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Conserved domains on  [gi|1332073272|gb|PNK70646|]
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tetrathionate reductase subunit TtrB [Hafnia paralvei]

Protein Classification

PRK14993 family protein( domain architecture ID 11487554)

PRK14993 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
7-250 3.73e-178

tetrathionate reductase subunit TtrB;


:

Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 489.00  E-value: 3.73e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272   7 MDSSKRQFLQRLGVLTAGASLVPLAQAQFPFSPERHEGSQQHRYAMLVDLRRCIGCQACTVSCAIENQTPQGEFRTLVNQ 86
Cdd:PRK14993    1 MDSSKRQFLQQLGVLTAGASLVPLAEAKFPFSPERHEGSPRHRYAMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  87 YQVQIEGQQSVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNTRCVGCAYCVQACPYDARFINHETQTADKCT 166
Cdd:PRK14993   81 YQVQREGSQEVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272 167 FCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRISQMLHEHHDAIKVLKPESGTSPHVFYLGLDEAFVTPLMGRAQPAL 246
Cdd:PRK14993  161 FCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRIATMLHQHRDAIKVLKPENGTSPHVFYLGLDDAFVTPLMGRAQPAL 240


                  ....
gi 1332073272 247 WQEV 250
Cdd:PRK14993  241 WQEV 244
 
Name Accession Description Interval E-value
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
7-250 3.73e-178

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 489.00  E-value: 3.73e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272   7 MDSSKRQFLQRLGVLTAGASLVPLAQAQFPFSPERHEGSQQHRYAMLVDLRRCIGCQACTVSCAIENQTPQGEFRTLVNQ 86
Cdd:PRK14993    1 MDSSKRQFLQQLGVLTAGASLVPLAEAKFPFSPERHEGSPRHRYAMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  87 YQVQIEGQQSVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNTRCVGCAYCVQACPYDARFINHETQTADKCT 166
Cdd:PRK14993   81 YQVQREGSQEVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272 167 FCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRISQMLHEHHDAIKVLKPESGTSPHVFYLGLDEAFVTPLMGRAQPAL 246
Cdd:PRK14993  161 FCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRIATMLHQHRDAIKVLKPENGTSPHVFYLGLDDAFVTPLMGRAQPAL 240


                  ....
gi 1332073272 247 WQEV 250
Cdd:PRK14993  241 WQEV 244
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 52-228 2.42e-95

polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial polysulfide reductase (PsrABC), an integral membrane-bound enzyme responsible for quinone-coupled reduction of polysulfides, a process important in extreme environments such as deep-sea vents and hot springs. Polysulfide reductase contains three subunits: a catalytic subunit PsrA, an electron transfer PsrB subunit and the hydrophobic transmembrane PsrC subunit. PsrB belongs to the DMSO reductase superfamily that contains [4Fe-4S] clusters which transfer the electrons from the A subunit to the hydrophobic integral membrane C subunit via the B subunit. In Shewanella oneidensis, which has highly diverse anaerobic respiratory pathways, PsrABC is responsible for H2S generation as well as its regulation via respiration of sulfur species. PsrB transfers electrons from PsrC (serving as quinol oxidase) to the catalytic subunit PsrA for reduction of corresponding electron acceptors. It has been shown that T. thermophilus polysulfide reductase could be a key energy-conserving enzyme of the respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane.


Pssm-ID: 319873 [Multi-domain]  Cd Length: 185  Bit Score: 277.11  E-value: 2.42e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  52 MLVDLRRCIGCQACTVSCAIENQTPQGEFRTLVNQYQVqiEGQQSVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIV 131
Cdd:cd10551     1 MVIDLRKCIGCGACVVACKAENNVPPGVFRNRVLEYEV--GEYPNVKRTFLPVLCNHCENPPCVKVCPTGATYKREDGIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272 132 VVDNTRCVGCAYCVQACPYDARFINHE------------TQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDIKDPHS 199
Cdd:cd10551    79 LVDYDKCIGCRYCMAACPYGARYFNPEephefgevpvrpKGVVEKCTFCYHRLDEGLLPACVEACPTGARIFGDLDDPNS 158

                         170       180
                  ....*....|....*....|....*....
gi 1332073272 200 RISQMLHEHHdaIKVLKPESGTSPHVFYL 228
Cdd:cd10551   159 EVSKLLAERR--AYVLKPELGTKPKVYYI 185
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 45-232 6.18e-85

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 251.02  E-value: 6.18e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  45 SQQHRYAMLVDLRRCIGCQACTVSCAIENQTPQGEFRTLVNQYQVQIEGQQSVTNVllPRLCNHCDNPPCVPVCPVQATF 124
Cdd:COG0437     1 LSMKRYGMVIDLTKCIGCRACVVACKEENNLPVGVTWRRVRRYEEGEFPNVEWLFV--PVLCNHCDDPPCVKVCPTGATY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272 125 QREDGIVVVDNTRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRISQM 204
Cdd:COG0437    79 KREDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVEACPTGALVFGDLDDPESEVSKR 158

                         170       180
                  ....*....|....*....|....*...
gi 1332073272 205 LHEHHDaiKVLKPESGTSPHVFYLGLDE 232
Cdd:COG0437   159 LAELPA--YRLLPELGTKPSVYYLPKRN 184
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 102-193 4.98e-35

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: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 120.82  E-value: 4.98e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272 102 LPRLCNHCDNPPCVPVCPVQATFQRE-DGIVVVDNTRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPAC 180
Cdd:pfam13247   6 FPEQCRHCLNPPCKASCPVGAIYKDEeTGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAGLLPAC 85

                          90
                  ....*....|...
gi 1332073272 181 VESCVGGARIIGD 193
Cdd:pfam13247  86 VQTCPTGAMNFGD 98
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 130-184 6.70e-04

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: 39.40  E-value: 6.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272 130 IVVVDNTRCVGCAYCVQACPYDA-----RFINheTQTADKCTFCvhrleagllPACVESC 184
Cdd:TIGR01944 107 VALIDEDNCIGCTKCIQACPVDAivgaaKAMH--TVIADECTGC---------DLCVEPC 155
 
Name Accession Description Interval E-value
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
7-250 3.73e-178

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 489.00  E-value: 3.73e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272   7 MDSSKRQFLQRLGVLTAGASLVPLAQAQFPFSPERHEGSQQHRYAMLVDLRRCIGCQACTVSCAIENQTPQGEFRTLVNQ 86
Cdd:PRK14993    1 MDSSKRQFLQQLGVLTAGASLVPLAEAKFPFSPERHEGSPRHRYAMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  87 YQVQIEGQQSVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNTRCVGCAYCVQACPYDARFINHETQTADKCT 166
Cdd:PRK14993   81 YQVQREGSQEVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272 167 FCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRISQMLHEHHDAIKVLKPESGTSPHVFYLGLDEAFVTPLMGRAQPAL 246
Cdd:PRK14993  161 FCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRIATMLHQHRDAIKVLKPENGTSPHVFYLGLDDAFVTPLMGRAQPAL 240


                  ....
gi 1332073272 247 WQEV 250
Cdd:PRK14993  241 WQEV 244
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 52-228 2.42e-95

polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial polysulfide reductase (PsrABC), an integral membrane-bound enzyme responsible for quinone-coupled reduction of polysulfides, a process important in extreme environments such as deep-sea vents and hot springs. Polysulfide reductase contains three subunits: a catalytic subunit PsrA, an electron transfer PsrB subunit and the hydrophobic transmembrane PsrC subunit. PsrB belongs to the DMSO reductase superfamily that contains [4Fe-4S] clusters which transfer the electrons from the A subunit to the hydrophobic integral membrane C subunit via the B subunit. In Shewanella oneidensis, which has highly diverse anaerobic respiratory pathways, PsrABC is responsible for H2S generation as well as its regulation via respiration of sulfur species. PsrB transfers electrons from PsrC (serving as quinol oxidase) to the catalytic subunit PsrA for reduction of corresponding electron acceptors. It has been shown that T. thermophilus polysulfide reductase could be a key energy-conserving enzyme of the respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane.


Pssm-ID: 319873 [Multi-domain]  Cd Length: 185  Bit Score: 277.11  E-value: 2.42e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  52 MLVDLRRCIGCQACTVSCAIENQTPQGEFRTLVNQYQVqiEGQQSVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIV 131
Cdd:cd10551     1 MVIDLRKCIGCGACVVACKAENNVPPGVFRNRVLEYEV--GEYPNVKRTFLPVLCNHCENPPCVKVCPTGATYKREDGIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272 132 VVDNTRCVGCAYCVQACPYDARFINHE------------TQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDIKDPHS 199
Cdd:cd10551    79 LVDYDKCIGCRYCMAACPYGARYFNPEephefgevpvrpKGVVEKCTFCYHRLDEGLLPACVEACPTGARIFGDLDDPNS 158

                         170       180
                  ....*....|....*....|....*....
gi 1332073272 200 RISQMLHEHHdaIKVLKPESGTSPHVFYL 228
Cdd:cd10551   159 EVSKLLAERR--AYVLKPELGTKPKVYYI 185
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 45-232 6.18e-85

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 251.02  E-value: 6.18e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  45 SQQHRYAMLVDLRRCIGCQACTVSCAIENQTPQGEFRTLVNQYQVQIEGQQSVTNVllPRLCNHCDNPPCVPVCPVQATF 124
Cdd:COG0437     1 LSMKRYGMVIDLTKCIGCRACVVACKEENNLPVGVTWRRVRRYEEGEFPNVEWLFV--PVLCNHCDDPPCVKVCPTGATY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272 125 QREDGIVVVDNTRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRISQM 204
Cdd:COG0437    79 KREDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVEACPTGALVFGDLDDPESEVSKR 158

                         170       180
                  ....*....|....*....|....*...
gi 1332073272 205 LHEHHDaiKVLKPESGTSPHVFYLGLDE 232
Cdd:COG0437   159 LAELPA--YRLLPELGTKPSVYYLPKRN 184
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 53-188 6.84e-54

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: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 170.44  E-value: 6.84e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  53 LVDLRRCIGCQACTVSCAIENQTPQGEFRTLVNQYQVQIEGQQSVTNVLLPrlCNHCDNPPCVPVCPVQATFQREDGIVV 132
Cdd:cd16371     3 YFDQERCIGCKACEIACKDKNDLPPGVNWRRVYEYEGGEFPEVFAYFLSMS--CNHCENPACVKVCPTGAITKREDGIVV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1332073272 133 VDNTRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGA 188
Cdd:cd16371    81 VDQDKCIGCGYCVWACPYGAPQYNPETGKMDKCDMCVDRLDEGEKPACVAACPTRA 136
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 52-192 1.33e-47

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: 154.08  E-value: 1.33e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  52 MLVDLRRCIGCQACTVSCAIENQTPQGEFRTLVnqyqvQIEGQQSVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIV 131
Cdd:cd04410     1 LVVDLDRCIGCGTCEVACKQEHGLRPGPDWSRI-----KVIEGGGLERAFLPVSCMHCEDPPCVKACPTGAIYKDEDGIV 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1332073272 132 VVDNTRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIG 192
Cdd:cd04410    76 LIDEDKCIGCGSCVEACPYGAIVFDPEPGKAVKCDLCGDRLDEGLEPACVKACPTGALTFG 136
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 47-227 6.55e-47

beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene dehydrogenase (EBDH, EC 1.17.99.2), a member of the DMSO reductase family. EBDH oxidizes the hydrocarbon ethylbenzene to (S)-1-phenylethanol. It is a heterotrimer, with the alpha subunit containing the catalytic center with a molybdenum held by two molybdopterin-guanine dinucleotides, the beta subunit containing four iron-sulfur clusters (the electron transfer subunit) and the gamma subunit containing a methionine and a lysine as axial heme ligands. During catalysis, electrons produced by substrate oxidation are transferred to a heme in the gamma subunit and then presumably to a separate cytochrome involved in nitrate respiration.


Pssm-ID: 319877 [Multi-domain]  Cd Length: 316  Bit Score: 158.23  E-value: 6.55e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  47 QHRYAMLVDLRRCIGCQACTVSCA----------------IENQTPQG-------------------------------- 78
Cdd:cd10555     2 KRQLAMVMDLNKCIGCQTCTVACKtlwtnrngreymywnnVETQPGKGypknwekkgggfkdkgelkpgiiptledygvp 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  79 -EFRTLVNQY-----QVQIEGQQSVT---------------NVL---LPRLCNHCDNPPCVPVCPVQATFQR-EDGIVVV 133
Cdd:cd10555    82 wEYNHEEELFegkggRVRPSPKGDPTwgpnwdedqgageypNSYyfyLPRICNHCTNPACLAACPRKAIYKReEDGIVLV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272 134 DNTRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRISQMLHEHHDAIK 213
Cdd:cd10555   162 DQDRCRGYRYCVEACPYKKIYFNPVEQKSEKCIFCYPRIEKGVAPACARQCVGRIRFVGYLDDEESPVYKLVKKWKVALP 241

                         250
                  ....*....|....
gi 1332073272 214 vLKPESGTSPHVFY 227
Cdd:cd10555   242 -LHPEYGTEPNVFY 254
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 52-231 8.05e-46

N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This family includes the beta subunit of pyrogallol-phloroglucinol transhydroxylase (TH), a cytoplasmic molybdenum (Mo) enzyme from anaerobic microorganisms like Pelobacter acidigallici and Desulfitobacterium hafniense which catalyzes the conversion of pyrogallol to phloroglucinol, an important building block of plant polymers. TH belongs to the DMSO reductase (DMSOR) family; it is a heterodimer consisting of a large alpha catalytic subunit and a small beta FeS subunit. The beta subunit has two domains with the N-terminal domain containing three [4Fe-4S] centers and a seven-stranded, mainly antiparallel beta-barrel domain. In the anaerobic bacterium Pelobacter acidigallici, gallic acid, pyrogallol, phloroglucinol, or phloroglucinol carboxylic acid are fermented to three molecules of acetate (plus CO2), and TH is the key enzyme in the fermentation pathway, which converts pyrogallol to phloroglucinol in the absence of O2.


Pssm-ID: 319874 [Multi-domain]  Cd Length: 186  Bit Score: 151.32  E-value: 8.05e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  52 MLVDLRRCIGCQACTVSCAIEN-----------QTPQGEFRTLVNQyqvQIEGQQSVTNV-LLPRLCNHCDNPPCVPVCP 119
Cdd:cd10552     1 LVIDVAKCNGCYNCFLACKDEHvgndwpgyaapQPRHGHFWMRILR---RERGQYPKVDVaYLPVPCNHCDNAPCIKAAK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272 120 VQATFQREDGIVVVDNTRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAG-LLPACVESCVGGARIIGDIKDPH 198
Cdd:cd10552    78 DGAVYKRDDGIVIIDPEKAKGQKQLVDACPYGAIYWNEELQVPQKCTFCAHLLDDGwKEPRCVQACPTGALRFGKLEDEE 157

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1332073272 199 SRISQmlheHHDAIKVLKPESGTSPHVFYLGLD 231
Cdd:cd10552   158 MAAKA----AEEGLEVLHPELGTKPRVYYKNLP 186
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 51-201 1.05e-43

the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 (Hyd-2), an enzyme that catalyzes the reversible oxidation of H2 to protons and electrons. Hyd-2 is membrane-associated and forms an unusual heterotetrameric [NiFe]-hydrogenase in that it lacks the typical cytochrome b membrane anchor subunit that transfers electrons to the quinone pool. The electron transfer subunit of Hyd-2 (HybA) which is predicted to contain four iron-sulfur clusters, is essential for electron transfer from Hyd-2 to menaquinone/demethylmenaquinone (MQ/DMQ) to couple hydrogen oxidation to fumarate reduction.


Pssm-ID: 319883 [Multi-domain]  Cd Length: 196  Bit Score: 146.20  E-value: 1.05e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  51 AMLVDLRRCIGCQACTVSCAIENQTPQGEF----------------RTLVNQYQVQIEGQQSVTnvlLPRLCNHCDNPPC 114
Cdd:cd10561     1 GVLYDTTRCIGCRACEVACKEWNGLPAEDTafgpgwdnprdlsaktYTVIKRYEVETGGKGFVF---VKRQCMHCLDPAC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272 115 VPVCPVQATFQREDGIVVVDNTRCVGCAYCVQACPYDA-RFinhETQTAD----KCTFCVHRLEAGLLPACVESCVGGAR 189
Cdd:cd10561    78 VSACPVGALRKTPEGPVTYDEDKCIGCRYCMVACPFNIpKY---EWDSANpkirKCTMCYDRLKEGKQPACVEACPTGAL 154

                         170
                  ....*....|....*.
gi 1332073272 190 IIGD----IKDPHSRI 201
Cdd:cd10561   155 LFGKreelLAEAKRRI 170
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 49-228 4.43e-40

beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several DMSO reductase superfamily, including nitrate reductase A, ethylbenzene dehydrogenase and selenate reductase. DMSO Reductase (DMSOR) family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. . The beta subunits of DMSOR 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. Nitrate reductase A contains three subunits (the catalytic subunit NarG, the catalytic subunit NarH with four [Fe-S] clusters, and integral membrane subunit NarI) and often forms a respiratory chain with the formate dehydrogenase via the lipid soluble quinol pool. Ethylbenzene dehydrogenase oxidizes the hydrocarbon ethylbenzene to (S)-1-phenylethanol. Selenate reductase catalyzes reduction of selenate to selenite in bacterial species that can obtain energy by respiring anaerobically with selenate as the terminal electron acceptor.


Pssm-ID: 319887 [Multi-domain]  Cd Length: 201  Bit Score: 137.33  E-value: 4.43e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  49 RYAMLVDLRRCIGCQACTVSCA----------------IENQTPQGEFRTLVNQYQVQieGQQSVTNVLLPRLCNHCDNP 112
Cdd:cd16365     2 QFAAVFNLNKCIGCQTCTVACKnawtyrkgqeymwwnnVETKPGGGYPQDWEVKTIDN--GGNTRFFFYLQRLCNHCTNP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272 113 PCVPVCPVQATFQR-EDGIVVVDNTRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARII 191
Cdd:cd16365    80 ACLAACPRGAIYKReEDGIVLIDQKRCRGYRKCVEQCPYKKIYFNGLSRVSEKCIACYPRIEGGDPTRCMSACVGRIRLQ 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1332073272 192 GDIKD-PHSRISQMLHEHHDAIKvLKPESGTSPHVFYL 228
Cdd:cd16365   160 GFLDDnPKSPVTKLIRHWKVALP-LHPEYGTEPNIYYV 196
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 52-193 9.12e-39

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: 132.43  E-value: 9.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  52 MLVDLRRCIGCQACTVSCAIENQTPqGEFRTLVNQYQ----------VQIEGQQSVTNVLLPRL------CNHCDNPPCV 115
Cdd:cd10562     1 MLVDTSKCTACRGCQVACKQWNQLP-AEKTPFTGSYQnppdltpntwTLIRFYEHEEDNGGIRWlfrkrqCMHCTDAACV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1332073272 116 PVCPVQATFQREDGIVVVDNTRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGD 193
Cdd:cd10562    80 KVCPTGALYKTENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCFDRIENGMQPACVKTCPTGALTFGD 157
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 52-188 1.05e-38

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: 132.14  E-value: 1.05e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  52 MLVDLRRCIGCQACTVSCAIENQTP--QGEFR--------------TLVNQYQVQIEGQQsVTNVLLPRLCNHCDNPPCV 115
Cdd:cd16366     1 FLVDTSRCTGCRACQVACKQWNGLPaeKTEFTgsyqnppdltahtwTLVRFYEVEKPGGD-LSWLFRKDQCMHCTDAGCL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1332073272 116 PVCPVQATFQREDGIVVVDNTRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGA 188
Cdd:cd16366    80 AACPTGAIIRTETGTVVVDPETCIGCGYCVNACPFDIPRFDEETGRVAKCTLCYDRISNGLQPACVKTCPTGA 152
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 49-188 1.05e-37

uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This family includes beta FeS subunits of anaerobic DMSO reductase (DMSOR) superfamily that have yet to be characterized. DMSOR consists of a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and the tungsten-containing formate dehydrogenase (FDH-T). Examples of 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: 319875 [Multi-domain]  Cd Length: 146  Bit Score: 129.02  E-value: 1.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  49 RYAMLVDLRRCIGCQACTVSCAIENQTPQGE-FRTLVNQYQVQIEGQQSVTNVLLPrlCNHCDNPPCVPVCPVQATFQRE 127
Cdd:cd10553     2 KYYLYHDSKRCIGCLACEVHCKVKNNLPVGPrLCRIFAVGPKMVGGKPRLKFVYMS--CFHCENPWCVKACPTGAMQKRE 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1332073272 128 -DGIVVVDNTRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGA 188
Cdd:cd10553    80 kDGIVYVDQELCIGCKACIEACPWGIPQWNPATGKVVKCDYCMDRIDQGLKPACVTGCTTHA 141
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 102-192 2.11e-37

beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes nitrate reductase A, a member of the DMSO reductase family. The respiratory nitrate reductase complex (NarGHI) from E. coli is a heterotrimer, with the catalytic subunit (NarG) with a molybdo-bis (molybdopterin guanine dinucleotide) cofactor and an [Fe-S] cluster, the electron transfer subunit (NarH) with four [Fe-S] clusters, and the integral membrane subunit (NarI) with two b-type hemes. Nitrate reductase A often forms a respiratory chain with the formate dehydrogenase via the lipid soluble quinol pool. Electron transfer from formate to nitrate is coupled to proton translocation across the cytoplasmic membrane generating proton motive force by a redox loop mechanism. Demethylmenaquinol (DMKH2) has been shown to be a good substrate for NarGHI in nitrate respiration in E. coli.


Pssm-ID: 319879 [Multi-domain]  Cd Length: 363  Bit Score: 134.41  E-value: 2.11e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272 102 LPRLCNHCDNPPCVPVCPVQATFQR-EDGIVVVDNTRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPAC 180
Cdd:cd10557   175 LPRICNHCLNPACVAACPSGAIYKReEDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSEKCIFCYPRLEAGQPTVC 254

                          90
                  ....*....|..
gi 1332073272 181 VESCVGGARIIG 192
Cdd:cd10557   255 SETCVGRIRYLG 266
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 53-196 2.27e-35

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: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 122.77  E-value: 2.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  53 LVDLRRCIGCQACTVSCAIENQtpqgefrtlvNQYQVQIEGQQSVTNVllPRLCNHCDNPPCVPVCPVQATFQREDGIVV 132
Cdd:cd16374     2 YVDPERCIGCRACEIACAREHS----------GKPRISVEVVEDLASV--PVRCRHCEDAPCMEVCPTGAIYRDEDGAVL 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1332073272 133 VDNTRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDIKD 196
Cdd:cd16374    70 VDPDKCIGCGMCAMACPFGVPRFDPSLKVAVKCDLCIDRRREGKLPACVEACPTGALKFGDIEE 133
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 102-193 4.98e-35

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: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 120.82  E-value: 4.98e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272 102 LPRLCNHCDNPPCVPVCPVQATFQRE-DGIVVVDNTRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPAC 180
Cdd:pfam13247   6 FPEQCRHCLNPPCKASCPVGAIYKDEeTGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAGLLPAC 85

                          90
                  ....*....|...
gi 1332073272 181 VESCVGGARIIGD 193
Cdd:pfam13247  86 VQTCPTGAMNFGD 98
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 102-192 2.01e-34

Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 440755 [Multi-domain]  Cd Length: 485  Bit Score: 128.77  E-value: 2.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272 102 LPRLCNHCDNPPCVPVCPVQATFQR-EDGIVVVDNTRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPAC 180
Cdd:COG1140   178 LPRICEHCLNPACVASCPSGAIYKReEDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGKAEKCIFCYPRIEAGQPTVC 257

                          90
                  ....*....|..
gi 1332073272 181 VESCVGGARIIG 192
Cdd:COG1140   258 SETCVGRIRYLG 269
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 35-228 2.60e-34

Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate reductase (SER), a member of the DMSO reductase family. SER catalyzes the reduction of selenate to selenite in bacterial species that can obtain energy by respiring anaerobically with selenate as the terminal electron acceptor. The enzyme comprises three subunits SerABC, forming a heterotrimer, with the catalytic component (alpha-subunit), iron-sulfur protein (beta-subunit) and monomeric b-type heme-containing gamma subunit. Beta subunit contains coordinating one [3Fe-4S] cluster and three [4Fe-4S] clusters and functions as electron carrier.


Pssm-ID: 319878 [Multi-domain]  Cd Length: 287  Bit Score: 124.49  E-value: 2.60e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  35 FPFSPERhegsQQHRYAMLVDLRRCIGCQACTVSC-----AIENQT---------------PQG-EFRTLVNQYQVQI-- 91
Cdd:cd10556     1 YPYEESR----PDKQFAMVFDTNKCIACQTCTMACkstwtSGKGQEymwwnnvetkpyggyPLGwDVRLLDEEGGQTWae 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  92 ----------EGQQSVTNVL----------------------------------------LPRLCNHCDNPPCVPVCPVQ 121
Cdd:cd10556    77 ggvyegktifEAAAAGEQVLgyrpededwrypnigedevngertpdtgsslpphpiwffyLPRICNHCTYPACLAACPRK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272 122 ATFQR-EDGIVVVDNTRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDIKDP--- 197
Cdd:cd10556   157 AIYKReEDGIVLIDQERCRGYRECVEACPYKKPMYNPTTRVSEKCIGCYPRIEEGDQTQCVSACIGKIRLQGFINTPpda 236

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1332073272 198 -----HSRISQMLHEHHDAIKVLKPESGTSPHVFYL 228
Cdd:cd10556   237 rwaddRDNPIDFLVHIKKVALPLYPQFGTEPNVYYI 272
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 51-232 8.40e-33

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: 119.03  E-value: 8.40e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  51 AMLVDLRRCIGCQACTVSCAIENQTPQGEFRTLVNQYQ------------VQIEGQQSVTNVLLPR----------LCNH 108
Cdd:cd10560     1 GFFTDTSICIGCKACEVACKQWNQLPADGYDFSGMSYDntgdlsastwrhVKFIERPTEDGPANEGgdlqwlfmsdVCKH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272 109 CDNPPCVPVCPVQATFQREDGIVVVDNTRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGA 188
Cdd:cd10560    81 CTDAGCLEACPTGAIFRTEFGTVYIQPDICNGCGYCVAACPFGVIDRNEETGRAHKCTLCYDRLKDGLEPACAKACPTGS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1332073272 189 RIIGDIKD----PHSRISQmLHEH--HDA-IKVLKPESGTSP-HVFYLGLDE 232
Cdd:cd10560   161 IQFGPLEElrerARARVEQ-LHEQgvVEAyLYGADPTEGYGGlNAFFLLLDK 211
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 51-196 1.25e-32

The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS subunit of formate dehydrogenase-N (FDH-N), a member of the DMSO reductase family. FDH-N 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. Thus, FDH-N is a major component of nitrate respiration of Escherichia coli. This integral membrane enzyme 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.


Pssm-ID: 319880 [Multi-domain]  Cd Length: 208  Bit Score: 117.87  E-value: 1.25e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  51 AMLVDLRRCIGCQACTVSCAIENQTPqGEFRTLVNQYQ---------------VQIEGQQSVTNVLLPRLCNHCDNPPCV 115
Cdd:cd10558     1 AKLIDVSKCIGCKACQVACKEWNDLR-AEVGHNVGTYQnpadlspetwtlmkfREVEDNGKLEWLIRKDGCMHCADPGCL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272 116 PVCPVQ-ATFQREDGIVVVDNTRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDI 194
Cdd:cd10558    80 KACPSPgAIVQYANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVGLEPACVKTCPTGALHFGTK 159


                  ..
gi 1332073272 195 KD 196
Cdd:cd10558   160 ED 161
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 52-188 8.10e-27

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: 100.73  E-value: 8.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  52 MLVDLRRCIGCQACTVSCAIENQtpqGEFRTLVNQYQVQIEGQQSVTNvllPRLCNHCDNPPCVPVCPVQA-TFQREDGI 130
Cdd:cd10550     1 LVVDPEKCTGCRTCELACSLKHE---GVFNPSLSRIRVVRFEPEGLDV---PVVCRQCEDAPCVEACPVGAiSRDEETGA 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1332073272 131 VVVDNTRCVGCAYCVQACPYDARFINHETQTADKCTFCvhrleaGLLPACVESCVGGA 188
Cdd:cd10550    75 VVVDEDKCIGCGMCVEACPFGAIRVDPETGKAIKCDLC------GGDPACVKVCPTGA 126
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
10-196 9.10e-27

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 105.52  E-value: 9.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  10 SKRQFLQRLGVLTAGASLVPLAQAQfpfsPERHEGSQQHRYAMLVDLRRCIGCQACTVSCAIENQT---PQGE------- 79
Cdd:PRK10882    2 NRRNFLKAASAGALLAGALPSVSHA----AAENRPPIPGALGMLYDSTLCVGCQACVTKCQEINFPernPQGEqtwdnpd 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  80 ------------FRTLVNQYQVQIEGQQSvtnvLLPRLCNHCDNPPCVPVCPVQA-TFQREDGIVVVDNTRCVGCAYCVQ 146
Cdd:PRK10882   78 klspytnniikvWKSGTGVNKDQEENGYA----YIKKQCMHCVDPNCVSVCPVSAlTKDPKTGIVHYDKDVCTGCRYCMV 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1332073272 147 ACPYDARFINHETQTAD--KCTFCVH----RLEAGLLPACVESCVGGARIIGDIKD 196
Cdd:PRK10882  154 ACPFNVPKYDYNNPFGAihKCELCNQkgveRLDKGGLPGCVEVCPTGAVIFGTREE 209
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 53-188 2.26e-25

CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the iron-sulfur subunit of carbon monoxide dehydrogenase (CODH), found in anaerobic bacteria and archaea. Carbon monoxide dehydrogenase is a key enzyme for carbon monoxide (CO) metabolism, where CooF is the proposed mediator of electron transfer between CODH and the CO-induced hydrogenase, catalyzing the reaction that uses CO as a single carbon and energy source, and producing only H2 and CO2. The ion-sulfur subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons in the protein complex during reaction.


Pssm-ID: 319885 [Multi-domain]  Cd Length: 140  Bit Score: 96.94  E-value: 2.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  53 LVDLRRCIGCQACTVSCAIENQTPQGEFRTLV----NQYQVQIEGqqsVTNVLLPRLCNHCDNPPCVPVCPVQA-TFQRE 127
Cdd:cd10563     3 FIDEEKCLGCKLCEVACAVAHSKSKDLIKAKLekerPRPRIRVEE---SGGRSFPLQCRHCDEPPCVKACMSGAmHKDPE 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1332073272 128 DGIVVVDNTRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEagllPACVESCVGGA 188
Cdd:cd10563    80 TGIVIHDEEKCVGCWMCVMVCPYGAIRPDKERKVALKCDLCPDRET----PACVEACPTGA 136
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 53-184 3.96e-25

HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 96.56  E-value: 3.96e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  53 LVDLRRCIGCQACTVSCAienqtpqgefrtlVNQYQVQIEGQQSVTNVLLPRL-------------CNHCDNPPCVPVCP 119
Cdd:cd10554     3 IADPDKCIGCRTCEVACA-------------AAHSGKGIFEAGTDGLPFLPRLrvvktgevtapvqCRQCEDAPCANVCP 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1332073272 120 VQATFQrEDGIVVVDNTRCVGCAYCVQACPYDA-----------RFINHETQTADKCTFCVHRLEAgllPACVESC 184
Cdd:cd10554    70 VGAISQ-EDGVVQVDEERCIGCKLCVLACPFGAiemapttvpgvDWERGPRAVAVKCDLCAGREGG---PACVEAC 141
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
53-184 1.87e-24

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 94.72  E-value: 1.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  53 LVDLRRCIGCQACTVSCAIENQTPQGEfrtlVNQYQVQIEGQQSVTNvllPRLCNHCDNPPCVPVCPVQAtFQREDGIVV 132
Cdd:COG1142     6 IADPEKCIGCRTCEAACAVAHEGEEGE----PFLPRIRVVRKAGVSA---PVQCRHCEDAPCAEVCPVGA-ITRDDGAVV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1332073272 133 VDNTRCVGCAYCVQACPYDARFINHETQ--TADKCTFCVHRLEaglLPACVESC 184
Cdd:COG1142    78 VDEEKCIGCGLCVLACPFGAITMVGEKSraVAVKCDLCGGREG---GPACVEAC 128
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 50-193 3.81e-24

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: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 94.76  E-value: 3.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  50 YAMLVDLRRCIGCQACTVSCAiENQTPQGEFRTLVNQyqvqIEGQQSVTNVllPRLCNHCDNPPCVPVCPVQATFQREDG 129
Cdd:cd16369     2 KEFFIDPSRCIGCRACVAACR-ECGTHRGKSMIHVDY----IDRGESTQTA--PTVCMHCEDPTCAEVCPADAIKVTEDG 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1332073272 130 IVV-VDNTRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGD 193
Cdd:cd16369    75 VVQsALKPRCIGCSNCVNACPFGVPKYDEERNLMMKCDMCYDRTSVGKAPMCASVCPSGALFYGT 139
PRK09898 PRK09898
ferredoxin-like protein;
58-196 2.00e-21

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 88.74  E-value: 2.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  58 RCIGCQACTVSCAIENQTPQGEFRTLVNQYQVQIEGQQSVTN--------VLLPRLCNHCDNPPCVPVCPVQA-TFQRED 128
Cdd:PRK09898   67 RCTGCHRCEISCTNFNDGSVGTFFSRIKIHRNYFFGDNGVGSggglygdlNYTADTCRQCKEPQCMNVCPIGAiTWQQKE 146

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1332073272 129 GIVVVDNTRCVGCAYCVQACPYDARFINHETQTADKCTFCvhrleagllPACVESCVGGARIIGDIKD 196
Cdd:PRK09898  147 GCITVDHKRCIGCSACTTACPWMMATVNTESKKSSKCVLC---------GECANACPTGALKIIEWKD 205
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 50-196 8.04e-21

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: 319890 [Multi-domain]  Cd Length: 200  Bit Score: 86.71  E-value: 8.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  50 YAMLVDLRRCIGCQ-----ACTVSCAIENQ--TPQGEFR-----------------------------TLVNQYQVQIEG 93
Cdd:cd16368     1 LATLIDLTKCDGCPgesipACVRACREKNQarFPEPVSKpiqpywprkriedwsdkrdvtdrltpynwLYVQKLTVDTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  94 QQSVtnVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNTRCVGCAYCVQACPYD--AR------FINHETQTAD-- 163
Cdd:cd16368    81 GEKE--VFIPRRCMHCDNPPCAKLCPFGAARKTPEGAVYIDDDLCFGGAKCRDVCPWHipQRqagvgiYLHLAPEYAGgg 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1332073272 164 ---KCTFCVHRLEAGLLPACVESCVGGARIIGDIKD 196
Cdd:cd16368   159 vmyKCDLCKDLLAQGKPPACIEACPKGAQYFGPRKE 194
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 51-218 1.14e-20

tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit of Tungsten-containing formate dehydrogenase (W-FDH), a member of the DMSO reductase family. 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: 319881 [Multi-domain]  Cd Length: 200  Bit Score: 86.33  E-value: 1.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  51 AMLVDLRRCIGCQACTVSCAIENQTP--QGEFR--------------TLVNQYQVQIEGQQSVTNvLLPRLCNHCDNPPC 114
Cdd:cd10559     1 SFLIDTTRCTACRGCQVACKQWNQLPaeQTKNTgshqnppdlsantyKLVRFNEVRNENGKPDWL-FFPDQCRHCVTPPC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272 115 VPVCPVQatfqrEDGIVVVDNTRCV--------GCAYCV-QACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCV 185
Cdd:cd10559    80 KDAADMV-----PGAVIQDEATGAVvftektaeLDFDDVlSACPYNIPRKNEATGRIVKCDMCIDRVSNGLQPACVKACP 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1332073272 186 GGARIIGDIKDphsrisqMLHEHHDAIKVLKPE 218
Cdd:cd10559   155 TGAMNFGDRDE-------MLAMASKRLEELKKR 180
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 43-190 3.31e-20

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: 319889 [Multi-domain]  Cd Length: 138  Bit Score: 83.51  E-value: 3.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  43 EGSQQHRYAMLVDLRRCIGCQACTVSCAienQTPQGEFRTLVNQYQVQiegqqsvtNVLLPRLCNHCDNPPCVPVCPVQA 122
Cdd:cd16367     5 YGLIQGTNLLVIDLDRCIRCDNCEKACA---DTHDGHSRLDRNGLRFG--------NLLVPTACRHCVDPVCMIGCPTGA 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1332073272 123 TFQREDGIVVVDNtRCVGCAYCVQACPYDARFInhetQTADKCTFCVHRLEagllPACVESCVGGARI 190
Cdd:cd16367    74 IHRDDGGEVVISD-ACCGCGNCASACPYGAIQM----VRAVKCDLCAGYAG----PACVSACPTGAAI 132
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 52-184 4.67e-19

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 85.95  E-value: 4.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  52 MLVDLRRCIGCQACTVSCAIENQtpQGEFRTLVNQYQVQI---EGQQSVTNVLlprlCNHCDNPPCVPVCPVQATFQRED 128
Cdd:PRK12769    5 IMANSQQCLGCHACEIACVMAHN--DEQHVLSQHHFHPRItviKHQQQRSAVT----CHHCEDAPCARSCPNGAISHVDD 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1332073272 129 GIVVVDNtRCVGCAYCVQACPYDARFI-------NHETQTADKCTFCVHRlEAGllPACVESC 184
Cdd:PRK12769   79 SIQVNQQ-KCIGCKSCVVACPFGTMQIvltpvaaGKVKATAHKCDLCAGR-ENG--PACVENC 137
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 52-184 2.37e-18

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 83.92  E-value: 2.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  52 MLVDLRRCIGCQACTVSCAI---ENQTPQ--GEFRTlvnqyQVQIEGQQSVTNvllPRLCNHCDNPPCVPVCPVQA-TFQ 125
Cdd:PRK12809    5 IAAEAAECIGCHACEIACAVahnQENWPLshSDFRP-----RIHVVGKGQAAN---PVACHHCNNAPCVTACPVNAlTFQ 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1332073272 126 REDgiVVVDNTRCVGCAYCVQACPYDArfINHETQTADKCTFCVHRLEAglLPACVESC 184
Cdd:PRK12809   77 SDS--VQLDEQKCIGCKRCAIACPFGV--VEMVDTIAQKCDLCNQRSSG--TQACIEVC 129
PRK10330 PRK10330
electron transport protein HydN;
52-184 3.68e-18

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 79.16  E-value: 3.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  52 MLVDLRRCIGCQACTVSCAIENQTPQGEFRTLVNQYQVQIEGQQSVtNVLLPRLCNHCDNPPCVPVCPVQAtFQREDGIV 131
Cdd:PRK10330    5 IIADASKCIGCRTCEVACVVSHQENQDCASLTPETFLPRIHVIKGV-NVSTATVCRQCEDAPCANVCPNGA-ISRDKGFV 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1332073272 132 VVDNTRCVGCAYCVQACPYDARFI---------------NHETQTADKCTFCVHRlEAGllPACVESC 184
Cdd:PRK10330   83 HVMQERCIGCKTCVVACPYGAMEVvvrpvirnsgaglnvRAEKAEANKCDLCNHR-EDG--PACMAAC 147
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 54-168 1.02e-15

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: 71.53  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  54 VDLRRCIGCQACTVSCAIENQTPQGEFRTLVN-QYQVQIEGQQSVtnvllpRLCNHCDNPPCVPVCPVQATFQREDGIVV 132
Cdd:cd16370     6 KDMERCIGCYSCMLACSRRVHKSASLSKSAIRvRTRGGLEGGFTV------VVCRACEDPPCAEACPTGALEPRKGGGVV 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1332073272 133 VDNTRCVGCAYCVQACPYDARFINHETQTADKCTFC 168
Cdd:cd16370    80 LDKEKCIGCGNCVKACIVGAIFWDEETNKPIICIHC 115
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 57-188 1.38e-13

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: 65.43  E-value: 1.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  57 RRCIGCQACTVSCA-IENQTPQGEfrtlvnQYQVQIEGQQSVTNvllPRLCNHCDNppCVPVCPVQATFQREDGIVVVDN 135
Cdd:cd16372     8 EKCIGCLQCEEACSkTFFKEEDRE------KSCIRITETEGGYA---INVCNQCGE--CIDVCPTGAITRDANGVVMINK 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1332073272 136 TRCVGCAYCVQACPYDARFINHETQTADKCTFCvhrleagllPACVESCVGGA 188
Cdd:cd16372    77 KLCVGCLMCVGFCPEGAMFKHEDYPEPFKCIAC---------GICVKACPTGA 120
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 54-152 6.91e-10

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: 55.48  E-value: 6.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  54 VDLRRCIGCQACTVSC---AIENQTPQGEFRTLVNQYQVQIEgqqsvtnvllprLCNHCDNppCVPVCPVQATFQREDGI 130
Cdd:cd10549    37 IDEDKCVFCGACVEVCptgAIELTPEGKEYVPKEKEAEIDEE------------KCIGCGL--CVKVCPVDAITLEDELE 102

                          90       100
                  ....*....|....*....|..
gi 1332073272 131 VVVDNTRCVGCAYCVQACPYDA 152
Cdd:cd10549   103 IVIDKEKCIGCGICAEVCPVNA 124
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
103-159 2.35e-09

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 52.43  E-value: 2.35e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1332073272 103 PRLCNHCDNppCVPVCPVQAtFQREDGIVVVDNTRCVGCAYCVQACPYDARFINHET 159
Cdd:COG2768    10 EEKCIGCGA--CVKVCPVGA-ISIEDGKAVIDPEKCIGCGACIEVCPVGAIKIEWEE 63
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 106-152 1.09e-08

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: 51.21  E-value: 1.09e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1332073272 106 CNHCDNppCVPVCPVQATFQREDGIVVVDNTRCVGCAYCVQACPYDA 152
Cdd:COG1144    32 CIGCGL--CWIVCPDGAIRVDDGKYYGIDYDYCKGCGICAEVCPVKA 76
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 105-157 2.04e-08

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 49.66  E-value: 2.04e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1332073272 105 LCNHCDNppCVPVCPVQAtFQREDGIVVVDNTRCVGCAYCVQACPYDARFINH 157
Cdd:COG2221    16 KCIGCGL--CVAVCPTGA-ISLDDGKLVIDEEKCIGCGACIRVCPTGAIKGEK 65
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 103-152 4.08e-08

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 49.27  E-value: 4.08e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1332073272 103 PRLCNHCDNppCVPVCPVQAtFQREDGIVVVDNTRCVGCAYCVQACPYDA 152
Cdd:COG4231    21 EDKCTGCGA--CVKVCPADA-IEEGDGKAVIDPDLCIGCGSCVQVCPVDA 67
NapF COG1145
Ferredoxin [Energy production and conversion];
106-163 1.26e-07

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 51.26  E-value: 1.26e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1332073272 106 CNHCDNppCVPVCPVQA-TFQREDGIVVVDNTRCVGCAYCVQACPYDArfINHETQTAD 163
Cdd:COG1145   184 CIGCGL--CVKVCPTGAiRLKDGKPQIVVDPDKCIGCGACVKVCPVGA--ISLEPKEIE 238
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 103-152 1.44e-07

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 47.42  E-value: 1.44e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1332073272 103 PRLCNHCDNppCVPVCPVQATFQREDGIVVVDNTRCVGCAYCVQACPYDA 152
Cdd:COG1149    10 EEKCIGCGL--CVEVCPEGAIKLDDGGAPVVDPDLCTGCGACVGVCPTGA 57
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 106-152 2.22e-07

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: 47.05  E-value: 2.22e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1332073272 106 CNHCDNppCVPVCPVQA---TFQREDGIVVVDNTRCVGCAYCVQACPYDA 152
Cdd:COG1143     4 CIGCGL--CVRVCPVDAitiEDGEPGKVYVIDPDKCIGCGLCVEVCPTGA 51
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
82-152 2.42e-07

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 51.01  E-value: 2.42e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1332073272  82 TLVNQYQVQIEGQQSVTNvllPRLCNHCDNppCVPVCPVQATFQREDGIVVVDNTRCVGCAYCVQACPYDA 152
Cdd:COG1148   477 QLLSKGELGVEPSVAEVD---PEKCTGCGR--CVEVCPYGAISIDEKGVAEVNPALCKGCGTCAAACPSGA 542
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
103-171 1.72e-06

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 48.65  E-value: 1.72e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1332073272 103 PRLCNHcdnpPCVPVCPVQAT------FQREDGIVVVDNTRCVGCAYCVQACPYDA-RFINHETQTADKctfCVHR 171
Cdd:PRK13409   14 PKKCNY----ECIKYCPVVRTgeetieIDEDDGKPVISEELCIGCGICVKKCPFDAiSIVNLPEELEEE---PVHR 82
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 103-152 3.50e-06

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: 47.47  E-value: 3.50e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1332073272 103 PRLCNHcdnpPCVPVCPVQAT------FQREDGIVVVDNTRCVGCAYCVQACPYDA 152
Cdd:COG1245    14 PKKCNY----ECIKYCPVNRTgkeaieIDEDDGKPVISEELCIGCGICVKKCPFDA 65
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
99-197 4.07e-06

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 47.33  E-value: 4.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  99 NVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNTRCVGCAYCVQACPYDARFINHETQT--ADKCTFCvhrleaGl 176
Cdd:COG4624    54 CCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCYPCVRACPVKAIKVDDGKAEidEEKCISC------G- 126

                          90       100
                  ....*....|....*....|....*....
gi 1332073272 177 lpACVESCVGGA--------RIIGDIKDP 197
Cdd:COG4624   127 --QCVAVCPFGAiteksdieKVKKALKDP 153
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 106-152 4.87e-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: 42.90  E-value: 4.87e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1332073272 106 CNHCDNppCVPVCPVQATFQREDG------IVVVDNTRCVGCAYCVQACPYDA 152
Cdd:pfam12838   1 CIGCGA--CVAACPVGAITLDEVGekkgtkTVVIDPERCVGCGACVAVCPTGA 51
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
106-152 9.27e-06

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 45.82  E-value: 9.27e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1332073272 106 CNHCDNppCVPVCPVqatfqredGIVV----VDNTRCVGCAYCVQACPYDA 152
Cdd:COG0348   212 CIDCGL--CVKVCPM--------GIDIrkgeINQSECINCGRCIDACPKDA 252
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
114-184 1.60e-05

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 45.05  E-value: 1.60e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1332073272 114 CVPVCPV---QATFQREDGIVV-VDNTRCVGCAYCVQACPYDArFINHETQTADKCTFCvhrleaGllpACVESC 184
Cdd:COG0348   184 CRYLCPYgafQGLLSDLSTLRVrYDRGDCIDCGLCVKVCPMGI-DIRKGEINQSECINC------G---RCIDAC 248
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 114-149 3.77e-05

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: 43.83  E-value: 3.77e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1332073272 114 CVPVCPVQATFQREDGIVVVDNTRCVGCAYCVQACP 149
Cdd:COG2878   145 CIKACPFDAIVGAAKGMHTVDEDKCTGCGLCVEACP 180
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 56-185 3.80e-05

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: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 42.63  E-value: 3.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  56 LRRCIGCQACTVSCaienqtPQGEFRTLVNQYQVQIegqqSVTNVLLPRL--CNHCDNPpCVPVCPVQA----TFQRED- 128
Cdd:cd16373    13 LALCIRCGLCVEAC------PTGVIQPAGLEDGLEG----GRTPYLDPREgpCDLCCDA-CVEVCPTGAlrplDLEEQKv 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1332073272 129 --GIVVVDNTRCV------GCAYCVQACPYDARFINHETQT------ADKCTFCvhrleaGllpACVESCV 185
Cdd:cd16373    82 kmGVAVIDKDRCLawqggtDCGVCVEACPTEAIAIVLEDDVlrpvvdEDKCVGC------G---LCEYVCP 143
NapF COG1145
Ferredoxin [Energy production and conversion];
100-184 4.74e-05

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 43.56  E-value: 4.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272 100 VLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNTRCVGCAYCVQACPYDA-RFINHETQT---ADKCTFCvhrleag 175
Cdd:COG1145   146 ILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVCPTGAiRLKDGKPQIvvdPDKCIGC------- 218


                  ....*....
gi 1332073272 176 llPACVESC 184
Cdd:COG1145   219 --GACVKVC 225
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
114-152 4.91e-05

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 41.47  E-value: 4.91e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1332073272 114 CVPVCPVQATFQREDGIVVVDNTRCVGCAYCVQACPYDA 152
Cdd:PRK09623   59 CWKFCPEPAIYIKEDGYVAIDYDYCKGCGICANECPTKA 97
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
114-151 5.77e-05

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 43.38  E-value: 5.77e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1332073272 114 CVPVCPVQAtFQREDGIVVVDNTRCVGCAYCVQACPYD 151
Cdd:PRK07118  147 CVAACPFDA-IHIENGLPVVDEDKCTGCGACVKACPRN 183
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
114-163 5.85e-05

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 42.18  E-value: 5.85e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1332073272 114 CVPVCPVQA----TFQREDGIVVVDN-----TRCVGCAYCVQACPYDA-----RFINHETQTAD 163
Cdd:PRK05888   66 CAAICPADAitieAAEREDGRRRTTRydinfGRCIFCGFCEEACPTDAivetpDFELATETREE 129
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 100-152 7.09e-05

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: 41.61  E-value: 7.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1332073272 100 VLLPRLCNHCDNppCVPVCPVQA-TFQREDGIV---VVDNTRCVGCAYCVQACPYDA 152
Cdd:cd10549     2 KYDPEKCIGCGI--CVKACPTDAiELGPNGAIArgpEIDEDKCVFCGACVEVCPTGA 56
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 100-149 9.59e-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: 39.16  E-value: 9.59e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1332073272 100 VLLPRLCNHCDNppCVPVCPVQATFQR------EDGIVVVDNTRCVGCAYCVQACP 149
Cdd:pfam13237   3 VIDPDKCIGCGR--CTAACPAGLTRVGaiverlEGEAVRIGVWKCIGCGACVEACP 56
porD PRK09625
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
 105-149 1.15e-04

pyruvate flavodoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 236596 [Multi-domain]  Cd Length: 133  Bit Score: 40.89  E-value: 1.15e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1332073272 105 LCNHCDNppCVPVCPVQATFQREDGIVVVDNTRCVGCAYCVQACP 149
Cdd:PRK09625   60 ICINCFN--CWVYCPDAAILSRDKKLKGVDYSHCKGCGVCVEVCP 102
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
54-164 1.35e-04

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 42.23  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  54 VDLRRCIGCQACTVSCaienqtPQG--EFRTLVNQYQVqiegqqsvtnvllprLCNHCDNPP---------------CVP 116
Cdd:PRK07118  165 VDEDKCTGCGACVKAC------PRNviELIPKSARVFV---------------ACNSKDKGKavkkvcevgcigcgkCVK 223

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1332073272 117 VCPVQAtFQREDGIVVVDNTRCVGCAYCVQACPydaRFINHETQTADK 164
Cdd:PRK07118  224 ACPAGA-ITMENNLAVIDQEKCTSCGKCVEKCP---TKAIRILNKPPK 267
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
126-197 1.69e-04

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 38.94  E-value: 1.69e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1332073272 126 REDGIVVVDNTRCVGCAYCVQACPYDArfINHETQTA----DKCTFCvhrleagllPACVESCVGGARIIGDIKDP 197
Cdd:COG2768     1 HSLGKPYVDEEKCIGCGACVKVCPVGA--ISIEDGKAvidpEKCIGC---------GACIEVCPVGAIKIEWEEDE 65
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 105-149 2.19e-04

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 42.17  E-value: 2.19e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1332073272 105 LCNHCDNppCVPVCPVQATFQ-REDGIVVVDNTRCVGCAYCVQACP 149
Cdd:PRK12771  511 NCFECDN--CYGACPQDAIIKlGPGRRYHFDYDKCTGCHICADVCP 554
PRK13795 PRK13795
hypothetical protein; Provisional
 137-185 3.81e-04

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 41.52  E-value: 3.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1332073272 137 RCVGCAYCVQACPYDARFINHETQT----ADKCTFCVhrleagllpACVESCV 185
Cdd:PRK13795  582 ECVGCGVCVGACPTGAIRIEEGKRKisvdEEKCIHCG---------KCTEVCP 625
PRK06991 PRK06991
electron transport complex subunit RsxB;
30-120 5.34e-04

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 40.55  E-value: 5.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  30 LAQAQFPFSPERheGSQQHRYAMLVDLRRCIGCQACTVSCAIEnqtpqgefrtlvnqyqvQIEGQQSVTNVLLPRLCNHC 109
Cdd:PRK06991   60 LGKPVIPLDPAN--GVERPRAVAVIDEQLCIGCTLCMQACPVD-----------------AIVGAPKQMHTVLADLCTGC 120

                          90
                  ....*....|.
gi 1332073272 110 DnpPCVPVCPV 120
Cdd:PRK06991  121 D--LCVPPCPV 129
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 130-184 6.70e-04

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: 39.40  E-value: 6.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272 130 IVVVDNTRCVGCAYCVQACPYDA-----RFINheTQTADKCTFCvhrleagllPACVESC 184
Cdd:TIGR01944 107 VALIDEDNCIGCTKCIQACPVDAivgaaKAMH--TVIADECTGC---------DLCVEPC 155
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 130-195 6.95e-04

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 37.34  E-value: 6.95e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1332073272 130 IVVVDNTRCVGCAYCVQACPYDARFINHETQT--ADKCTFCVHrleagllpaCVESCVGGARIIGDIK 195
Cdd:COG2221     9 PPKIDEEKCIGCGLCVAVCPTGAISLDDGKLVidEEKCIGCGA---------CIRVCPTGAIKGEKPK 67
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 129-188 7.04e-04

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 37.00  E-value: 7.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1332073272 129 GIVVVDNTRCVGCAYCVQACPYDARFINHETQTA-----DKCTFCvhrleagllPACVESCVGGA 188
Cdd:COG1146     1 MMPVIDTDKCIGCGACVEVCPVDVLELDEEGKKAlvinpEECIGC---------GACELVCPVGA 56
napF TIGR00402
ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of ...
 77-169 1.08e-03

ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of the periplasmic nitrate reductase system, as in Escherichia coli. NapF interacts with the catalytic subunit, NapA, and may be an accessory protein for NapA maturation. [Energy metabolism, Electron transport]


Pssm-ID: 273060 [Multi-domain]  Cd Length: 101  Bit Score: 37.62  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272  77 QGEFRTLVN-QYQVQIEGQQSVTNVLLPRLCNHCDNppCVPVCPvQATFQREDGI---VVVDNTRCVGCAYCVQACPYDA 152
Cdd:TIGR00402   6 RGVFPATSStIEKTQIRPPWSARESLFSAVCTRCGE--CASACE-NNILQLGQQGqptVEFDNAECDFCGKCAEACPTNA 82

                          90
                  ....*....|....*..
gi 1332073272 153 RFINHETQTADKCTFCV 169
Cdd:TIGR00402  83 FHPRFPGDWLLRPQISS 99
PRK13795 PRK13795
hypothetical protein; Provisional
 105-161 1.12e-03

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 39.98  E-value: 1.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1332073272 105 LCNHCDnpPCVPVCPVQAtFQREDG--IVVVDNTRCVGCAYCVQACPYdARFINHETQT 161
Cdd:PRK13795  582 ECVGCG--VCVGACPTGA-IRIEEGkrKISVDEEKCIHCGKCTEVCPV-VKYKDKRNGS 636
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 130-188 1.29e-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: 36.24  E-value: 1.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1332073272 130 IVVVDNTRCVGCAYCVQACPYDA-RFINHETQT--ADKCTFCVhrleagllpACVESCVGGA 188
Cdd:COG1149     5 IPVIDEEKCIGCGLCVEVCPEGAiKLDDGGAPVvdPDLCTGCG---------ACVGVCPTGA 57
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 131-152 1.52e-03

4Fe-4S binding 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.


Pssm-ID: 459642 [Multi-domain]  Cd Length: 24  Bit Score: 35.30  E-value: 1.52e-03
                          10        20
                  ....*....|....*....|..
gi 1332073272 131 VVVDNTRCVGCAYCVQACPYDA 152
Cdd:pfam00037   1 VVIDEEKCIGCGACVEVCPVGA 22
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 132-184 1.69e-03

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: 37.38  E-value: 1.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332073272 132 VVDNTRCVGCAYCVQACPYDA-------RFINHETQTADKCTFCvhrleaGllpACVESC 184
Cdd:cd10549     2 KYDPEKCIGCGICVKACPTDAielgpngAIARGPEIDEDKCVFC------G---ACVEVC 52
PRK06991 PRK06991
electron transport complex subunit RsxB;
113-168 2.06e-03

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 38.62  E-value: 2.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1332073272 113 PCVPVCPVQATfQREDGIVVVDNTRCVGCAYCVQACPYDArfI-----NHETQTADKCTFC 168
Cdd:PRK06991   63 PVIPLDPANGV-ERPRAVAVIDEQLCIGCTLCMQACPVDA--IvgapkQMHTVLADLCTGC 120
porD PRK09624
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
 114-160 2.31e-03

pyruvate ferredoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 170017 [Multi-domain]  Cd Length: 105  Bit Score: 36.55  E-value: 2.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1332073272 114 CVPVCPVQATFQREDGIVVVDNTRCVGCAYCVQACPYDARFINHETQ 160
Cdd:PRK09624   59 CYIYCPEPAIYLDEEGYPVFDYDYCKGCGICANECPTKAIEMVRETK 105
Fer4_9 pfam13187
4Fe-4S dicluster domain;
106-152 2.79e-03

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 34.84  E-value: 2.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1332073272 106 CNHCDNppCVPVCPVQATFQREDGIVVV---DNTRCVGCAYCVQACPYDA 152
Cdd:pfam13187   2 CTGCGA--CVAACPAGAIVPDLVGQTIRgdiAGLACIGCGACVDACPRGA 49
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
128-188 2.80e-03

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 38.69  E-value: 2.80e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1332073272 128 DGIV-VVDNTRCVGCAYCVQACPYDARFINhETQTAD----KCTFCvhrleaGllpACVESCVGGA 188
Cdd:COG1148   487 EPSVaEVDPEKCTGCGRCVEVCPYGAISID-EKGVAEvnpaLCKGC------G---TCAAACPSGA 542
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 137-188 2.92e-03

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: 35.49  E-value: 2.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1332073272 137 RCVGCAYCVQACPYDARFINHETQT------ADKCTFCVhrleagllpACVESCVGGA 188
Cdd:COG1143     3 KCIGCGLCVRVCPVDAITIEDGEPGkvyvidPDKCIGCG---------LCVEVCPTGA 51
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
137-184 6.36e-03

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 36.40  E-value: 6.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1332073272 137 RCVGCAYCVQACPYDArfINHETQTAD--------------KCTFCvhrleaGLlpaCVESC 184
Cdd:PRK05888   59 RCIACKLCAAICPADA--ITIEAAEREdgrrrttrydinfgRCIFC------GF---CEEAC 109
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 134-184 7.78e-03

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: 36.90  E-value: 7.78e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1332073272 134 DNTRCVGCAYCVQACPYDARFINHE---TQTADKCTFCvhrleaGLlpaCVESC 184
Cdd:COG2878   135 CEYGCIGCGDCIKACPFDAIVGAAKgmhTVDEDKCTGC------GL---CVEAC 179
 
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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