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Conserved domains on  [gi|18478646|gb|AAL73229|]
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p53-responsive gene 3 [Homo sapiens]

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];
76-355 4.04e-37

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


:

Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 137.96  E-value: 4.04e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646  76 NFRQGLVVGIDLKNQMVLLQGGEALPFSHLILATGSTGPFPGkfNE--------VSSQQAAIQAYEDMVRQVQRS----- 142
Cdd:COG1252  72 RFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFG--IPglaehalpLKTLEDALALRERLLAAFERAerrrl 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646 143 -RF---------IvvvgggsagvEMAAEI------KTEYPEK-----EVTLIHsqvalADKELLP----SVRQEVKEILL 197
Cdd:COG1252 150 lTIvvvgggptgV----------ELAGELaellrkLLRYPGIdpdkvRITLVE-----AGPRILPglgeKLSEAAEKELE 214

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646 198 RKGVQLLLSERVSNLEELplneyreyiKVQTDKGTEVATNLVILCTGIKINSSAYRKAFEsrLASSGALRVNEHLQVEGH 277
Cdd:COG1252 215 KRGVEVHTGTRVTEVDAD---------GVTLEDGEEIPADTVIWAAGVKAPPLLADLGLP--TDRRGRVLVDPTLQVPGH 283

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646 278 SNVYAIGDCADVR------TPKMAYLAGLHANIAVANIVNSVKQRPLQAYKPGALTFLLSMGRNDGVGQISGFYVGRLMV 351
Cdd:COG1252 284 PNVFAIGDCAAVPdpdgkpVPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGGLKLSGFLA 363


                ....
gi 18478646 352 RLTK 355
Cdd:COG1252 364 WLLK 367
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
76-355 4.04e-37

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 137.96  E-value: 4.04e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646  76 NFRQGLVVGIDLKNQMVLLQGGEALPFSHLILATGSTGPFPGkfNE--------VSSQQAAIQAYEDMVRQVQRS----- 142
Cdd:COG1252  72 RFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFG--IPglaehalpLKTLEDALALRERLLAAFERAerrrl 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646 143 -RF---------IvvvgggsagvEMAAEI------KTEYPEK-----EVTLIHsqvalADKELLP----SVRQEVKEILL 197
Cdd:COG1252 150 lTIvvvgggptgV----------ELAGELaellrkLLRYPGIdpdkvRITLVE-----AGPRILPglgeKLSEAAEKELE 214

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646 198 RKGVQLLLSERVSNLEELplneyreyiKVQTDKGTEVATNLVILCTGIKINSSAYRKAFEsrLASSGALRVNEHLQVEGH 277
Cdd:COG1252 215 KRGVEVHTGTRVTEVDAD---------GVTLEDGEEIPADTVIWAAGVKAPPLLADLGLP--TDRRGRVLVDPTLQVPGH 283

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646 278 SNVYAIGDCADVR------TPKMAYLAGLHANIAVANIVNSVKQRPLQAYKPGALTFLLSMGRNDGVGQISGFYVGRLMV 351
Cdd:COG1252 284 PNVFAIGDCAAVPdpdgkpVPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGGLKLSGFLA 363


                ....
gi 18478646 352 RLTK 355
Cdd:COG1252 364 WLLK 367
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
77-310 1.92e-15

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 76.88  E-value: 1.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646   77 FRQGLVVGIDLKNQMVLLQGgEALPFSHLILATGSTG---PFPGkfNEV----SSQQAaIQAYEDMVRQVQRsrfIVVVG 149
Cdd:PRK04965  76 FPHTWVTDIDAEAQVVKSQG-NQWQYDKLVLATGASAfvpPIPG--RELmltlNSQQE-YRAAETQLRDAQR---VLVVG 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646  150 GGSAGVEMAAEIKTEypEKEVTLIHSQVALADKELLPSVRQEVKEILLRKGVQLLLSERVSNLEELplneyREYIKVQTD 229
Cdd:PRK04965 149 GGLIGTELAMDLCRA--GKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKT-----DSGIRATLD 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646  230 KGTEVATNLVILCTGIKINSSAyrkAFESRLASSGALRVNEHLQVEgHSNVYAIGDCADVRTPKMAYL--AGLHANIAVA 307
Cdd:PRK04965 222 SGRSIEVDAVIAAAGLRPNTAL---ARRAGLAVNRGIVVDSYLQTS-APDIYALGDCAEINGQVLPFLqpIQLSAMALAK 297


                 ...
gi 18478646  308 NIV 310
Cdd:PRK04965 298 NLL 300
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 19-302 1.50e-07

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: 52.32  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646    19 GGFGGIAAASQLQALNVPFMLVDMKDSFHHN----VAALRASVETGFAKKTFISYSVTFK---DNFRQGL-------VVG 84
Cdd:pfam07992   8 GGPAGLAAALTLAQLGGKVTLIEDEGTCPYGgcvlSKALLGAAEAPEIASLWADLYKRKEevvKKLNNGIevllgteVVS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646    85 IDLKNQMVLLQ-----GGEALPFSHLILATGSTG---PFPGKFNEVSSQQAAIQAYEDMVRQVQRSR-------FIvvvg 149
Cdd:pfam07992  88 IDPGAKKVVLEelvdgDGETITYDRLVIATGARPrlpPIPGVELNVGFLVRTLDSAEALRLKLLPKRvvvvgggYI---- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646   150 ggsaGVEMAAEIkTEYPeKEVTLIHSQVALAdKELLPSVRQEVKEILLRKGVQLLLSERVSNLEELPlneyrEYIKVQTD 229
Cdd:pfam07992 164 ----GVELAAAL-AKLG-KEVTLIEALDRLL-RAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDG-----DGVEVILK 231

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18478646   230 KGTEVATNLVILCTGIKINSSAYRKA-FEsrLASSGALRVNEHLQVEgHSNVYAIGDCaDVRTPKMAYLAGLHA 302
Cdd:pfam07992 232 DGTEIDADLVVVAIGRRPNTELLEAAgLE--LDERGGIVVDEYLRTS-VPGIYAAGDC-RVGGPELAQNAVAQG 301
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 82-290 1.30e-06

nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 50.21  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646    82 VVGIDLKNQMVLLQGGEALPFSHLILATGSTG---PFPGkfnevSSQQAA--------IQAYEDMVRQVQRSRFIVVVGG 150
Cdd:TIGR02374  77 VIQIDTDQKQVITDAGRTLSYDKLILATGSYPfilPIPG-----ADKKGVyvfrtiedLDAIMAMAQRFKKAAVIGGGLL 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646   151 GsagveMAAEIKTEYPEKEVTLIHSQVALADKELLPSVRQEVKEILLRKGVQLLLSErvsNLEELPLNEYREYIKVQtdK 230
Cdd:TIGR02374 152 G-----LEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEK---DTVEIVGATKADRIRFK--D 221

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646   231 GTEVATNLVILCTGIKINSSAyrkAFESRLASSGALRVNEHLQVEgHSNVYAIGDCADVR 290
Cdd:TIGR02374 222 GSSLEADLIVMAAGIRPNDEL---AVSAGIKVNRGIIVNDSMQTS-DPDIYAVGECAEHN 277
 
Name Accession Description Interval E-value
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
76-355 4.04e-37

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 137.96  E-value: 4.04e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646  76 NFRQGLVVGIDLKNQMVLLQGGEALPFSHLILATGSTGPFPGkfNE--------VSSQQAAIQAYEDMVRQVQRS----- 142
Cdd:COG1252  72 RFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFG--IPglaehalpLKTLEDALALRERLLAAFERAerrrl 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646 143 -RF---------IvvvgggsagvEMAAEI------KTEYPEK-----EVTLIHsqvalADKELLP----SVRQEVKEILL 197
Cdd:COG1252 150 lTIvvvgggptgV----------ELAGELaellrkLLRYPGIdpdkvRITLVE-----AGPRILPglgeKLSEAAEKELE 214

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646 198 RKGVQLLLSERVSNLEELplneyreyiKVQTDKGTEVATNLVILCTGIKINSSAYRKAFEsrLASSGALRVNEHLQVEGH 277
Cdd:COG1252 215 KRGVEVHTGTRVTEVDAD---------GVTLEDGEEIPADTVIWAAGVKAPPLLADLGLP--TDRRGRVLVDPTLQVPGH 283

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646 278 SNVYAIGDCADVR------TPKMAYLAGLHANIAVANIVNSVKQRPLQAYKPGALTFLLSMGRNDGVGQISGFYVGRLMV 351
Cdd:COG1252 284 PNVFAIGDCAAVPdpdgkpVPKTAQAAVQQAKVLAKNIAALLRGKPLKPFRYRDKGCLASLGRGAAVADVGGLKLSGFLA 363


                ....
gi 18478646 352 RLTK 355
Cdd:COG1252 364 WLLK 367
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 64-310 2.70e-24

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: 101.43  E-value: 2.70e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646  64 KTFISYSVTFKdnfRQGLVVGIDLKNQMVLLQGGEALPFSHLILATGST---GPFPG-KFNEVSSqqaaIQAYEDMVR-- 137
Cdd:COG0446  44 ESFERKGIDVR---TGTEVTAIDPEAKTVTLRDGETLSYDKLVLATGARprpPPIPGlDLPGVFT----LRTLDDADAlr 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646 138 ------QVQR-----SRFIvvvgggsaGVEMAAEIKTEypEKEVTLIH--SQV-ALADKEllpsVRQEVKEILLRKGVQL 203
Cdd:COG0446 117 ealkefKGKRavvigGGPI--------GLELAEALRKR--GLKVTLVEraPRLlGVLDPE----MAALLEEELREHGVEL 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646 204 LLSERVSNLEElplneyREYIKVQTDKGTEVATNLVILCTGIKINSSAyrkAFESRLA--SSGALRVNEHLQVeGHSNVY 281
Cdd:COG0446 183 RLGETVVAIDG------DDKVAVTLTDGEEIPADLVVVAPGVRPNTEL---AKDAGLAlgERGWIKVDETLQT-SDPDVY 252

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 18478646 282 AIGDCADVR---TPKMAYLA-GLHAN----IAVANIV 310
Cdd:COG0446 253 AAGDCAEVPhpvTGKTVYIPlASAANkqgrVAAENIL 289
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
82-310 1.83e-15

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 77.10  E-value: 1.83e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646  82 VVGIDLKNQMVLLQGGEALPFSHLILATGSTgPF----PGkfnevsSQQAAIQAY------EDMVRQVQRSR-------- 143
Cdd:COG1251  79 VTAIDRAARTVTLADGETLPYDKLVLATGSR-PRvppiPG------ADLPGVFTLrtlddaDALRAALAPGKrvvviggg 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646 144 FIvvvgggsaGVEMAAEIKTEypEKEVTLIHSQVALADKELLPSVRQEVKEILLRKGVQLLLSERVSNLEElplNEYREy 223
Cdd:COG1251 152 LI--------GLEAAAALRKR--GLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEG---DDRVT- 217

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646 224 iKVQTDKGTEVATNLVILCTGIKINSSAyrkAFESRLASSGALRVNEHLQVeGHSNVYAIGDCADVRTPkmayLAGLHAN 303
Cdd:COG1251 218 -GVRLADGEELPADLVVVAIGVRPNTEL---ARAAGLAVDRGIVVDDYLRT-SDPDIYAAGDCAEHPGP----VYGRRVL 288


                ....*..
gi 18478646 304 IAVANIV 310
Cdd:COG1251 289 ELVAPAY 295
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
77-310 1.92e-15

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 76.88  E-value: 1.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646   77 FRQGLVVGIDLKNQMVLLQGgEALPFSHLILATGSTG---PFPGkfNEV----SSQQAaIQAYEDMVRQVQRsrfIVVVG 149
Cdd:PRK04965  76 FPHTWVTDIDAEAQVVKSQG-NQWQYDKLVLATGASAfvpPIPG--RELmltlNSQQE-YRAAETQLRDAQR---VLVVG 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646  150 GGSAGVEMAAEIKTEypEKEVTLIHSQVALADKELLPSVRQEVKEILLRKGVQLLLSERVSNLEELplneyREYIKVQTD 229
Cdd:PRK04965 149 GGLIGTELAMDLCRA--GKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKT-----DSGIRATLD 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646  230 KGTEVATNLVILCTGIKINSSAyrkAFESRLASSGALRVNEHLQVEgHSNVYAIGDCADVRTPKMAYL--AGLHANIAVA 307
Cdd:PRK04965 222 SGRSIEVDAVIAAAGLRPNTAL---ARRAGLAVNRGIVVDSYLQTS-APDIYALGDCAEINGQVLPFLqpIQLSAMALAK 297


                 ...
gi 18478646  308 NIV 310
Cdd:PRK04965 298 NLL 300
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 77-344 6.73e-12

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 66.33  E-value: 6.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646   77 FRQGLVVGIDLKNQMVL----------LQGGEALPFSHLILATGSTgpfPGKFNevssqqaaIQAYEDMV---RQVQRSR 143
Cdd:PTZ00318  79 YLRAVVYDVDFEEKRVKcgvvsksnnaNVNTFSVPYDKLVVAHGAR---PNTFN--------IPGVEERAfflKEVNHAR 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646  144 FIVVVGGGSAgveMAAEIKTEYPEKEVTLIHSQVA------------LAD------KELLPSVRQEVKEILLRKGVQLLL 205
Cdd:PTZ00318 148 GIRKRIVQCI---ERASLPTTSVEERKRLLHFVVVgggptgvefaaeLADffrddvRNLNPELVEECKVTVLEAGSEVLG 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646  206 S--ERVSNLEELPLNEYREYIKVQ------------TDKGTEVATNLVILCTGIkiNSSAYRKAFESRLASSGALRVNEH 271
Cdd:PTZ00318 225 SfdQALRKYGQRRLRRLGVDIRTKtavkevldkevvLKDGEVIPTGLVVWSTGV--GPGPLTKQLKVDKTSRGRISVDDH 302

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18478646  272 LQVEGHSNVYAIGDCADVRT---PKMAYLAGLHANIAVANIVNSVKQRPLQayKPGALTFLLSM---GRNDGVGQISGF 344
Cdd:PTZ00318 303 LRVKPIPNVFALGDCAANEErplPTLAQVASQQGVYLAKEFNNELKGKPMS--KPFVYRSLGSLaylGNYSAIVQLGAF 379
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 156-289 1.59e-11

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 65.45  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646  156 EMAAEIKTEypEKEVTLI-HSQVALA---DKELLPSVRQEVKEillrKGVQLLLSERVSNLEelplNEYREYiKVQTDKG 231
Cdd:PRK09564 163 EAVEAAKHL--GKNVRIIqLEDRILPdsfDKEITDVMEEELRE----NGVELHLNEFVKSLI----GEDKVE-GVVTDKG 231

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18478646  232 tEVATNLVILCTGIKINSSAYRKAFESRLAsSGALRVNEhlqvEGHS---NVYAIGDCADV 289
Cdd:PRK09564 232 -EYEADVVIVATGVKPNTEFLEDTGLKTLK-NGAIIVDE----YGETsieNIYAAGDCATI 286
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 92-311 2.43e-08

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: 55.48  E-value: 2.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646  92 VLLQGGEALPFSHLILATGSTG---PFPGKFNE--VSSQQAaiqayEDMVRQVQR-----SRFIvvvgggsaGVEMA--- 158
Cdd:COG1249 121 VEVTGGETLTADHIVIATGSRPrvpPIPGLDEVrvLTSDEA-----LELEELPKSlvvigGGYI--------GLEFAqif 187

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646 159 AEIKTeypekEVTLIHSQ---VALADKEllpsVRQEVKEILLRKGVQLLLSERVSNLEELPlneyrEYIKVQTDKGTEVA 235
Cdd:COG1249 188 ARLGS-----EVTLVERGdrlLPGEDPE----ISEALEKALEKEGIDILTGAKVTSVEKTG-----DGVTVTLEDGGGEE 253

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646 236 TN---LVILCTGIKINSSAYrkAFES---RLASSGALRVNEHLQVeGHSNVYAIGDCADvrTPKMAYLAGLHANIAVANI 309
Cdd:COG1249 254 AVeadKVLVATGRRPNTDGL--GLEAagvELDERGGIKVDEYLRT-SVPGIYAIGDVTG--GPQLAHVASAEGRVAAENI 328


                ..
gi 18478646 310 VN 311
Cdd:COG1249 329 LG 330
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 19-302 1.50e-07

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: 52.32  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646    19 GGFGGIAAASQLQALNVPFMLVDMKDSFHHN----VAALRASVETGFAKKTFISYSVTFK---DNFRQGL-------VVG 84
Cdd:pfam07992   8 GGPAGLAAALTLAQLGGKVTLIEDEGTCPYGgcvlSKALLGAAEAPEIASLWADLYKRKEevvKKLNNGIevllgteVVS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646    85 IDLKNQMVLLQ-----GGEALPFSHLILATGSTG---PFPGKFNEVSSQQAAIQAYEDMVRQVQRSR-------FIvvvg 149
Cdd:pfam07992  88 IDPGAKKVVLEelvdgDGETITYDRLVIATGARPrlpPIPGVELNVGFLVRTLDSAEALRLKLLPKRvvvvgggYI---- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646   150 ggsaGVEMAAEIkTEYPeKEVTLIHSQVALAdKELLPSVRQEVKEILLRKGVQLLLSERVSNLEELPlneyrEYIKVQTD 229
Cdd:pfam07992 164 ----GVELAAAL-AKLG-KEVTLIEALDRLL-RAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDG-----DGVEVILK 231

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18478646   230 KGTEVATNLVILCTGIKINSSAYRKA-FEsrLASSGALRVNEHLQVEgHSNVYAIGDCaDVRTPKMAYLAGLHA 302
Cdd:pfam07992 232 DGTEIDADLVVVAIGRRPNTELLEAAgLE--LDERGGIVVDEYLRTS-VPGIYAAGDC-RVGGPELAQNAVAQG 301
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 82-290 1.30e-06

nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 50.21  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646    82 VVGIDLKNQMVLLQGGEALPFSHLILATGSTG---PFPGkfnevSSQQAA--------IQAYEDMVRQVQRSRFIVVVGG 150
Cdd:TIGR02374  77 VIQIDTDQKQVITDAGRTLSYDKLILATGSYPfilPIPG-----ADKKGVyvfrtiedLDAIMAMAQRFKKAAVIGGGLL 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646   151 GsagveMAAEIKTEYPEKEVTLIHSQVALADKELLPSVRQEVKEILLRKGVQLLLSErvsNLEELPLNEYREYIKVQtdK 230
Cdd:TIGR02374 152 G-----LEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEK---DTVEIVGATKADRIRFK--D 221

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646   231 GTEVATNLVILCTGIKINSSAyrkAFESRLASSGALRVNEHLQVEgHSNVYAIGDCADVR 290
Cdd:TIGR02374 222 GSSLEADLIVMAAGIRPNDEL---AVSAGIKVNRGIIVNDSMQTS-DPDIYAVGECAEHN 277
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 96-309 1.34e-06

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: 49.95  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646    96 GGEALPFSHLILATGS-----TGPFPGKFNEVSSQQAAIQayedmVRQVQRSRFIVVvgggsagvemAAEIKTEYPE--- 167
Cdd:TIGR01350 126 GEETLEAKNIIIATGSrprslPGPFDFDGKVVITSTGALN-----LEEVPESLVIIG----------GGVIGIEFASifa 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18478646   168 ---KEVTLIHSQvaladKELLP----SVRQEVKEILLRKGVQLLLSERVSNLEELplneyREYIKVQTDKGTEVAT--NL 238
Cdd:TIGR01350 191 slgSKVTVIEML-----DRILPgedaEVSKVLQKALKKKGVKILTNTKVTAVEKN-----DDQVTYENKGGETETLtgEK 260

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18478646   239 VILCTGIKINSSAY-RKAFESRLASSGALRVNEHLQVeGHSNVYAIGDCadVRTPKMAYLAGLHANIAVANI 309
Cdd:TIGR01350 261 VLVAVGRKPNTEGLgLEKLGVELDERGRIVVDEYMRT-NVPGIYAIGDV--IGGPMLAHVASHEGIVAAENI 329
PLN02507 PLN02507
glutathione reductase
 210-285 4.00e-03

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 39.03  E-value: 4.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18478646  210 SNLEELPLNEyrEYIKVQTDKGTEVATNLVILCTGIKINSSAYR-KAFESRLASSGALRVNEHLQVEGHSnVYAIGD 285
Cdd:PLN02507 265 TNLTQLTKTE--GGIKVITDHGEEFVADVVLFATGRAPNTKRLNlEAVGVELDKAGAVKVDEYSRTNIPS-IWAIGD 338
 
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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