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Conserved domains on  [gi|1965217581|ref|XP_039014454|]
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alternative NAD(P)H-ubiquinone oxidoreductase C1, chloroplastic/mitochondrial-like isoform X2 [Hibiscus syriacus]

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

 Zoom to residue level

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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];
1-311 9.74e-51

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


:

Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 172.24  E-value: 9.74e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581   1 MLYELLSGEVDDWEIAPRFSELLANTGVQFLQDKVKILHPSDHwgmnghkqsscggTVLLESGLLIEYDWLVLALGVEAK 80
Cdd:COG1252    44 LLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTGIDPEAR-------------TVTLADGRTLSYDYLVIATGSVTN 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581  81 LDVVQGALEFALPFSTLDDACKVNKKLRT-LERMKfgKDSLICVAVVGCGYSGVELAATISERLQDRGIVQAINVE---- 155
Cdd:COG1252   111 FFGIPGLAEHALPLKTLEDALALRERLLAaFERAE--RRRLLTIVVVGGGPTGVELAGELAELLRKLLRYPGIDPDkvri 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581 156 ------TTICPTAPAGNREAALKVLSSRKVQLLLGyfvrcvrrvtdmetsgdATVKREGKDIAESNSEkyvldlqpaekg 229
Cdd:COG1252   189 tlveagPRILPGLGEKLSEAAEKELEKRGVEVHTG-----------------TRVTEVDADGVTLEDG------------ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581 230 lesQILEADLVLWTVGSKA--LLPELepcdkphELPLNARGQAETDETLRVKGHPRIFAIGDSSSLRDSAGRLLPATAQH 307
Cdd:COG1252   240 ---EEIPADTVIWAAGVKAppLLADL-------GLPTDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPDPDGKPVPKTAQA 309


                  ....
gi 1965217581 308 CQSQ 311
Cdd:COG1252   310 AVQQ 313
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
1-311 9.74e-51

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 172.24  E-value: 9.74e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581   1 MLYELLSGEVDDWEIAPRFSELLANTGVQFLQDKVKILHPSDHwgmnghkqsscggTVLLESGLLIEYDWLVLALGVEAK 80
Cdd:COG1252    44 LLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTGIDPEAR-------------TVTLADGRTLSYDYLVIATGSVTN 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581  81 LDVVQGALEFALPFSTLDDACKVNKKLRT-LERMKfgKDSLICVAVVGCGYSGVELAATISERLQDRGIVQAINVE---- 155
Cdd:COG1252   111 FFGIPGLAEHALPLKTLEDALALRERLLAaFERAE--RRRLLTIVVVGGGPTGVELAGELAELLRKLLRYPGIDPDkvri 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581 156 ------TTICPTAPAGNREAALKVLSSRKVQLLLGyfvrcvrrvtdmetsgdATVKREGKDIAESNSEkyvldlqpaekg 229
Cdd:COG1252   189 tlveagPRILPGLGEKLSEAAEKELEKRGVEVHTG-----------------TRVTEVDADGVTLEDG------------ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581 230 lesQILEADLVLWTVGSKA--LLPELepcdkphELPLNARGQAETDETLRVKGHPRIFAIGDSSSLRDSAGRLLPATAQH 307
Cdd:COG1252   240 ---EEIPADTVIWAAGVKAppLLADL-------GLPTDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPDPDGKPVPKTAQA 309


                  ....
gi 1965217581 308 CQSQ 311
Cdd:COG1252   310 AVQQ 313
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 1-311 6.15e-19

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: 85.06  E-value: 6.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581   1 MLYELLSGEVDDWEIAPRFSELLA---------NTGVQFLQD--KVKILHpsdhwgmnGHKQSSCGGTVLlESGLLIEYD 69
Cdd:pfam07992  41 VLSKALLGAAEAPEIASLWADLYKrkeevvkklNNGIEVLLGteVVSIDP--------GAKKVVLEELVD-GDGETITYD 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581  70 WLVLALGVEAKLDVVQGALEFA-LPFSTLDDACKVNKKLrTLERmkfgkdslicVAVVGCGYSGVELAATISERLQDRGI 148
Cdd:pfam07992 112 RLVIATGARPRLPPIPGVELNVgFLVRTLDSAEALRLKL-LPKR----------VVVVGGGYIGVELAAALAKLGKEVTL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581 149 VQAinvETTICPTAPAGNREAALKVLSSRKVQLLLGYFVRcvrrvtdmetsgdaTVKREGKDIAESNSEKyvldlqpaek 228
Cdd:pfam07992 181 IEA---LDRLLRAFDEEISAALEKALEKNGVEVRLGTSVK--------------EIIGDGDGVEVILKDG---------- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581 229 glesQILEADLVLWTVGSKALLPELEPCDkpheLPLNARGQAETDETLRVKgHPRIFAIGDssslrdsAGRLLPATAQHC 308
Cdd:pfam07992 234 ----TEIDADLVVVAIGRRPNTELLEAAG----LELDERGGIVVDEYLRTS-VPGIYAAGD-------CRVGGPELAQNA 297


                  ...
gi 1965217581 309 QSQ 311
Cdd:pfam07992 298 VAQ 300
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 23-311 1.76e-15

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 76.34  E-value: 1.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581  23 LANTGVQFLQDKVKILHPSDhwgmnghKQSSCGGTVLLESGLL----IEYDWLVLALGVEAKLDVVQGALEFALPFSTLD 98
Cdd:PTZ00318   72 LAKLPNRYLRAVVYDVDFEE-------KRVKCGVVSKSNNANVntfsVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVN 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581  99 DACKVNKKL-RTLERMKFG------KDSLICVAVVGCGYSGVELAATISERLQDrgivQAINVETTICPTAPAGNREAAL 171
Cdd:PTZ00318  145 HARGIRKRIvQCIERASLPttsveeRKRLLHFVVVGGGPTGVEFAAELADFFRD----DVRNLNPELVEECKVTVLEAGS 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581 172 KVLSSrkvqlllgyFVRCVRRVTDMEtsgdatVKREGKDIAESNSEKYVLDLQPAEKglESQILEADLVLWT--VGSKAL 249
Cdd:PTZ00318  221 EVLGS---------FDQALRKYGQRR------LRRLGVDIRTKTAVKEVLDKEVVLK--DGEVIPTGLVVWStgVGPGPL 283

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1965217581 250 LPELePCDKphelplNARGQAETDETLRVKGHPRIFAIGDSSSLRDsagRLLPATAQHCQSQ 311
Cdd:PTZ00318  284 TKQL-KVDK------TSRGRISVDDHLRVKPIPNVFALGDCAANEE---RPLPTLAQVASQQ 335
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
1-311 9.74e-51

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 172.24  E-value: 9.74e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581   1 MLYELLSGEVDDWEIAPRFSELLANTGVQFLQDKVKILHPSDHwgmnghkqsscggTVLLESGLLIEYDWLVLALGVEAK 80
Cdd:COG1252    44 LLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTGIDPEAR-------------TVTLADGRTLSYDYLVIATGSVTN 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581  81 LDVVQGALEFALPFSTLDDACKVNKKLRT-LERMKfgKDSLICVAVVGCGYSGVELAATISERLQDRGIVQAINVE---- 155
Cdd:COG1252   111 FFGIPGLAEHALPLKTLEDALALRERLLAaFERAE--RRRLLTIVVVGGGPTGVELAGELAELLRKLLRYPGIDPDkvri 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581 156 ------TTICPTAPAGNREAALKVLSSRKVQLLLGyfvrcvrrvtdmetsgdATVKREGKDIAESNSEkyvldlqpaekg 229
Cdd:COG1252   189 tlveagPRILPGLGEKLSEAAEKELEKRGVEVHTG-----------------TRVTEVDADGVTLEDG------------ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581 230 lesQILEADLVLWTVGSKA--LLPELepcdkphELPLNARGQAETDETLRVKGHPRIFAIGDSSSLRDSAGRLLPATAQH 307
Cdd:COG1252   240 ---EEIPADTVIWAAGVKAppLLADL-------GLPTDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPDPDGKPVPKTAQA 309


                  ....
gi 1965217581 308 CQSQ 311
Cdd:COG1252   310 AVQQ 313
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 1-311 6.15e-19

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: 85.06  E-value: 6.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581   1 MLYELLSGEVDDWEIAPRFSELLA---------NTGVQFLQD--KVKILHpsdhwgmnGHKQSSCGGTVLlESGLLIEYD 69
Cdd:pfam07992  41 VLSKALLGAAEAPEIASLWADLYKrkeevvkklNNGIEVLLGteVVSIDP--------GAKKVVLEELVD-GDGETITYD 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581  70 WLVLALGVEAKLDVVQGALEFA-LPFSTLDDACKVNKKLrTLERmkfgkdslicVAVVGCGYSGVELAATISERLQDRGI 148
Cdd:pfam07992 112 RLVIATGARPRLPPIPGVELNVgFLVRTLDSAEALRLKL-LPKR----------VVVVGGGYIGVELAAALAKLGKEVTL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581 149 VQAinvETTICPTAPAGNREAALKVLSSRKVQLLLGYFVRcvrrvtdmetsgdaTVKREGKDIAESNSEKyvldlqpaek 228
Cdd:pfam07992 181 IEA---LDRLLRAFDEEISAALEKALEKNGVEVRLGTSVK--------------EIIGDGDGVEVILKDG---------- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581 229 glesQILEADLVLWTVGSKALLPELEPCDkpheLPLNARGQAETDETLRVKgHPRIFAIGDssslrdsAGRLLPATAQHC 308
Cdd:pfam07992 234 ----TEIDADLVVVAIGRRPNTELLEAAG----LELDERGGIVVDEYLRTS-VPGIYAAGD-------CRVGGPELAQNA 297


                  ...
gi 1965217581 309 QSQ 311
Cdd:pfam07992 298 VAQ 300
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 23-311 1.76e-15

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 76.34  E-value: 1.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581  23 LANTGVQFLQDKVKILHPSDhwgmnghKQSSCGGTVLLESGLL----IEYDWLVLALGVEAKLDVVQGALEFALPFSTLD 98
Cdd:PTZ00318   72 LAKLPNRYLRAVVYDVDFEE-------KRVKCGVVSKSNNANVntfsVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVN 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581  99 DACKVNKKL-RTLERMKFG------KDSLICVAVVGCGYSGVELAATISERLQDrgivQAINVETTICPTAPAGNREAAL 171
Cdd:PTZ00318  145 HARGIRKRIvQCIERASLPttsveeRKRLLHFVVVGGGPTGVEFAAELADFFRD----DVRNLNPELVEECKVTVLEAGS 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581 172 KVLSSrkvqlllgyFVRCVRRVTDMEtsgdatVKREGKDIAESNSEKYVLDLQPAEKglESQILEADLVLWT--VGSKAL 249
Cdd:PTZ00318  221 EVLGS---------FDQALRKYGQRR------LRRLGVDIRTKTAVKEVLDKEVVLK--DGEVIPTGLVVWStgVGPGPL 283

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1965217581 250 LPELePCDKphelplNARGQAETDETLRVKGHPRIFAIGDSSSLRDsagRLLPATAQHCQSQ 311
Cdd:PTZ00318  284 TKQL-KVDK------TSRGRISVDDHLRVKPIPNVFALGDCAANEE---RPLPTLAQVASQQ 335
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 57-295 2.72e-15

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: 75.23  E-value: 2.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581  57 TVLLESGLLIEYDWLVLALGVEAKLDVVQGA-LEFALPFSTLDDACKVNKKLRTLErmkfGKDslicVAVVGCGYSGVEL 135
Cdd:COG0446    68 TVTLRDGETLSYDKLVLATGARPRPPPIPGLdLPGVFTLRTLDDADALREALKEFK----GKR----AVVIGGGPIGLEL 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581 136 AATiserLQDRGI-VQAINVETTICPTAPAGNREAALKVLSSRKVQLLLGYfvrcvrRVTDMETSGDATVKREGKdiaes 214
Cdd:COG0446   140 AEA----LRKRGLkVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGE------TVVAIDGDDKVAVTLTDG----- 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581 215 nsekyvldlqpaekglesQILEADLVLWTVGskaLLPELEPCDKPHeLPLNARGQAETDETLRVkGHPRIFAIGDSSSLR 294
Cdd:COG0446   205 ------------------EEIPADLVVVAPG---VRPNTELAKDAG-LALGERGWIKVDETLQT-SDPDVYAAGDCAEVP 261


                  .
gi 1965217581 295 D 295
Cdd:COG0446   262 H 262
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
1-289 4.00e-09

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 57.07  E-value: 4.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581   1 MLYELLSGEVDDWEIAPRFSELLANTGVQF-LQDKVKILHPSDHwgmnghkqsscggTVLLESGLLIEYDWLVLALGVEA 79
Cdd:COG1251    44 PLSKVLAGETDEEDLLLRPADFYEENGIDLrLGTRVTAIDRAAR-------------TVTLADGETLPYDKLVLATGSRP 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581  80 -KLDVVQGALEFALPFSTLDDAckvnKKLRtlERMKFGKDslicVAVVGCGYSGVELAATiserLQDRGivqainVETTI 158
Cdd:COG1251   111 rVPPIPGADLPGVFTLRTLDDA----DALR--AALAPGKR----VVVIGGGLIGLEAAAA----LRKRG------LEVTV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581 159 CPTAP------AGNREAAL--KVLSSRKVQLLLGYFVRCVR---RVTDMETSgDATVkregkdiaesnsekyvldlqpae 227
Cdd:COG1251   171 VERAPrllprqLDEEAGALlqRLLEALGVEVRLGTGVTEIEgddRVTGVRLA-DGEE----------------------- 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1965217581 228 kglesqiLEADLVLWTVGSKallPELE-------PCDkphelplnaRGqAETDETLRVkGHPRIFAIGD 289
Cdd:COG1251   227 -------LPADLVVVAIGVR---PNTElaraaglAVD---------RG-IVVDDYLRT-SDPDIYAAGD 274
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 123-289 5.64e-08

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 53.64  E-value: 5.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581 123 VAVVGCGYSGVELAATISeRLqdrGI-VQAINVETTICPTAPAGNREAALKVLsSRKVQLLLGYfvrcvrRVTDMETSGD 201
Cdd:PRK06292  172 LAVIGGGVIGLELGQALS-RL---GVkVTVFERGDRILPLEDPEVSKQAQKIL-SKEFKIKLGA------KVTSVEKSGD 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581 202 ATVKREgkdiaesnsekyvldlqpaEKGLESQILEADLVLWTVGSKALLPELepcdKPHEL--PLNARGQAETDETLRvK 279
Cdd:PRK06292  241 EKVEEL-------------------EKGGKTETIEADYVLVATGRRPNTDGL----GLENTgiELDERGRPVVDEHTQ-T 296

                         170
                  ....*....|
gi 1965217581 280 GHPRIFAIGD 289
Cdd:PRK06292  297 SVPGIYAAGD 306
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 123-289 5.89e-07

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: 50.47  E-value: 5.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581 123 VAVVGCGYSGVELAA---------TISERLqDRgivqainvettICPTAPAGNREAALKVLSSRKVQLLLGYfvrcvrRV 193
Cdd:COG1249   171 LVVIGGGYIGLEFAQifarlgsevTLVERG-DR-----------LLPGEDPEISEALEKALEKEGIDILTGA------KV 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581 194 TDMETSGDatvkregkdiaesnseKYVLDLqpaEKGLESQILEADLVLWTVGSKALLPELEPcdkphE---LPLNARGQA 270
Cdd:COG1249   233 TSVEKTGD----------------GVTVTL---EDGGGEEAVEADKVLVATGRRPNTDGLGL-----EaagVELDERGGI 288

                         170
                  ....*....|....*....
gi 1965217581 271 ETDETLRVkGHPRIFAIGD 289
Cdd:COG1249   289 KVDEYLRT-SVPGIYAIGD 306
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 58-310 1.20e-04

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 43.38  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581  58 VLLESGLLIEYDWLVLALGVEAK-LDVVQGALEFALPFSTLDDACKVNKKLRTLERmkfgkdslicVAVVGCGYSGVELA 136
Cdd:PRK09754   91 LVLTNGESWHWDQLFIATGAAARpLPLLDALGERCFTLRHAGDAARLREVLQPERS----------VVIVGAGTIGLELA 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581 137 ATISERlqdRGIVQAINVETTIC-PTAPAGNREAALKVLSSRKVQLLLGyfvrcvrrvTDMETSGDAtvkregkdiaesn 215
Cdd:PRK09754  161 ASATQR---RCKVTVIELAATVMgRNAPPPVQRYLLQRHQQAGVRILLN---------NAIEHVVDG------------- 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581 216 sEKYVLDLQPAEKglesqiLEADLVLWTVGSKALlpelepcDK-PHELPLNARGQAETDETLRVkGHPRIFAIGDSSSLR 294
Cdd:PRK09754  216 -EKVELTLQSGET------LQADVVIYGIGISAN-------DQlAREANLDTANGIVIDEACRT-CDPAIFAGGDVAITR 280

                         250
                  ....*....|....*.
gi 1965217581 295 DSAGRLlpataQHCQS 310
Cdd:PRK09754  281 LDNGAL-----HRCES 291
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 123-289 3.20e-04

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 42.06  E-value: 3.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581 123 VAVVGCGYSGVELAatiserlqdrGIVQAINVETTIC-------PTAPAGNREAALKVLSSRKVQLLLGYFVRCVrrvtd 195
Cdd:PRK06416  175 LVVIGGGYIGVEFA----------SAYASLGAEVTIVealprilPGEDKEISKLAERALKKRGIKIKTGAKAKKV----- 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965217581 196 METSGDATVKregkdiaesnsekyvldlqpAEKGLESQILEADLVLWTVGSKallPELEpcdkphELPLNA------RGQ 269
Cdd:PRK06416  240 EQTDDGVTVT--------------------LEDGGKEETLEADYVLVAVGRR---PNTE------NLGLEElgvktdRGF 290

                         170       180
                  ....*....|....*....|
gi 1965217581 270 AETDETLRvKGHPRIFAIGD 289
Cdd:PRK06416  291 IEVDEQLR-TNVPNIYAIGD 309
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 231-289 1.35e-03

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 40.12  E-value: 1.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1965217581 231 ESQILEADLVLWTVGSKallPELEPCDKPHELPLNARGQAETDETLRVKGHPRIFAIGD 289
Cdd:COG0493   354 SEFTLPADLVILAIGQT---PDPSGLEEELGLELDKRGTIVVDEETYQTSLPGVFAGGD 409
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 224-289 6.21e-03

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 38.32  E-value: 6.21e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1965217581 224 QPAEKglESQILEADLVLWTVGSKAllpELEPCDKPHELPlNARGQAETDETLRVKGHPRIFAIGD 289
Cdd:PRK12771  358 SPVTG--EEETLEADLVVLAIGQDI---DSAGLESVPGVE-VGRGVVQVDPNFMMTGRPGVFAGGD 417
 
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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