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Conserved domains on  [gi|486156319|ref|WP_001520059|]
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MULTISPECIES: tetrathionate reductase subunit TtrB [Salmonella]

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;
1-244 5.23e-178

tetrathionate reductase subunit TtrB;


:

Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 488.62  E-value: 5.23e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319   1 MDSSKRQFLQQLGVLTAGASLVPLAEAKFPFSPERHEGSPRHRYAMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQ 80
Cdd:PRK14993   1 MDSSKRQFLQQLGVLTAGASLVPLAEAKFPFSPERHEGSPRHRYAMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  81 YQVQREGSQEVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCT 160
Cdd:PRK14993  81 YQVQREGSQEVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319 161 FCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRISTLLHQHRDTIKVLKPENGTSPHVFYLGLDDAFVTPLMGRAQPAL 240
Cdd:PRK14993 161 FCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRIATMLHQHRDAIKVLKPENGTSPHVFYLGLDDAFVTPLMGRAQPAL 240


                 ....
gi 486156319 241 WQEV 244
Cdd:PRK14993 241 WQEV 244
 
Name Accession Description Interval E-value
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
1-244 5.23e-178

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 488.62  E-value: 5.23e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319   1 MDSSKRQFLQQLGVLTAGASLVPLAEAKFPFSPERHEGSPRHRYAMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQ 80
Cdd:PRK14993   1 MDSSKRQFLQQLGVLTAGASLVPLAEAKFPFSPERHEGSPRHRYAMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  81 YQVQREGSQEVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCT 160
Cdd:PRK14993  81 YQVQREGSQEVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319 161 FCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRISTLLHQHRDTIKVLKPENGTSPHVFYLGLDDAFVTPLMGRAQPAL 240
Cdd:PRK14993 161 FCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRIATMLHQHRDAIKVLKPENGTSPHVFYLGLDDAFVTPLMGRAQPAL 240


                 ....
gi 486156319 241 WQEV 244
Cdd:PRK14993 241 WQEV 244
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 46-222 9.36e-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: 275.57  E-value: 9.36e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  46 MLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQYQVqrEGSQEVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIV 125
Cdd:cd10551    1 MVIDLRKCIGCGACVVACKAENNVPPGVFRNRVLEYEV--GEYPNVKRTFLPVLCNHCENPPCVKVCPTGATYKREDGIV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319 126 VVDNKRCVGCAYCVQACPYDARFINHE------------TQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDIKDPHS 193
Cdd:cd10551   79 LVDYDKCIGCRYCMAACPYGARYFNPEephefgevpvrpKGVVEKCTFCYHRLDEGLLPACVEACPTGARIFGDLDDPNS 158

                        170       180
                 ....*....|....*....|....*....
gi 486156319 194 RISTLLHQHRdtIKVLKPENGTSPHVFYL 222
Cdd:cd10551  159 EVSKLLAERR--AYVLKPELGTKPKVYYI 185
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 42-226 2.65e-83

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 246.40  E-value: 2.65e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  42 HRYAMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQYQVQREGSQEVTNVllPRLCNHCDNPPCVPVCPVQATFQRE 121
Cdd:COG0437    4 KRYGMVIDLTKCIGCRACVVACKEENNLPVGVTWRRVRRYEEGEFPNVEWLFV--PVLCNHCDDPPCVKVCPTGATYKRE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319 122 DGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRISTLLHQ 201
Cdd:COG0437   82 DGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVEACPTGALVFGDLDDPESEVSKRLAE 161

                        170       180
                 ....*....|....*....|....*
gi 486156319 202 HRDtiKVLKPENGTSPHVFYLGLDD 226
Cdd:COG0437  162 LPA--YRLLPELGTKPSVYYLPKRN 184
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 96-187 1.73e-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: 121.59  E-value: 1.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319   96 LPRLCNHCDNPPCVPVCPVQATFQR-EDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPAC 174
Cdd:pfam13247   6 FPEQCRHCLNPPCKASCPVGAIYKDeETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAGLLPAC 85

                          90
                  ....*....|...
gi 486156319  175 VESCVGGARIIGD 187
Cdd:pfam13247  86 VQTCPTGAMNFGD 98
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 124-178 1.93e-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: 40.94  E-value: 1.93e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  124 IVVVDNKRCVGCAYCVQACPYDA-----RFINheTQTADKCTFCvhrleagllPACVESC 178
Cdd:TIGR01944 107 VALIDEDNCIGCTKCIQACPVDAivgaaKAMH--TVIADECTGC---------DLCVEPC 155
 
Name Accession Description Interval E-value
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
1-244 5.23e-178

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 488.62  E-value: 5.23e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319   1 MDSSKRQFLQQLGVLTAGASLVPLAEAKFPFSPERHEGSPRHRYAMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQ 80
Cdd:PRK14993   1 MDSSKRQFLQQLGVLTAGASLVPLAEAKFPFSPERHEGSPRHRYAMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  81 YQVQREGSQEVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCT 160
Cdd:PRK14993  81 YQVQREGSQEVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319 161 FCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRISTLLHQHRDTIKVLKPENGTSPHVFYLGLDDAFVTPLMGRAQPAL 240
Cdd:PRK14993 161 FCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRIATMLHQHRDAIKVLKPENGTSPHVFYLGLDDAFVTPLMGRAQPAL 240


                 ....
gi 486156319 241 WQEV 244
Cdd:PRK14993 241 WQEV 244
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 46-222 9.36e-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: 275.57  E-value: 9.36e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  46 MLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQYQVqrEGSQEVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIV 125
Cdd:cd10551    1 MVIDLRKCIGCGACVVACKAENNVPPGVFRNRVLEYEV--GEYPNVKRTFLPVLCNHCENPPCVKVCPTGATYKREDGIV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319 126 VVDNKRCVGCAYCVQACPYDARFINHE------------TQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDIKDPHS 193
Cdd:cd10551   79 LVDYDKCIGCRYCMAACPYGARYFNPEephefgevpvrpKGVVEKCTFCYHRLDEGLLPACVEACPTGARIFGDLDDPNS 158

                        170       180
                 ....*....|....*....|....*....
gi 486156319 194 RISTLLHQHRdtIKVLKPENGTSPHVFYL 222
Cdd:cd10551  159 EVSKLLAERR--AYVLKPELGTKPKVYYI 185
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 42-226 2.65e-83

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 246.40  E-value: 2.65e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  42 HRYAMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQYQVQREGSQEVTNVllPRLCNHCDNPPCVPVCPVQATFQRE 121
Cdd:COG0437    4 KRYGMVIDLTKCIGCRACVVACKEENNLPVGVTWRRVRRYEEGEFPNVEWLFV--PVLCNHCDDPPCVKVCPTGATYKRE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319 122 DGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRISTLLHQ 201
Cdd:COG0437   82 DGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVEACPTGALVFGDLDDPESEVSKRLAE 161

                        170       180
                 ....*....|....*....|....*
gi 486156319 202 HRDtiKVLKPENGTSPHVFYLGLDD 226
Cdd:COG0437  162 LPA--YRLLPELGTKPSVYYLPKRN 184
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 47-182 9.67e-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: 169.67  E-value: 9.67e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  47 LIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQYQVQREGSQEVTNVLLPrlCNHCDNPPCVPVCPVQATFQREDGIVV 126
Cdd:cd16371    3 YFDQERCIGCKACEIACKDKNDLPPGVNWRRVYEYEGGEFPEVFAYFLSMS--CNHCENPACVKVCPTGAITKREDGIVV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 486156319 127 VDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGA 182
Cdd:cd16371   81 VDQDKCIGCGYCVWACPYGAPQYNPETGKMDKCDMCVDRLDEGEKPACVAACPTRA 136
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 40-221 2.81e-48

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: 161.32  E-value: 2.81e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  40 PRHRYAMLIDLRRCIGCQSCTVSC----TIENQTPQ----------------------GAFRT----------TVNQY-- 81
Cdd:cd10555    1 SKRQLAMVMDLNKCIGCQTCTVACktlwTNRNGREYmywnnvetqpgkgypknwekkgGGFKDkgelkpgiipTLEDYgv 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  82 ----------------QVQREGSQEVT---------------NVL---LPRLCNHCDNPPCVPVCPVQATFQR-EDGIVV 126
Cdd:cd10555   81 pweynheeelfegkggRVRPSPKGDPTwgpnwdedqgageypNSYyfyLPRICNHCTNPACLAACPRKAIYKReEDGIVL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319 127 VDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRISTLLHQHrdti 206
Cdd:cd10555  161 VDQDRCRGYRYCVEACPYKKIYFNPVEQKSEKCIFCYPRIEKGVAPACARQCVGRIRFVGYLDDEESPVYKLVKKW---- 236

                        250
                 ....*....|....*...
gi 486156319 207 KV---LKPENGTSPHVFY 221
Cdd:cd10555  237 KValpLHPEYGTEPNVFY 254
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 46-186 1.72e-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: 153.70  E-value: 1.72e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  46 MLIDLRRCIGCQSCTVSCTIENQTPQGAFRTtvnqyQVQREGSQEVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIV 125
Cdd:cd04410    1 LVVDLDRCIGCGTCEVACKQEHGLRPGPDWS-----RIKVIEGGGLERAFLPVSCMHCEDPPCVKACPTGAIYKDEDGIV 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 486156319 126 VVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIG 186
Cdd:cd04410   76 LIDEDKCIGCGSCVEACPYGAIVFDPEPGKAVKCDLCGDRLDEGLEPACVKACPTGALTFG 136
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 46-225 5.42e-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: 151.71  E-value: 5.42e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  46 MLIDLRRCIGCQSCTVSCTIEN-----------QTPQGAFRTTVNQyQVQREGSQeVTNVLLPRLCNHCDNPPCVPVCPV 114
Cdd:cd10552    1 LVIDVAKCNGCYNCFLACKDEHvgndwpgyaapQPRHGHFWMRILR-RERGQYPK-VDVAYLPVPCNHCDNAPCIKAAKD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319 115 QATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAG-LLPACVESCVGGARIIGDIKDPHS 193
Cdd:cd10552   79 GAVYKRDDGIVIIDPEKAKGQKQLVDACPYGAIYWNEELQVPQKCTFCAHLLDDGwKEPRCVQACPTGALRFGKLEDEEM 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 486156319 194 RISTLlhqhRDTIKVLKPENGTSPHVFYLGLD 225
Cdd:cd10552  159 AAKAA----EEGLEVLHPELGTKPRVYYKNLP 186
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 45-195 8.28e-42

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: 141.20  E-value: 8.28e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  45 AMLIDLRRCIGCQSCTVSCTIENQTP--QGAF--------------RTTVNQYQVQREGSQEVTnvlLPRLCNHCDNPPC 108
Cdd:cd10561    1 GVLYDTTRCIGCRACEVACKEWNGLPaeDTAFgpgwdnprdlsaktYTVIKRYEVETGGKGFVF---VKRQCMHCLDPAC 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319 109 VPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDA-RFinhETQTAD----KCTFCVHRLEAGLLPACVESCVGGAR 183
Cdd:cd10561   78 VSACPVGALRKTPEGPVTYDEDKCIGCRYCMVACPFNIpKY---EWDSANpkirKCTMCYDRLKEGKQPACVEACPTGAL 154

                        170
                 ....*....|....*.
gi 486156319 184 IIGD----IKDPHSRI 195
Cdd:cd10561  155 LFGKreelLAEAKRRI 170
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 43-222 3.94e-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: 136.94  E-value: 3.94e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  43 RYAMLIDLRRCIGCQSCTVSC----------------TIENQtPQGAFRTTvnqYQVQREGSQEVTNVL--LPRLCNHCD 104
Cdd:cd16365    2 QFAAVFNLNKCIGCQTCTVACknawtyrkgqeymwwnNVETK-PGGGYPQD---WEVKTIDNGGNTRFFfyLQRLCNHCT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319 105 NPPCVPVCPVQATFQR-EDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGAR 183
Cdd:cd16365   78 NPACLAACPRGAIYKReEDGIVLIDQKRCRGYRKCVEQCPYKKIYFNGLSRVSEKCIACYPRIEGGDPTRCMSACVGRIR 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 486156319 184 IIGDIKD-PHSRISTLLHQHRDTIKvLKPENGTSPHVFYL 222
Cdd:cd16365  158 LQGFLDDnPKSPVTKLIRHWKVALP-LHPEYGTEPNIYYV 196
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 46-182 9.48e-39

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: 9.48e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  46 MLIDLRRCIGCQSCTVSC---------------TIENQTPQGAFRTTVNQYQVQREGSQEVTNVLLPRLCNHCDNPPCVP 110
Cdd:cd16366    1 FLVDTSRCTGCRACQVACkqwnglpaekteftgSYQNPPDLTAHTWTLVRFYEVEKPGGDLSWLFRKDQCMHCTDAGCLA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 486156319 111 VCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGA 182
Cdd:cd16366   81 ACPTGAIIRTETGTVVVDPETCIGCGYCVNACPFDIPRFDEETGRVAKCTLCYDRISNGLQPACVKTCPTGA 152
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 46-187 6.53e-38

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: 130.12  E-value: 6.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  46 MLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTvNQYQVQREGSQEVTNVL----------------LPRLCNHCDNPPCV 109
Cdd:cd10562    1 MLVDTSKCTACRGCQVACKQWNQLPAEKTPFT-GSYQNPPDLTPNTWTLIrfyeheednggirwlfRKRQCMHCTDAACV 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 486156319 110 PVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGD 187
Cdd:cd10562   80 KVCPTGALYKTENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCFDRIENGMQPACVKTCPTGALTFGD 157
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 29-222 4.05e-37

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: 131.81  E-value: 4.05e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  29 FPFSPERhegsPRHRYAMLIDLRRCIGCQSCTVSC----------------------------------TIENQTPQGA- 73
Cdd:cd10556    1 YPYEESR----PDKQFAMVFDTNKCIACQTCTMACkstwtsgkgqeymwwnnvetkpyggyplgwdvrlLDEEGGQTWAe 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  74 ----------------------------------FRTTVNQYQVQREGSQEVTNVL----LPRLCNHCDNPPCVPVCPVQ 115
Cdd:cd10556   77 ggvyegktifeaaaageqvlgyrpededwrypniGEDEVNGERTPDTGSSLPPHPIwffyLPRICNHCTYPACLAACPRK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319 116 ATFQR-EDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDIKDP--- 191
Cdd:cd10556  157 AIYKReEDGIVLIDQERCRGYRECVEACPYKKPMYNPTTRVSEKCIGCYPRIEEGDQTQCVSACIGKIRLQGFINTPpda 236

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 486156319 192 -----HSRISTLLHQHRDTIKVLKPENGTSPHVFYL 222
Cdd:cd10556  237 rwaddRDNPIDFLVHIKKVALPLYPQFGTEPNVYYI 272
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 96-186 6.35e-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: 132.87  E-value: 6.35e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  96 LPRLCNHCDNPPCVPVCPVQATFQR-EDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPAC 174
Cdd:cd10557  175 LPRICNHCLNPACVAACPSGAIYKReEDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSEKCIFCYPRLEAGQPTVC 254

                         90
                 ....*....|..
gi 486156319 175 VESCVGGARIIG 186
Cdd:cd10557  255 SETCVGRIRYLG 266
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 43-182 1.74e-36

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: 125.94  E-value: 1.74e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  43 RYAMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTV-NQYQVQREGSQEVTNVLLPrlCNHCDNPPCVPVCPVQATFQRE 121
Cdd:cd10553    2 KYYLYHDSKRCIGCLACEVHCKVKNNLPVGPRLCRIfAVGPKMVGGKPRLKFVYMS--CFHCENPWCVKACPTGAMQKRE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 486156319 122 -DGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGA 182
Cdd:cd10553   80 kDGIVYVDQELCIGCKACIEACPWGIPQWNPATGKVVKCDYCMDRIDQGLKPACVTGCTTHA 141
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 96-187 1.73e-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: 121.59  E-value: 1.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319   96 LPRLCNHCDNPPCVPVCPVQATFQR-EDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPAC 174
Cdd:pfam13247   6 FPEQCRHCLNPPCKASCPVGAIYKDeETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAGLLPAC 85

                          90
                  ....*....|...
gi 486156319  175 VESCVGGARIIGD 187
Cdd:pfam13247  86 VQTCPTGAMNFGD 98
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 96-186 1.77e-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: 1.77e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  96 LPRLCNHCDNPPCVPVCPVQATFQR-EDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPAC 174
Cdd:COG1140  178 LPRICEHCLNPACVASCPSGAIYKReEDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGKAEKCIFCYPRIEAGQPTVC 257

                         90
                 ....*....|..
gi 486156319 175 VESCVGGARIIG 186
Cdd:COG1140  258 SETCVGRIRYLG 269
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 47-190 3.02e-34

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: 119.69  E-value: 3.02e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  47 LIDLRRCIGCQSCTVSCTIENQtpqGAFRTTVnqYQVQregsqEVTNVllPRLCNHCDNPPCVPVCPVQATFQREDGIVV 126
Cdd:cd16374    2 YVDPERCIGCRACEIACAREHS---GKPRISV--EVVE-----DLASV--PVRCRHCEDAPCMEVCPTGAIYRDEDGAVL 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 486156319 127 VDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDIKD 190
Cdd:cd16374   70 VDPDKCIGCGMCAMACPFGVPRFDPSLKVAVKCDLCIDRRREGKLPACVEACPTGALKFGDIEE 133
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 45-226 1.67e-32

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: 117.87  E-value: 1.67e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  45 AMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQYQ---------------VQREGSQEVTN-------VLLPRLCNH 102
Cdd:cd10560    1 GFFTDTSICIGCKACEVACKQWNQLPADGYDFSGMSYDntgdlsastwrhvkfIERPTEDGPANeggdlqwLFMSDVCKH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319 103 CDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGA 182
Cdd:cd10560   81 CTDAGCLEACPTGAIFRTEFGTVYIQPDICNGCGYCVAACPFGVIDRNEETGRAHKCTLCYDRLKDGLEPACAKACPTGS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 486156319 183 RIIGDIKDphsristLLHQHRDTIKVLKpENGTSP---------------HVFYLGLDD 226
Cdd:cd10560  161 IQFGPLEE-------LRERARARVEQLH-EQGVVEaylygadptegygglNAFFLLLDK 211
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 45-190 1.71e-31

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: 114.79  E-value: 1.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  45 AMLIDLRRCIGCQSCTVSCTIENQTPqGAFRTTVNQYQVQREGSQEVTNVL---------------LPRLCNHCDNPPCV 109
Cdd:cd10558    1 AKLIDVSKCIGCKACQVACKEWNDLR-AEVGHNVGTYQNPADLSPETWTLMkfrevedngklewliRKDGCMHCADPGCL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319 110 PVCPVQ-ATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDI 188
Cdd:cd10558   80 KACPSPgAIVQYANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVGLEPACVKTCPTGALHFGTK 159


                 ..
gi 486156319 189 KD 190
Cdd:cd10558  160 ED 161
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 46-182 4.57e-28

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: 103.43  E-value: 4.57e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  46 MLIDLRRCIGCQSCTVSCTIENQtpqGAFRTTVNQYQVQREGSQEVTNvllPRLCNHCDNPPCVPVCPVQA-TFQREDGI 124
Cdd:cd10550    1 LVVDPEKCTGCRTCELACSLKHE---GVFNPSLSRIRVVRFEPEGLDV---PVVCRQCEDAPCVEACPVGAiSRDEETGA 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 486156319 125 VVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCvhrleaGLLPACVESCVGGA 182
Cdd:cd10550   75 VVVDEDKCIGCGMCVEACPFGAIRVDPETGKAIKCDLC------GGDPACVKVCPTGA 126
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
4-190 4.46e-27

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 106.29  E-value: 4.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319   4 SKRQFLQQLGVLTAGASLVPLAeakfpfSPERHEGSPRHRYA--MLIDLRRCIGCQSCTVSC-----TIENQTPQGAFRT 76
Cdd:PRK10882   2 NRRNFLKAASAGALLAGALPSV------SHAAAENRPPIPGAlgMLYDSTLCVGCQACVTKCqeinfPERNPQGEQTWDN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  77 -------TVNQYQVQREGSQEVTNVL------LPRLCNHCDNPPCVPVCPVQA-TFQREDGIVVVDNKRCVGCAYCVQAC 142
Cdd:PRK10882  76 pdklspyTNNIIKVWKSGTGVNKDQEengyayIKKQCMHCVDPNCVSVCPVSAlTKDPKTGIVHYDKDVCTGCRYCMVAC 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 486156319 143 PYDARFINHETQTAD--KCTFCVH----RLEAGLLPACVESCVGGARIIGDIKD 190
Cdd:PRK10882 156 PFNVPKYDYNNPFGAihKCELCNQkgveRLDKGGLPGCVEVCPTGAVIFGTREE 209
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 47-182 7.57e-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: 95.40  E-value: 7.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  47 LIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQYQVQREGSQEVTN-VLLPRLCNHCDNPPCVPVCPVQA-TFQREDGI 124
Cdd:cd10563    3 FIDEEKCLGCKLCEVACAVAHSKSKDLIKAKLEKERPRPRIRVEESGgRSFPLQCRHCDEPPCVKACMSGAmHKDPETGI 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 486156319 125 VVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEagllPACVESCVGGA 182
Cdd:cd10563   83 VIHDEEKCVGCWMCVMVCPYGAIRPDKERKVALKCDLCPDRET----PACVEACPTGA 136
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 44-187 5.92e-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: 94.38  E-value: 5.92e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  44 YAMLIDLRRCIGCQSCTVSCTiENQTPQGAFRTTVnqYQVQREGSQEVTnvllPRLCNHCDNPPCVPVCPVQATFQREDG 123
Cdd:cd16369    2 KEFFIDPSRCIGCRACVAACR-ECGTHRGKSMIHV--DYIDRGESTQTA----PTVCMHCEDPTCAEVCPADAIKVTEDG 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 486156319 124 IVVVDNK-RCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGD 187
Cdd:cd16369   75 VVQSALKpRCIGCSNCVNACPFGVPKYDEERNLMMKCDMCYDRTSVGKAPMCASVCPSGALFYGT 139
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 49-178 1.47e-23

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: 92.32  E-value: 1.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  49 DLRRCIGCQSCTVSCTienqtpqgafrttVNQYQVQREGSQEVTNVLLPRL-------------CNHCDNPPCVPVCPVQ 115
Cdd:cd10554    5 DPDKCIGCRTCEVACA-------------AAHSGKGIFEAGTDGLPFLPRLrvvktgevtapvqCRQCEDAPCANVCPVG 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 486156319 116 ATFQrEDGIVVVDNKRCVGCAYCVQACPYDA-----------RFINHETQTADKCTFCVHRLEAgllPACVESC 178
Cdd:cd10554   72 AISQ-EDGVVQVDEERCIGCKLCVLACPFGAiemapttvpgvDWERGPRAVAVKCDLCAGREGG---PACVEAC 141
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
47-178 2.38e-23

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 91.64  E-value: 2.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  47 LIDLRRCIGCQSCTVSCTIENQTPQGafrtTVNQYQVQREGSQEVTNvllPRLCNHCDNPPCVPVCPVQAtFQREDGIVV 126
Cdd:COG1142    6 IADPEKCIGCRTCEAACAVAHEGEEG----EPFLPRIRVVRKAGVSA---PVQCRHCEDAPCAEVCPVGA-ITRDDGAVV 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 486156319 127 VDNKRCVGCAYCVQACPYDARFINHETQ--TADKCTFCVHRLEaglLPACVESC 178
Cdd:COG1142   78 VDEEKCIGCGLCVLACPFGAITMVGEKSraVAVKCDLCGGREG---GPACVEAC 128
PRK09898 PRK09898
ferredoxin-like protein;
52-190 5.15e-23

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 92.59  E-value: 5.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  52 RCIGCQSCTVSCTIENQTPQGAFRTTVNQYQVQREGSQEVTN--------VLLPRLCNHCDNPPCVPVCPVQA-TFQRED 122
Cdd:PRK09898  67 RCTGCHRCEISCTNFNDGSVGTFFSRIKIHRNYFFGDNGVGSggglygdlNYTADTCRQCKEPQCMNVCPIGAiTWQQKE 146

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 486156319 123 GIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCvhrleagllPACVESCVGGARIIGDIKD 190
Cdd:PRK09898 147 GCITVDHKRCIGCSACTTACPWMMATVNTESKKSSKCVLC---------GECANACPTGALKIIEWKD 205
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 44-190 4.23e-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: 87.48  E-value: 4.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  44 YAMLIDLRRCIGCQ-----SCTVSCTIENQ--TPQGAF-----------------------RTT------VNQYQVQREG 87
Cdd:cd16368    1 LATLIDLTKCDGCPgesipACVRACREKNQarFPEPVSkpiqpywprkriedwsdkrdvtdRLTpynwlyVQKLTVDTAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  88 SQEVtnVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYD--AR------FINHETQTAD-- 157
Cdd:cd16368   81 GEKE--VFIPRRCMHCDNPPCAKLCPFGAARKTPEGAVYIDDDLCFGGAKCRDVCPWHipQRqagvgiYLHLAPEYAGgg 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 486156319 158 ---KCTFCVHRLEAGLLPACVESCVGGARIIGDIKD 190
Cdd:cd16368  159 vmyKCDLCKDLLAQGKPPACIEACPKGAQYFGPRKE 194
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 45-190 5.45e-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: 84.41  E-value: 5.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  45 AMLIDLRRCIGCQSCTVSCTIENQTP--QGAFRTT--------VNQYQVQREGSQEVTN-----VLLPRLCNHCDNPPCV 109
Cdd:cd10559    1 SFLIDTTRCTACRGCQVACKQWNQLPaeQTKNTGShqnppdlsANTYKLVRFNEVRNENgkpdwLFFPDQCRHCVTPPCK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319 110 PVCPVQ--ATFQRED-GIVVVDNKRCVGCAYCV-QACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARII 185
Cdd:cd10559   81 DAADMVpgAVIQDEAtGAVVFTEKTAELDFDDVlSACPYNIPRKNEATGRIVKCDMCIDRVSNGLQPACVKACPTGAMNF 160


                 ....*
gi 486156319 186 GDIKD 190
Cdd:cd10559  161 GDRDE 165
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 37-184 1.06e-19

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: 81.97  E-value: 1.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  37 EGSPRHRYAMLIDLRRCIGCQSCTVSCTienQTPQGAFRttvnqyqVQREGSQeVTNVLLPRLCNHCDNPPCVPVCPVQA 116
Cdd:cd16367    5 YGLIQGTNLLVIDLDRCIRCDNCEKACA---DTHDGHSR-------LDRNGLR-FGNLLVPTACRHCVDPVCMIGCPTGA 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 486156319 117 TFQREDGIVVVDNKrCVGCAYCVQACPYDARFInhetQTADKCTFCVHRLEagllPACVESCVGGARI 184
Cdd:cd16367   74 IHRDDGGEVVISDA-CCGCGNCASACPYGAIQM----VRAVKCDLCAGYAG----PACVSACPTGAAI 132
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 49-178 1.46e-19

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 87.11  E-value: 1.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  49 DLRRCIGCQSCTVSCTI---ENQTP--QGAF--RTTVNQYQVQREGsqeVTnvllprlCNHCDNPPCVPVCPVQATFQRE 121
Cdd:PRK12769   8 NSQQCLGCHACEIACVMahnDEQHVlsQHHFhpRITVIKHQQQRSA---VT-------CHHCEDAPCARSCPNGAISHVD 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 486156319 122 DGIVVVDNKrCVGCAYCVQACPYDARFI-------NHETQTADKCTFCVHRlEAGllPACVESC 178
Cdd:PRK12769  78 DSIQVNQQK-CIGCKSCVVACPFGTMQIvltpvaaGKVKATAHKCDLCAGR-ENG--PACVENC 137
PRK10330 PRK10330
electron transport protein HydN;
46-178 2.35e-18

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 79.55  E-value: 2.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  46 MLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQYQVQREGSQEVtNVLLPRLCNHCDNPPCVPVCPVQAtFQREDGIV 125
Cdd:PRK10330   5 IIADASKCIGCRTCEVACVVSHQENQDCASLTPETFLPRIHVIKGV-NVSTATVCRQCEDAPCANVCPNGA-ISRDKGFV 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 486156319 126 VVDNKRCVGCAYCVQACPYDARFI---------------NHETQTADKCTFCVHRlEAGllPACVESC 178
Cdd:PRK10330  83 HVMQERCIGCKTCVVACPYGAMEVvvrpvirnsgaglnvRAEKAEANKCDLCNHR-EDG--PACMAAC 147
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 48-162 2.39e-17

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: 75.77  E-value: 2.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  48 IDLRRCIGCQSCTVSCTIENQtpqGAFRTTVNQYQVQREGSQEvtNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVV 127
Cdd:cd16370    6 KDMERCIGCYSCMLACSRRVH---KSASLSKSAIRVRTRGGLE--GGFTVVVCRACEDPPCAEACPTGALEPRKGGGVVL 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 486156319 128 DNKRCVGCAYCVQACPYDARFINHETQTADKCTFC 162
Cdd:cd16370   81 DKEKCIGCGNCVKACIVGAIFWDEETNKPIICIHC 115
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 49-178 8.22e-17

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 79.30  E-value: 8.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  49 DLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQYQVQREGSQEVTNvllPRLCNHCDNPPCVPVCPVQA-TFQREDgiVVV 127
Cdd:PRK12809   8 EAAECIGCHACEIACAVAHNQENWPLSHSDFRPRIHVVGKGQAAN---PVACHHCNNAPCVTACPVNAlTFQSDS--VQL 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 486156319 128 DNKRCVGCAYCVQACPYDArfINHETQTADKCTFCVHRLEAglLPACVESC 178
Cdd:PRK12809  83 DEQKCIGCKRCAIACPFGV--VEMVDTIAQKCDLCNQRSSG--TQACIEVC 129
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 51-182 3.17e-14

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: 66.98  E-value: 3.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  51 RRCIGCQSCTVSCTI----ENQTPQGAFRTTvnqyqvqregsqEVTNVLLPRLCNHCDNppCVPVCPVQATFQREDGIVV 126
Cdd:cd16372    8 EKCIGCLQCEEACSKtffkEEDREKSCIRIT------------ETEGGYAINVCNQCGE--CIDVCPTGAITRDANGVVM 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 486156319 127 VDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCvhrleagllPACVESCVGGA 182
Cdd:cd16372   74 INKKLCVGCLMCVGFCPEGAMFKHEDYPEPFKCIAC---------GICVKACPTGA 120
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 48-146 5.50e-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: 55.87  E-value: 5.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  48 IDLRRCIGCQSCTVSCtienqtPQGAFR-TTVNQYQVQREGSQEVTNvllpRLCNHCDNppCVPVCPVQATFQREDGIVV 126
Cdd:cd10549   37 IDEDKCVFCGACVEVC------PTGAIElTPEGKEYVPKEKEAEIDE----EKCIGCGL--CVKVCPVDAITLEDELEIV 104

                         90       100
                 ....*....|....*....|
gi 486156319 127 VDNKRCVGCAYCVQACPYDA 146
Cdd:cd10549  105 IDKEKCIGCGICAEVCPVNA 124
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
97-153 1.16e-09

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 53.20  E-value: 1.16e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 486156319  97 PRLCNHCDNppCVPVCPVQAtFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHET 153
Cdd:COG2768   10 EEKCIGCGA--CVKVCPVGA-ISIEDGKAVIDPEKCIGCGACIEVCPVGAIKIEWEE 63
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 100-146 1.24e-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: 50.82  E-value: 1.24e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 486156319 100 CNHCDNppCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDA 146
Cdd:COG1144   32 CIGCGL--CWIVCPDGAIRVDDGKYYGIDYDYCKGCGICAEVCPVKA 76
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 99-151 1.63e-08

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 50.05  E-value: 1.63e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 486156319  99 LCNHCDNppCVPVCPVQAtFQREDGIVVVDNKRCVGCAYCVQACPYDARFINH 151
Cdd:COG2221   16 KCIGCGL--CVAVCPTGA-ISLDDGKLVIDEEKCIGCGACIRVCPTGAIKGEK 65
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 97-146 1.01e-07

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 48.12  E-value: 1.01e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 486156319  97 PRLCNHCDNppCVPVCPVQAtFQREDGIVVVDNKRCVGCAYCVQACPYDA 146
Cdd:COG4231   21 EDKCTGCGA--CVKVCPADA-IEEGDGKAVIDPDLCIGCGSCVQVCPVDA 67
NapF COG1145
Ferredoxin [Energy production and conversion];
100-157 1.29e-07

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 50.88  E-value: 1.29e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 486156319 100 CNHCDNppCVPVCPVQA-TFQREDGIVVVDNKRCVGCAYCVQACPYDArfINHETQTAD 157
Cdd:COG1145  184 CIGCGL--CVKVCPTGAiRLKDGKPQIVVDPDKCIGCGACVKVCPVGA--ISLEPKEIE 238
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 97-146 1.33e-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: 1.33e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 486156319  97 PRLCNHCDNppCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDA 146
Cdd:COG1149   10 EEKCIGCGL--CVEVCPEGAIKLDDGGAPVVDPDLCTGCGACVGVCPTGA 57
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 100-146 2.57e-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: 46.66  E-value: 2.57e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 486156319 100 CNHCDNppCVPVCPVQA---TFQREDGIVVVDNKRCVGCAYCVQACPYDA 146
Cdd:COG1143    4 CIGCGL--CVRVCPVDAitiEDGEPGKVYVIDPDKCIGCGLCVEVCPTGA 51
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
97-165 1.66e-06

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 48.27  E-value: 1.66e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 486156319  97 PRLCNHcdnpPCVPVCPVQAT------FQREDGIVVVDNKRCVGCAYCVQACPYDA-RFINHETQTADKctfCVHR 165
Cdd:PRK13409  14 PKKCNY----ECIKYCPVVRTgeetieIDEDDGKPVISEELCIGCGICVKKCPFDAiSIVNLPEELEEE---PVHR 82
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 97-146 2.46e-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: 47.86  E-value: 2.46e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 486156319  97 PRLCNHcdnpPCVPVCPVQAT------FQREDGIVVVDNKRCVGCAYCVQACPYDA 146
Cdd:COG1245   14 PKKCNY----ECIKYCPVNRTgkeaieIDEDDGKPVISEELCIGCGICVKKCPFDA 65
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
93-191 5.90e-06

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 46.56  E-value: 5.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  93 NVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQT--ADKCTFCvhrleaGl 170
Cdd:COG4624   54 CCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCYPCVRACPVKAIKVDDGKAEidEEKCISC------G- 126

                         90       100
                 ....*....|....*....|....*....
gi 486156319 171 lpACVESCVGGA--------RIIGDIKDP 191
Cdd:COG4624  127 --QCVAVCPFGAiteksdieKVKKALKDP 153
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
97-146 6.50e-06

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 46.78  E-value: 6.50e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 486156319  97 PRLCNHCDNppCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDA 146
Cdd:COG1148  495 PEKCTGCGR--CVEVCPYGAISIDEKGVAEVNPALCKGCGTCAAACPSGA 542
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 100-146 7.14e-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: 42.13  E-value: 7.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 486156319  100 CNHCDNppCVPVCPVQATFQREDG------IVVVDNKRCVGCAYCVQACPYDA 146
Cdd:pfam12838   1 CIGCGA--CVAACPVGAITLDEVGekkgtkTVVIDPERCVGCGACVAVCPTGA 51
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 50-179 7.39e-06

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: 44.55  E-value: 7.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  50 LRRCIGCQSCTVSCtienqtPQGAFRTTVNQYqvqregsqEVTNVLLPRL------CNHCDNPpCVPVCPVQA----TFQ 119
Cdd:cd16373   13 LALCIRCGLCVEAC------PTGVIQPAGLED--------GLEGGRTPYLdpregpCDLCCDA-CVEVCPTGAlrplDLE 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 486156319 120 RED---GIVVVDNKRCV------GCAYCVQACPYDARFINHETQT------ADKCTFCvhrleaGllpACVESCV 179
Cdd:cd16373   78 EQKvkmGVAVIDKDRCLawqggtDCGVCVEACPTEAIAIVLEDDVlrpvvdEDKCVGC------G---LCEYVCP 143
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
100-146 1.35e-05

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 45.05  E-value: 1.35e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 486156319 100 CNHCDNppCVPVCPVqatfqredGIVV----VDNKRCVGCAYCVQACPYDA 146
Cdd:COG0348  212 CIDCGL--CVKVCPM--------GIDIrkgeINQSECINCGRCIDACPKDA 252
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
108-178 1.77e-05

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 44.67  E-value: 1.77e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 486156319 108 CVPVCPV---QATFQREDGIVV-VDNKRCVGCAYCVQACPYDArFINHETQTADKCTFCvhrleaGllpACVESC 178
Cdd:COG0348  184 CRYLCPYgafQGLLSDLSTLRVrYDRGDCIDCGLCVKVCPMGI-DIRKGEINQSECINC------G---RCIDAC 248
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 108-143 2.54e-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: 44.21  E-value: 2.54e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 486156319 108 CVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACP 143
Cdd:COG2878  145 CIKACPFDAIVGAAKGMHTVDEDKCTGCGLCVEACP 180
NapF COG1145
Ferredoxin [Energy production and conversion];
94-178 3.78e-05

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 43.56  E-value: 3.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  94 VLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDA-RFINHETQT---ADKCTFCvhrleag 169
Cdd:COG1145  146 ILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVCPTGAiRLKDGKPQIvvdPDKCIGC------- 218


                 ....*....
gi 486156319 170 llPACVESC 178
Cdd:COG1145  219 --GACVKVC 225
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
120-191 5.21e-05

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 40.48  E-value: 5.21e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 486156319 120 REDGIVVVDNKRCVGCAYCVQACPYDArfINHETQTA----DKCTFCvhrleagllPACVESCVGGARIIGDIKDP 191
Cdd:COG2768    1 HSLGKPYVDEEKCIGCGACVKVCPVGA--ISIEDGKAvidpEKCIGC---------GACIEVCPVGAIKIEWEEDE 65
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
108-145 5.27e-05

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 43.38  E-value: 5.27e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 486156319 108 CVPVCPVQAtFQREDGIVVVDNKRCVGCAYCVQACPYD 145
Cdd:PRK07118 147 CVAACPFDA-IHIENGLPVVDEDKCTGCGACVKACPRN 183
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
108-146 6.06e-05

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 41.09  E-value: 6.06e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 486156319 108 CVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDA 146
Cdd:PRK09623  59 CWKFCPEPAIYIKEDGYVAIDYDYCKGCGICANECPTKA 97
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 94-146 8.21e-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: 41.23  E-value: 8.21e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 486156319  94 VLLPRLCNHCDNppCVPVCPVQA-TFQREDGIV---VVDNKRCVGCAYCVQACPYDA 146
Cdd:cd10549    2 KYDPEKCIGCGI--CVKACPTDAiELGPNGAIArgpEIDEDKCVFCGACVEVCPTGA 56
porD PRK09625
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
 99-143 1.39e-04

pyruvate flavodoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 236596 [Multi-domain]  Cd Length: 133  Bit Score: 40.50  E-value: 1.39e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 486156319  99 LCNHCDNppCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACP 143
Cdd:PRK09625  60 ICINCFN--CWVYCPDAAILSRDKKLKGVDYSHCKGCGVCVEVCP 102
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 124-178 1.93e-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: 40.94  E-value: 1.93e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  124 IVVVDNKRCVGCAYCVQACPYDA-----RFINheTQTADKCTFCvhrleagllPACVESC 178
Cdd:TIGR01944 107 VALIDEDNCIGCTKCIQACPVDAivgaaKAMH--TVIADECTGC---------DLCVEPC 155
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 94-143 2.00e-04

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: 38.39  E-value: 2.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 486156319   94 VLLPRLCNHCDNppCVPVCPVQATFQR------EDGIVVVDNKRCVGCAYCVQACP 143
Cdd:pfam13237   3 VIDPDKCIGCGR--CTAACPAGLTRVGaiverlEGEAVRIGVWKCIGCGACVEACP 56
NapF COG1145
Ferredoxin [Energy production and conversion];
12-116 2.45e-04

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 41.25  E-value: 2.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  12 LGVLTAGASLVPLAEAKFPFSPERHEGSPRHRYAMLIDLRRCIGCQSCTVSCtienqtPQGAFRTTVNQYQVqregsqev 91
Cdd:COG1145  143 GLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVC------PTGAIRLKDGKPQI-------- 208

                         90       100
                 ....*....|....*....|....*
gi 486156319  92 tnVLLPRLCNHCDNppCVPVCPVQA 116
Cdd:COG1145  209 --VVDPDKCIGCGA--CVKVCPVGA 229
PRK13795 PRK13795
hypothetical protein; Provisional
 99-155 3.08e-04

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 41.52  E-value: 3.08e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 486156319  99 LCNHCDnpPCVPVCPVQAtFQREDG--IVVVDNKRCVGCAYCVQACPYdARFINHETQT 155
Cdd:PRK13795 582 ECVGCG--VCVGACPTGA-IRIEEGkrKISVDEEKCIHCGKCTEVCPV-VKYKDKRNGS 636
PRK13795 PRK13795
hypothetical protein; Provisional
 131-179 3.59e-04

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 41.52  E-value: 3.59e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 486156319 131 RCVGCAYCVQACPYDARFINHETQT----ADKCTFCVhrleagllpACVESCV 179
Cdd:PRK13795 582 ECVGCGVCVGACPTGAIRIEEGKRKisvdEEKCIHCG---------KCTEVCP 625
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 99-143 5.28e-04

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 40.63  E-value: 5.28e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 486156319  99 LCNHCDNppCVPVCPVQATFQ-REDGIVVVDNKRCVGCAYCVQACP 143
Cdd:PRK12771 511 NCFECDN--CYGACPQDAIIKlGPGRRYHFDYDKCTGCHICADVCP 554
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
108-157 6.02e-04

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 39.48  E-value: 6.02e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 486156319 108 CVPVCPVQA----TFQREDGIVVVDNK-----RCVGCAYCVQACPYDA-----RFINHETQTAD 157
Cdd:PRK05888  66 CAAICPADAitieAAEREDGRRRTTRYdinfgRCIFCGFCEEACPTDAivetpDFELATETREE 129
PRK06991 PRK06991
electron transport complex subunit RsxB;
24-114 6.05e-04

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 40.16  E-value: 6.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319  24 LAEAKFPFSPERheGSPRHRYAMLIDLRRCIGCQSCTVSCtienqtPQGAFrttvnqyqvqrEGSQEVTNVLLPRLCNHC 103
Cdd:PRK06991  60 LGKPVIPLDPAN--GVERPRAVAVIDEQLCIGCTLCMQAC------PVDAI-----------VGAPKQMHTVLADLCTGC 120

                         90
                 ....*....|.
gi 486156319 104 DnpPCVPVCPV 114
Cdd:PRK06991 121 D--LCVPPCPV 129
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 124-189 6.62e-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: 6.62e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 486156319 124 IVVVDNKRCVGCAYCVQACPYDARFINHETQT--ADKCTFCVHrleagllpaCVESCVGGARIIGDIK 189
Cdd:COG2221    9 PPKIDEEKCIGCGLCVAVCPTGAISLDDGKLVidEEKCIGCGA---------CIRVCPTGAIKGEKPK 67
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 123-182 8.50e-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: 8.50e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 486156319 123 GIVVVDNKRCVGCAYCVQACPYDARFINHETQTA-----DKCTFCvhrleagllPACVESCVGGA 182
Cdd:COG1146    1 MMPVIDTDKCIGCGACVEVCPVDVLELDEEGKKAlvinpEECIGC---------GACELVCPVGA 56
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 126-178 1.20e-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: 37.76  E-value: 1.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 486156319 126 VVDNKRCVGCAYCVQACPYDA-------RFINHETQTADKCTFCvhrleaGllpACVESC 178
Cdd:cd10549    2 KYDPEKCIGCGICVKACPTDAielgpngAIARGPEIDEDKCVFC------G---ACVEVC 52
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 124-182 1.52e-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: 1.52e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 486156319 124 IVVVDNKRCVGCAYCVQACPYDA-RFINHETQT--ADKCTFCVhrleagllpACVESCVGGA 182
Cdd:COG1149    5 IPVIDEEKCIGCGLCVEVCPEGAiKLDDGGAPVvdPDLCTGCG---------ACVGVCPTGA 57
PRK06991 PRK06991
electron transport complex subunit RsxB;
107-162 1.81e-03

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 38.62  E-value: 1.81e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 486156319 107 PCVPVCPVQATfQREDGIVVVDNKRCVGCAYCVQACPYDArfI-----NHETQTADKCTFC 162
Cdd:PRK06991  63 PVIPLDPANGV-ERPRAVAVIDEQLCIGCTLCMQACPVDA--IvgapkQMHTVLADLCTGC 120
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
108-158 1.82e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 38.76  E-value: 1.82e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 486156319 108 CVPVCPVQAtFQREDGIVVVDNKRCVGCAYCVQACPydaRFINHETQTADK 158
Cdd:PRK07118 221 CVKACPAGA-ITMENNLAVIDQEKCTSCGKCVEKCP---TKAIRILNKPPK 267
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 125-146 1.89e-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: 34.92  E-value: 1.89e-03
                          10        20
                  ....*....|....*....|..
gi 486156319  125 VVVDNKRCVGCAYCVQACPYDA 146
Cdd:pfam00037   1 VVIDEEKCIGCGACVEVCPVGA 22
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
122-182 2.14e-03

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 39.07  E-value: 2.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 486156319 122 DGIV-VVDNKRCVGCAYCVQACPYDARFINhETQTAD----KCTFCvhrleaGllpACVESCVGGA 182
Cdd:COG1148  487 EPSVaEVDPEKCTGCGRCVEVCPYGAISID-EKGVAEvnpaLCKGC------G---TCAAACPSGA 542
porD PRK09624
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
 108-154 2.47e-03

pyruvate ferredoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 170017 [Multi-domain]  Cd Length: 105  Bit Score: 36.55  E-value: 2.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 486156319 108 CVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQ 154
Cdd:PRK09624  59 CYIYCPEPAIYLDEEGYPVFDYDYCKGCGICANECPTKAIEMVRETK 105
Fer4_9 pfam13187
4Fe-4S dicluster domain;
100-146 2.71e-03

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 34.84  E-value: 2.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 486156319  100 CNHCDNppCVPVCPVQATFQREDGIVVV---DNKRCVGCAYCVQACPYDA 146
Cdd:pfam13187   2 CTGCGA--CVAACPAGAIVPDLVGQTIRgdiAGLACIGCGACVDACPRGA 49
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 131-182 3.46e-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: 35.11  E-value: 3.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 486156319 131 RCVGCAYCVQACPYDARFINHETQT------ADKCTFCVhrleagllpACVESCVGGA 182
Cdd:COG1143    3 KCIGCGLCVRVCPVDAITIEDGEPGkvyvidPDKCIGCG---------LCVEVCPTGA 51
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 132-178 7.18e-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: 7.18e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 486156319 132 CVGCAYCVQACPYDARFINHE---TQTADKCTFCvhrleaGLlpaCVESC 178
Cdd:COG2878  139 CIGCGDCIKACPFDAIVGAAKgmhTVDEDKCTGC------GL---CVEAC 179
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
129-178 9.92e-03

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 35.63  E-value: 9.92e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 486156319 129 NKRCVGCAYCVQACPYDARFInhetQTAD----------------KCTFCvhrleaGLlpaCVESC 178
Cdd:PRK05888  57 EERCIACKLCAAICPADAITI----EAAEredgrrrttrydinfgRCIFC------GF---CEEAC 109
 
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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