NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2053417210|gb|QWS62040|]
View 

NADH-quinone oxidoreductase subunit NuoF [Clostridioides difficile]

Protein Classification

NADH-quinone oxidoreductase subunit NuoF( domain architecture ID 11554698)

NADH-quinone oxidoreductase subunit NuoF is part of the dehydrogenase domain of the complex I of the respiratory chain that couples the transfer of electrons from NADH to quinone with the translocation of protons across the membrane; contains a thioredoxin-like ferredoxin domain

CATH:  3.40.30.10
EC:  7.1.1.-
Gene Ontology:  GO:0051539|GO:0010181
PubMed:  23417064|15558583
SCOP:  3000031

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NuoF COG1894
NADH:ubiquinone oxidoreductase, NADH-binding 51 kD subunit (chain F) [Energy production and ...
 142-562 0e+00

NADH:ubiquinone oxidoreductase, NADH-binding 51 kD subunit (chain F) [Energy production and conversion]; NADH:ubiquinone oxidoreductase, NADH-binding 51 kD subunit (chain F) is part of the Pathway/BioSystem: NADH dehydrogenase


:

Pssm-ID: 441498 [Multi-domain]  Cd Length: 418  Bit Score: 819.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 142 KKQLRIALKNCGLIDPDSIEEYIANDGYLALGKCLTSLTPQEVIAEVKTSGLRGRGGAGFPTGSKWEAASKNPAGPtdkK 221
Cdd:COG1894     1 KKQTRVLLRNCGIIDPESLEDYIARGGYQALRKALTEMTPEEVIEEVKDSGLRGRGGAGFPTGLKWSFVPKAPGDP---K 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 222 FVVCNADEGDPGAFMDRSVLEGDPHSVLEAMAICGYAIGSDTGYIYIRAEYPKSIERLKVAIAQAEKYGLLGENILGTGF 301
Cdd:COG1894    78 YLVCNADEGEPGTFKDRSLLEGDPHQLIEGMIIAAYAIGATKGYIYIRGEYPLAIERLEKAIEEAREAGLLGKNILGSGF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 302 NFKLELKYGAGAFVCGEGTALMHSIEGRRGEPRMKTYSSSKSGLWKSPTCLNNVETFANIPAIILKGGDWFANLGTEDSS 381
Cdd:COG1894   158 DFDIEVHRGAGAYICGEETALLESLEGKRGQPRLKPPFPAVSGLWGKPTVVNNVETLANVPHIIRNGAEWFASIGTEKSK 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 382 GTKVFALGGKVENVGLVEVPMGTTLRDIVFEIGGGIPEGKKFKAVQTGGPSGGCIPTEHLDTPIDFGSLSSIGSMMGSGG 461
Cdd:COG1894   238 GTKLFSLSGHVKNPGLYEVPMGTTLRELIYDIGGGIRGGRKLKAVQPGGPSGGCLPAEHLDTPMDYESLAAAGSMLGSGG 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 462 MLVLDESDCMVDIAKFFLEFTVEESCGKCTPCRIGTTRLLEILTKITEGNGTLQDLDDLENLAETIQTASLCGLGKAAPN 541
Cdd:COG1894   318 MIVMDETTCMVDVARFFLEFYAHESCGKCTPCREGTGWMLEILDRIEAGEGTEEDLDLLEDLADTIKGTSLCALGDAAPN 397

                         410       420
                  ....*....|....*....|.
gi 2053417210 542 PVLSTLQYFKDEYIAHVVDKK 562
Cdd:COG1894   398 PVLSTLKYFRDEFEAHIKDKR 418
COG3411 COG3411
2Fe-2S ferredoxin [Energy production and conversion]; 2Fe-2S ferredoxin is part of the Pathway ...
 34-118 1.20e-30

2Fe-2S ferredoxin [Energy production and conversion]; 2Fe-2S ferredoxin is part of the Pathway/BioSystem: 2Fe2S


:

Pssm-ID: 442637  Cd Length: 96  Bit Score: 115.37  E-value: 1.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210  34 RRELLVCCDTgCTSSNSLEIVSELENEIKKSGIQDKVSVRLTGCFGFCAQGPIVKVYPDNVFYVKVEPSDAEKIVQSHLI 113
Cdd:COG3411     5 RHHVLVCTGS-CGAAGAEEVLDALKEELKERGLDGDVRVTKTGCLGRCEQGPVVVVYPEGVWYGNVTPEDVPEIVEEHLL 83


                  ....*
gi 2053417210 114 RNTVV 118
Cdd:COG3411    84 GGRPV 88
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 574-628 8.12e-13

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


:

Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 63.91  E-value: 8.12e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2053417210 574 YFI-TDDCKGCTKCSRVCPAGCITGSvKEQHTIDTSKCLKCGACIDNCTFNAIIKK 628
Cdd:COG4231    17 YVIdEDKCTGCGACVKVCPADAIEEG-DGKAVIDPDLCIGCGSCVQVCPVDAIKLE 71
 
Name Accession Description Interval E-value
NuoF COG1894
NADH:ubiquinone oxidoreductase, NADH-binding 51 kD subunit (chain F) [Energy production and ...
 142-562 0e+00

NADH:ubiquinone oxidoreductase, NADH-binding 51 kD subunit (chain F) [Energy production and conversion]; NADH:ubiquinone oxidoreductase, NADH-binding 51 kD subunit (chain F) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 441498 [Multi-domain]  Cd Length: 418  Bit Score: 819.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 142 KKQLRIALKNCGLIDPDSIEEYIANDGYLALGKCLTSLTPQEVIAEVKTSGLRGRGGAGFPTGSKWEAASKNPAGPtdkK 221
Cdd:COG1894     1 KKQTRVLLRNCGIIDPESLEDYIARGGYQALRKALTEMTPEEVIEEVKDSGLRGRGGAGFPTGLKWSFVPKAPGDP---K 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 222 FVVCNADEGDPGAFMDRSVLEGDPHSVLEAMAICGYAIGSDTGYIYIRAEYPKSIERLKVAIAQAEKYGLLGENILGTGF 301
Cdd:COG1894    78 YLVCNADEGEPGTFKDRSLLEGDPHQLIEGMIIAAYAIGATKGYIYIRGEYPLAIERLEKAIEEAREAGLLGKNILGSGF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 302 NFKLELKYGAGAFVCGEGTALMHSIEGRRGEPRMKTYSSSKSGLWKSPTCLNNVETFANIPAIILKGGDWFANLGTEDSS 381
Cdd:COG1894   158 DFDIEVHRGAGAYICGEETALLESLEGKRGQPRLKPPFPAVSGLWGKPTVVNNVETLANVPHIIRNGAEWFASIGTEKSK 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 382 GTKVFALGGKVENVGLVEVPMGTTLRDIVFEIGGGIPEGKKFKAVQTGGPSGGCIPTEHLDTPIDFGSLSSIGSMMGSGG 461
Cdd:COG1894   238 GTKLFSLSGHVKNPGLYEVPMGTTLRELIYDIGGGIRGGRKLKAVQPGGPSGGCLPAEHLDTPMDYESLAAAGSMLGSGG 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 462 MLVLDESDCMVDIAKFFLEFTVEESCGKCTPCRIGTTRLLEILTKITEGNGTLQDLDDLENLAETIQTASLCGLGKAAPN 541
Cdd:COG1894   318 MIVMDETTCMVDVARFFLEFYAHESCGKCTPCREGTGWMLEILDRIEAGEGTEEDLDLLEDLADTIKGTSLCALGDAAPN 397

                         410       420
                  ....*....|....*....|.
gi 2053417210 542 PVLSTLQYFKDEYIAHVVDKK 562
Cdd:COG1894   398 PVLSTLKYFRDEFEAHIKDKR 418
nuoF_fam TIGR01959
NADH-quinone oxidoreductase, F subunit; This model describes the F chain of complexes that ...
 156-558 3.51e-173

NADH-quinone oxidoreductase, F subunit; This model describes the F chain of complexes that resemble NADH-quinone oxidoreductases. The electron acceptor is a quinone, ubiquinone, in mitochondria and most bacteria, including Escherichia coli, where the recommended gene symbol is nuoF. This family does not have any members in chloroplast or cyanobacteria, where the quinone may be plastoquinone and NADH may be replaced by NADPH, nor in Methanosarcina, where NADH is replaced by F420H2. [Energy metabolism, Electron transport]


Pssm-ID: 131014  Cd Length: 411  Bit Score: 498.40  E-value: 3.51e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 156 DPDSIEEYIANDGYLALGKCLTSLTPQEVIAEVKTSGLRGRGGAGFPTGSKWEAASKNPAgpTDKKFVVCNADEGDPGAF 235
Cdd:TIGR01959  10 ESWTLEEYEKRGGYDALRKALEEMSPDDIIEEVKDSGLRGRGGAGFPTGLKWSFMPKDDS--PKPKYLVCNADESEPGTC 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 236 MDRSVLEGDPHSVLEAMAICGYAIGSDTGYIYIRAEYPKSIERLKVAIAQAEKYGLLGENILGTGFNFKLELKYGAGAFV 315
Cdd:TIGR01959  88 KDRDLMEFDPHQLIEGMIIAAYAIGAHRGYIYIRGEFIKEAENLEAAIAEAYAAGLLGKNILGSGFDFELFVHRGAGAYI 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 316 CGEGTALMHSIEGRRGEPRMKTYSSSKSGLWKSPTCLNNVETFANIPAIILKGGDWFANLGTEDSSGTKVFALGGKVENV 395
Cdd:TIGR01959 168 CGEETALLESLEGKRGQPRLKPPFPAVFGLYGKPTVINNVETLASVPAILRRGADWYRKLGKEKSPGTKLFSVSGHVNKP 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 396 GLVEVPMGTTLRDIVFEIGGGIPEGKKFKAVQTGGPSGGCIPTE-HLDTPIDFGSLSSIGSMMGSGGMLVLDESDCMVDI 474
Cdd:TIGR01959 248 GNYELPLGTPLRELLEDYAGGMRGGWKLKAVIPGGSSTPVLPAEqHLDAPMDYDSLAAAGSMLGTGAVIVMDESTCMVKA 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 475 AKFFLEFTVEESCGKCTPCRIGTTRLLEILTKITEGNGTLQDLDDLENLAETIQTASLCGLGKAAPNPVLSTLQYFKDEY 554
Cdd:TIGR01959 328 VRRLSEFYAHESCGQCTPCREGTGWMVKILERIEEGEGTKEDIDLLLSVCKQIEGKTICALGDAAAWPVQSAIKHFRDEF 407


                  ....
gi 2053417210 555 IAHV 558
Cdd:TIGR01959 408 EAHI 411
PRK11278 PRK11278
NADH-quinone oxidoreductase subunit NuoF;
157-559 9.31e-123

NADH-quinone oxidoreductase subunit NuoF;


Pssm-ID: 236891 [Multi-domain]  Cd Length: 448  Bit Score: 371.06  E-value: 9.31e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 157 PDSIEEYIANDGYLALGKCLTSLTPQEVIAEVKTSGLRGRGGAGFPTGSKWEAASKNPAgpTDKKFVVCNADEGDPGAFM 236
Cdd:PRK11278   24 PVWLDEYRSKNGYEGARKALTGMSPDEIVNQVKDAGLKGRGGAGFSTGLKWSLMPKDES--MNIRYLLCNADEMEPGTYK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 237 DRSVLEGDPHSVLEAMAICGYAIGSDTGYIYIRAEYPKSIERLKVAIAQAEKYGLLGENILGTGFNFKLELKYGAGAFVC 316
Cdd:PRK11278  102 DRLLMEQLPHLLVEGMLISAFALKAYRGYIFLRGEYIEAAVNLRRAIAEATEAGLLGKNIMGTGFDFELFVHTGAGRYIC 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 317 GEGTALMHSIEGRRGEPRMKTYSSSKSGLWKSPTCLNNVETFANIPAIILKGGDWFANLGTEDS--SGTKVFALGGKVEN 394
Cdd:PRK11278  182 GEETALINSLEGRRANPRSKPPFPATSGVWGKPTCVNNVETLCNVPAILANGVEWYQNISKGKSkdAGTKLMGFSGRVKN 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 395 VGLVEVPMGTTLRDIVFEIGGGIPEGKKFKAVQTGGPSGGCIPTEHLDTPIDFGSLSSIGSMMGSGGMLVLDESDCMVDI 474
Cdd:PRK11278  262 PGLWELPFGTTAREILEDYAGGMRDGLKFKAWQPGGAGTDFLTEAHLDLPMEFESIGKAGSRLGTALAMAVDHEINMVSL 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 475 AKFFLEFTVEESCGKCTPCRIGTTRLLEILTKITEGNGTLQDLDDLENLAETIQTA-SLCGLGKAAPNPVLSTLQYFKDE 553
Cdd:PRK11278  342 VRNLEEFFARESCGWCTPCRDGLPWSVKILRALERGEGQPGDIETLEQLCRFLGPGkTFCAHAPGAVEPLQSAIKYFREE 421


                  ....*.
gi 2053417210 554 YIAHVV 559
Cdd:PRK11278  422 FEAGIK 427
Complex1_51K pfam01512
Respiratory-chain NADH dehydrogenase 51 Kd subunit;
188-362 4.55e-51

Respiratory-chain NADH dehydrogenase 51 Kd subunit;


Pssm-ID: 460237 [Multi-domain]  Cd Length: 150  Bit Score: 173.08  E-value: 4.55e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 188 VKTSGLRGRGGAGFPTGSKWEAASKnpagpTDKKFVVCNADEGDPGAFMDRSVLEGDPHSVLEAMAICGYAIGSDTGYIY 267
Cdd:pfam01512   1 VKEAGIVGRGGAGFPTHVKLSPPPK-----KKIKYLIVNGAECEPGLTKDRRLMRERPHEIIEGIKIAAYALGAKRGVIG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 268 IRAEYPKSIERLKVAIAQAEKYGllgenilgtgfnFKLELKYGAGAFVCGEGTALMHSIEGrRGEPRMKtySSSKSGLwk 347
Cdd:pfam01512  76 IRDEKPEAIAALEKAIAEARAAG------------FDIEVHRGAGAYPCGEEKALIYSLTG-RGVPRGK--PPADVGV-- 138

                         170
                  ....*....|....*
gi 2053417210 348 sptCLNNVETFANIP 362
Cdd:pfam01512 139 ---VVNNVETLAAVP 150
COG3411 COG3411
2Fe-2S ferredoxin [Energy production and conversion]; 2Fe-2S ferredoxin is part of the Pathway ...
 34-118 1.20e-30

2Fe-2S ferredoxin [Energy production and conversion]; 2Fe-2S ferredoxin is part of the Pathway/BioSystem: 2Fe2S


Pssm-ID: 442637  Cd Length: 96  Bit Score: 115.37  E-value: 1.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210  34 RRELLVCCDTgCTSSNSLEIVSELENEIKKSGIQDKVSVRLTGCFGFCAQGPIVKVYPDNVFYVKVEPSDAEKIVQSHLI 113
Cdd:COG3411     5 RHHVLVCTGS-CGAAGAEEVLDALKEELKERGLDGDVRVTKTGCLGRCEQGPVVVVYPEGVWYGNVTPEDVPEIVEEHLL 83


                  ....*
gi 2053417210 114 RNTVV 118
Cdd:COG3411    84 GGRPV 88
TRX_Fd_family cd02980
Thioredoxin (TRX)-like [2Fe-2S] Ferredoxin (Fd) family; composed of [2Fe-2S] Fds with a TRX ...
 35-111 3.27e-21

Thioredoxin (TRX)-like [2Fe-2S] Ferredoxin (Fd) family; composed of [2Fe-2S] Fds with a TRX fold (TRX-like Fds) and proteins containing domains similar to TRX-like Fd including formate dehydrogenases, NAD-reducing hydrogenases and the subunit E of NADH:ubiquinone oxidoreductase (NuoE). TRX-like Fds are soluble low-potential electron carriers containing a single [2Fe-2S] cluster. The exact role of TRX-like Fd is still unclear. It has been suggested that it may be involved in nitrogen fixation. Its homologous domains in large redox enzymes (such as Nuo and hydrogenases) function as electron carriers.


Pssm-ID: 239278 [Multi-domain]  Cd Length: 77  Bit Score: 87.68  E-value: 3.27e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2053417210  35 RELLVCCDTGCTSSNSLEIVSELENEIKKSGIQDKVSVRLTGCFGFCAQGPIVKVYPDNVFYVKVEPSDAEKIVQSH 111
Cdd:cd02980     1 HHILVCTGTACGLRGAEELLEALEKELGIRGGDGRVTVERVGCLGACGLAPVVVVYPDGVWYGRVTPEDVEEIVEEL 77
NADH_4Fe-4S smart00928
NADH-ubiquinone oxidoreductase-F iron-sulfur binding region;
472-517 1.58e-20

NADH-ubiquinone oxidoreductase-F iron-sulfur binding region;


Pssm-ID: 197996 [Multi-domain]  Cd Length: 46  Bit Score: 84.89  E-value: 1.58e-20
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2053417210  472 VDIAKFFLEFTVEESCGKCTPCRIGTTRLLEILTKITEGNGTLQDL 517
Cdd:smart00928   1 VDAARRLMEFYAHESCGKCTPCREGTGWLLEILDRIEEGEGTEEDL 46
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 574-628 8.12e-13

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 63.91  E-value: 8.12e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2053417210 574 YFI-TDDCKGCTKCSRVCPAGCITGSvKEQHTIDTSKCLKCGACIDNCTFNAIIKK 628
Cdd:COG4231    17 YVIdEDKCTGCGACVKVCPADAIEEG-DGKAVIDPDLCIGCGSCVQVCPVDAIKLE 71
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 578-625 2.39e-11

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 61.26  E-value: 2.39e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2053417210 578 DDCKGCTKCSRVCPAGCITGSVKEQHTIDTSKCLKCGACIDNCTFNAI 625
Cdd:cd10549    78 EKCIGCGLCVKVCPVDAITLEDELEIVIDKEKCIGCGICAEVCPVNAI 125
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 578-625 7.84e-08

electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 52.11  E-value: 7.84e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2053417210 578 DDCKGCTKCSRVCPAGCITGSVKEQHTIDTSKCLKCGACIDNCTFNAI 625
Cdd:TIGR01944 113 DNCIGCTKCIQACPVDAIVGAAKAMHTVIADECTGCDLCVEPCPTDCI 160
PRK08764 PRK08764
Rnf electron transport complex subunit RnfB;
572-625 3.73e-07

Rnf electron transport complex subunit RnfB;


Pssm-ID: 181550 [Multi-domain]  Cd Length: 135  Bit Score: 49.53  E-value: 3.73e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2053417210 572 LSYFITDDCKGCTKCSRVCPAGCITGSVKEQHTIDTSKCLKCGACIDNCTFNAI 625
Cdd:PRK08764   79 VAWIVEADCIGCTKCIQACPVDAIVGGAKHMHTVIAPLCTGCELCVPACPVDCI 132
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 580-624 1.82e-06

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 45.21  E-value: 1.82e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2053417210 580 CKGCTKCSRVCPAGCITGSVKEQH------TIDTSKCLKCGACIDNCTFNA 624
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKkgtktvVIDPERCVGCGACVAVCPTGA 51
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 573-625 1.93e-06

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 49.47  E-value: 1.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2053417210 573 SYFITDDCKGCTKCSRVCPAGCITgsVKEQHTIDTSKCLKCGACIDNCTFNAI 625
Cdd:NF038196  180 KFHVTDKCIGCGICAKVCPVNNIE--MEDGKPVWGHNCTHCLACIHRCPKEAI 230
 
Name Accession Description Interval E-value
NuoF COG1894
NADH:ubiquinone oxidoreductase, NADH-binding 51 kD subunit (chain F) [Energy production and ...
 142-562 0e+00

NADH:ubiquinone oxidoreductase, NADH-binding 51 kD subunit (chain F) [Energy production and conversion]; NADH:ubiquinone oxidoreductase, NADH-binding 51 kD subunit (chain F) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 441498 [Multi-domain]  Cd Length: 418  Bit Score: 819.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 142 KKQLRIALKNCGLIDPDSIEEYIANDGYLALGKCLTSLTPQEVIAEVKTSGLRGRGGAGFPTGSKWEAASKNPAGPtdkK 221
Cdd:COG1894     1 KKQTRVLLRNCGIIDPESLEDYIARGGYQALRKALTEMTPEEVIEEVKDSGLRGRGGAGFPTGLKWSFVPKAPGDP---K 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 222 FVVCNADEGDPGAFMDRSVLEGDPHSVLEAMAICGYAIGSDTGYIYIRAEYPKSIERLKVAIAQAEKYGLLGENILGTGF 301
Cdd:COG1894    78 YLVCNADEGEPGTFKDRSLLEGDPHQLIEGMIIAAYAIGATKGYIYIRGEYPLAIERLEKAIEEAREAGLLGKNILGSGF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 302 NFKLELKYGAGAFVCGEGTALMHSIEGRRGEPRMKTYSSSKSGLWKSPTCLNNVETFANIPAIILKGGDWFANLGTEDSS 381
Cdd:COG1894   158 DFDIEVHRGAGAYICGEETALLESLEGKRGQPRLKPPFPAVSGLWGKPTVVNNVETLANVPHIIRNGAEWFASIGTEKSK 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 382 GTKVFALGGKVENVGLVEVPMGTTLRDIVFEIGGGIPEGKKFKAVQTGGPSGGCIPTEHLDTPIDFGSLSSIGSMMGSGG 461
Cdd:COG1894   238 GTKLFSLSGHVKNPGLYEVPMGTTLRELIYDIGGGIRGGRKLKAVQPGGPSGGCLPAEHLDTPMDYESLAAAGSMLGSGG 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 462 MLVLDESDCMVDIAKFFLEFTVEESCGKCTPCRIGTTRLLEILTKITEGNGTLQDLDDLENLAETIQTASLCGLGKAAPN 541
Cdd:COG1894   318 MIVMDETTCMVDVARFFLEFYAHESCGKCTPCREGTGWMLEILDRIEAGEGTEEDLDLLEDLADTIKGTSLCALGDAAPN 397

                         410       420
                  ....*....|....*....|.
gi 2053417210 542 PVLSTLQYFKDEYIAHVVDKK 562
Cdd:COG1894   398 PVLSTLKYFRDEFEAHIKDKR 418
nuoF_fam TIGR01959
NADH-quinone oxidoreductase, F subunit; This model describes the F chain of complexes that ...
 156-558 3.51e-173

NADH-quinone oxidoreductase, F subunit; This model describes the F chain of complexes that resemble NADH-quinone oxidoreductases. The electron acceptor is a quinone, ubiquinone, in mitochondria and most bacteria, including Escherichia coli, where the recommended gene symbol is nuoF. This family does not have any members in chloroplast or cyanobacteria, where the quinone may be plastoquinone and NADH may be replaced by NADPH, nor in Methanosarcina, where NADH is replaced by F420H2. [Energy metabolism, Electron transport]


Pssm-ID: 131014  Cd Length: 411  Bit Score: 498.40  E-value: 3.51e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 156 DPDSIEEYIANDGYLALGKCLTSLTPQEVIAEVKTSGLRGRGGAGFPTGSKWEAASKNPAgpTDKKFVVCNADEGDPGAF 235
Cdd:TIGR01959  10 ESWTLEEYEKRGGYDALRKALEEMSPDDIIEEVKDSGLRGRGGAGFPTGLKWSFMPKDDS--PKPKYLVCNADESEPGTC 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 236 MDRSVLEGDPHSVLEAMAICGYAIGSDTGYIYIRAEYPKSIERLKVAIAQAEKYGLLGENILGTGFNFKLELKYGAGAFV 315
Cdd:TIGR01959  88 KDRDLMEFDPHQLIEGMIIAAYAIGAHRGYIYIRGEFIKEAENLEAAIAEAYAAGLLGKNILGSGFDFELFVHRGAGAYI 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 316 CGEGTALMHSIEGRRGEPRMKTYSSSKSGLWKSPTCLNNVETFANIPAIILKGGDWFANLGTEDSSGTKVFALGGKVENV 395
Cdd:TIGR01959 168 CGEETALLESLEGKRGQPRLKPPFPAVFGLYGKPTVINNVETLASVPAILRRGADWYRKLGKEKSPGTKLFSVSGHVNKP 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 396 GLVEVPMGTTLRDIVFEIGGGIPEGKKFKAVQTGGPSGGCIPTE-HLDTPIDFGSLSSIGSMMGSGGMLVLDESDCMVDI 474
Cdd:TIGR01959 248 GNYELPLGTPLRELLEDYAGGMRGGWKLKAVIPGGSSTPVLPAEqHLDAPMDYDSLAAAGSMLGTGAVIVMDESTCMVKA 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 475 AKFFLEFTVEESCGKCTPCRIGTTRLLEILTKITEGNGTLQDLDDLENLAETIQTASLCGLGKAAPNPVLSTLQYFKDEY 554
Cdd:TIGR01959 328 VRRLSEFYAHESCGQCTPCREGTGWMVKILERIEEGEGTKEDIDLLLSVCKQIEGKTICALGDAAAWPVQSAIKHFRDEF 407


                  ....
gi 2053417210 555 IAHV 558
Cdd:TIGR01959 408 EAHI 411
PRK11278 PRK11278
NADH-quinone oxidoreductase subunit NuoF;
157-559 9.31e-123

NADH-quinone oxidoreductase subunit NuoF;


Pssm-ID: 236891 [Multi-domain]  Cd Length: 448  Bit Score: 371.06  E-value: 9.31e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 157 PDSIEEYIANDGYLALGKCLTSLTPQEVIAEVKTSGLRGRGGAGFPTGSKWEAASKNPAgpTDKKFVVCNADEGDPGAFM 236
Cdd:PRK11278   24 PVWLDEYRSKNGYEGARKALTGMSPDEIVNQVKDAGLKGRGGAGFSTGLKWSLMPKDES--MNIRYLLCNADEMEPGTYK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 237 DRSVLEGDPHSVLEAMAICGYAIGSDTGYIYIRAEYPKSIERLKVAIAQAEKYGLLGENILGTGFNFKLELKYGAGAFVC 316
Cdd:PRK11278  102 DRLLMEQLPHLLVEGMLISAFALKAYRGYIFLRGEYIEAAVNLRRAIAEATEAGLLGKNIMGTGFDFELFVHTGAGRYIC 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 317 GEGTALMHSIEGRRGEPRMKTYSSSKSGLWKSPTCLNNVETFANIPAIILKGGDWFANLGTEDS--SGTKVFALGGKVEN 394
Cdd:PRK11278  182 GEETALINSLEGRRANPRSKPPFPATSGVWGKPTCVNNVETLCNVPAILANGVEWYQNISKGKSkdAGTKLMGFSGRVKN 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 395 VGLVEVPMGTTLRDIVFEIGGGIPEGKKFKAVQTGGPSGGCIPTEHLDTPIDFGSLSSIGSMMGSGGMLVLDESDCMVDI 474
Cdd:PRK11278  262 PGLWELPFGTTAREILEDYAGGMRDGLKFKAWQPGGAGTDFLTEAHLDLPMEFESIGKAGSRLGTALAMAVDHEINMVSL 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 475 AKFFLEFTVEESCGKCTPCRIGTTRLLEILTKITEGNGTLQDLDDLENLAETIQTA-SLCGLGKAAPNPVLSTLQYFKDE 553
Cdd:PRK11278  342 VRNLEEFFARESCGWCTPCRDGLPWSVKILRALERGEGQPGDIETLEQLCRFLGPGkTFCAHAPGAVEPLQSAIKYFREE 421


                  ....*.
gi 2053417210 554 YIAHVV 559
Cdd:PRK11278  422 FEAGIK 427
PRK13596 PRK13596
NADH-quinone oxidoreductase subunit NuoF;
174-553 5.67e-114

NADH-quinone oxidoreductase subunit NuoF;


Pssm-ID: 237441  Cd Length: 433  Bit Score: 347.73  E-value: 5.67e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 174 KCLTSLTPQEVIAEVKTSGLRGRGGAGFPTGSKWEAASKNPAG-PTdkkFVVCNADEGDPGAFMDRSVLEGDPHSVLEAM 252
Cdd:PRK13596   33 KAILDKGRDWIIEEMKASGLRGRGGAGFPTGLKWSFMPKESDGrPH---YLVVNADESEPGTCKDRDILRHDPHKLIEGC 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 253 AICGYAIGSDTGYIYIRAEYPKSIERLKVAIAQAEKYGLLGENILGTGFNFKLELKYGAGAFVCGEGTALMHSIEGRRGE 332
Cdd:PRK13596  110 LIASFAMGAHAAYIYIRGEFIREREALQAAIDEAYEAGLIGKNACGSGWDFDIYVHHGAGAYICGEETALLESLEGKKGQ 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 333 PRMKTYSSSKSGLWKSPTCLNNVETFANIPAIILKGGDWFANLGTEDSSGTKVFALGGKVENVGLVEVPMGTTLRDIVFE 412
Cdd:PRK13596  190 PRLKPPFPANVGLYGCPTTVNNVESIAVVPTILRRGAAWFASIGRPNNTGTKLFCISGHVNKPCNVEEAMGIPFRELIEK 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 413 IGGGIPEG-KKFKAVQTGGPSGGCIPTEHLDT-PIDFGSLSSIGSMMGSGGMLVLDES----DCMVDIAKFFLeftvEES 486
Cdd:PRK13596  270 HAGGVRGGwDNLLAVIPGGSSVPLIPAEQCEDaIMDFDSLRAVGSGLGTAAVIVMDKStdiiKAIARLSYFYK----HES 345

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2053417210 487 CGKCTPCRIGTTRLLEILTKITEGNGTLQDLDDLENLAETIQTASLCGLGKAAPNPVLSTLQYFKDE 553
Cdd:PRK13596  346 CGQCTPCREGTGWMWRVMERMVKGRAQKREIDMLLDVTKQIEGHTICALGDAAAWPIQGLIRHFRPE 412
PTZ00304 PTZ00304
NADH dehydrogenase [ubiquinone] flavoprotein 1; Provisional
 184-553 1.58e-98

NADH dehydrogenase [ubiquinone] flavoprotein 1; Provisional


Pssm-ID: 185547 [Multi-domain]  Cd Length: 461  Bit Score: 309.02  E-value: 1.58e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 184 VIAEVKTSGLRGRGGAGFPTGSKWEAASKNPagPTDK-KFVVCNADEGDPGAFMDRSVLEGDPHSVLEAMAICGYAIGSD 262
Cdd:PTZ00304   63 IIDEIKKSGLRGRGGAGFPSGLKWSFMPKVK--PDGRpSYLVVNADESEPGTCKDREIMRHDPHKLVEGALLAGFAMRAR 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 263 TGYIYIRAEYPKSIERLKVAIAQAEKYGLLGENILGTGFNFKLELKYGAGAFVCGEGTALMHSIEGRRGEPRMKTYSSSK 342
Cdd:PTZ00304  141 AAYIYIRGEFYNEARALQQAIDEAYKKGFLGKNACGSGYDFDVYVHRGAGAYICGEETALIESIEGKPGKPRLKPPFPAN 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 343 SGLWKSPTCLNNVETFANIPAIILKGGDWFANLGTEDSSGTKVFALGGKVENVGLVEVPMGTTLRDIVFEIGGGIPEG-K 421
Cdd:PTZ00304  221 VGLYGCPTTVTNVETVAVSPTILRRGPQWFASFGRPNNAGTKLFCISGHVNNPCTVEEEMSIPLRELIERHCGGVRGGwD 300

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 422 KFKAVQTGGPSGGCIPTEHLDTPI-DFGSLSSIGSMMGSGGMLVLDESDCMVDIAKFFLEFTVEESCGKCTPCRIGTTRL 500
Cdd:PTZ00304  301 NLLCVIPGGSSVPLIPKEICDNVLmDFDALKEVQSGLGTAAVIVMDKSTDIIDAILRLSKFYKHESCGQCTPCREGTPWL 380

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2053417210 501 LEILTKITEGNGTLQDLDDLENLAETIQTASLCGLGKAAPNPVLSTLQYFKDE 553
Cdd:PTZ00304  381 VKMMERFVVGNADKEEIDTLEEVSKQIEGHTICALGDAAAWPVQGLIRHFRPE 433
PLN03132 PLN03132
NADH dehydrogenase (ubiquinone) flavoprotein 1; Provisional
 174-553 1.86e-96

NADH dehydrogenase (ubiquinone) flavoprotein 1; Provisional


Pssm-ID: 178678 [Multi-domain]  Cd Length: 461  Bit Score: 303.33  E-value: 1.86e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 174 KCLTSLTPQEVIAEVKTSGLRGRGGAGFPTGSKWEAASKNPAG-PTdkkFVVCNADEGDPGAFMDRSVLEGDPHSVLEAM 252
Cdd:PLN03132   64 KDLVLKGPDWIVNEMKKSGLRGRGGAGFPSGLKWSFMPKVSDGrPS---YLVVNADESEPGTCKDREIMRHDPHKLLEGC 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 253 AICGYAIGSDTGYIYIRAEYPKSIERLKVAIAQAEKYGLLGENILGTGFNFKLELKYGAGAFVCGEGTALMHSIEGRRGE 332
Cdd:PLN03132  141 LIAGVGMRARAAYIYIRGEYVNERLNLERARHEAYAAGLLGKNACGSGYDFDVYIHYGAGAYICGEETALLESLEGKQGK 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 333 PRMKTYSSSKSGLWKSPTCLNNVETFANIPAIILKGGDWFANLGTEDSSGTKVFALGGKVENVGLVEVPMGTTLRDIVFE 412
Cdd:PLN03132  221 PRLKPPFPANVGLYGCPTTVTNVETVAVSPTILRRGPEWFASFGRKNNAGTKLFCISGHVNKPCTVEEEMSIPLKELIER 300

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 413 IGGGIPEG-KKFKAVQTGGPSGGCIPTEHLDTPI-DFGSLSSIGSMMGSGGMLVLDESDCMVDIAKFFLEFTVEESCGKC 490
Cdd:PLN03132  301 HCGGVRGGwDNLLAIIPGGSSVPLLPKKICDDVLmDFDALKAVQSGLGTAAVIVMDKSTDVVDAIARLSYFYKHESCGQC 380

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2053417210 491 TPCRIGTTRLLEILTKITEGNGTLQDLDDLENLAETIQTASLCGLGKAAPNPVLSTLQYFKDE 553
Cdd:PLN03132  381 TPCREGTGWLWDIMERMKVGNAKLEEIDMLQEVTKQIEGHTICALGDAAAWPVQGLIRHFRPE 443
Complex1_51K pfam01512
Respiratory-chain NADH dehydrogenase 51 Kd subunit;
188-362 4.55e-51

Respiratory-chain NADH dehydrogenase 51 Kd subunit;


Pssm-ID: 460237 [Multi-domain]  Cd Length: 150  Bit Score: 173.08  E-value: 4.55e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 188 VKTSGLRGRGGAGFPTGSKWEAASKnpagpTDKKFVVCNADEGDPGAFMDRSVLEGDPHSVLEAMAICGYAIGSDTGYIY 267
Cdd:pfam01512   1 VKEAGIVGRGGAGFPTHVKLSPPPK-----KKIKYLIVNGAECEPGLTKDRRLMRERPHEIIEGIKIAAYALGAKRGVIG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 268 IRAEYPKSIERLKVAIAQAEKYGllgenilgtgfnFKLELKYGAGAFVCGEGTALMHSIEGrRGEPRMKtySSSKSGLwk 347
Cdd:pfam01512  76 IRDEKPEAIAALEKAIAEARAAG------------FDIEVHRGAGAYPCGEEKALIYSLTG-RGVPRGK--PPADVGV-- 138

                         170
                  ....*....|....*
gi 2053417210 348 sptCLNNVETFANIP 362
Cdd:pfam01512 139 ---VVNNVETLAAVP 150
NADH_4Fe-4S pfam10589
NADH-ubiquinone oxidoreductase-F iron-sulfur binding region;
473-557 8.92e-46

NADH-ubiquinone oxidoreductase-F iron-sulfur binding region;


Pssm-ID: 463160 [Multi-domain]  Cd Length: 85  Bit Score: 156.48  E-value: 8.92e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 473 DIAKFFLEFTVEESCGKCTPCRIGTTRLLEILTKITEGNGTLQDLDDLENLAETIQTASLCGLGKAAPNPVLSTLQYFKD 552
Cdd:pfam10589   1 DVARRFLEFYAHESCGKCTPCREGTKWLAEILERIVDGEGTEEDLDLLEELARTIKGRSLCGLGDGAANPVLSALRYFRD 80


                  ....*
gi 2053417210 553 EYIAH 557
Cdd:pfam10589  81 EFEAH 85
COG3411 COG3411
2Fe-2S ferredoxin [Energy production and conversion]; 2Fe-2S ferredoxin is part of the Pathway ...
 34-118 1.20e-30

2Fe-2S ferredoxin [Energy production and conversion]; 2Fe-2S ferredoxin is part of the Pathway/BioSystem: 2Fe2S


Pssm-ID: 442637  Cd Length: 96  Bit Score: 115.37  E-value: 1.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210  34 RRELLVCCDTgCTSSNSLEIVSELENEIKKSGIQDKVSVRLTGCFGFCAQGPIVKVYPDNVFYVKVEPSDAEKIVQSHLI 113
Cdd:COG3411     5 RHHVLVCTGS-CGAAGAEEVLDALKEELKERGLDGDVRVTKTGCLGRCEQGPVVVVYPEGVWYGNVTPEDVPEIVEEHLL 83


                  ....*
gi 2053417210 114 RNTVV 118
Cdd:COG3411    84 GGRPV 88
NapF COG1145
Ferredoxin [Energy production and conversion];
394-625 5.58e-22

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 95.56  E-value: 5.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 394 NVGLVEVPMGTTLRDIVFEIGGGIPEGKKFKAVQTGGPSGGCIPTEHLDTPIDFGSLSSIGSMMGSGGMLVLDESDCMVD 473
Cdd:COG1145     6 DLKEALSPKLKVLYAVVTGILGKIILNVIAGALLKAVALGGLLPIIGILAKEAFDALKDVLGILGAIVIGIGAGEIVRVG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 474 IAKFFLEFTVEESCGKCTPCRIGTTRLLEILTKITEGNGTLQDLDDLENLAETIQTASLCGLGKAAPNPVLSTLQYFKDE 553
Cdd:COG1145    86 IAAADLNLKAVALVLLLALAVAGAAKRLIISAVKLVAGLVVAAGEVLLVIAAALAEAGLAILGAAAPVDALAISGGKKIE 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2053417210 554 YIAHVVDKKCPAgkcqnllsYFITDDCKGCTKCSRVCPAGCIT-GSVKEQHTIDTSKCLKCGACIDNCTFNAI 625
Cdd:COG1145   166 EELKIAIKKAKA--------VIDAEKCIGCGLCVKVCPTGAIRlKDGKPQIVVDPDKCIGCGACVKVCPVGAI 230
TRX_Fd_family cd02980
Thioredoxin (TRX)-like [2Fe-2S] Ferredoxin (Fd) family; composed of [2Fe-2S] Fds with a TRX ...
 35-111 3.27e-21

Thioredoxin (TRX)-like [2Fe-2S] Ferredoxin (Fd) family; composed of [2Fe-2S] Fds with a TRX fold (TRX-like Fds) and proteins containing domains similar to TRX-like Fd including formate dehydrogenases, NAD-reducing hydrogenases and the subunit E of NADH:ubiquinone oxidoreductase (NuoE). TRX-like Fds are soluble low-potential electron carriers containing a single [2Fe-2S] cluster. The exact role of TRX-like Fd is still unclear. It has been suggested that it may be involved in nitrogen fixation. Its homologous domains in large redox enzymes (such as Nuo and hydrogenases) function as electron carriers.


Pssm-ID: 239278 [Multi-domain]  Cd Length: 77  Bit Score: 87.68  E-value: 3.27e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2053417210  35 RELLVCCDTGCTSSNSLEIVSELENEIKKSGIQDKVSVRLTGCFGFCAQGPIVKVYPDNVFYVKVEPSDAEKIVQSH 111
Cdd:cd02980     1 HHILVCTGTACGLRGAEELLEALEKELGIRGGDGRVTVERVGCLGACGLAPVVVVYPDGVWYGRVTPEDVEEIVEEL 77
NADH_4Fe-4S smart00928
NADH-ubiquinone oxidoreductase-F iron-sulfur binding region;
472-517 1.58e-20

NADH-ubiquinone oxidoreductase-F iron-sulfur binding region;


Pssm-ID: 197996 [Multi-domain]  Cd Length: 46  Bit Score: 84.89  E-value: 1.58e-20
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2053417210  472 VDIAKFFLEFTVEESCGKCTPCRIGTTRLLEILTKITEGNGTLQDL 517
Cdd:smart00928   1 VDAARRLMEFYAHESCGKCTPCREGTGWLLEILDRIEEGEGTEEDL 46
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 574-628 8.12e-13

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 63.91  E-value: 8.12e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2053417210 574 YFI-TDDCKGCTKCSRVCPAGCITGSvKEQHTIDTSKCLKCGACIDNCTFNAIIKK 628
Cdd:COG4231    17 YVIdEDKCTGCGACVKVCPADAIEEG-DGKAVIDPDLCIGCGSCVQVCPVDAIKLE 71
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
574-626 1.05e-12

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 63.60  E-value: 1.05e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2053417210 574 YFITDDCKGCTKCSRVCPAGCITGsVKEQHTIDTSKCLKCGACIDNCTFNAII 626
Cdd:COG2768     7 YVDEEKCIGCGACVKVCPVGAISI-EDGKAVIDPEKCIGCGACIEVCPVGAIK 58
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 577-625 1.24e-11

Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 60.14  E-value: 1.24e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2053417210 577 TDDCKGCTKCSRVCPAGCITGSVKE---QHTIDTSKCLKCGACIDNCTFNAI 625
Cdd:COG1143     1 EDKCIGCGLCVRVCPVDAITIEDGEpgkVYVIDPDKCIGCGLCVEVCPTGAI 52
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 578-625 2.39e-11

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 61.26  E-value: 2.39e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2053417210 578 DDCKGCTKCSRVCPAGCITGSVKEQHTIDTSKCLKCGACIDNCTFNAI 625
Cdd:cd10549    78 EKCIGCGLCVKVCPVDAITLEDELEIVIDKEKCIGCGICAEVCPVNAI 125
rnfC TIGR01945
electron transport complex, RnfABCDGE type, C subunit; The six subunit complex RnfABCDGE in ...
 150-490 3.11e-10

electron transport complex, RnfABCDGE type, C subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the C subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273888 [Multi-domain]  Cd Length: 435  Bit Score: 62.75  E-value: 3.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 150 KNCGLIDPDSIEEYIAndgyLALGKCLTSLTPQEVIAEVKTSGLRGRGGAGFPTgskweAASKNPAGPTDKKFVVCNADE 229
Cdd:TIGR01945  94 VPAIVIEPDGEDEWIE----LEPIPDFENLSPEEILEKIRAAGIVGLGGATFPT-----HVKLNPPPEKKIETLIINGAE 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 230 GDPGAFMDRSVLEGDPHSVLEAMAICGYAIGSDTGYIYIRAEYPKSIERLKVAIaqaekygllgenilgTGFNFK---LE 306
Cdd:TIGR01945 165 CEPYLTCDDRLMRERAEEIIGGIRILLKILGVKKVVIGIEDNKPEAIAALKKAL---------------GGYNIKvrvLP 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 307 LKYGAGafvcGEgTALMHSIEGR----RGEPrmktyssSKSGLwksptCLNNVETFANIPAIILKGGDWFANLGTedssg 382
Cdd:TIGR01945 230 TKYPQG----GE-KQLIYALTGRevpsGGLP-------ADIGV-----VVQNVGTAFAIYEAVVNGKPLIERVVT----- 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 383 tkvfALGGKVENVGLVEVPMGTTLRDIVfEIGGGIPEgKKFKAVqTGGPSGGcIPTEHLDTPIdfgslssigsMMGSGGM 462
Cdd:TIGR01945 288 ----VTGDAIRRPKNLWVLIGTPVSDIL-AFCGGFRE-KPERLI-MGGPMMG-LALPSLDVPV----------TKGTSGI 349

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2053417210 463 LVLD--------ESDCMvdiakffleftveeSCGKC 490
Cdd:TIGR01945 350 LALDkeetpespEKPCI--------------RCGKC 371
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 578-625 4.35e-10

Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 55.83  E-value: 4.35e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2053417210 578 DDCKGCTKCSRVCPAGCITGSVKEQHtIDTSKCLKCGACIDNCTFNAI 625
Cdd:COG2221    15 EKCIGCGLCVAVCPTGAISLDDGKLV-IDEEKCIGCGACIRVCPTGAI 61
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 575-625 5.60e-10

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 55.50  E-value: 5.60e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2053417210 575 FITDDCKGCTKCSRVCPAGCITGSVKEQHTIDTSKCLKCGACIDNCTFNAI 625
Cdd:COG1149     8 IDEEKCIGCGLCVEVCPEGAIKLDDGGAPVVDPDLCTGCGACVGVCPTGAI 58
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
555-625 1.45e-09

Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 60.42  E-value: 1.45e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2053417210 555 IAHVVDKKCPAGKCQNllsyfitDDCKGCTKCSRVCPAGCItGSVKEQHTIDTSKCLKCGACIDNCTFNAI 625
Cdd:COG4624    75 GIIIIDKRGPSIIRDK-------EKCKNCYPCVRACPVKAI-KVDDGKAEIDEEKCISCGQCVAVCPFGAI 137
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
563-625 5.22e-09

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 57.38  E-value: 5.22e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 563 CPAGKCQNLLSYF-------ITDDCKGCTKCSRVCPAGCITgsvkEQHTIDTSKCLKCGACIDNCTFNAI 625
Cdd:COG0348   188 CPYGAFQGLLSDLstlrvryDRGDCIDCGLCVKVCPMGIDI----RKGEINQSECINCGRCIDACPKDAI 253
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 574-625 1.66e-08

NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 51.25  E-value: 1.66e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2053417210 574 YFITDDCKGCTKCSRVCPAGCITGSVKEQHT--IDTSKCLKCGACIDNCTFNAI 625
Cdd:COG1146     4 VIDTDKCIGCGACVEVCPVDVLELDEEGKKAlvINPEECIGCGACELVCPVGAI 57
RnfC COG4656
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and ...
 155-288 2.08e-08

Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase


Pssm-ID: 443694 [Multi-domain]  Cd Length: 451  Bit Score: 57.07  E-value: 2.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 155 IDPDSIEEYIANDGYLALgkclTSLTPQEVIAEVKTSGLRGRGGAGFPTGSKWEAASKNPAgptdkKFVVCNADEGDPGA 234
Cdd:COG4656    99 IEPDGEDEWIELEPLADY----EDLSPEEIIERIREAGIVGLGGAGFPTHVKLSPPPDKKI-----DTLIINGAECEPYL 169

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2053417210 235 FMDRSVLEGDPHSVLEAMAICGYAIGSDTGYIYIRAEYPKSIERLKVAIAQAEK 288
Cdd:COG4656   170 TCDDRLMRERAEEIIEGIRILMKALGAKKVIIGIEDNKPEAIAALRKALAGDDD 223
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 577-620 6.37e-08

Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 54.23  E-value: 6.37e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2053417210 577 TDDCKGCTKCSRVCPAGCITGSVKEQHTIDTSKCLKCGACIDNC 620
Cdd:COG2878   136 EYGCIGCGDCIKACPFDAIVGAAKGMHTVDEDKCTGCGLCVEAC 179
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 578-625 7.84e-08

electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 52.11  E-value: 7.84e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2053417210 578 DDCKGCTKCSRVCPAGCITGSVKEQHTIDTSKCLKCGACIDNCTFNAI 625
Cdd:TIGR01944 113 DNCIGCTKCIQACPVDAIVGAAKAMHTVIADECTGCDLCVEPCPTDCI 160
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 575-625 1.72e-07

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 50.47  E-value: 1.72e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2053417210 575 FITDDCKGCTKCSRVCPAGCIT----GSVKEQHTIDTSKCLKCGACIDNCTFNAI 625
Cdd:cd10549     3 YDPEKCIGCGICVKACPTDAIElgpnGAIARGPEIDEDKCVFCGACVEVCPTGAI 57
PRK08764 PRK08764
Rnf electron transport complex subunit RnfB;
572-625 3.73e-07

Rnf electron transport complex subunit RnfB;


Pssm-ID: 181550 [Multi-domain]  Cd Length: 135  Bit Score: 49.53  E-value: 3.73e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2053417210 572 LSYFITDDCKGCTKCSRVCPAGCITGSVKEQHTIDTSKCLKCGACIDNCTFNAI 625
Cdd:PRK08764   79 VAWIVEADCIGCTKCIQACPVDAIVGGAKHMHTVIAPLCTGCELCVPACPVDCI 132
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 580-624 1.82e-06

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 45.21  E-value: 1.82e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2053417210 580 CKGCTKCSRVCPAGCITGSVKEQH------TIDTSKCLKCGACIDNCTFNA 624
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKkgtktvVIDPERCVGCGACVAVCPTGA 51
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
580-625 1.91e-06

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 48.34  E-value: 1.91e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2053417210 580 CKGCTKCSRVCPAGCIT--------GS-VKEQHTIDTSKCLKCGACIDNCTFNAI 625
Cdd:PRK05888   60 CIACKLCAAICPADAITieaaeredGRrRTTRYDINFGRCIFCGFCEEACPTDAI 114
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 573-625 1.93e-06

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 49.47  E-value: 1.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2053417210 573 SYFITDDCKGCTKCSRVCPAGCITgsVKEQHTIDTSKCLKCGACIDNCTFNAI 625
Cdd:NF038196  180 KFHVTDKCIGCGICAKVCPVNNIE--MEDGKPVWGHNCTHCLACIHRCPKEAI 230
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 575-625 2.05e-06

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 46.20  E-value: 2.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2053417210 575 FITDDCKGCTKCSRVCPAGCITGSVKEQHTIDTSKCLKCGACIDNCTFNAI 625
Cdd:COG1144    27 VDEDKCIGCGLCWIVCPDGAIRVDDGKYYGIDYDYCKGCGICAEVCPVKAI 77
Fer4_9 pfam13187
4Fe-4S dicluster domain;
579-625 3.89e-06

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 44.08  E-value: 3.89e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2053417210 579 DCKGCTKCSRVCPAGCITGSVKEQ---HTIDTSKCLKCGACIDNCTFNAI 625
Cdd:pfam13187   1 KCTGCGACVAACPAGAIVPDLVGQtirGDIAGLACIGCGACVDACPRGAI 50
PRK05113 PRK05113
electron transport complex protein RnfB; Provisional
 578-625 4.08e-06

electron transport complex protein RnfB; Provisional


Pssm-ID: 235347 [Multi-domain]  Cd Length: 191  Bit Score: 47.63  E-value: 4.08e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2053417210 578 DDCKGCTKCSRVCPAGCITGSVKEQHTIDTSKCLKCGACIDNCTFNAI 625
Cdd:PRK05113  114 DNCIGCTKCIQACPVDAIVGATKAMHTVISDLCTGCDLCVAPCPTDCI 161
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 578-628 7.74e-06

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 45.47  E-value: 7.74e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2053417210 578 DDCKGCTKCSRVCPAGCIT--------GSVKEQHTIDTSKCLKCGACIDNCTFNAIIKK 628
Cdd:cd10549    40 DKCVFCGACVEVCPTGAIEltpegkeyVPKEKEAEIDEEKCIGCGLCVKVCPVDAITLE 98
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 574-620 2.29e-05

4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 42.24  E-value: 2.29e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2053417210 574 YFITDDCKGCTKCSRVCPAGCITGSVKEQHT------IDTSKCLKCGACIDNC 620
Cdd:pfam13237   3 VIDPDKCIGCGRCTAACPAGLTRVGAIVERLegeavrIGVWKCIGCGACVEAC 55
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
580-626 2.30e-05

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 46.46  E-value: 2.30e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2053417210 580 CKGCTKCSRVCPAGCIT--GSVKEqhtIDTSKCLKCGACIDNCTFNAII 626
Cdd:PRK07118  215 CIGCGKCVKACPAGAITmeNNLAV---IDQEKCTSCGKCVEKCPTKAIR 260
PRK13795 PRK13795
hypothetical protein; Provisional
 580-620 2.56e-05

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 47.30  E-value: 2.56e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2053417210 580 CKGCTKCSRVCPAGCIT-GSVKEQHTIDTSKCLKCGACIDNC 620
Cdd:PRK13795  583 CVGCGVCVGACPTGAIRiEEGKRKISVDEEKCIHCGKCTEVC 624
NuoE COG1905
NADH:ubiquinone oxidoreductase 24 kD subunit (chain E) [Energy production and conversion]; ...
 27-110 3.16e-05

NADH:ubiquinone oxidoreductase 24 kD subunit (chain E) [Energy production and conversion]; NADH:ubiquinone oxidoreductase 24 kD subunit (chain E) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 441509  Cd Length: 159  Bit Score: 44.36  E-value: 3.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210  27 YSKENVLRRELLVCCDTGCTSSNSLEIVSELENEIkksGIQD-------KVSVRLTGCFGFCAQGPIVKVypDNVFYVKV 99
Cdd:COG1905    71 FRLKPVGKHVIRVCTGTACHLRGAEELLEALEEKL---GIKPgettadgKFTLEEVECLGACGLAPVMMV--NDDVYGRL 145

                          90
                  ....*....|.
gi 2053417210 100 EPSDAEKIVQS 110
Cdd:COG1905   146 TPEKVDEILDE 156
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 578-625 5.43e-05

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 42.90  E-value: 5.43e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2053417210 578 DDCKGCTKCSRVCPAGCITgSVKEQH--TIDTSKCLKCGACIDNCTFNAI 625
Cdd:PRK08348   42 DKCVGCRMCVTVCPAGVFV-YLPEIRkvALWTGRCVFCGQCVDVCPTGAL 90
PRK06991 PRK06991
electron transport complex subunit RsxB;
580-625 6.28e-05

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 45.17  E-value: 6.28e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2053417210 580 CKGCTKCSRVCPAGCITGSVKEQHTIDTSKCLKCGACIDNCTFNAI 625
Cdd:PRK06991   87 CIGCTLCMQACPVDAIVGAPKQMHTVLADLCTGCDLCVPPCPVDCI 132
Fer4_21 pfam14697
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 578-620 7.42e-05

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 434137 [Multi-domain]  Cd Length: 59  Bit Score: 40.73  E-value: 7.42e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2053417210 578 DDCKGCTKCSRVCPAG---CITGSVKEQHTIDTSKCLKCGACIDNC 620
Cdd:pfam14697   6 DTCIGCGKCYIACPDTshqAIVGDGKRHHTVIEDECTGCNLCVSVC 51
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 574-625 7.69e-05

Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319870 [Multi-domain]  Cd Length: 136  Bit Score: 42.76  E-value: 7.69e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2053417210 574 YFITDDCKGCT--KCSRVCPAGCI----TGSVKeqhtIDTSKCLKCGACIDNCTFNAI 625
Cdd:cd04410    44 AFLPVSCMHCEdpPCVKACPTGAIykdeDGIVL----IDEDKCIGCGSCVEACPYGAI 97
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 574-625 8.88e-05

uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes the beta-subunit of formate dehydrogenases that are as yet uncharacterized. Members of the DMSO reductase family include formate dehydrogenase N and O (FDH-N, FDH-O) and tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N, a major component of nitrate respiration of Escherichia coli, is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. It forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.


Pssm-ID: 319884 [Multi-domain]  Cd Length: 161  Bit Score: 43.45  E-value: 8.88e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2053417210 574 YFITDDCKGCTK--CSRVCPAGCI----TGSVkeqhTIDTSKCLKCGACIDNCTFNAI 625
Cdd:cd10562    64 LFRKRQCMHCTDaaCVKVCPTGALykteNGAV----VVDEDKCIGCGYCVAACPFDVP 117
PRK09898 PRK09898
ferredoxin-like protein;
575-628 1.12e-04

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 43.67  E-value: 1.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2053417210 575 FITDDCKGCT--KCSRVCPAGCITGSVKEQH-TIDTSKCLKCGACIDNC-----TFNAIIKK 628
Cdd:PRK09898  118 YTADTCRQCKepQCMNVCPIGAITWQQKEGCiTVDHKRCIGCSACTTACpwmmaTVNTESKK 179
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 580-627 1.30e-04

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 41.94  E-value: 1.30e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2053417210 580 CKGCTKCSRVCPAGCITGSVKEQHTIDTSKCLKCGACIDNCTFNAIIK 627
Cdd:cd16372    49 CNQCGECIDVCPTGAITRDANGVVMINKKLCVGCLMCVGFCPEGAMFK 96
SLBB pfam10531
SLBB domain;
385-434 1.32e-04

SLBB domain;


Pssm-ID: 463136 [Multi-domain]  Cd Length: 56  Bit Score: 39.96  E-value: 1.32e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2053417210 385 VFALGGKVENVGLVEVPMGTTLRDIVFEIGGGIPEGKKFKAVQTGGPSGG 434
Cdd:pfam10531   1 VVTVTGEVKRPGNYEVPIGTTLSDLIELAGGFTDDADLDINLRRLKRPGG 50
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 566-625 1.40e-04

Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 43.01  E-value: 1.40e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2053417210 566 GKCQNLLSYFITDDCKGCTK--CSRVCPAGCI----TGSVkeqhTIDTSKCLKCGACIDNCTFNAI 625
Cdd:COG0437    46 GEFPNVEWLFVPVLCNHCDDppCVKVCPTGATykreDGIV----LVDYDKCIGCRYCVAACPYGAP 107
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
573-625 1.57e-04

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 44.85  E-value: 1.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2053417210 573 SYFITDDCKGCTKCSRVCPAGCItgSVKEQHT--IDTSKCLKCGACIDNCTFNAI 625
Cdd:COG1148   491 AEVDPEKCTGCGRCVEVCPYGAI--SIDEKGVaeVNPALCKGCGTCAAACPSGAI 543
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 578-628 2.17e-04

bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 43.14  E-value: 2.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2053417210 578 DDCKGCTKCSRVCPAGCItGSVKEQHTIDTSKCLKCGACIDNCTFNAIIKK 628
Cdd:cd03110    64 EKCIRCGNCERVCKFGAI-LEFFQKLIVDESLCEGCGACVIICPRGAIYLK 113
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 575-625 2.58e-04

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 41.49  E-value: 2.58e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2053417210 575 FITDDCKGCTK--CSRVCPAGCIT----GSVKeqhtIDTSKCLKCGACIDNCTFNAI 625
Cdd:cd16370    48 FTVVVCRACEDppCAEACPTGALEprkgGGVV----LDKEKCIGCGNCVKACIVGAI 100
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 575-625 3.01e-04

beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family contains beta FeS subunits of several dehydrogenases in the DMSO reductase superfamily, including formate dehydrogenase N (FDH-N), tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N is a major component of nitrate respiration of Escherichia coli; it catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate to a cytochrome. W-FDH contains a tungsten instead of molybdenum at the catalytic center and seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate.


Pssm-ID: 319888 [Multi-domain]  Cd Length: 156  Bit Score: 41.62  E-value: 3.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2053417210 575 FITDDCKGCTK--CSRVCPAGCI----TGSVkeqhTIDTSKCLKCGACIDNCTFNAI 625
Cdd:cd16366    65 FRKDQCMHCTDagCLAACPTGAIirteTGTV----VVDPETCIGCGYCVNACPFDIP 117
PRK13984 PRK13984
putative oxidoreductase; Provisional
 580-621 5.28e-04

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 43.22  E-value: 5.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2053417210 580 CKGCTKCSRVCPAGCIT-----------GSVKEQHTIDTSKCLKCGACIDNCT 621
Cdd:PRK13984   47 CIGCGTCSKICPTDAITmvevpdlpqeyGKKPQRPVIDYGRCSFCALCVDICT 99
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
580-625 7.27e-04

Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 40.03  E-value: 7.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2053417210 580 CKGCT--KCSRVCPAGCIT---GSVKeqhtIDTSKCLKCGACIDNCTFNAI 625
Cdd:COG1142    52 CRHCEdaPCAEVCPVGAITrddGAVV----VDEEKCIGCGLCVLACPFGAI 98
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
580-623 8.54e-04

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 38.24  E-value: 8.54e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2053417210 580 CKGCTKCSRVCPAGCITGSV---------------------KEQHTIDTSKCLKCGACIDNCTFN 623
Cdd:pfam13484   1 CGSCGKCIDACPTGAIVGPEgvldarrcisyltiekkglipDELRCLLGNRCYGCDICQDVCPWN 65
TRX_Fd_NuoE cd03064
TRX-like [2Fe-2S] Ferredoxin (Fd) family, NADH:ubiquinone oxidoreductase (Nuo) subunit E ...
 37-110 1.14e-03

TRX-like [2Fe-2S] Ferredoxin (Fd) family, NADH:ubiquinone oxidoreductase (Nuo) subunit E subfamily; Nuo, also called respiratory chain Complex 1, is the entry point for electrons into the respiratory chains of bacteria and the mitochondria of eukaryotes. It is a multisubunit complex with at least 14 core subunits. It catalyzes the electron transfer of NADH to quinone coupled with the transfer of protons across the membrane, providing the proton motive force required for energy-consuming processes. Electrons are transferred from NADH to quinone through a chain of iron-sulfur clusters in Nuo, including the [2Fe-2S] cluster present in NuoE core subunit, also called the 24 kD subunit of Complex 1. This subfamily also include formate dehydrogenases, NiFe hydrogenases and NAD-reducing hydrogenases, that contain a NuoE domain. A subset of these proteins contain both NuoE and NuoF in a single chain. NuoF, also called the 51 kD subunit of Complex 1, contains one [4Fe-4S] cluster and also binds the NADH substrate and FMN.


Pssm-ID: 239362 [Multi-domain]  Cd Length: 80  Bit Score: 38.27  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210  37 LLVCCDTGCTSSNSLEIVSELEneiKKSGIQ-------DKVSVRLTGCFGFCAQGPIVKVypDNVFYVKVEPSDAEKIVQ 109
Cdd:cd03064     4 IRVCTGTACHLRGAEALLEALE---KKLGIKpgettpdGRFTLEEVECLGACDLAPVMMI--NDDVYGRLTPEKVDAILE 78


                  .
gi 2053417210 110 S 110
Cdd:cd03064    79 A 79
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 575-596 1.22e-03

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 38.11  E-value: 1.22e-03
                          10        20
                  ....*....|....*....|..
gi 2053417210 575 FITDDCKGCTKCSRVCPAGCIT 596
Cdd:COG1144    57 IDYDYCKGCGICAEVCPVKAIE 78
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 151-289 1.45e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 41.86  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053417210 151 NCGLIDPDSIEEYIANDGYLALgkclTSLTPQEVIAEVKTSGLRGRGGAGFPTgskweaASKNPAGPTDKKFVVCNADEG 230
Cdd:PRK05035  101 LCVVIEPDGEDRWIERQPWADY----RQLSPEELIERIRQAGIAGLGGAGFPT------AVKLQPGGDKIETLIINGAEC 170

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2053417210 231 DPGAFMDRSVLEGDPHSVLEAMAICGYAIGSDTGYIYIRAEYPKSIERLKVAIAQAEKY 289
Cdd:PRK05035  171 EPYITADDRLMRERADEIIEGIRILAHLLQPKEVLIGIEDNKPEAIAALRAALAGADDI 229
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 604-626 1.87e-03

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 37.01  E-value: 1.87e-03
                          10        20
                  ....*....|....*....|...
gi 2053417210 604 TIDTSKCLKCGACIDNCTFNAII 626
Cdd:COG1149     7 VIDEEKCIGCGLCVEVCPEGAIK 29
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 575-625 3.52e-03

beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes beta subunit of formate dehydrogenase family O (FDH-O), which is highly homologous to formate dehydrogenase N (FDH-N), a member of the DMSO reductase family. In E. coli three formate dehydrogenases are synthesized that are capable of oxidizing formate; Fdh-H, couples formate disproportionation to hydrogen and CO2, and is part of the cytoplasmically oriented formate hydrogenlyase complex, while FDH-N and FDH-O indicate their respective induction after growth with nitrate and oxygen. Little is known about FDH-O, although it shows formate oxidase activity during aerobic growth and is also synthesized during nitrate respiration, similar to FDH-N.


Pssm-ID: 319882 [Multi-domain]  Cd Length: 225  Bit Score: 39.29  E-value: 3.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2053417210 575 FITDDCKGCTK--CSRVCPAGCITGSvkEQHT--IDTSKCLKCGACIDNCTFNAI 625
Cdd:cd10560    73 FMSDVCKHCTDagCLEACPTGAIFRT--EFGTvyIQPDICNGCGYCVAACPFGVI 125
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 578-625 3.94e-03

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 40.15  E-value: 3.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2053417210 578 DDCKG--CTK-CSRVCP-----AGCIT-GSVKEQHTIDTSKCLKCGACIDNCTFNAI 625
Cdd:COG1245    10 DRCQPkkCNYeCIKYCPvnrtgKEAIEiDEDDGKPVISEELCIGCGICVKKCPFDAI 66
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 580-626 4.58e-03

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 37.56  E-value: 4.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2053417210 580 CKGCTK--CSRVCPAGCI-----TGSVkeqhTIDTSKCLKCGACIDNCTFNAII 626
Cdd:cd10550    49 CRQCEDapCVEACPVGAIsrdeeTGAV----VVDEDKCIGCGMCVEACPFGAIR 98
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 578-625 6.27e-03

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 37.32  E-value: 6.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2053417210 578 DDCKGCTKCSRVCPAGCItgsVKEQHTIDTSKCLKCGACIDNCTFNAI 625
Cdd:cd16372    77 KLCVGCLMCVGFCPEGAM---FKHEDYPEPFKCIACGICVKACPTGAL 121
PRK09898 PRK09898
ferredoxin-like protein;
580-625 6.47e-03

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 38.28  E-value: 6.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2053417210 580 CKGCTKCSRVCPAGCITGSVKEQhtiDTSKCLKCGACIDNCTFNAI 625
Cdd:PRK09898  156 CIGCSACTTACPWMMATVNTESK---KSSKCVLCGECANACPTGAL 198
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
551-628 9.42e-03

Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 38.85  E-value: 9.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2053417210 551 KDEYIAHVVDKKCPAGKCQNLLSYFITDDCKGCTKCSRVCPAGCITGSVKEQ-HTIDTSKCLKCGACIDNCTFNAIIKK 628
Cdd:COG4624    33 ILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPsIIRDKEKCKNCYPCVRACPVKAIKVD 111
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH