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Conserved domains on  [gi|613307026|gb|EZZ12123|]
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hypothetical protein U935_02511 [Staphylococcus aureus Sau 46]

Protein Classification

FAD/NAD(P)-binding oxidoreductase( domain architecture ID 11418561)

FAD/NAD(P)-binding 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

CATH:  3.50.50.60
EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0000166

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
25-351 8.87e-70

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: 222.38  E-value: 8.87e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026  25 RKNQNLKekIAIIDPADHHYYQP--LWTLVGAGVSSLKS-SRKDMESVIPEGAHWIKQA-VSSFQPENNSVILGDNTVVY 100
Cdd:COG0446    1 RLGPDAE--ITVIEKGPHHSYQPcgLPYYVGGGIKDPEDlLVRTPESFERKGIDVRTGTeVTAIDPEAKTVTLRDGETLS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026 101 YDFLVVAPGLQINWSSIKGLKEnigkNGVCSNYSPDYVNETWNQISNFKQGNAIFThpntpikcGGAPmkIMYLAEDYFR 180
Cdd:COG0446   79 YDKLVLATGARPRPPPIPGLDL----PGVFTLRTLDDADALREALKEFKGKRAVVI--------GGGP--IGLELAEALR 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026 181 KHKIrsNANVIYATPkdALFdvGKYNKE----LERIVEERNITVNYNYNLVEIDGDKKVAtfehIKTYDRKTISYDMLHV 256
Cdd:COG0446  145 KRGL--KVTLVERAP--RLL--GVLDPEmaalLEEELREHGVELRLGETVVAIDGDDKVA----VTLTDGEEIPADLVVV 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026 257 TPPMGP-LDVVKESTLS-DSEGWVDVNPtTLQHkSYSNVFALGDASNVP---TSKT-----GAAIRKQAPIVANNLL--Q 324
Cdd:COG0446  215 APGVRPnTELAKDAGLAlGERGWIKVDE-TLQT-SDPDVYAAGDCAEVPhpvTGKTvyiplASAANKQGRVAAENILggP 292
                        330       340
                 ....*....|....*....|....*..
gi 613307026 325 VMNNQMLTHHYDGYTSCPIVTGYNRLI 351
Cdd:COG0446  293 APFPGLGTFISKVFDLCIASTGTGRLL 319
Pyr_redox_2 super family cl39093
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
3-42 3.83e-03

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.


The actual alignment was detected with superfamily member PRK06292:

Pssm-ID: 476868 [Multi-domain]  Cd Length: 460  Bit Score: 39.39  E-value: 3.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 613307026   3 KHYQIVIIGGGTAGVTVASRLLRknqnLKEKIAIIDPADH 42
Cdd:PRK06292   2 EKYDVIVIGAGPAGYVAARRAAK----LGKKVALIEKGPL 37
 
Name Accession Description Interval E-value
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
25-351 8.87e-70

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: 222.38  E-value: 8.87e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026  25 RKNQNLKekIAIIDPADHHYYQP--LWTLVGAGVSSLKS-SRKDMESVIPEGAHWIKQA-VSSFQPENNSVILGDNTVVY 100
Cdd:COG0446    1 RLGPDAE--ITVIEKGPHHSYQPcgLPYYVGGGIKDPEDlLVRTPESFERKGIDVRTGTeVTAIDPEAKTVTLRDGETLS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026 101 YDFLVVAPGLQINWSSIKGLKEnigkNGVCSNYSPDYVNETWNQISNFKQGNAIFThpntpikcGGAPmkIMYLAEDYFR 180
Cdd:COG0446   79 YDKLVLATGARPRPPPIPGLDL----PGVFTLRTLDDADALREALKEFKGKRAVVI--------GGGP--IGLELAEALR 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026 181 KHKIrsNANVIYATPkdALFdvGKYNKE----LERIVEERNITVNYNYNLVEIDGDKKVAtfehIKTYDRKTISYDMLHV 256
Cdd:COG0446  145 KRGL--KVTLVERAP--RLL--GVLDPEmaalLEEELREHGVELRLGETVVAIDGDDKVA----VTLTDGEEIPADLVVV 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026 257 TPPMGP-LDVVKESTLS-DSEGWVDVNPtTLQHkSYSNVFALGDASNVP---TSKT-----GAAIRKQAPIVANNLL--Q 324
Cdd:COG0446  215 APGVRPnTELAKDAGLAlGERGWIKVDE-TLQT-SDPDVYAAGDCAEVPhpvTGKTvyiplASAANKQGRVAAENILggP 292
                        330       340
                 ....*....|....*....|....*..
gi 613307026 325 VMNNQMLTHHYDGYTSCPIVTGYNRLI 351
Cdd:COG0446  293 APFPGLGTFISKVFDLCIASTGTGRLL 319
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
7-324 4.43e-10

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 60.94  E-value: 4.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026   7 IVIIGGGTAGvtvaSRLLRKNQNLKEKIAIIDPADHHYYQPLwtLVGAGVSSLKSsRKDMESVIPEGAH----WIKQAVS 82
Cdd:PTZ00318  13 VVVLGTGWAG----AYFVRNLDPKKYNITVISPRNHMLFTPL--LPQTTTGTLEF-RSICEPVRPALAKlpnrYLRAVVY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026  83 SFQPENNSVILG----------DNTVVYYDFLVVAPGLQINWSSIKGLKENIgkngvcsnYSPDYVNETWNQISNFKQGN 152
Cdd:PTZ00318  86 DVDFEEKRVKCGvvsksnnanvNTFSVPYDKLVVAHGARPNTFNIPGVEERA--------FFLKEVNHARGIRKRIVQCI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026 153 AIFTHPNTPIK----------CGGAPMKIMYLAE--DYFRKHKIRSNANVIyATPKDALFDVGK-----YNKELERIVEE 215
Cdd:PTZ00318 158 ERASLPTTSVEerkrllhfvvVGGGPTGVEFAAElaDFFRDDVRNLNPELV-EECKVTVLEAGSevlgsFDQALRKYGQR 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026 216 R----NITVNYNYNLVEIDgDKKVATfehiKTYDRktISYDMLHVTPPMGPLDVVKESTLS-DSEGWVDVNpTTLQHKSY 290
Cdd:PTZ00318 237 RlrrlGVDIRTKTAVKEVL-DKEVVL----KDGEV--IPTGLVVWSTGVGPGPLTKQLKVDkTSRGRISVD-DHLRVKPI 308
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 613307026 291 SNVFALGDASNV---PTSKTGAAIRKQAPIVA---NNLLQ 324
Cdd:PTZ00318 309 PNVFALGDCAANeerPLPTLAQVASQQGVYLAkefNNELK 348
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
5-298 2.75e-09

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: 57.71  E-value: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026    5 YQIVIIGGGTAGVTVASRLLRKNQnlkeKIAII-DPADHHYYQPLWTLV-------GAGVSSLKSSRKDMESVIPEGAHW 76
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGG----KVTLIeDEGTCPYGGCVLSKAllgaaeaPEIASLWADLYKRKEEVVKKLNNG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026   77 IK----QAVSSFQPENNSVIL-----GDNTVVYYDFLVVAPGLQINWSSIKGLKENIGKNgvcsnyspdyvnetwnqISN 147
Cdd:pfam07992  77 IEvllgTEVVSIDPGAKKVVLeelvdGDGETITYDRLVIATGARPRLPPIPGVELNVGFL-----------------VRT 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026  148 FKQGNAIFtHPNTPIK---CGGAPMKIMyLAEDYfrkHKIRSNANVIYATPKdALFDVGKYN-KELERIVEERNITVNYN 223
Cdd:pfam07992 140 LDSAEALR-LKLLPKRvvvVGGGYIGVE-LAAAL---AKLGKEVTLIEALDR-LLRAFDEEIsAALEKALEKNGVEVRLG 213
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613307026  224 YNLVEIDGDKKVATfehIKTYDRKTISYDMLHVTPPMGPLDVVKEST--LSDSEGWVDVNPTtlQHKSYSNVFALGD 298
Cdd:pfam07992 214 TSVKEIIGDGDGVE---VILKDGTEIDADLVVVAIGRRPNTELLEAAglELDERGGIVVDEY--LRTSVPGIYAAGD 285
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
3-42 3.83e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 39.39  E-value: 3.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 613307026   3 KHYQIVIIGGGTAGVTVASRLLRknqnLKEKIAIIDPADH 42
Cdd:PRK06292   2 EKYDVIVIGAGPAGYVAARRAAK----LGKKVALIEKGPL 37
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
2-38 5.57e-03

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: 38.53  E-value: 5.57e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 613307026   2 NKHYQIVIIGGGTAGVTVASRLLRknqnLKEKIAIID 38
Cdd:COG1249    1 MKDYDLVVIGAGPGGYVAAIRAAQ----LGLKVALVE 33
 
Name Accession Description Interval E-value
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
25-351 8.87e-70

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: 222.38  E-value: 8.87e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026  25 RKNQNLKekIAIIDPADHHYYQP--LWTLVGAGVSSLKS-SRKDMESVIPEGAHWIKQA-VSSFQPENNSVILGDNTVVY 100
Cdd:COG0446    1 RLGPDAE--ITVIEKGPHHSYQPcgLPYYVGGGIKDPEDlLVRTPESFERKGIDVRTGTeVTAIDPEAKTVTLRDGETLS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026 101 YDFLVVAPGLQINWSSIKGLKEnigkNGVCSNYSPDYVNETWNQISNFKQGNAIFThpntpikcGGAPmkIMYLAEDYFR 180
Cdd:COG0446   79 YDKLVLATGARPRPPPIPGLDL----PGVFTLRTLDDADALREALKEFKGKRAVVI--------GGGP--IGLELAEALR 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026 181 KHKIrsNANVIYATPkdALFdvGKYNKE----LERIVEERNITVNYNYNLVEIDGDKKVAtfehIKTYDRKTISYDMLHV 256
Cdd:COG0446  145 KRGL--KVTLVERAP--RLL--GVLDPEmaalLEEELREHGVELRLGETVVAIDGDDKVA----VTLTDGEEIPADLVVV 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026 257 TPPMGP-LDVVKESTLS-DSEGWVDVNPtTLQHkSYSNVFALGDASNVP---TSKT-----GAAIRKQAPIVANNLL--Q 324
Cdd:COG0446  215 APGVRPnTELAKDAGLAlGERGWIKVDE-TLQT-SDPDVYAAGDCAEVPhpvTGKTvyiplASAANKQGRVAAENILggP 292
                        330       340
                 ....*....|....*....|....*..
gi 613307026 325 VMNNQMLTHHYDGYTSCPIVTGYNRLI 351
Cdd:COG0446  293 APFPGLGTFISKVFDLCIASTGTGRLL 319
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
7-349 7.58e-50

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 172.62  E-value: 7.58e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026   7 IVIIGGGTAGVTVASRLlRKNQNLKEKIAIIDPADHHYYQPLWTLVGAGVSSLKSSRKDMESVIPE-GAHWIKQAVSSFQ 85
Cdd:COG1252    4 IVIVGGGFAGLEAARRL-RKKLGGDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRaGVRFIQGEVTGID 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026  86 PENNSVILGDNTVVYYDFLVVAPGLQINWSSIKGLKENIgkngvCSNYSPDYVNETWNQISNFKQGNAIFTHPNTPIkCG 165
Cdd:COG1252   83 PEARTVTLADGRTLSYDYLVIATGSVTNFFGIPGLAEHA-----LPLKTLEDALALRERLLAAFERAERRRLLTIVV-VG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026 166 GAP------MKIMYLAEDYFRKHKIR-SNANVIYATPKDALF-----DVGKYnkeLERIVEERNITVNYNYNLVEIDGDk 233
Cdd:COG1252  157 GGPtgvelaGELAELLRKLLRYPGIDpDKVRITLVEAGPRILpglgeKLSEA---AEKELEKRGVEVHTGTRVTEVDAD- 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026 234 kvatfeHIKTYDRKTISYDMLHVTPPMGPLDVVKESTLS-DSEGWVDVNPtTLQHKSYSNVFALGDASNVPTS------K 306
Cdd:COG1252  233 ------GVTLEDGEEIPADTVIWAAGVKAPPLLADLGLPtDRRGRVLVDP-TLQVPGHPNVFAIGDCAAVPDPdgkpvpK 305
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 613307026 307 TGAAIRKQAPIVANNLLQVMNNQ-MLTHHYDGYtSCPIVTGYNR 349
Cdd:COG1252  306 TAQAAVQQAKVLAKNIAALLRGKpLKPFRYRDK-GCLASLGRGA 348
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
7-324 4.43e-10

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 60.94  E-value: 4.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026   7 IVIIGGGTAGvtvaSRLLRKNQNLKEKIAIIDPADHHYYQPLwtLVGAGVSSLKSsRKDMESVIPEGAH----WIKQAVS 82
Cdd:PTZ00318  13 VVVLGTGWAG----AYFVRNLDPKKYNITVISPRNHMLFTPL--LPQTTTGTLEF-RSICEPVRPALAKlpnrYLRAVVY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026  83 SFQPENNSVILG----------DNTVVYYDFLVVAPGLQINWSSIKGLKENIgkngvcsnYSPDYVNETWNQISNFKQGN 152
Cdd:PTZ00318  86 DVDFEEKRVKCGvvsksnnanvNTFSVPYDKLVVAHGARPNTFNIPGVEERA--------FFLKEVNHARGIRKRIVQCI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026 153 AIFTHPNTPIK----------CGGAPMKIMYLAE--DYFRKHKIRSNANVIyATPKDALFDVGK-----YNKELERIVEE 215
Cdd:PTZ00318 158 ERASLPTTSVEerkrllhfvvVGGGPTGVEFAAElaDFFRDDVRNLNPELV-EECKVTVLEAGSevlgsFDQALRKYGQR 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026 216 R----NITVNYNYNLVEIDgDKKVATfehiKTYDRktISYDMLHVTPPMGPLDVVKESTLS-DSEGWVDVNpTTLQHKSY 290
Cdd:PTZ00318 237 RlrrlGVDIRTKTAVKEVL-DKEVVL----KDGEV--IPTGLVVWSTGVGPGPLTKQLKVDkTSRGRISVD-DHLRVKPI 308
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 613307026 291 SNVFALGDASNV---PTSKTGAAIRKQAPIVA---NNLLQ 324
Cdd:PTZ00318 309 PNVFALGDCAANeerPLPTLAQVASQQGVYLAkefNNELK 348
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
5-298 2.75e-09

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: 57.71  E-value: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026    5 YQIVIIGGGTAGVTVASRLLRKNQnlkeKIAII-DPADHHYYQPLWTLV-------GAGVSSLKSSRKDMESVIPEGAHW 76
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGG----KVTLIeDEGTCPYGGCVLSKAllgaaeaPEIASLWADLYKRKEEVVKKLNNG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026   77 IK----QAVSSFQPENNSVIL-----GDNTVVYYDFLVVAPGLQINWSSIKGLKENIGKNgvcsnyspdyvnetwnqISN 147
Cdd:pfam07992  77 IEvllgTEVVSIDPGAKKVVLeelvdGDGETITYDRLVIATGARPRLPPIPGVELNVGFL-----------------VRT 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026  148 FKQGNAIFtHPNTPIK---CGGAPMKIMyLAEDYfrkHKIRSNANVIYATPKdALFDVGKYN-KELERIVEERNITVNYN 223
Cdd:pfam07992 140 LDSAEALR-LKLLPKRvvvVGGGYIGVE-LAAAL---AKLGKEVTLIEALDR-LLRAFDEEIsAALEKALEKNGVEVRLG 213
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613307026  224 YNLVEIDGDKKVATfehIKTYDRKTISYDMLHVTPPMGPLDVVKEST--LSDSEGWVDVNPTtlQHKSYSNVFALGD 298
Cdd:pfam07992 214 TSVKEIIGDGDGVE---VILKDGTEIDADLVVVAIGRRPNTELLEAAglELDERGGIVVDEY--LRTSVPGIYAAGD 285
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
4-109 9.60e-06

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 47.44  E-value: 9.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026   4 HYQIVIIGGGTAGVTVASRLLRKNQNLkeKIAIIDPADHHYYQ--PLwtlvgagvSSLKSSRKDMESVIPEGAHWIKQ-- 79
Cdd:COG1251    1 KMRIVIIGAGMAGVRAAEELRKLDPDG--EITVIGAEPHPPYNrpPL--------SKVLAGETDEEDLLLRPADFYEEng 70
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 613307026  80 -------AVSSFQPENNSVILGDNTVVYYDFLVVAPG 109
Cdd:COG1251   71 idlrlgtRVTAIDRAARTVTLADGETLPYDKLVLATG 107
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
206-323 5.38e-05

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 45.17  E-value: 5.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026 206 NKELERIVEERnITVNYNYNLVEIDGDKKVATFEHIKTYDRKTISYDMLHV-------TPPMGP--LDVVKestlsDSEG 276
Cdd:PRK06292 213 SKQAQKILSKE-FKIKLGAKVTSVEKSGDEKVEELEKGGKTETIEADYVLVatgrrpnTDGLGLenTGIEL-----DERG 286
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 613307026 277 WVDVNPTTLQhkSYSNVFALGDASNVPTSKTGAAirKQAPIVANNLL 323
Cdd:PRK06292 287 RPVVDEHTQT--SVPGIYAAGDVNGKPPLLHEAA--DEGRIAAENAA 329
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
209-298 1.24e-03

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 40.49  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613307026 209 LERIVEERNITVNYNYNLVEIDGDKKV--ATFEHIKTYDRKTISYDMLHV----TPPMGPLdvvKESTLS-DSEGWVDVN 281
Cdd:COG0492  183 VERLRANPKIEVLWNTEVTEIEGDGRVegVTLKNVKTGEEKELEVDGVFVaiglKPNTELL---KGLGLElDEDGYIVVD 259
                         90
                 ....*....|....*..
gi 613307026 282 PTTlqHKSYSNVFALGD 298
Cdd:COG0492  260 EDM--ETSVPGVFAAGD 274
YdhS COG4529
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
7-56 2.97e-03

Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];


Pssm-ID: 443597 [Multi-domain]  Cd Length: 466  Bit Score: 39.55  E-value: 2.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 613307026   7 IVIIGGGTAGVTVASRLLRkNQNLKEKIAIIDPADHhyyqplwtlVGAGV 56
Cdd:COG4529    8 IAIIGGGASGTALAIHLLR-RAPEPLRITLFEPRPE---------LGRGV 47
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
1-58 3.29e-03

L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 39.36  E-value: 3.29e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 613307026   1 MNKHYQIVIIGGGTAGVTVAsRLLRKNQNLkeKIAIIDPADHhyyqplwtlVGAGVSS 58
Cdd:COG0579    1 MMEMYDVVIIGAGIVGLALA-RELSRYEDL--KVLVLEKEDD---------VAQESSG 46
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
3-42 3.83e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 39.39  E-value: 3.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 613307026   3 KHYQIVIIGGGTAGVTVASRLLRknqnLKEKIAIIDPADH 42
Cdd:PRK06292   2 EKYDVIVIGAGPAGYVAARRAAK----LGKKVALIEKGPL 37
NAD_binding_9 pfam13454
FAD-NAD(P)-binding;
8-42 5.47e-03

FAD-NAD(P)-binding;


Pssm-ID: 433222 [Multi-domain]  Cd Length: 155  Bit Score: 37.26  E-value: 5.47e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 613307026    8 VIIGGGTAGVTVASRLLRKNQNLKEKIAIIDPADH 42
Cdd:pfam13454   1 AIVGGGPSGLALLERLLARAPKRPLEITLFDPSPP 35
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
2-38 5.57e-03

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: 38.53  E-value: 5.57e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 613307026   2 NKHYQIVIIGGGTAGVTVASRLLRknqnLKEKIAIID 38
Cdd:COG1249    1 MKDYDLVVIGAGPGGYVAAIRAAQ----LGLKVALVE 33
 
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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