase (H(+)-translocating) NDE1 [Saccharomyces cerevisiae S288C]

Protein Classification

NAD(P)H-binding domain containing protein( domain architecture ID 1001497)

NAD(P)H-binding domain containing protein similar to the mitochondrial internal alternative NAD(P)H-ubiquinone oxidoreductase A, an NADH-ubiquinone oxidoreductase which catalyzes the oxidation of mitochondrial NADH, but does not translocate protons across the inner mitochondrial membrane

EC:  1.6.-.-
Gene Ontology:  GO:0003959|GO:0016491
PubMed:  8805537

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00318 super family cl33177
NADH dehydrogenase-like protein; Provisional
 111-559 5.54e-122

NADH dehydrogenase-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00318:

Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 365.63  E-value: 5.54e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794   111 KRKTLVILGSGWGSVSLLKNLDTTLYNVVVVSPRNYFLFTPLLPSTPVGTIELKSIVEPVRTiaRRSHGEVHYYEAEAYD 190
Cdd:PTZ00318   9 KKPNVVVLGTGWAGAYFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRP--ALAKLPNRYLRAVVYD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794   191 VDPENKTIKVKSSAKN---NDYDLDLKYDYLVVGVGAQPNTFGTPGVYEYSSFLKEISDAQEIRLKIMSSIEkAASLSPK 267
Cdd:PTZ00318  87 VDFEEKRVKCGVVSKSnnaNVNTFSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIE-RASLPTT 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794   268 DPE-RARLLSFVVVGGGPTGVEFAAELRDYVDQDLRKWMPELSKEIKVTLVEALPNILNMFDKYLVDYAQDLFKEEKIDL 346
Cdd:PTZ00318 166 SVEeRKRLLHFVVVGGGPTGVEFAAELADFFRDDVRNLNPELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDI 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794   347 RLKTMVKKVDATTITAKTGdgdiENIPYGVLVWATGNAPREVSKNLMTkleEQDSRRGLLIDNKLQLLGAKgSIFAIGDC 426
Cdd:PTZ00318 246 RTKTAVKEVLDKEVVLKDG----EVIPTGLVVWSTGVGPGPLTKQLKV---DKTSRGRISVDDHLRVKPIP-NVFALGDC 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794   427 TF--HPGLFPTAQVAHQEGEYLAQYFkkaykidqlnwkmthakddsevarlkNQIVKTQSQIEDFKYNHKGALAYIGSDK 504
Cdd:PTZ00318 318 AAneERPLPTLAQVASQQGVYLAKEF--------------------------NNELKGKPMSKPFVYRSLGSLAYLGNYS 371

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6323794   505 AIADLAVgeakYRLAGSFTFLFWKSAYLAMCLSFRNRVLVAMDWAKVYFLGRDSS 559
Cdd:PTZ00318 372 AIVQLGA----FDLSGFKALLFWRSAYLTILGSWRSKLYVLVNWAGTAIFGRDIT 422
 
Name Accession Description Interval E-value
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 111-559 5.54e-122

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 365.63  E-value: 5.54e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794   111 KRKTLVILGSGWGSVSLLKNLDTTLYNVVVVSPRNYFLFTPLLPSTPVGTIELKSIVEPVRTiaRRSHGEVHYYEAEAYD 190
Cdd:PTZ00318   9 KKPNVVVLGTGWAGAYFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRP--ALAKLPNRYLRAVVYD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794   191 VDPENKTIKVKSSAKN---NDYDLDLKYDYLVVGVGAQPNTFGTPGVYEYSSFLKEISDAQEIRLKIMSSIEkAASLSPK 267
Cdd:PTZ00318  87 VDFEEKRVKCGVVSKSnnaNVNTFSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIE-RASLPTT 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794   268 DPE-RARLLSFVVVGGGPTGVEFAAELRDYVDQDLRKWMPELSKEIKVTLVEALPNILNMFDKYLVDYAQDLFKEEKIDL 346
Cdd:PTZ00318 166 SVEeRKRLLHFVVVGGGPTGVEFAAELADFFRDDVRNLNPELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDI 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794   347 RLKTMVKKVDATTITAKTGdgdiENIPYGVLVWATGNAPREVSKNLMTkleEQDSRRGLLIDNKLQLLGAKgSIFAIGDC 426
Cdd:PTZ00318 246 RTKTAVKEVLDKEVVLKDG----EVIPTGLVVWSTGVGPGPLTKQLKV---DKTSRGRISVDDHLRVKPIP-NVFALGDC 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794   427 TF--HPGLFPTAQVAHQEGEYLAQYFkkaykidqlnwkmthakddsevarlkNQIVKTQSQIEDFKYNHKGALAYIGSDK 504
Cdd:PTZ00318 318 AAneERPLPTLAQVASQQGVYLAKEF--------------------------NNELKGKPMSKPFVYRSLGSLAYLGNYS 371

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6323794   505 AIADLAVgeakYRLAGSFTFLFWKSAYLAMCLSFRNRVLVAMDWAKVYFLGRDSS 559
Cdd:PTZ00318 372 AIVQLGA----FDLSGFKALLFWRSAYLTILGSWRSKLYVLVNWAGTAIFGRDIT 422
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
112-546 7.75e-82

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 260.84  E-value: 7.75e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794  112 RKTLVILGSGWGSVSLLKNLDTTL---YNVVVVSPRNYFLFTPLLPSTPVGTIELKSIVEPVRTIARRSHgeVHYYEAEA 188
Cdd:COG1252   1 MKRIVIVGGGFAGLEAARRLRKKLggdAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAG--VRFIQGEV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794  189 YDVDPENKTIKVKSSAknndydlDLKYDYLVVGVGAQPNTFGTPGVYEYSSFLKEISDAQEIRLKIMSSIEKAaslspkd 268
Cdd:COG1252  79 TGIDPEARTVTLADGR-------TLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERA------- 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794  269 pERARLLSFVVVGGGPTGVEFAAELRDYVDQDLRkwMPELS-KEIKVTLVEALPNILNMFDKYLVDYAQDLFKEEKIDLR 347
Cdd:COG1252 145 -ERRRLLTIVVVGGGPTGVELAGELAELLRKLLR--YPGIDpDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVH 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794  348 LKTMVKKVDATTITAKTGdgdiENIPYGVLVWATGNAPREVSKNLmtKLeEQDSRRGLLIDNKLQLLGAKGsIFAIGDCT 427
Cdd:COG1252 222 TGTRVTEVDADGVTLEDG----EEIPADTVIWAAGVKAPPLLADL--GL-PTDRRGRVLVDPTLQVPGHPN-VFAIGDCA 293

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794  428 FHPGLF-----PTAQVAHQEGEYLAqyfkkaykiDQLnwkmthakddseVARLKNQivktqsQIEDFKYNHKGALAYIGS 502
Cdd:COG1252 294 AVPDPDgkpvpKTAQAAVQQAKVLA---------KNI------------AALLRGK------PLKPFRYRDKGCLASLGR 346

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 6323794  503 DKAIADLavgeAKYRLAGSFTFLFWKSAYLAMCLSFRNRVLVAM 546
Cdd:COG1252 347 GAAVADV----GGLKLSGFLAWLLKRAIHLYFLPGFRGRLRVLL 386
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 115-443 3.18e-34

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: 131.29  E-value: 3.18e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794    115 LVILGSGWGSVSLLKNLDTTLYNVVVVS-PRNYFLFTPLLPSTPVGTIE-------LKSIVEPVRTIARRSHGEVHYY-E 185
Cdd:pfam07992   3 VVVIGGGPAGLAAALTLAQLGGKVTLIEdEGTCPYGGCVLSKALLGAAEapeiaslWADLYKRKEEVVKKLNNGIEVLlG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794    186 AEAYDVDPENKTIKVKSSAKNNDYDLdlKYDYLVVGVGAQPNTFGTPGVYEYSSFL-KEISDAQEIRLKIMssiekaasl 264
Cdd:pfam07992  83 TEVVSIDPGAKKVVLEELVDGDGETI--TYDRLVIATGARPRLPPIPGVELNVGFLvRTLDSAEALRLKLL--------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794    265 spkdPER-----ARLLSfvvvgggptgVEFAAELRDYVdqdlrkwmpelskeIKVTLVEALPNILNMFDKYLVDYAQDLF 339
Cdd:pfam07992 152 ----PKRvvvvgGGYIG----------VELAAALAKLG--------------KEVTLIEALDRLLRAFDEEISAALEKAL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794    340 KEEKIDLRLKTMVKKV--DATTITAKTGDGDIenIPYGVLVWATGnapREVSKNLMTKLE-EQDSRRGLLIDNKLQLlgA 416
Cdd:pfam07992 204 EKNGVEVRLGTSVKEIigDGDGVEVILKDGTE--IDADLVVVAIG---RRPNTELLEAAGlELDERGGIVVDEYLRT--S 276

                         330       340
                  ....*....|....*....|....*..
gi 6323794    417 KGSIFAIGDCTFhpGLFPTAQVAHQEG 443
Cdd:pfam07992 277 VPGIYAAGDCRV--GGPELAQNAVAQG 301
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 160-450 3.32e-07

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: 53.03  E-value: 3.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794    160 TIELKSIVEPVRTIARRSHGEVHY---------YEAEAYDVDPenKTIKVKSSaknnDYDLDLKYDYLVVGVGAQPNTFg 230
Cdd:TIGR01350  74 SVDWEKMQKRKNKVVKKLVGGVSGllkknkvtvIKGEAKFLDP--GTVSVTGE----NGEETLEAKNIIIATGSRPRSL- 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794    231 tPGVYEYSsflkeisdaqeiRLKIMSSiEKAASLsPKDPErarllSFVVVGGGPTGVEFAAELRDYvdqdlrkwmpelsk 310
Cdd:TIGR01350 147 -PGPFDFD------------GKVVITS-TGALNL-EEVPE-----SLVIIGGGVIGIEFASIFASL-------------- 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794    311 EIKVTLVEALPNILNMFDKYLVDYAQDLFKEEKIDLRLKTMVKKV--DATTITAKTGDGDIENIPYGVLVWATGNAPREV 388
Cdd:TIGR01350 193 GSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVekNDDQVTYENKGGETETLTGEKVLVAVGRKPNTE 272

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323794    389 SKNLmTKLE-EQDSRRGLLIDNKLQlLGAKGsIFAIGDCTFHPGLfptAQVAHQEGEYLAQYF 450
Cdd:TIGR01350 273 GLGL-EKLGvELDERGRIVVDEYMR-TNVPG-IYAIGDVIGGPML---AHVASHEGIVAAENI 329
 
Name Accession Description Interval E-value
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 111-559 5.54e-122

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 365.63  E-value: 5.54e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794   111 KRKTLVILGSGWGSVSLLKNLDTTLYNVVVVSPRNYFLFTPLLPSTPVGTIELKSIVEPVRTiaRRSHGEVHYYEAEAYD 190
Cdd:PTZ00318   9 KKPNVVVLGTGWAGAYFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRP--ALAKLPNRYLRAVVYD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794   191 VDPENKTIKVKSSAKN---NDYDLDLKYDYLVVGVGAQPNTFGTPGVYEYSSFLKEISDAQEIRLKIMSSIEkAASLSPK 267
Cdd:PTZ00318  87 VDFEEKRVKCGVVSKSnnaNVNTFSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIE-RASLPTT 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794   268 DPE-RARLLSFVVVGGGPTGVEFAAELRDYVDQDLRKWMPELSKEIKVTLVEALPNILNMFDKYLVDYAQDLFKEEKIDL 346
Cdd:PTZ00318 166 SVEeRKRLLHFVVVGGGPTGVEFAAELADFFRDDVRNLNPELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDI 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794   347 RLKTMVKKVDATTITAKTGdgdiENIPYGVLVWATGNAPREVSKNLMTkleEQDSRRGLLIDNKLQLLGAKgSIFAIGDC 426
Cdd:PTZ00318 246 RTKTAVKEVLDKEVVLKDG----EVIPTGLVVWSTGVGPGPLTKQLKV---DKTSRGRISVDDHLRVKPIP-NVFALGDC 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794   427 TF--HPGLFPTAQVAHQEGEYLAQYFkkaykidqlnwkmthakddsevarlkNQIVKTQSQIEDFKYNHKGALAYIGSDK 504
Cdd:PTZ00318 318 AAneERPLPTLAQVASQQGVYLAKEF--------------------------NNELKGKPMSKPFVYRSLGSLAYLGNYS 371

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6323794   505 AIADLAVgeakYRLAGSFTFLFWKSAYLAMCLSFRNRVLVAMDWAKVYFLGRDSS 559
Cdd:PTZ00318 372 AIVQLGA----FDLSGFKALLFWRSAYLTILGSWRSKLYVLVNWAGTAIFGRDIT 422
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
112-546 7.75e-82

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 260.84  E-value: 7.75e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794  112 RKTLVILGSGWGSVSLLKNLDTTL---YNVVVVSPRNYFLFTPLLPSTPVGTIELKSIVEPVRTIARRSHgeVHYYEAEA 188
Cdd:COG1252   1 MKRIVIVGGGFAGLEAARRLRKKLggdAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAG--VRFIQGEV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794  189 YDVDPENKTIKVKSSAknndydlDLKYDYLVVGVGAQPNTFGTPGVYEYSSFLKEISDAQEIRLKIMSSIEKAaslspkd 268
Cdd:COG1252  79 TGIDPEARTVTLADGR-------TLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERA------- 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794  269 pERARLLSFVVVGGGPTGVEFAAELRDYVDQDLRkwMPELS-KEIKVTLVEALPNILNMFDKYLVDYAQDLFKEEKIDLR 347
Cdd:COG1252 145 -ERRRLLTIVVVGGGPTGVELAGELAELLRKLLR--YPGIDpDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVH 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794  348 LKTMVKKVDATTITAKTGdgdiENIPYGVLVWATGNAPREVSKNLmtKLeEQDSRRGLLIDNKLQLLGAKGsIFAIGDCT 427
Cdd:COG1252 222 TGTRVTEVDADGVTLEDG----EEIPADTVIWAAGVKAPPLLADL--GL-PTDRRGRVLVDPTLQVPGHPN-VFAIGDCA 293

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794  428 FHPGLF-----PTAQVAHQEGEYLAqyfkkaykiDQLnwkmthakddseVARLKNQivktqsQIEDFKYNHKGALAYIGS 502
Cdd:COG1252 294 AVPDPDgkpvpKTAQAAVQQAKVLA---------KNI------------AALLRGK------PLKPFRYRDKGCLASLGR 346

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 6323794  503 DKAIADLavgeAKYRLAGSFTFLFWKSAYLAMCLSFRNRVLVAM 546
Cdd:COG1252 347 GAAVADV----GGLKLSGFLAWLLKRAIHLYFLPGFRGRLRVLL 386
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 115-443 3.18e-34

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: 131.29  E-value: 3.18e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794    115 LVILGSGWGSVSLLKNLDTTLYNVVVVS-PRNYFLFTPLLPSTPVGTIE-------LKSIVEPVRTIARRSHGEVHYY-E 185
Cdd:pfam07992   3 VVVIGGGPAGLAAALTLAQLGGKVTLIEdEGTCPYGGCVLSKALLGAAEapeiaslWADLYKRKEEVVKKLNNGIEVLlG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794    186 AEAYDVDPENKTIKVKSSAKNNDYDLdlKYDYLVVGVGAQPNTFGTPGVYEYSSFL-KEISDAQEIRLKIMssiekaasl 264
Cdd:pfam07992  83 TEVVSIDPGAKKVVLEELVDGDGETI--TYDRLVIATGARPRLPPIPGVELNVGFLvRTLDSAEALRLKLL--------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794    265 spkdPER-----ARLLSfvvvgggptgVEFAAELRDYVdqdlrkwmpelskeIKVTLVEALPNILNMFDKYLVDYAQDLF 339
Cdd:pfam07992 152 ----PKRvvvvgGGYIG----------VELAAALAKLG--------------KEVTLIEALDRLLRAFDEEISAALEKAL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794    340 KEEKIDLRLKTMVKKV--DATTITAKTGDGDIenIPYGVLVWATGnapREVSKNLMTKLE-EQDSRRGLLIDNKLQLlgA 416
Cdd:pfam07992 204 EKNGVEVRLGTSVKEIigDGDGVEVILKDGTE--IDADLVVVAIG---RRPNTELLEAAGlELDERGGIVVDEYLRT--S 276

                         330       340
                  ....*....|....*....|....*..
gi 6323794    417 KGSIFAIGDCTFhpGLFPTAQVAHQEG 443
Cdd:pfam07992 277 VPGIYAAGDCRV--GGPELAQNAVAQG 301
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 185-448 1.20e-22

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: 98.73  E-value: 1.20e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794  185 EAEAYDVDPENKTIKVKSSAKnndydldLKYDYLVVGVGAQPNTFGTPG-----VYeyssFLKEISDAQEIRlkimssie 259
Cdd:COG0446  56 GTEVTAIDPEAKTVTLRDGET-------LSYDKLVLATGARPRPPPIPGldlpgVF----TLRTLDDADALR-------- 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794  260 kaASLSPKDPERA-------RLLsfvvvgggptgvEFAAELRDyvdqdlrkwmpelsKEIKVTLVEALPNILNMFDKYLV 332
Cdd:COG0446 117 --EALKEFKGKRAvvigggpIGL------------ELAEALRK--------------RGLKVTLVERAPRLLGVLDPEMA 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794  333 DYAQDLFKEEKIDLRLKTMVKKVDATT-ITAKTGDGdiENIPYGVLVWATGNAPR-EVSKNLmtKLEEqDSRRGLLIDNK 410
Cdd:COG0446 169 ALLEEELREHGVELRLGETVVAIDGDDkVAVTLTDG--EEIPADLVVVAPGVRPNtELAKDA--GLAL-GERGWIKVDET 243

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 6323794  411 LQlLGAKGsIFAIGDCT--FHPG-----LFPTAQVAHQEGEYLAQ 448
Cdd:COG0446 244 LQ-TSDPD-VYAAGDCAevPHPVtgktvYIPLASAANKQGRVAAE 286
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 313-457 4.60e-18

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: 87.06  E-value: 4.60e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794  313 KVTLVEALPNILNMFDKYLVDYAQDLFKEEKIDLRLKTMVKKVDAT----TITAKTGDGdIENIPYGVLVWATGNAPRev 388
Cdd:COG1249 193 EVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTgdgvTVTLEDGGG-EEAVEADKVLVATGRRPN-- 269

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323794  389 SKNLmtKLEEQ----DSRRGLLIDNKLQlLGAKGsIFAIGDCTfhpGLFPTAQVAHQEGEYLAQ--YFKKAYKID 457
Cdd:COG1249 270 TDGL--GLEAAgvelDERGGIKVDEYLR-TSVPG-IYAIGDVT---GGPQLAHVASAEGRVAAEniLGKKPRPVD 337
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 285-443 1.46e-08

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 57.08  E-value: 1.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794   285 TGVEFAAELRDYvdqdlrkwmpelskEIKVTLVEALPNILNMFDKYLVDYAQDLFKEEKIDLRLKTMVKKV--DATTITA 362
Cdd:PRK06416 183 IGVEFASAYASL--------------GAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKKVeqTDDGVTV 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794   363 KT-GDGDIENIPYGVLVWATGNAPreVSKNLmtKLEEQDSR--RGL-LIDNKLQlLGAKGsIFAIGDCTfhpglfPTAQV 438
Cdd:PRK06416 249 TLeDGGKEETLEADYVLVAVGRRP--NTENL--GLEELGVKtdRGFiEVDEQLR-TNVPN-IYAIGDIV------GGPML 316


                 ....*...
gi 6323794   439 AH---QEG 443
Cdd:PRK06416 317 AHkasAEG 324
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 160-450 3.32e-07

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: 53.03  E-value: 3.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794    160 TIELKSIVEPVRTIARRSHGEVHY---------YEAEAYDVDPenKTIKVKSSaknnDYDLDLKYDYLVVGVGAQPNTFg 230
Cdd:TIGR01350  74 SVDWEKMQKRKNKVVKKLVGGVSGllkknkvtvIKGEAKFLDP--GTVSVTGE----NGEETLEAKNIIIATGSRPRSL- 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794    231 tPGVYEYSsflkeisdaqeiRLKIMSSiEKAASLsPKDPErarllSFVVVGGGPTGVEFAAELRDYvdqdlrkwmpelsk 310
Cdd:TIGR01350 147 -PGPFDFD------------GKVVITS-TGALNL-EEVPE-----SLVIIGGGVIGIEFASIFASL-------------- 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794    311 EIKVTLVEALPNILNMFDKYLVDYAQDLFKEEKIDLRLKTMVKKV--DATTITAKTGDGDIENIPYGVLVWATGNAPREV 388
Cdd:TIGR01350 193 GSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVekNDDQVTYENKGGETETLTGEKVLVAVGRKPNTE 272

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323794    389 SKNLmTKLE-EQDSRRGLLIDNKLQlLGAKGsIFAIGDCTFHPGLfptAQVAHQEGEYLAQYF 450
Cdd:TIGR01350 273 GLGL-EKLGvELDERGRIVVDEYMR-TNVPG-IYAIGDVIGGPML---AHVASHEGIVAAENI 329
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 288-359 3.45e-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: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 45.27  E-value: 3.45e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323794    288 EFAAELRDYVDqdlrkwmpelskeiKVTLVEALPNILNMFDKYLVDYAQDLFKEEKIDLRLKTMVKKVDATT 359
Cdd:pfam00070  13 ELAGALARLGS--------------KVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNG 70
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
191-448 6.41e-06

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 48.60  E-value: 6.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794  191 VDPENKTIKVKSSAKnndydldLKYDYLVVGVGAQPNTFGTPG-----VYEYSSflkeISDAQEIRlKIMSSIEKA---- 261
Cdd:COG1251  82 IDRAARTVTLADGET-------LPYDKLVLATGSRPRVPPIPGadlpgVFTLRT----LDDADALR-AALAPGKRVvvig 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794  262 ASlspkdperarllsfvvvgggPTGVEFAAELRDyvdqdlrkwmpelsKEIKVTLVEALPNILN-MFDKYLVDYAQDLFK 340
Cdd:COG1251 150 GG--------------------LIGLEAAAALRK--------------RGLEVTVVERAPRLLPrQLDEEAGALLQRLLE 195

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794  341 EEKIDLRLKTMVKKVDATT--ITAKTGDGdiENIPYGVLVWATGNAPRevsknlmTKLEEQ---DSRRGLLIDNKLQlLG 415
Cdd:COG1251 196 ALGVEVRLGTGVTEIEGDDrvTGVRLADG--EELPADLVVVAIGVRPN-------TELARAaglAVDRGIVVDDYLR-TS 265

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 6323794  416 AKGsIFAIGDCTFHPG------LFPTAQVAHQEGEYLAQ 448
Cdd:COG1251 266 DPD-IYAAGDCAEHPGpvygrrVLELVAPAYEQARVAAA 303
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 314-443 5.41e-05

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 45.69  E-value: 5.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794   314 VTLVEALPNILNMFDKYLVDYAQDLFKEEKIDLRLKTMVKKVDAT----TITAKTGDGDIENIPYGVLVWATGNAPREVS 389
Cdd:PRK06327 209 VTILEALPAFLAAADEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGgkgvSVAYTDADGEAQTLEVDKLIVSIGRVPNTDG 288

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794   390 KNLMT---KLEEqdsrRGLL-IDNKLQ--LLGakgsIFAIGDCTFHPGLfptAQVAHQEG 443
Cdd:PRK06327 289 LGLEAvglKLDE----RGFIpVDDHCRtnVPN----VYAIGDVVRGPML---AHKAEEEG 337
PRK06116 PRK06116
glutathione reductase; Validated
 286-447 2.36e-04

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 43.61  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794   286 GVEFAAELRdyvdqdlrkwmpELSKEikVTLVEALPNILNMFDKYLVDYAQDLFKEEKIDLRLKTMVKKVDAT---TITA 362
Cdd:PRK06116 179 AVEFAGVLN------------GLGSE--THLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNadgSLTL 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794   363 KTGDGDIENIpyGVLVWATGNAPREVSKNLMT---KLEEqdsrRGLLIDNKLQLLGAKGsIFAIGDCTFHPGLFPtaqVA 439
Cdd:PRK06116 245 TLEDGETLTV--DCLIWAIGREPNTDGLGLENagvKLNE----KGYIIVDEYQNTNVPG-IYAVGDVTGRVELTP---VA 314


                 ....*...
gi 6323794   440 HQEGEYLA 447
Cdd:PRK06116 315 IAAGRRLS 322
Nterm_to_SelD TIGR03169
pyridine nucleotide-disulfide oxidoreductase family protein; Members of this protein family ...
 181-448 4.25e-04

pyridine nucleotide-disulfide oxidoreductase family protein; Members of this protein family include N-terminal sequence regions of (probable) bifunctional proteins whose C-terminal sequences are SelD, or selenide,water dikinase, the selenium donor protein necessary for selenium incorporation into protein (as selenocysteine), tRNA (as 2-selenouridine), or both. However, some members of this family occur in species that do not show selenium incorporation, and the function of this protein family is unknown.


Pssm-ID: 274465  Cd Length: 364  Bit Score: 42.57  E-value: 4.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794    181 VHYYEAEAYDVDPENKTIKVKSSAknndydlDLKYDYLVVGVGAQPNTFGTPGVYEYS--------------SFLKEISD 246
Cdd:TIGR03169  69 ARLILDRAIGLDLAAKQVICAGRP-------PIAYDVLSIDIGSTPALPDVPGFAEHAipakplgqfaqrwqRFLERAKP 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794    247 AQEIRLKIM----SSIEKAaslspkdperarllsfvvvgggptgveFAAELRdyvdqdlrkwMPELSKEIKVTLVEALPN 322
Cdd:TIGR03169 142 QQPPRIAVIgggaAGVELA---------------------------LAMAHR----------LRQLGRNAEVTLIDRGNV 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794    323 ILNMFDKYLVDYAQDLFKEEKIDLRLKTMVKKVDATTITAKTGdgdiENIPYGVLVWATGNAPREVSKNlmTKLEeQDSR 402
Cdd:TIGR03169 185 LLPGHNARVRRRLERALQERGVTLHLGATVAEVTADAVRLEDG----QTLPADFTFWATGARPPGWLAE--SGLA-LDED 257

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 6323794    403 RGLLIDNKLQLLGAKGsIFAIGDC-TFHPGLFPTAQV-AHQEGEYLAQ 448
Cdd:TIGR03169 258 GFIRVGPTLQSLSHPD-IFAAGDCaHLVHAPRPKAGVfAVRQAPVLAE 304
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 307-386 1.07e-03

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: 41.34  E-value: 1.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794  307 ELSKEIKVTLVEALPNIlnMFD-----KYL---VDYAQDL-------FKEEKIDLRLKTMVKKVD--ATTITAKTGdgdi 369
Cdd:COG0446   1 RLGPDAEITVIEKGPHH--SYQpcglpYYVgggIKDPEDLlvrtpesFERKGIDVRTGTEVTAIDpeAKTVTLRDG---- 74

                        90
                ....*....|....*..
gi 6323794  370 ENIPYGVLVWATGNAPR 386
Cdd:COG0446  75 ETLSYDKLVLATGARPR 91
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 284-448 5.68e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 39.39  E-value: 5.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794   284 PTGVEFAAELRdyvdqdlrkwmpelSKEIKVTLVEALPNILNMFDKYLVDYAQDLFKEEkIDLRLKTMVKKVDAT---TI 360
Cdd:PRK06292 179 VIGLELGQALS--------------RLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIKLGAKVTSVEKSgdeKV 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323794   361 TAKTGDGDIENIPYGVLVWATGNAPreVSKNLmtKLEEQD---SRRGL-LIDNKLQlLGAKGsIFAIGDCTfhpGLFPTA 436
Cdd:PRK06292 244 EELEKGGKTETIEADYVLVATGRRP--NTDGL--GLENTGielDERGRpVVDEHTQ-TSVPG-IYAAGDVN---GKPPLL 314

                        170
                 ....*....|..
gi 6323794   437 QVAHQEGEYLAQ 448
Cdd:PRK06292 315 HEAADEGRIAAE 326
 
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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