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Conserved domains on  [gi|1167382396|gb|OQB99012|]
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Dihydrolipoyl dehydrogenase [Spirochaetes bacterium ADurb.Bin110]

Protein Classification

dihydrolipoyl dehydrogenase family protein( domain architecture ID 1903490)

dihydrolipoyl dehydrogenase family protein belonging to the class-I pyridine nucleotide-disulfide oxidoreductase superfamily may function as a FAD/NAD(P)-dependent oxidoreductase, similar to dihydrolipoyl dehydrogenase which catalyzes the oxidation of dihydrolipoamide to lipoamide and is often a component of multienzyme 2-oxo-acid dehydrogenase complexes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Lpd super family cl43366
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 1-164 3.11e-56

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


The actual alignment was detected with superfamily member COG1249:

Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 182.98  E-value: 3.11e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   1 MRTNLPGIWAIGDVTGKSQLAHAAYRMAEVAVsDILAGQNAQHSDqifvAETVPWALYSLPEAAGVGLTEQDARAKGYDI 80
Cdd:COG1249   294 LRTSVPGIYAIGDVTGGPQLAHVASAEGRVAA-ENILGKKPRPVD----YRAIPSVVFTDPEIASVGLTEEEAREAGIDV 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  81 QVVRMPYNVSGRFVAENGfsAPGSIKIIIEKSSERLLGIHLLGAYASEQIWGAALALERKLPISALRNMVFPHPTVSEVI 160
Cdd:COG1249   369 KVGKFPFAANGRALALGE--TEGFVKLIADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEAL 446


                  ....
gi 1167382396 161 REAA 164
Cdd:COG1249   447 KEAA 450
 
Name Accession Description Interval E-value
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 1-164 3.11e-56

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: 182.98  E-value: 3.11e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   1 MRTNLPGIWAIGDVTGKSQLAHAAYRMAEVAVsDILAGQNAQHSDqifvAETVPWALYSLPEAAGVGLTEQDARAKGYDI 80
Cdd:COG1249   294 LRTSVPGIYAIGDVTGGPQLAHVASAEGRVAA-ENILGKKPRPVD----YRAIPSVVFTDPEIASVGLTEEEAREAGIDV 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  81 QVVRMPYNVSGRFVAENGfsAPGSIKIIIEKSSERLLGIHLLGAYASEQIWGAALALERKLPISALRNMVFPHPTVSEVI 160
Cdd:COG1249   369 KVGKFPFAANGRALALGE--TEGFVKLIADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEAL 446


                  ....
gi 1167382396 161 REAA 164
Cdd:COG1249   447 KEAA 450
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 1-164 6.54e-50

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: 166.66  E-value: 6.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   1 MRTNLPGIWAIGDVTGKSQLAHAAYRMAEVAVsDILAGQNAQHSDqifvAETVPWALYSLPEAAGVGLTEQDARAKGYDI 80
Cdd:TIGR01350 295 MRTNVPGIYAIGDVIGGPMLAHVASHEGIVAA-ENIAGKEPAHID----YDAVPSVIYTDPEVASVGLTEEQAKEAGYDV 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  81 QVVRMPYNVSGRFVAENGfsAPGSIKIIIEKSSERLLGIHLLGAYASEQIWGAALALERKLPISALRNMVFPHPTVSEVI 160
Cdd:TIGR01350 370 KIGKFPFAANGKALALGE--TDGFVKIIADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAI 447


                  ....
gi 1167382396 161 REAA 164
Cdd:TIGR01350 448 KEAA 451
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 1-169 8.74e-43

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 148.02  E-value: 8.74e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   1 MRTNLPGIWAIGDVTGKSQLAHAAYRMAEVAVsDILAGQNAQHSDqifvAETVPWALYSLPEAAGVGLTEQDARAKGYDI 80
Cdd:PRK06292  294 TQTSVPGIYAAGDVNGKPPLLHEAADEGRIAA-ENAAGDVAGGVR----YHPIPSVVFTDPQIASVGLTEEELKAAGIDY 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  81 QVVRMPYNVSGRFVAEN---GFsapgsIKIIIEKSSERLLGIHLLGAYASEQIWGAALALERKLPISALRNMVFPHPTVS 157
Cdd:PRK06292  369 VVGEVPFEAQGRARVMGkndGF-----VKVYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLS 443

                         170
                  ....*....|..
gi 1167382396 158 EVIREAAWSVQA 169
Cdd:PRK06292  444 EGLRTALRDLFS 455
Pyr_redox_dim pfam02852
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ...
 53-163 4.81e-34

Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.


Pssm-ID: 427019 [Multi-domain]  Cd Length: 109  Bit Score: 116.11  E-value: 4.81e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  53 VPWALYSLPEAAGVGLTEQDARAKGYDIQVVRMPYNVSGRFVAENGfsAPGSIKIIIEKSSERLLGIHLLGAYASEQIWG 132
Cdd:pfam02852   1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGD--TDGFVKLVADRETGKILGAHIVGPNAGELIQE 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1167382396 133 AALALERKLPISALRNMVFPHPTVSEVIREA 163
Cdd:pfam02852  79 AALAIKMGATVEDLANTIHIHPTLSEALVEA 109
 
Name Accession Description Interval E-value
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 1-164 3.11e-56

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: 182.98  E-value: 3.11e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   1 MRTNLPGIWAIGDVTGKSQLAHAAYRMAEVAVsDILAGQNAQHSDqifvAETVPWALYSLPEAAGVGLTEQDARAKGYDI 80
Cdd:COG1249   294 LRTSVPGIYAIGDVTGGPQLAHVASAEGRVAA-ENILGKKPRPVD----YRAIPSVVFTDPEIASVGLTEEEAREAGIDV 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  81 QVVRMPYNVSGRFVAENGfsAPGSIKIIIEKSSERLLGIHLLGAYASEQIWGAALALERKLPISALRNMVFPHPTVSEVI 160
Cdd:COG1249   369 KVGKFPFAANGRALALGE--TEGFVKLIADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEAL 446


                  ....
gi 1167382396 161 REAA 164
Cdd:COG1249   447 KEAA 450
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 1-164 6.54e-50

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: 166.66  E-value: 6.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   1 MRTNLPGIWAIGDVTGKSQLAHAAYRMAEVAVsDILAGQNAQHSDqifvAETVPWALYSLPEAAGVGLTEQDARAKGYDI 80
Cdd:TIGR01350 295 MRTNVPGIYAIGDVIGGPMLAHVASHEGIVAA-ENIAGKEPAHID----YDAVPSVIYTDPEVASVGLTEEQAKEAGYDV 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  81 QVVRMPYNVSGRFVAENGfsAPGSIKIIIEKSSERLLGIHLLGAYASEQIWGAALALERKLPISALRNMVFPHPTVSEVI 160
Cdd:TIGR01350 370 KIGKFPFAANGKALALGE--TDGFVKIIADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAI 447


                  ....
gi 1167382396 161 REAA 164
Cdd:TIGR01350 448 KEAA 451
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 1-169 8.74e-43

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 148.02  E-value: 8.74e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   1 MRTNLPGIWAIGDVTGKSQLAHAAYRMAEVAVsDILAGQNAQHSDqifvAETVPWALYSLPEAAGVGLTEQDARAKGYDI 80
Cdd:PRK06292  294 TQTSVPGIYAAGDVNGKPPLLHEAADEGRIAA-ENAAGDVAGGVR----YHPIPSVVFTDPQIASVGLTEEELKAAGIDY 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  81 QVVRMPYNVSGRFVAEN---GFsapgsIKIIIEKSSERLLGIHLLGAYASEQIWGAALALERKLPISALRNMVFPHPTVS 157
Cdd:PRK06292  369 VVGEVPFEAQGRARVMGkndGF-----VKVYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLS 443

                         170
                  ....*....|..
gi 1167382396 158 EVIREAAWSVQA 169
Cdd:PRK06292  444 EGLRTALRDLFS 455
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 1-164 1.24e-41

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 144.90  E-value: 1.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   1 MRTNLPGIWAIGDVTGKSQLAHAAYRMAEVAVSDIlAGQNAQHSDqifvaETVPWALYSLPEAAGVGLTEQDARAKGYDI 80
Cdd:PRK06416  297 LRTNVPNIYAIGDIVGGPMLAHKASAEGIIAAEAI-AGNPHPIDY-----RGIPAVTYTHPEVASVGLTEAKAKEEGFDV 370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  81 QVVRMPYNVSGRFVAENGfsAPGSIKIIIEKSSERLLGIHLLGAYASEQIWGAALALERKLPISALRNMVFPHPTVSEVI 160
Cdd:PRK06416  371 KVVKFPFAGNGKALALGE--TDGFVKLIFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEAL 448


                  ....
gi 1167382396 161 REAA 164
Cdd:PRK06416  449 GEAA 452
PRK06370 PRK06370
FAD-containing oxidoreductase;
2-164 3.07e-39

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 138.41  E-value: 3.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   2 RTNLPGIWAIGDVTGKSQLAHAAYRMAEVAVSDILAGQNAQHSDQIfvaetVPWALYSLPEAAGVGLTEQDARAKGYDIQ 81
Cdd:PRK06370  298 RTTNPGIYAAGDCNGRGAFTHTAYNDARIVAANLLDGGRRKVSDRI-----VPYATYTDPPLARVGMTEAEARKSGRRVL 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  82 VVRMPYNVSGRFVaENGFSApGSIKIIIEKSSERLLGIHLLGAYASEQIWGAALALERKLPISALRNMVFPHPTVSEVIR 161
Cdd:PRK06370  373 VGTRPMTRVGRAV-EKGETQ-GFMKVVVDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIP 450


                  ...
gi 1167382396 162 EAA 164
Cdd:PRK06370  451 TLA 453
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 1-167 4.89e-38

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 135.44  E-value: 4.89e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   1 MRTNLPGIWAIGDVTGKSQLAHAAYRMAeVAVSDILAGQNAqHSDqifvAETVPWALYSLPEAAGVGLTEQDARAKGYDI 80
Cdd:PRK06327  310 CRTNVPNVYAIGDVVRGPMLAHKAEEEG-VAVAERIAGQKG-HID----YNTIPWVIYTSPEIAWVGKTEQQLKAEGVEY 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  81 QVVRMPYNVSGRFVAENgfSAPGSIKIIIEKSSERLLGIHLLGAYASEQIWGAALALERKLPISALRNMVFPHPTVSEVI 160
Cdd:PRK06327  384 KAGKFPFMANGRALAMG--EPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVW 461


                  ....*..
gi 1167382396 161 REAAWSV 167
Cdd:PRK06327  462 HEAALAV 468
Pyr_redox_dim pfam02852
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ...
 53-163 4.81e-34

Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.


Pssm-ID: 427019 [Multi-domain]  Cd Length: 109  Bit Score: 116.11  E-value: 4.81e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  53 VPWALYSLPEAAGVGLTEQDARAKGYDIQVVRMPYNVSGRFVAENGfsAPGSIKIIIEKSSERLLGIHLLGAYASEQIWG 132
Cdd:pfam02852   1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGD--TDGFVKLVADRETGKILGAHIVGPNAGELIQE 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1167382396 133 AALALERKLPISALRNMVFPHPTVSEVIREA 163
Cdd:pfam02852  79 AALAIKMGATVEDLANTIHIHPTLSEALVEA 109
PRK07846 PRK07846
mycothione reductase; Reviewed
 2-163 9.91e-23

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 93.48  E-value: 9.91e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   2 RTNLPGIWAIGDVTGKSQLAHAAYRMAEVAVSDILAGQNAQHSDQIFVaetvPWALYSLPEAAGVGLTEQDARAKGYDIQ 81
Cdd:PRK07846  289 RTSAEGVFALGDVSSPYQLKHVANHEARVVQHNLLHPDDLIASDHRFV----PAAVFTHPQIASVGLTENEARAAGLDIT 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  82 VVRMPY-NVSGRFVAENgfsAPGSIKIIIEKSSERLLGIHLLGAYASEQIWGAALALERKLPISAL-RNMVFPHPTVSEV 159
Cdd:PRK07846  365 VKVQNYgDVAYGWAMED---TTGFVKLIADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMaRGQYWIHPALPEV 441


                  ....
gi 1167382396 160 IREA 163
Cdd:PRK07846  442 VENA 445
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
 1-162 1.24e-22

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 93.15  E-value: 1.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   1 MRTNLPGIWAIGDVTGKSQLAHAA---YRMaevaVSDILAGQNAQHSDQifvAETVPWALYSLPEAAGVGLTEQDARAKG 77
Cdd:PRK08010  280 LHTTADNIWAMGDVTGGLQFTYISlddYRI----VRDELLGEGKRSTDD---RKNVPYSVFMTPPLSRVGMTEEQARESG 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  78 YDIQVVRMPYNVSGRFVAENgfSAPGSIKIIIEKSSERLLGIHLLGAYASEQIWGAALALERKLPISALRNMVFPHPTVS 157
Cdd:PRK08010  353 ADIQVVTLPVAAIPRARVMN--DTRGVLKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMS 430


                  ....*
gi 1167382396 158 EVIRE 162
Cdd:PRK08010  431 ESLND 435
PTZ00153 PTZ00153
lipoamide dehydrogenase; Provisional
 7-165 1.64e-21

lipoamide dehydrogenase; Provisional


Pssm-ID: 173442 [Multi-domain]  Cd Length: 659  Bit Score: 90.36  E-value: 1.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   7 GIWAIGDVTGKSQLAHAAYRMAEVAVSDILAGQNAQHSDQI-------FVAETVPWALYSLPEAAGVGLTEQDARAKGY- 78
Cdd:PTZ00153  464 NIFCIGDANGKQMLAHTASHQALKVVDWIEGKGKENVNINVenwaskpIIYKNIPSVCYTTPELAFIGLTEKEAKELYPp 543

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  79 -DIQVVRMPYNVSGRFVAENGFSAP--------------------GSIKIIIEKSSERLLGIHLLGAYASEQIWGAALAL 137
Cdd:PTZ00153  544 dNVGVEISFYKANSKVLCENNISFPnnsknnsynkgkyntvdnteGMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAI 623

                         170       180
                  ....*....|....*....|....*...
gi 1167382396 138 ERKLPISALRNMVFPHPTVSEVIrEAAW 165
Cdd:PTZ00153  624 NLKLSVKDLAHMVHSHPTISEVL-DAAF 650
PRK06116 PRK06116
glutathione reductase; Validated
 1-158 2.66e-20

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 86.75  E-value: 2.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   1 MRTNLPGIWAIGDVTGKSQL---AHAAYRmaevAVSDILAGQNaqhSDQIFVAETVPWALYSLPEAAGVGLTEQDARAKG 77
Cdd:PRK06116  291 QNTNVPGIYAVGDVTGRVELtpvAIAAGR----RLSERLFNNK---PDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQY 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  78 YD--IQVVR-----MPYNVSGRfvaengfSAPGSIKIIIEKSSERLLGIHLLGAYASEQIWGAALALERKLPISALRNMV 150
Cdd:PRK06116  364 GEdnVKVYRssftpMYTALTGH-------RQPCLMKLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTV 436


                  ....*...
gi 1167382396 151 FPHPTVSE 158
Cdd:PRK06116  437 AIHPTAAE 444
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 2-158 2.74e-17

trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.


Pssm-ID: 200098 [Multi-domain]  Cd Length: 486  Bit Score: 78.09  E-value: 2.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   2 RTNLPGIWAIGDVTGKSQLAHAAYRMAeVAVSDILAGQNAQHSDQIFVAEtvpwALYSLPEAAGVGLTEQDArAKGYDIQ 81
Cdd:TIGR01423 315 RTNVPNIYAIGDVTDRVMLTPVAINEG-AAFVDTVFGNKPRKTDHTRVAS----AVFSIPPIGTCGLVEEDA-AKKFEKV 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  82 VVRMP------YNVSG----RFVAengfsapgsiKIIIEKSSERLLGIHLLGAYASEQIWGAALALERKLPISALRNMVF 151
Cdd:TIGR01423 389 AVYESsftplmHNISGskykKFVA----------KIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIG 458


                  ....*..
gi 1167382396 152 PHPTVSE 158
Cdd:TIGR01423 459 VHPTSAE 465
PRK07251 PRK07251
FAD-containing oxidoreductase;
3-158 3.22e-17

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 77.87  E-value: 3.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   3 TNLPGIWAIGDVTGKSQLAHAA---YRMaevaVSDILAGQNA-QHSDQifvaETVPWALYSLPEAAGVGLTEQDARAKGY 78
Cdd:PRK07251  281 TSVPGVFAVGDVNGGPQFTYISlddFRI----VFGYLTGDGSyTLEDR----GNVPTTMFITPPLSQVGLTEKEAKEAGL 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  79 DIQVVRMPynVSGRFVAENGFSAPGSIKIIIEKSSERLLGIHLLGAYASEQIWGAALALERKLPISALRNMVFPHPTVSE 158
Cdd:PRK07251  353 PYAVKELL--VAAMPRAHVNNDLRGAFKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAE 430
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
2-164 5.74e-17

Si-specific NAD(P)(+) transhydrogenase;


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 77.12  E-value: 5.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   2 RTNLPGIWAIGDVTGKSQLAHAAYRMAEVAVSDILaGQNAQHsdqifVAETVPWALYSLPEAAGVGLTEQDARAKGYDIQ 81
Cdd:PRK05249  299 QTAVPHIYAVGDVIGFPSLASASMDQGRIAAQHAV-GEATAH-----LIEDIPTGIYTIPEISSVGKTEQELTAAKVPYE 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  82 VVRMPY------NVSGRFVaengfsapGSIKIIIEKSSERLLGIHLLGAYASEQIW-GAAlALERKLPISALRNMVFPHP 154
Cdd:PRK05249  373 VGRARFkelaraQIAGDNV--------GMLKILFHRETLEILGVHCFGERATEIIHiGQA-IMEQKGTIEYFVNTTFNYP 443

                         170
                  ....*....|
gi 1167382396 155 TVSEVIREAA 164
Cdd:PRK05249  444 TMAEAYRVAA 453
PRK13748 PRK13748
putative mercuric reductase; Provisional
 1-164 1.29e-16

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 76.34  E-value: 1.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   1 MRTNLPGIWAIGDVTGKSQLAHAAyrmaevAVSDILAGQNAQHSDQIFVAETVPWALYSLPEAAGVGLTEQDARAKGY-- 78
Cdd:PRK13748  391 MRTSVPHIYAAGDCTDQPQFVYVA------AAAGTRAAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIet 464

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  79 DIQVVRMPyNVSgRFVAEngFSAPGSIKIIIEKSSERLLGIHLLGAYASEQIWGAALALERKLPISALRNMVFPHPTVSE 158
Cdd:PRK13748  465 DSRTLTLD-NVP-RALAN--FDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVE 540


                  ....*.
gi 1167382396 159 VIREAA 164
Cdd:PRK13748  541 GLKLAA 546
PLN02507 PLN02507
glutathione reductase
 2-171 5.46e-15

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 71.77  E-value: 5.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   2 RTNLPGIWAIGDVTGKSQLAHAAYRMAEVAVSDILAGQNAQHSdqifvAETVPWALYSLPEAAGVGLTEQDA--RAKGyD 79
Cdd:PLN02507  327 RTNIPSIWAIGDVTNRINLTPVALMEGTCFAKTVFGGQPTKPD-----YENVACAVFCIPPLSVVGLSEEEAveQAKG-D 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  80 IQVVRMPYN-----VSGRfvAENGFsapgsIKIIIEKSSERLLGIHLLGAYASEQIWGAALALERKLPISALRNMVFPHP 154
Cdd:PLN02507  401 ILVFTSSFNpmkntISGR--QEKTV-----MKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHP 473

                         170       180
                  ....*....|....*....|
gi 1167382396 155 TVSE---VIREAAWSVQASG 171
Cdd:PLN02507  474 SAAEefvTMRSVTRRVTAKG 493
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
 2-159 7.30e-15

thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.


Pssm-ID: 273624 [Multi-domain]  Cd Length: 484  Bit Score: 71.04  E-value: 7.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   2 RTNLPGIWAIGDVT-GKSQLAHAAYRMAEvavsdILAGQNAQHSDQIFVAETVPWALYSLPEAAGVGLTEQDARAK-GYD 79
Cdd:TIGR01438 307 QTNVPYIYAVGDILeDKPELTPVAIQAGR-----LLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKfGEE 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  80 -IQVVRMPYNVSGRFVAENGFSAPGSIKII-IEKSSERLLGIHLLGAYASEQIWGAALALERKLPISALRNMVFPHPTVS 157
Cdd:TIGR01438 382 nVEVFHSYFWPLEWTIPSRDNHNKCYAKLVcNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCA 461


                  ..
gi 1167382396 158 EV 159
Cdd:TIGR01438 462 EV 463
PLN02546 PLN02546
glutathione reductase
 2-158 3.87e-14

glutathione reductase


Pssm-ID: 215301 [Multi-domain]  Cd Length: 558  Bit Score: 69.13  E-value: 3.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   2 RTNLPGIWAIGDVTGKSQLAHAAYrMAEVAVSDILAGQNAQHSDQifvaETVPWALYSLPEAAGVGLTEQDARAKGYDIQ 81
Cdd:PLN02546  377 RTSVPSIWAVGDVTDRINLTPVAL-MEGGALAKTLFGNEPTKPDY----RAVPSAVFSQPPIGQVGLTEEQAIEEYGDVD 451

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1167382396  82 VvrmpYNVSGRFVAENGFSAPGSI--KIIIEKSSERLLGIHLLGAYASEQIWGAALALERKLPISALRNMVFPHPTVSE 158
Cdd:PLN02546  452 V----FTANFRPLKATLSGLPDRVfmKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAE 526
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
 3-172 2.66e-10

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 57.91  E-value: 2.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   3 TNLPGIWAIGDVT-GKSQLAHAAYRMAEvavsdILAGQNAQHSDQIFVAETVPWALYSLPEAAGVGLTEQDARAK--GYD 79
Cdd:PTZ00052  305 TNIPNIFAVGDVVeGRPELTPVAIKAGI-----LLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKygEDD 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  80 IQVVRMPYN------------VSGR------FVAENGFSapgsiKIIIEKS-SERLLGIHLLGAYASEQIWGAALALERK 140
Cdd:PTZ00052  380 IEEYLQEFNtleiaavhrekhERARkdeydfDVSSNCLA-----KLVCVKSeDNKVVGFHFVGPNAGEITQGFSLALKLG 454

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1167382396 141 LPISALRNMVFPHPTVSE------VIREAAWSVQASGG 172
Cdd:PTZ00052  455 AKKSDFDSMIGIHPTDAEvfmnlsVTRRSGESFAAKGG 492
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
 2-164 2.11e-09

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 55.25  E-value: 2.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   2 RTNLPGIWAIGDVTGKSQLAHAAYRMAEVAVSDILaGQNAQHSDQIFVAETVpwalYSLPEAAGVGLTEQDARAKGYDIQ 81
Cdd:PRK07845  301 RTSVPGIYAAGDCTGVLPLASVAAMQGRIAMYHAL-GEAVSPLRLKTVASNV----FTRPEIATVGVSQAAIDSGEVPAR 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  82 VVRMPYNVSGRfvA-----ENGFsapgsIKIIIEKSSERLLGIHLLGAYASEQIWGAALALERKLPISALRNMVFPHPTV 156
Cdd:PRK07845  376 TVMLPLATNPR--AkmsglRDGF-----VKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSL 448


                  ....*...
gi 1167382396 157 SEVIREAA 164
Cdd:PRK07845  449 SGSITEAA 456
PTZ00058 PTZ00058
glutathione reductase; Provisional
 2-160 3.81e-06

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 45.76  E-value: 3.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   2 RTNLPGIWAIGDVTG------------------------KSQLAHAAYRMAEVAVSDILAGQNAqhSDQIFVA------- 50
Cdd:PTZ00058  362 RTSVKHIYAVGDCCMvkknqeiedlnllklyneepylkkKENTSGESYYNVQLTPVAINAGRLL--ADRLFGPfsrttny 439

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  51 ETVPWALYSLPEAAGVGLTEQDA-------RAKGYDIQVVRMPYNVsgrFVAENGFSAPGSIKIIIEKSSERLLGIHLLG 123
Cdd:PTZ00058  440 KLIPSVIFSHPPIGTIGLSEQEAidiygkeNVKIYESRFTNLFFSV---YDMDPAQKEKTYLKLVCVGKEELIKGLHIVG 516

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1167382396 124 AYASEQIWGAALALERKLPISALRNMVFPHPTVSEVI 160
Cdd:PTZ00058  517 LNADEILQGFAVALKMNATKADFDETIPIHPTAAEEF 553
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
1-84 8.25e-06

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 44.75  E-value: 8.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   1 MRTNLPGIWAIGDV-------TGKSQLAH--AAYRMAEVAVsDILAGQNA--QHSDQIFVAET--VPWALYSLPEAAGVG 67
Cdd:COG1251   262 LRTSDPDIYAAGDCaehpgpvYGRRVLELvaPAYEQARVAA-ANLAGGPAayEGSVPSTKLKVfgVDVASAGDAEGDEEV 340

                          90
                  ....*....|....*..
gi 1167382396  68 LTEQDARAKGYDIQVVR 84
Cdd:COG1251   341 VVRGDPARGVYKKLVLR 357
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 2-151 5.28e-05

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 42.33  E-value: 5.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396   2 RTNLPGIWAIGD-------VTGKSQ---LAHAAYRMAEVaVSDILAGQNAQH-----SDQIFVAETvpwalyslpEAAGV 66
Cdd:PRK09564  271 ETSIENIYAAGDcatiyniVSNKNVyvpLATTANKLGRM-VGENLAGRHVSFkgtlgSACIKVLDL---------EAART 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167382396  67 GLTEQDARAKGYDIQVVrmpynvsgrFVAENGFSA--PGS----IKIIIEKSSERLLGIHLLGAY-ASEQIWGAALALER 139
Cdd:PRK09564  341 GLTEEEAKKLGIDYKTV---------FIKDKNHTNyyPGQedlyVKLIYEADTKVILGGQIIGKKgAVLRIDALAVAIYA 411

                         170
                  ....*....|..
gi 1167382396 140 KLPISALRNMVF 151
Cdd:PRK09564  412 KLTTQELGMMDF 423
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 1-46 6.33e-05

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


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 42.11  E-value: 6.33e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1167382396   1 MRTNLPGIWAIGD-------VTGKS---QLAHAAYRMAEVAVsDILAGQNAQHSDQ 46
Cdd:COG0446   244 LQTSDPDVYAAGDcaevphpVTGKTvyiPLASAANKQGRVAA-ENILGGPAPFPGL 298
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 1-28 1.78e-04

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: 40.76  E-value: 1.78e-04
                          10        20
                  ....*....|....*....|....*....
gi 1167382396   1 MRTNLPGIWAIGDVT-GKSQLAHAAYRMA 28
Cdd:pfam07992 273 LRTSVPGIYAAGDCRvGGPELAQNAVAQG 301
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
1-43 2.70e-04

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 40.10  E-value: 2.70e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1167382396   1 MRTNLPGIWAIGDVTGKSqlahaaYRMAEVAVSD-ILAGQNAQH 43
Cdd:COG0492   262 METSVPGVFAAGDVRDYK------YRQAATAAGEgAIAALSAAR 299
 
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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