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Conserved domains on  [gi|1083021138|gb|OGD23128|]
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MAG: 4Fe-4S ferredoxin [Candidatus Aminicenantes bacterium RBG_16_63_16]

Protein Classification

4Fe-4S dicluster domain-containing protein( domain architecture ID 11586797)

4Fe-4S dicluster domain-containing protein such as Salmonella enterica thiosulfate reductase electron transfer subunit PhsB, a component of the PhsABC thiosulfate reductase that catalyzes the reduction of thiosulfate to sulfite and hydrogen sulfide, with menaquinol as the sole electron donor

Gene Ontology:  GO:0016491|GO:0046872|GO:0051539
SCOP:  3000020

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 52-247 1.13e-78

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: 235.12  E-value: 1.13e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  52 MGIAIDKCIGCGRCADACKKENDVPTGpfFFRTWIERYvilEGGEVvvdsPNGgldgfklqpqektviRSFFVPKLCNQC 131
Cdd:cd10551     1 MVIDLRKCIGCGACVVACKAENNVPPG--VFRNRVLEY---EVGEY----PNV---------------KRTFLPVLCNHC 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 132 DSPPCVQVCPVGATFKTRDGVILVDSKRCIGCRYCLQACPYGARFIDP------------RSRTAEKCTFCYHRIVKGLV 199
Cdd:cd10551    57 ENPPCVKVCPTGATYKREDGIVLVDYDKCIGCRYCMAACPYGARYFNPeephefgevpvrPKGVVEKCTFCYHRLDEGLL 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1083021138 200 PACVEVCPSQARIFGETKGGASPLARFMRMYKIGVLKPSLNTSPKVYY 247
Cdd:cd10551   137 PACVEACPTGARIFGDLDDPNSEVSKLLAERRAYVLKPELGTKPKVYY 184
 
Name Accession Description Interval E-value
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 52-247 1.13e-78

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: 235.12  E-value: 1.13e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  52 MGIAIDKCIGCGRCADACKKENDVPTGpfFFRTWIERYvilEGGEVvvdsPNGgldgfklqpqektviRSFFVPKLCNQC 131
Cdd:cd10551     1 MVIDLRKCIGCGACVVACKAENNVPPG--VFRNRVLEY---EVGEY----PNV---------------KRTFLPVLCNHC 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 132 DSPPCVQVCPVGATFKTRDGVILVDSKRCIGCRYCLQACPYGARFIDP------------RSRTAEKCTFCYHRIVKGLV 199
Cdd:cd10551    57 ENPPCVKVCPTGATYKREDGIVLVDYDKCIGCRYCMAACPYGARYFNPeephefgevpvrPKGVVEKCTFCYHRLDEGLL 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1083021138 200 PACVEVCPSQARIFGETKGGASPLARFMRMYKIGVLKPSLNTSPKVYY 247
Cdd:cd10551   137 PACVEACPTGARIFGDLDDPNSEVSKLLAERRAYVLKPELGTKPKVYY 184
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 45-247 1.19e-69

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 212.11  E-value: 1.19e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  45 PRSHSWGMGIAIDKCIGCGRCADACKKENDVPTGPFffRTWIERYVILEGGEVvvdspnggldgfklqpqektviRSFFV 124
Cdd:COG0437     1 LSMKRYGMVIDLTKCIGCRACVVACKEENNLPVGVT--WRRVRRYEEGEFPNV----------------------EWLFV 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 125 PKLCNQCDSPPCVQVCPVGATFKTRDGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAEKCTFCYHRIVKGLVPACVE 204
Cdd:COG0437    57 PVLCNHCDDPPCVKVCPTGATYKREDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVE 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1083021138 205 VCPSQARIFGETKGGASPLARFMRMYKIGVLKPSLNTSPKVYY 247
Cdd:COG0437   137 ACPTGALVFGDLDDPESEVSKRLAELPAYRLLPELGTKPSVYY 179
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
8-251 9.03e-66

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 204.72  E-value: 9.03e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138   8 RREFLRQLllSCFSLGGILAGKGTAGPAVSRSAEEYDPRsHSWGMGIAIDKCIGCGRCADACKKENDVPTGPFffRTWIE 87
Cdd:PRK14993    5 KRQFLQQL--GVLTAGASLVPLAEAKFPFSPERHEGSPR-HRYAMLIDLRRCIGCQSCTVSCTIENQTPQGAF--RTTVN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  88 RYvileggevvvdspnggldgfKLQPQEKTVIRSFFVPKLCNQCDSPPCVQVCPVGATFKTRDGVILVDSKRCIGCRYCL 167
Cdd:PRK14993   80 QY--------------------QVQREGSQEVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 168 QACPYGARFIDPRSRTAEKCTFCYHRIVKGLVPACVEVCPSQARIFGETKGGASPLARFMRMYK--IGVLKPSLNTSPKV 245
Cdd:PRK14993  140 QACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRIATMLHQHRdaIKVLKPENGTSPHV 219


                  ....*.
gi 1083021138 246 YYAGLD 251
Cdd:PRK14993  220 FYLGLD 225
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 122-215 3.91e-29

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: 105.79  E-value: 3.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 122 FFVPKLCNQCDSPPCVQVCPVGATFKTR-DGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAEKCTFCYHRIVKGLVP 200
Cdd:pfam13247   4 LFFPEQCRHCLNPPCKASCPVGAIYKDEeTGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAGLLP 83

                          90
                  ....*....|....*
gi 1083021138 201 ACVEVCPSQARIFGE 215
Cdd:pfam13247  84 ACVQTCPTGAMNFGD 98
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 152-210 6.29e-04

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


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 39.40  E-value: 6.29e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1083021138 152 VILVDSKRCIGCRYCLQACPY-----GARFIdpRSRTAEKCTFCyhrivkglvPACVEVCPSQA 210
Cdd:TIGR01944 107 VALIDEDNCIGCTKCIQACPVdaivgAAKAM--HTVIADECTGC---------DLCVEPCPTDC 159
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 157-210 6.61e-03

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


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 37.15  E-value: 6.61e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1083021138 157 SKRCIGCRYCLQACPYGA-RFIDPRSRTAEKCTFCYhrivkglvpACVEVCPSQA 210
Cdd:NF038196  184 TDKCIGCGICAKVCPVNNiEMEDGKPVWGHNCTHCL---------ACIHRCPKEA 229
 
Name Accession Description Interval E-value
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 52-247 1.13e-78

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: 235.12  E-value: 1.13e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  52 MGIAIDKCIGCGRCADACKKENDVPTGpfFFRTWIERYvilEGGEVvvdsPNGgldgfklqpqektviRSFFVPKLCNQC 131
Cdd:cd10551     1 MVIDLRKCIGCGACVVACKAENNVPPG--VFRNRVLEY---EVGEY----PNV---------------KRTFLPVLCNHC 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 132 DSPPCVQVCPVGATFKTRDGVILVDSKRCIGCRYCLQACPYGARFIDP------------RSRTAEKCTFCYHRIVKGLV 199
Cdd:cd10551    57 ENPPCVKVCPTGATYKREDGIVLVDYDKCIGCRYCMAACPYGARYFNPeephefgevpvrPKGVVEKCTFCYHRLDEGLL 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1083021138 200 PACVEVCPSQARIFGETKGGASPLARFMRMYKIGVLKPSLNTSPKVYY 247
Cdd:cd10551   137 PACVEACPTGARIFGDLDDPNSEVSKLLAERRAYVLKPELGTKPKVYY 184
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 45-247 1.19e-69

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 212.11  E-value: 1.19e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  45 PRSHSWGMGIAIDKCIGCGRCADACKKENDVPTGPFffRTWIERYVILEGGEVvvdspnggldgfklqpqektviRSFFV 124
Cdd:COG0437     1 LSMKRYGMVIDLTKCIGCRACVVACKEENNLPVGVT--WRRVRRYEEGEFPNV----------------------EWLFV 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 125 PKLCNQCDSPPCVQVCPVGATFKTRDGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAEKCTFCYHRIVKGLVPACVE 204
Cdd:COG0437    57 PVLCNHCDDPPCVKVCPTGATYKREDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVE 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1083021138 205 VCPSQARIFGETKGGASPLARFMRMYKIGVLKPSLNTSPKVYY 247
Cdd:COG0437   137 ACPTGALVFGDLDDPESEVSKRLAELPAYRLLPELGTKPSVYY 179
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
8-251 9.03e-66

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 204.72  E-value: 9.03e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138   8 RREFLRQLllSCFSLGGILAGKGTAGPAVSRSAEEYDPRsHSWGMGIAIDKCIGCGRCADACKKENDVPTGPFffRTWIE 87
Cdd:PRK14993    5 KRQFLQQL--GVLTAGASLVPLAEAKFPFSPERHEGSPR-HRYAMLIDLRRCIGCQSCTVSCTIENQTPQGAF--RTTVN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  88 RYvileggevvvdspnggldgfKLQPQEKTVIRSFFVPKLCNQCDSPPCVQVCPVGATFKTRDGVILVDSKRCIGCRYCL 167
Cdd:PRK14993   80 QY--------------------QVQREGSQEVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 168 QACPYGARFIDPRSRTAEKCTFCYHRIVKGLVPACVEVCPSQARIFGETKGGASPLARFMRMYK--IGVLKPSLNTSPKV 245
Cdd:PRK14993  140 QACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRIATMLHQHRdaIKVLKPENGTSPHV 219


                  ....*.
gi 1083021138 246 YYAGLD 251
Cdd:PRK14993  220 FYLGLD 225
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 57-214 7.33e-46

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: 150.02  E-value: 7.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  57 DKCIGCGRCADACKKENDVPTGPFFfrtwieRYVI-LEGGEvvvdspnggldgfklqpqeKTVIRSFFVPKLCNQCDSPP 135
Cdd:cd16371     7 ERCIGCKACEIACKDKNDLPPGVNW------RRVYeYEGGE-------------------FPEVFAYFLSMSCNHCENPA 61

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083021138 136 CVQVCPVGATFKTRDGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAEKCTFCYHRIVKGLVPACVEVCPSQARIFG 214
Cdd:cd16371    62 CVKVCPTGAITKREDGIVVVDQDKCIGCGYCVWACPYGAPQYNPETGKMDKCDMCVDRLDEGEKPACVAACPTRALDFG 140
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 57-214 3.46e-45

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: 148.31  E-value: 3.46e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  57 DKCIGCGRCADACKKENDVPTGPFFFRTWIERYVILEGgevvvdspnggldgfklqpqektvirsFFVPKLCNQCDSPPC 136
Cdd:cd04410     6 DRCIGCGTCEVACKQEHGLRPGPDWSRIKVIEGGGLER---------------------------AFLPVSCMHCEDPPC 58

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083021138 137 VQVCPVGATFKTRDGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAEKCTFCYHRIVKGLVPACVEVCPSQARIFG 214
Cdd:cd04410    59 VKACPTGAIYKDEDGIVLIDEDKCIGCGSCVEACPYGAIVFDPEPGKAVKCDLCGDRLDEGLEPACVKACPTGALTFG 136
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 53-217 3.09e-43

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


Pssm-ID: 319883 [Multi-domain]  Cd Length: 196  Bit Score: 145.05  E-value: 3.09e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  53 GIAID--KCIGCGRCADACKKENDVPTGPFFFrtwieryvileggEVVVDSPNggldgfKLQPQEKTVIRSF-------- 122
Cdd:cd10561     1 GVLYDttRCIGCRACEVACKEWNGLPAEDTAF-------------GPGWDNPR------DLSAKTYTVIKRYevetggkg 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 123 --FVPKLCNQCDSPPCVQVCPVGATFKTRDGVILVDSKRCIGCRYCLQACPYGA-RF----IDPRSRtaeKCTFCYHRIV 195
Cdd:cd10561    62 fvFVKRQCMHCLDPACVSACPVGALRKTPEGPVTYDEDKCIGCRYCMVACPFNIpKYewdsANPKIR---KCTMCYDRLK 138

                         170       180
                  ....*....|....*....|..
gi 1083021138 196 KGLVPACVEVCPSQARIFGETK 217
Cdd:cd10561   139 EGKQPACVEACPTGALLFGKRE 160
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 51-247 3.24e-38

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: 135.89  E-value: 3.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  51 GMGIAIDKCIGCGRCADACKKE------------NDVPT--GPFFFRTWIERYVILEGGEVVVDSPNGGLDGF------- 109
Cdd:cd10555     6 AMVMDLNKCIGCQTCTVACKTLwtnrngreymywNNVETqpGKGYPKNWEKKGGGFKDKGELKPGIIPTLEDYgvpweyn 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 110 -----------KLQPQEKTVIRS------------------FFVPKLCNQCDSPPCVQVCPVGATFK-TRDGVILVDSKR 159
Cdd:cd10555    86 heeelfegkggRVRPSPKGDPTWgpnwdedqgageypnsyyFYLPRICNHCTNPACLAACPRKAIYKrEEDGIVLVDQDR 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 160 CIGCRYCLQACPYGARFIDPRSRTAEKCTFCYHRIVKGLVPACVEVCPSQARIFGETKGGASPLARFMRMYKIGV-LKPS 238
Cdd:cd10555   166 CRGYRYCVEACPYKKIYFNPVEQKSEKCIFCYPRIEKGVAPACARQCVGRIRFVGYLDDEESPVYKLVKKWKVALpLHPE 245


                  ....*....
gi 1083021138 239 LNTSPKVYY 247
Cdd:cd10555   246 YGTEPNVFY 254
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 54-214 3.39e-36

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: 125.98  E-value: 3.39e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  54 IAIDKCIGCGRCADACKKENDVPTGPFFFRTWIERYVILEGGevvvdspNGGLDGFKLQPQEKTVIRSFFVPKLCNQCDS 133
Cdd:cd16366     3 VDTSRCTGCRACQVACKQWNGLPAEKTEFTGSYQNPPDLTAH-------TWTLVRFYEVEKPGGDLSWLFRKDQCMHCTD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 134 PPCVQVCPVGATFKTRDGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAEKCTFCYHRIVKGLVPACVEVCPSQARIF 213
Cdd:cd16366    76 AGCLAACPTGAIIRTETGTVVVDPETCIGCGYCVNACPFDIPRFDEETGRVAKCTLCYDRISNGLQPACVKTCPTGALTF 155


                  .
gi 1083021138 214 G 214
Cdd:cd16366   156 G 156
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 51-247 2.00e-35

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: 125.39  E-value: 2.00e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  51 GMGIAIDKCIGCGRCADACKKE------------NDVPTGPF--FFRTWiERYVILEGGEvvvdspnggldgfklqpqek 116
Cdd:cd16365     4 AAVFNLNKCIGCQTCTVACKNAwtyrkgqeymwwNNVETKPGggYPQDW-EVKTIDNGGN-------------------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 117 tvIRSFF-VPKLCNQCDSPPCVQVCPVGATFKTR-DGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAEKCTFCYHRI 194
Cdd:cd16365    63 --TRFFFyLQRLCNHCTNPACLAACPRGAIYKREeDGIVLIDQKRCRGYRKCVEQCPYKKIYFNGLSRVSEKCIACYPRI 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1083021138 195 VKGLVPACVEVCPSQARIFGE-TKGGASPLARFMRMYKIGV-LKPSLNTSPKVYY 247
Cdd:cd16365   141 EGGDPTRCMSACVGRIRLQGFlDDNPKSPVTKLIRHWKVALpLHPEYGTEPNIYY 195
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 52-215 2.95e-34

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: 120.87  E-value: 2.95e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  52 MGIAIDKCIGCGRCADACKKENDVPTGPFFFRTWIERYVILEGGEVVVDSpnggldgFKLQPQEKTVIRSFFVPKLCNQC 131
Cdd:cd10562     1 MLVDTSKCTACRGCQVACKQWNQLPAEKTPFTGSYQNPPDLTPNTWTLIR-------FYEHEEDNGGIRWLFRKRQCMHC 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 132 DSPPCVQVCPVGATFKTRDGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAEKCTFCYHRIVKGLVPACVEVCPSQAR 211
Cdd:cd10562    74 TDAACVKVCPTGALYKTENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCFDRIENGMQPACVKTCPTGAL 153


                  ....
gi 1083021138 212 IFGE 215
Cdd:cd10562   154 TFGD 157
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 52-251 5.67e-34

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: 120.89  E-value: 5.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  52 MGIAIDKCIGCGRCADACKKE---NDVP--------TGPFFFRtwIERYvilEGGEVvvdspnggldgfklqpqekTVIR 120
Cdd:cd10552     1 LVIDVAKCNGCYNCFLACKDEhvgNDWPgyaapqprHGHFWMR--ILRR---ERGQY-------------------PKVD 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 121 SFFVPKLCNQCDSPPCVQVCPVGATFKTRDGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAEKCTFCYHRIVKG-LV 199
Cdd:cd10552    57 VAYLPVPCNHCDNAPCIKAAKDGAVYKRDDGIVIIDPEKAKGQKQLVDACPYGAIYWNEELQVPQKCTFCAHLLDDGwKE 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1083021138 200 PACVEVCPSQARIFGETKGGASplARFMRMYKIGVLKPSLNTSPKVYYAGLD 251
Cdd:cd10552   137 PRCVQACPTGALRFGKLEDEEM--AAKAAEEGLEVLHPELGTKPRVYYKNLP 186
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 41-247 1.70e-32

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: 119.87  E-value: 1.70e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  41 EEYDPRSHsWGMGIAIDKCIGCGRCADACKKE------------NDVPTGPFFF--RTWIERYVILEGGEV--------- 97
Cdd:cd10556     4 EESRPDKQ-FAMVFDTNKCIACQTCTMACKSTwtsgkgqeymwwNNVETKPYGGypLGWDVRLLDEEGGQTwaeggvyeg 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  98 ---------------------VVDSPNGGLDGFKLQPQEKTVIRS-------FFVPKLCNQCDSPPCVQVCPVGATFKTR 149
Cdd:cd10556    83 ktifeaaaageqvlgyrpedeDWRYPNIGEDEVNGERTPDTGSSLpphpiwfFYLPRICNHCTYPACLAACPRKAIYKRE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 150 -DGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAEKCTFCYHRIVKGLVPACVEVCPSQARIFG---------ETKGG 219
Cdd:cd10556   163 eDGIVLIDQERCRGYRECVEACPYKKPMYNPTTRVSEKCIGCYPRIEEGDQTQCVSACIGKIRLQGfintppdarWADDR 242

                         250       260
                  ....*....|....*....|....*....
gi 1083021138 220 ASPLARFMRMYKIGV-LKPSLNTSPKVYY 247
Cdd:cd10556   243 DNPIDFLVHIKKVALpLYPQFGTEPNVYY 271
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
7-217 4.99e-32

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 119.77  E-value: 4.99e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138   7 QRREFLRQLllscfSLGGILAGkgTAGPAVSRSAEEYDPRSHSWGMGIAIDKCIGCGRCADACKKENDVPTGPfffrtwi 86
Cdd:PRK10882    2 NRRNFLKAA-----SAGALLAG--ALPSVSHAAAENRPPIPGALGMLYDSTLCVGCQACVTKCQEINFPERNP------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  87 eryvileGGEVVVDSPNggldgfKLQPQEKTVIRSF----------------FVPKLCNQCDSPPCVQVCPVGATFK-TR 149
Cdd:PRK10882   68 -------QGEQTWDNPD------KLSPYTNNIIKVWksgtgvnkdqeengyaYIKKQCMHCVDPNCVSVCPVSALTKdPK 134

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1083021138 150 DGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAE--KCTFCYH----RIVKGLVPACVEVCPSQARIFGETK 217
Cdd:PRK10882  135 TGIVHYDKDVCTGCRYCMVACPFNVPKYDYNNPFGAihKCELCNQkgveRLDKGGLPGCVEVCPTGAVIFGTRE 208
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 51-215 4.10e-31

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: 114.79  E-value: 4.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  51 GMGIAIDKCIGCGRCADACKKENDVPTGPFFF-------------RTWieRYV-ILEggevVVDSPNGGLDGFKLQpqek 116
Cdd:cd10560     1 GFFTDTSICIGCKACEVACKQWNQLPADGYDFsgmsydntgdlsaSTW--RHVkFIE----RPTEDGPANEGGDLQ---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 117 tvirSFFVPKLCNQCDSPPCVQVCPVGATFKTRDGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAEKCTFCYHRIVK 196
Cdd:cd10560    71 ----WLFMSDVCKHCTDAGCLEACPTGAIFRTEFGTVYIQPDICNGCGYCVAACPFGVIDRNEETGRAHKCTLCYDRLKD 146

                         170
                  ....*....|....*....
gi 1083021138 197 GLVPACVEVCPSQARIFGE 215
Cdd:cd10560   147 GLEPACAKACPTGSIQFGP 165
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 57-214 2.21e-30

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: 110.53  E-value: 2.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  57 DKCIGCGRCADACKKENDVPTGPFFFRtwieryVILEGGEVVvdspnggldgfklqpQEKTVIRSFFVPklCNQCDSPPC 136
Cdd:cd10553    10 KRCIGCLACEVHCKVKNNLPVGPRLCR------IFAVGPKMV---------------GGKPRLKFVYMS--CFHCENPWC 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083021138 137 VQVCPVGATFK-TRDGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAEKCTFCYHRIVKGLVPACVEVCPSQARIFG 214
Cdd:cd10553    67 VKACPTGAMQKrEKDGIVYVDQELCIGCKACIEACPWGIPQWNPATGKVVKCDYCMDRIDQGLKPACVTGCTTHALSFV 145
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 54-215 4.11e-30

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: 109.67  E-value: 4.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  54 IAIDKCIGCGRCADACKKENDVptgpfffrtwIERYVILEGGEvvvdspnggldgfklqpqektvirSFFVPKLCNQCDS 133
Cdd:cd16374     3 VDPERCIGCRACEIACAREHSG----------KPRISVEVVED------------------------LASVPVRCRHCED 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 134 PPCVQVCPVGATFKTRDGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAEKCTFCYHRIVKGLVPACVEVCPSQARIF 213
Cdd:cd16374    49 APCMEVCPTGAIYRDEDGAVLVDPDKCIGCGMCAMACPFGVPRFDPSLKVAVKCDLCIDRRREGKLPACVEACPTGALKF 128


                  ..
gi 1083021138 214 GE 215
Cdd:cd16374   129 GD 130
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 122-215 3.91e-29

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: 105.79  E-value: 3.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 122 FFVPKLCNQCDSPPCVQVCPVGATFKTR-DGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAEKCTFCYHRIVKGLVP 200
Cdd:pfam13247   4 LFFPEQCRHCLNPPCKASCPVGAIYKDEeTGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAGLLP 83

                          90
                  ....*....|....*
gi 1083021138 201 ACVEVCPSQARIFGE 215
Cdd:pfam13247  84 ACVQTCPTGAMNFGD 98
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 57-210 1.49e-27

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


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 102.66  E-value: 1.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  57 DKCIGCGRCADACKKENDVPTGPFFFRTWIERyvileggevvvDSPNGgldgfklqpqektvirsFFVPKLCNQCDSPPC 136
Cdd:cd10550     6 EKCTGCRTCELACSLKHEGVFNPSLSRIRVVR-----------FEPEG-----------------LDVPVVCRQCEDAPC 57

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083021138 137 VQVCPVGA-TFKTRDGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAEKCTFCyhrivkGLVPACVEVCPSQA 210
Cdd:cd10550    58 VEACPVGAiSRDEETGAVVVDEDKCIGCGMCVEACPFGAIRVDPETGKAIKCDLC------GGDPACVKVCPTGA 126
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 122-214 3.38e-27

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: 107.45  E-value: 3.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 122 FFVPKLCNQCDSPPCVQVCPVGATFK-TRDGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAEKCTFCYHRIVKGLVP 200
Cdd:cd10557   173 FYLPRICNHCLNPACVAACPSGAIYKrEEDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSEKCIFCYPRLEAGQPT 252

                          90
                  ....*....|....
gi 1083021138 201 ACVEVCPSQARIFG 214
Cdd:cd10557   253 VCSETCVGRIRYLG 266
PRK09898 PRK09898
ferredoxin-like protein;
3-210 2.54e-26

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 101.84  E-value: 2.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138   3 ETACQRREFLRqlllscfslggiLAGKGTAGPAVSRS------AEEYDPRSHSWGM-----GIAI---DKCIGCGRCADA 68
Cdd:PRK09898   10 DIGLTRLEFLR------------ISGKGLAGLTIAPAllsllgCKQEDIDSGTVGLintpkGVLVtqrARCTGCHRCEIS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  69 CKKENDVPTGPFFFRTWIERYVILegGEVVVDSpNGGLDGFKLqpqektvirsfFVPKLCNQCDSPPCVQVCPVGA-TFK 147
Cdd:PRK09898   78 CTNFNDGSVGTFFSRIKIHRNYFF--GDNGVGS-GGGLYGDLN-----------YTADTCRQCKEPQCMNVCPIGAiTWQ 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083021138 148 TRDGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAEKCTFCyhrivkglvPACVEVCPSQA 210
Cdd:PRK09898  144 QKEGCITVDHKRCIGCSACTTACPWMMATVNTESKKSSKCVLC---------GECANACPTGA 197
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
54-210 4.79e-26

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 98.96  E-value: 4.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  54 IAIDKCIGCGRCADACKKENDVPTGPFFfrtwIERYVILEGGEvvvdspnggldgfklqpqektvirsFFVPKLCNQCDS 133
Cdd:COG1142     7 ADPEKCIGCRTCEAACAVAHEGEEGEPF----LPRIRVVRKAG-------------------------VSAPVQCRHCED 57

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083021138 134 PPCVQVCPVGATFKTrDGVILVDSKRCIGCRYCLQACPYGARFIDPRS--RTAEKCTFCYHRIVkglVPACVEVCPSQA 210
Cdd:COG1142    58 APCAEVCPVGAITRD-DGAVVVDEEKCIGCGLCVLACPFGAITMVGEKsrAVAVKCDLCGGREG---GPACVEACPTGA 132
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 124-214 3.47e-25

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: 97.84  E-value: 3.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 124 VPKLCNQCDSPPCVQVCPVGATFKTRDGVIL-VDSKRCIGCRYCLQACPYGARFIDPRSRTAEKCTFCYHRIVKGLVPAC 202
Cdd:cd16369    47 APTVCMHCEDPTCAEVCPADAIKVTEDGVVQsALKPRCIGCSNCVNACPFGVPKYDEERNLMMKCDMCYDRTSVGKAPMC 126

                          90
                  ....*....|..
gi 1083021138 203 VEVCPSQARIFG 214
Cdd:cd16369   127 ASVCPSGALFYG 138
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 57-210 7.94e-24

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: 93.48  E-value: 7.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  57 DKCIGCGRCADACkkendvptgpfffrtwieryvileggeVVV----DSPNGGLDGFKLQPQEKTV-IRSFFVPKLCNQC 131
Cdd:cd10554     7 DKCIGCRTCEVAC---------------------------AAAhsgkGIFEAGTDGLPFLPRLRVVkTGEVTAPVQCRQC 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 132 DSPPCVQVCPVGATFKtRDGVILVDSKRCIGCRYCLQACPYGArfIDPRSRT-------------AEKCTFCYHRIVKgl 198
Cdd:cd10554    60 EDAPCANVCPVGAISQ-EDGVVQVDEERCIGCKLCVLACPFGA--IEMAPTTvpgvdwergpravAVKCDLCAGREGG-- 134

                         170
                  ....*....|..
gi 1083021138 199 vPACVEVCPSQA 210
Cdd:cd10554   135 -PACVEACPTKA 145
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 54-225 1.38e-23

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: 94.38  E-value: 1.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  54 IAID--KCIGCGRCADACKKENDVPTGPFFF---------RTWiERYVILEGGEVVvdsPNGGLdgfklqpqektviRSF 122
Cdd:cd10558     2 KLIDvsKCIGCKACQVACKEWNDLRAEVGHNvgtyqnpadLSP-ETWTLMKFREVE---DNGKL-------------EWL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 123 FVPKLCNQCDSPPCVQVCP-VGATFKTRDGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAEKCTFCYHRIVKGLVPA 201
Cdd:cd10558    65 IRKDGCMHCADPGCLKACPsPGAIVQYANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVGLEPA 144

                         170       180
                  ....*....|....*....|....
gi 1083021138 202 CVEVCPSQARIFGeTKGGASPLAR 225
Cdd:cd10558   145 CVKTCPTGALHFG-TKEDMLALAE 167
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 115-206 2.82e-23

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


Pssm-ID: 440755 [Multi-domain]  Cd Length: 485  Bit Score: 97.96  E-value: 2.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 115 EKTVIrsFFVPKLCNQCDSPPCVQVCPVGATFK-TRDGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAEKCTFCYHR 193
Cdd:COG1140   171 ENTFM--FYLPRICEHCLNPACVASCPSGAIYKrEEDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGKAEKCIFCYPR 248

                          90
                  ....*....|...
gi 1083021138 194 IVKGLVPACVEVC 206
Cdd:COG1140   249 IEAGQPTVCSETC 261
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 54-217 1.16e-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: 89.40  E-value: 1.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  54 IAIDKCIGC-----GRCADACKKEN--------DVPTGPFFFRTWIERYvilEGGEVVVD--SPNGGLDGFKLQPQEKTV 118
Cdd:cd16368     5 IDLTKCDGCpgesiPACVRACREKNqarfpepvSKPIQPYWPRKRIEDW---SDKRDVTDrlTPYNWLYVQKLTVDTAGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 119 IRSFFVPKLCNQCDSPPCVQVCPVGATFKTRDGVILVDSKRCIGCRYCLQACPYG--AR--------FIDPRSRTAE--- 185
Cdd:cd16368    82 EKEVFIPRRCMHCDNPPCAKLCPFGAARKTPEGAVYIDDDLCFGGAKCRDVCPWHipQRqagvgiylHLAPEYAGGGvmy 161

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1083021138 186 KCTFCYHRIVKGLVPACVEVCPSQARIFGETK 217
Cdd:cd16368   162 KCDLCKDLLAQGKPPACIEACPKGAQYFGPRK 193
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 57-214 3.64e-21

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: 86.16  E-value: 3.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  57 DKCIGCGRCADACKKENDVPTGPFFFrtwieryvILEGGE----VVVDSPNGgldgfklqpqektviRSFfvPKLCNQCD 132
Cdd:cd10563     7 EKCLGCKLCEVACAVAHSKSKDLIKA--------KLEKERprprIRVEESGG---------------RSF--PLQCRHCD 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 133 SPPCVQVCPVGATFKT-RDGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAEKCTFCYHRIvkglVPACVEVCPSQAR 211
Cdd:cd10563    62 EPPCVKACMSGAMHKDpETGIVIHDEEKCVGCWMCVMVCPYGAIRPDKERKVALKCDLCPDRE----TPACVEACPTGAL 137


                  ...
gi 1083021138 212 IFG 214
Cdd:cd10563   138 VLE 140
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 51-215 9.45e-18

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: 78.63  E-value: 9.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  51 GMGIAIDKCIGCGRCADACKKENDVPTGPFFFRTWIEryvileggevvvDSPNGGLDGFKL-----QPQEKTVIRSFFVP 125
Cdd:cd10559     1 SFLIDTTRCTACRGCQVACKQWNQLPAEQTKNTGSHQ------------NPPDLSANTYKLvrfneVRNENGKPDWLFFP 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 126 KLCNQCDSPPCVQVCPV--GATFKT-RDGVILVDSKRCIGCRY-CLQACPYGARFIDPRSRTAEKCTFCYHRIVKGLVPA 201
Cdd:cd10559    69 DQCRHCVTPPCKDAADMvpGAVIQDeATGAVVFTEKTAELDFDdVLSACPYNIPRKNEATGRIVKCDMCIDRVSNGLQPA 148

                         170
                  ....*....|....
gi 1083021138 202 CVEVCPSQARIFGE 215
Cdd:cd10559   149 CVKACPTGAMNFGD 162
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 58-210 2.34e-16

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 78.25  E-value: 2.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  58 KCIGCGRCADACkkendvptgpfffrtwieryVILEGGEVVVDSPN---GGLDGFKLQPQEKTVIrsffvpklCNQCDSP 134
Cdd:PRK12769   11 QCLGCHACEIAC--------------------VMAHNDEQHVLSQHhfhPRITVIKHQQQRSAVT--------CHHCEDA 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 135 PCVQVCPVGATFKTRDGVILVDSKrCIGCRYCLQACPYGARFI-------DPRSRTAEKCTFCYHRiVKGlvPACVEVCP 207
Cdd:PRK12769   63 PCARSCPNGAISHVDDSIQVNQQK-CIGCKSCVVACPFGTMQIvltpvaaGKVKATAHKCDLCAGR-ENG--PACVENCP 138


                  ...
gi 1083021138 208 SQA 210
Cdd:PRK12769  139 ADA 141
PRK10330 PRK10330
electron transport protein HydN;
127-212 4.91e-16

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 73.77  E-value: 4.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 127 LCNQCDSPPCVQVCPVGATFKTRdGVILVDSKRCIGCRYCLQACPYGARFIDPR---------------SRTAEKCTFCY 191
Cdd:PRK10330   57 VCRQCEDAPCANVCPNGAISRDK-GFVHVMQERCIGCKTCVVACPYGAMEVVVRpvirnsgaglnvraeKAEANKCDLCN 135

                          90       100
                  ....*....|....*....|.
gi 1083021138 192 HRIVKglvPACVEVCPSQARI 212
Cdd:PRK10330  136 HREDG---PACMAACPTHALI 153
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 125-255 1.55e-15

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 75.83  E-value: 1.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 125 PKLCNQCDSPPCVQVCPVGATFKTRDGVILvDSKRCIGCRYCLQACPYGArfIDPRSRTAEKCTFCYHRivKGLVPACVE 204
Cdd:PRK12809   53 PVACHHCNNAPCVTACPVNALTFQSDSVQL-DEQKCIGCKRCAIACPFGV--VEMVDTIAQKCDLCNQR--SSGTQACIE 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1083021138 205 VCPSQARIFGETKGGASplARFMRMYKIGVLKPSLNTSPKVYYAGLDMEVR 255
Cdd:PRK12809  128 VCPTQALRLMDDKGLQQ--IKVARQRKTAAGKASSDAQPSRSAALLPVNSR 176
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 57-210 1.59e-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: 68.13  E-value: 1.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  57 DKCIGCGRCADACKKendvptgpfffrTWieryvileggevvvdspnggldgFKLQPQEKTVIR-----SFFVPKLCNQC 131
Cdd:cd16372     8 EKCIGCLQCEEACSK------------TF-----------------------FKEEDREKSCIRiteteGGYAINVCNQC 52

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083021138 132 DSppCVQVCPVGATFKTRDGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAEKCTFCyhrivkglvPACVEVCPSQA 210
Cdd:cd16372    53 GE--CIDVCPTGAITRDANGVVMINKKLCVGCLMCVGFCPEGAMFKHEDYPEPFKCIAC---------GICVKACPTGA 120
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 54-207 2.27e-13

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


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 64.99  E-value: 2.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  54 IAIDKCIGCGRCADACKkendvptgpfffRTWIERYvileggevvvdspngGLDGFKLQPQEKTVIRSFFVPKLCNQCDS 133
Cdd:cd16370     6 KDMERCIGCYSCMLACS------------RRVHKSA---------------SLSKSAIRVRTRGGLEGGFTVVVCRACED 58

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1083021138 134 PPCVQVCPVGATFKTRDGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAEKCTFCyhrivkglvPACVEVCP 207
Cdd:cd16370    59 PPCAEACPTGALEPRKGGGVVLDKEKCIGCGNCVKACIVGAIFWDEETNKPIICIHC---------GYCARYCP 123
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 54-212 4.54e-12

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: 61.94  E-value: 4.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  54 IAIDKCIGCGRCADACKkendvptgpfffrtwiERYvileggevvvdspngglDGFKLQPQEKTVIRSFFVPKLCNQCDS 133
Cdd:cd16367    16 IDLDRCIRCDNCEKACA----------------DTH-----------------DGHSRLDRNGLRFGNLLVPTACRHCVD 62

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083021138 134 PPCVQVCPVGATFKTRDGVILVDSKrCIGCRYCLQACPYGArfidPRSRTAEKCTFCyhriVKGLVPACVEVCPSQARI 212
Cdd:cd16367    63 PVCMIGCPTGAIHRDDGGEVVISDA-CCGCGNCASACPYGA----IQMVRAVKCDLC----AGYAGPACVSACPTGAAI 132
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 57-210 2.64e-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: 56.64  E-value: 2.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  57 DKCIGCGRCADACkkendvptgpfffrtwieryvileggevvvdsPNGGLdgfKLQPQEKTVIRSFFVPKLCNQCDSppC 136
Cdd:cd10549     6 EKCIGCGICVKAC--------------------------------PTDAI---ELGPNGAIARGPEIDEDKCVFCGA--C 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 137 VQVCPVGA--------TFKTRDGVILVDSKRCIGCRYCLQACPYGARFIDPRSRT---AEKCTFCyhrivkglvPACVEV 205
Cdd:cd10549    49 VEVCPTGAieltpegkEYVPKEKEAEIDEEKCIGCGLCVKVCPVDAITLEDELEIvidKEKCIGC---------GICAEV 119


                  ....*
gi 1083021138 206 CPSQA 210
Cdd:cd10549   120 CPVNA 124
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 56-208 2.54e-09

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: 54.57  E-value: 2.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  56 IDKCIGCGRCADACkkendvPTGpfffrtwIERYVILEGGEVVVDSPnggldgfklqpqektvirsFFVPKL--CNQCDS 133
Cdd:cd16373    13 LALCIRCGLCVEAC------PTG-------VIQPAGLEDGLEGGRTP-------------------YLDPREgpCDLCCD 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 134 PpCVQVCPVGA-------TFKTRDGVILVDSKRCI------GCRYCLQACPYGARFIDPRSRT------AEKCTFCyhri 194
Cdd:cd16373    61 A-CVEVCPTGAlrpldleEQKVKMGVAVIDKDRCLawqggtDCGVCVEACPTEAIAIVLEDDVlrpvvdEDKCVGC---- 135

                         170
                  ....*....|....
gi 1083021138 195 vkGlvpACVEVCPS 208
Cdd:cd16373   136 --G---LCEYVCPV 144
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
124-179 5.33e-09

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 51.66  E-value: 5.33e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1083021138 124 VPKLCNQCDSppCVQVCPVGAtFKTRDGVILVDSKRCIGCRYCLQACPYGARFIDP 179
Cdd:COG2768     9 DEEKCIGCGA--CVKVCPVGA-ISIEDGKAVIDPEKCIGCGACIEVCPVGAIKIEW 61
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 125-181 9.45e-08

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 48.19  E-value: 9.45e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1083021138 125 PKLCNQCDSppCVQVCPVGATFKTRDGVILVDSKRCIGCRYCLQACPYGARFIDPRS 181
Cdd:COG1149    10 EEKCIGCGL--CVEVCPEGAIKLDDGGAPVVDPDLCTGCGACVGVCPTGAITLEERE 64
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
118-211 2.54e-07

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 50.79  E-value: 2.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 118 VIRSFFVPKLCNQCDSPPCVQVCPVGATFKTRDGVILVDSKRCIGCRYCLQACPYGARFIDPRSRT--AEKCTFCyhriv 195
Cdd:COG4624    51 CPRCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCYPCVRACPVKAIKVDDGKAEidEEKCISC----- 125

                          90
                  ....*....|....*.
gi 1083021138 196 kGlvpACVEVCPSQAR 211
Cdd:COG4624   126 -G---QCVAVCPFGAI 137
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
136-210 3.01e-07

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 50.06  E-value: 3.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 136 CVQVCPVGAT----FKTRDGVILVDSKRCIGCRYCLQACPYGarfIDPR--SRTAEKCTFCYhrivkglvpACVEVCPSQ 209
Cdd:COG0348   184 CRYLCPYGAFqgllSDLSTLRVRYDRGDCIDCGLCVKVCPMG---IDIRkgEINQSECINCG---------RCIDACPKD 251


                  .
gi 1083021138 210 A 210
Cdd:COG0348   252 A 252
PRK13795 PRK13795
hypothetical protein; Provisional
 94-180 3.25e-07

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 50.76  E-value: 3.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  94 GGEVVVDSPNGGLDGFKLQPQEKTVIRSFfvpkLCNQCDSppCVQVCPVGA-TFKTRDGVILVDSKRCIGCRYCLQACPY 172
Cdd:PRK13795  553 SGNIWARSEDKEAAASLFKDAARLLRRAA----ECVGCGV--CVGACPTGAiRIEEGKRKISVDEEKCIHCGKCTEVCPV 626


                  ....*...
gi 1083021138 173 gARFIDPR 180
Cdd:PRK13795  627 -VKYKDKR 633
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 125-174 3.73e-07

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 46.20  E-value: 3.73e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1083021138 125 PKLCNQCDSppCVQVCPVGAtFKTRDGVILVDSKRCIGCRYCLQACPYGA 174
Cdd:COG2221    14 EEKCIGCGL--CVAVCPTGA-ISLDDGKLVIDEEKCIGCGACIRVCPTGA 60
NapF COG1145
Ferredoxin [Energy production and conversion];
125-180 8.74e-07

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 48.57  E-value: 8.74e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1083021138 125 PKLCNQCDSppCVQVCPVGA-TFKTRDGVILVDSKRCIGCRYCLQACPYGARFIDPR 180
Cdd:COG1145   181 AEKCIGCGL--CVKVCPTGAiRLKDGKPQIVVDPDKCIGCGACVKVCPVGAISLEPK 235
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 116-174 9.15e-07

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 45.42  E-value: 9.15e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1083021138 116 KTVIRSFFVPKLCNQCDSppCVQVCPVGAtFKTRDGVILVDSKRCIGCRYCLQACPYGA 174
Cdd:COG4231    12 TTAMRYVIDEDKCTGCGA--CVKVCPADA-IEEGDGKAVIDPDLCIGCGSCVQVCPVDA 67
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 152-220 1.45e-06

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 44.72  E-value: 1.45e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1083021138 152 VILVDSKRCIGCRYCLQACPYGA-RFIDPRSRT--AEKCTFCYhrivkglvpACVEVCPSQARIFGETKGGA 220
Cdd:COG1149     5 IPVIDEEKCIGCGLCVEVCPEGAiKLDDGGAPVvdPDLCTGCG---------ACVGVCPTGAITLEEREAGK 67
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 125-186 1.63e-06

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: 44.35  E-value: 1.63e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1083021138 125 PKLCNQCDSppCVQVCPVGA---TFKTRDGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAEK 186
Cdd:COG1143     1 EDKCIGCGL--CVRVCPVDAitiEDGEPGKVYVIDPDKCIGCGLCVEVCPTGAISMTPFELAVED 63
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
114-174 1.85e-06

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 48.32  E-value: 1.85e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083021138 114 QEKTVIRSFFVPKLCNQCDSppCVQVCPVGATFKTRDGVILVDSKRCIGCRYCLQACPYGA 174
Cdd:COG1148   484 LGVEPSVAEVDPEKCTGCGR--CVEVCPYGAISIDEKGVAEVNPALCKGCGTCAAACPSGA 542
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
149-213 5.92e-06

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 43.18  E-value: 5.92e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1083021138 149 RDGVILVDSKRCIGCRYCLQACPYGARFIDPRSRT--AEKCTFCYhrivkglvpACVEVCPSQARIF 213
Cdd:COG2768     2 SLGKPYVDEEKCIGCGACVKVCPVGAISIEDGKAVidPEKCIGCG---------ACIEVCPVGAIKI 59
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 152-210 6.03e-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: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 45.46  E-value: 6.03e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083021138 152 VILVDSKRCIGCRYCLQAC----PYGAR------FIDPRSRTAEKCTFCYHRIvkglVPACVEVCPSQA 210
Cdd:cd16369     3 EFFIDPSRCIGCRACVAACrecgTHRGKsmihvdYIDRGESTQTAPTVCMHCE----DPTCAEVCPADA 67
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 128-174 8.33e-06

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


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 43.12  E-value: 8.33e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1083021138 128 CNQCDSppCVQVCPVGATFKTRDGVILVDSKRCIGCRYCLQACPYGA 174
Cdd:COG1144    32 CIGCGL--CWIVCPDGAIRVDDGKYYGIDYDYCKGCGICAEVCPVKA 76
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
155-210 8.52e-06

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 46.39  E-value: 8.52e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 155 VDSKRCIGCRYCLQACPYGARFIDPRsRTAE----KCTFCyhrivkGlvpACVEVCPSQA 210
Cdd:COG1148   493 VDPEKCTGCGRCVEVCPYGAISIDEK-GVAEvnpaLCKGC------G---TCAAACPSGA 542
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 160-210 1.30e-05

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 41.74  E-value: 1.30e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 160 CIGCRYCLQACPYGARFIDPRSRT---------AEKCTFCYhrivkglvpACVEVCPSQA 210
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKkgtktvvidPERCVGCG---------ACVAVCPTGA 51
PRK13795 PRK13795
hypothetical protein; Provisional
 154-207 1.42e-05

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 45.76  E-value: 1.42e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1083021138 154 LVDSKRCIGCRYCLQACPYGARFIDPRSRT----AEKCTFCYhrivkglvpACVEVCP 207
Cdd:PRK13795  577 LRRAAECVGCGVCVGACPTGAIRIEEGKRKisvdEEKCIHCG---------KCTEVCP 625
NapF COG1145
Ferredoxin [Energy production and conversion];
155-210 1.99e-05

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 44.71  E-value: 1.99e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 155 VDSKRCIGCRYCLQACPYGA-RFIDPRSRT---AEKCTFCYhrivkglvpACVEVCPSQA 210
Cdd:COG1145   179 IDAEKCIGCGLCVKVCPTGAiRLKDGKPQIvvdPDKCIGCG---------ACVKVCPVGA 229
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 155-210 2.43e-05

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 41.57  E-value: 2.43e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1083021138 155 VDSKRCIGCRYCLQACPYGARFIDPRSRT--AEKCTFCYhrivkglvpACVEVCPSQA 210
Cdd:COG4231    19 IDEDKCTGCGACVKVCPADAIEEGDGKAVidPDLCIGCG---------SCVQVCPVDA 67
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 159-210 2.75e-05

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: 41.27  E-value: 2.75e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1083021138 159 RCIGCRYCLQACPYGARFIDPRSRT------AEKCTFCYhrivkglvpACVEVCPSQA 210
Cdd:COG1143     3 KCIGCGLCVRVCPVDAITIEDGEPGkvyvidPDKCIGCG---------LCVEVCPTGA 51
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 136-171 3.27e-05

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


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 43.83  E-value: 3.27e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1083021138 136 CVQVCPVGATFKTRDGVILVDSKRCIGCRYCLQACP 171
Cdd:COG2878   145 CIKACPFDAIVGAAKGMHTVDEDKCTGCGLCVEACP 180
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 153-210 3.83e-05

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 40.80  E-value: 3.83e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 153 ILVDSKRCIGCRYCLQACPYGA-RFIDPRSRT-AEKCTFCYHrivkglvpaCVEVCPSQA 210
Cdd:COG2221    10 PKIDEEKCIGCGLCVAVCPTGAiSLDDGKLVIdEEKCIGCGA---------CIRVCPTGA 60
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 153-210 4.20e-05

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 40.46  E-value: 4.20e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083021138 153 ILVDSKRCIGCRYCLQACPYGARFIDPRSRTA-----EKCTFCYhrivkglvpACVEVCPSQA 210
Cdd:COG1146     3 PVIDTDKCIGCGACVEVCPVDVLELDEEGKKAlvinpEECIGCG---------ACELVCPVGA 56
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 113-210 6.06e-05

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 41.36  E-value: 6.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 113 PQEKTVIRSFFVPKLCNQCdspPCVQVCPVGATFKtrdGVILVDSKRCIGCRYCLQACPYGARFIDPRSRTAE----KCT 188
Cdd:PRK08348    3 PLLPTVLRNLFKKPATNLF---PATEPVPVPEDFR---GKILYDVDKCVGCRMCVTVCPAGVFVYLPEIRKVAlwtgRCV 76

                          90       100
                  ....*....|....*....|..
gi 1083021138 189 FCYHrivkglvpaCVEVCPSQA 210
Cdd:PRK08348   77 FCGQ---------CVDVCPTGA 89
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 122-180 7.45e-05

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 40.08  E-value: 7.45e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083021138 122 FFVPKLCNQCDSppCVQVCPVGATFKTRDG--VILVDSKRCIGCRYCLQACPYGARFIDPR 180
Cdd:COG1146     4 VIDTDKCIGCGA--CVEVCPVDVLELDEEGkkALVINPEECIGCGACELVCPVGAITVEDD 62
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 125-210 8.22e-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: 8.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 125 PKLCNQCDSppCVQVCPVGATFKTRDGVI----LVDSKRCIGCRYCLQACPYGA-RFIDPRSRTA----------EKCTF 189
Cdd:cd10549     5 PEKCIGCGI--CVKACPTDAIELGPNGAIargpEIDEDKCVFCGACVEVCPTGAiELTPEGKEYVpkekeaeideEKCIG 82

                          90       100
                  ....*....|....*....|.
gi 1083021138 190 CyhrivkGLvpaCVEVCPSQA 210
Cdd:cd10549    83 C------GL---CVKVCPVDA 94
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 153-207 1.25e-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: 39.16  E-value: 1.25e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1083021138 153 ILVDSKRCIGCRYCLQACP---------YGARFIDPRSRTAEKCTFCYhrivkglvpACVEVCP 207
Cdd:pfam13237   2 VVIDPDKCIGCGRCTAACPagltrvgaiVERLEGEAVRIGVWKCIGCG---------ACVEACP 56
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 125-171 1.43e-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: 38.77  E-value: 1.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1083021138 125 PKLCNQCDSppCVQVCPVGAT------FKTRDGVILVDSKRCIGCRYCLQACP 171
Cdd:pfam13237   6 PDKCIGCGR--CTAACPAGLTrvgaivERLEGEAVRIGVWKCIGCGACVEACP 56
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 56-210 1.66e-04

NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. 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 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: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 40.69  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  56 IDKCIGCGRCADACkkendvPTGPFffrtwieryVILEGGEVVVDSPNGGldgfklqpqektvirsffvpklCNQCDSpp 135
Cdd:cd10564    12 LDLCTRCGDCVEAC------PEGII---------VRGDGGFPELDFSRGE----------------------CTFCGA-- 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 136 CVQVCPVGAtFKTRDG----VILVDSKRC-----IGCRYCLQACPYGA-RFIDPRSRTA------EKCTFCyhrivkGlv 199
Cdd:cd10564    53 CAEACPEGA-LDPAREapwpLRAEIGDSClalqgVECRSCQDACPTQAiRFRPRLGGIAlpeldaDACTGC------G-- 123

                         170
                  ....*....|.
gi 1083021138 200 pACVEVCPSQA 210
Cdd:cd10564   124 -ACVSVCPVGA 133
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 143-210 2.24e-04

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


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 38.88  E-value: 2.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083021138 143 GATFKTRD---GVILVDSKRCIGCRYCLQACPYGArfIDPRSRTA-----EKCTFCyhrivkGLvpaCVEVCPSQA 210
Cdd:COG1144    12 TAAYKTGGwrvERPVVDEDKCIGCGLCWIVCPDGA--IRVDDGKYygidyDYCKGC------GI---CAEVCPVKA 76
napG PRK09476
quinol dehydrogenase periplasmic component; Provisional
 7-171 2.39e-04

quinol dehydrogenase periplasmic component; Provisional


Pssm-ID: 236534 [Multi-domain]  Cd Length: 254  Bit Score: 41.53  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138   7 QRREFLRQLllscFSLGGILAGKGTAGPAVSRSAEEYdprshswgmGIAI------------DKCIGCGRCADAC----- 69
Cdd:PRK09476   10 GRRRFLRDV----VRTAGGLAAVGVALGLQQQQARAS---------GVALrppgalnendflSACIRCGLCVQACpydtl 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  70 ---KKENDVPTG-PFFfrtwIERyvileggevvvDSPnggldgfklqpqektvirsffvpklCNQCDSPPCVQVCPVGA- 144
Cdd:PRK09476   77 klaTLASGLSAGtPYF----VAR-----------DIP-------------------------CEMCEDIPCVKACPSGAl 116

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1083021138 145 ------TFKTRDGV-ILVDSKRCIG-----CRYCLQACP 171
Cdd:PRK09476  117 drelvdIDDARMGLaVLVDQENCLNfqglrCDVCYRVCP 155
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 55-143 3.21e-04

Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 41.60  E-value: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  55 AIDKCIGCGRCADAC------KKENDVPTG-PFFFRTWIERYVILEGGEVVVDSpnggLDgfklqpqektvirsffvpkL 127
Cdd:COG0247    76 ALDACVGCGFCRAMCpsykatGDEKDSPRGrINLLREVLEGELPLDLSEEVYEV----LD-------------------L 132

                          90
                  ....*....|....*.
gi 1083021138 128 CNQCDSppCVQVCPVG 143
Cdd:COG0247   133 CLTCKA--CETACPSG 146
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 128-174 3.81e-04

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: 37.51  E-value: 3.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1083021138 128 CNQCDSppCVQVCPVGA------TFKTRDGVILVDSKRCIGCRYCLQACPYGA 174
Cdd:pfam12838   1 CIGCGA--CVAACPVGAitldevGEKKGTKTVVIDPERCVGCGACVAVCPTGA 51
Fer4_9 pfam13187
4Fe-4S dicluster domain;
159-210 4.72e-04

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 37.15  E-value: 4.72e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1083021138 159 RCIGCRYCLQACPYGA------RFIDPRSRTAEKCTFCYhrivkglvpACVEVCPSQA 210
Cdd:pfam13187   1 KCTGCGACVAACPAGAivpdlvGQTIRGDIAGLACIGCG---------ACVDACPRGA 49
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
59-210 5.07e-04

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 40.69  E-value: 5.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  59 CIGCGRCADACkkendvptgPFffrtwieRYVILEGGEVVVDS-------------PNGGLDgfkLQPQEKTVirsfFVP 125
Cdd:PRK07118  141 CLGLGSCVAAC---------PF-------DAIHIENGLPVVDEdkctgcgacvkacPRNVIE---LIPKSARV----FVA 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 126 klCNQCDSPPCV-QVCPVGatfktrdgvilvdskrCIGCRYCLQACPYGA-------RFIDPrsrtaEKCTFCyhrivkg 197
Cdd:PRK07118  198 --CNSKDKGKAVkKVCEVG----------------CIGCGKCVKACPAGAitmennlAVIDQ-----EKCTSC------- 247

                         170
                  ....*....|...
gi 1083021138 198 lvPACVEVCPSQA 210
Cdd:PRK07118  248 --GKCVEKCPTKA 258
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 152-210 6.29e-04

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


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 39.40  E-value: 6.29e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1083021138 152 VILVDSKRCIGCRYCLQACPY-----GARFIdpRSRTAEKCTFCyhrivkglvPACVEVCPSQA 210
Cdd:TIGR01944 107 VALIDEDNCIGCTKCIQACPVdaivgAAKAM--HTVIADECTGC---------DLCVEPCPTDC 159
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 127-174 7.01e-04

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 40.63  E-value: 7.01e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1083021138 127 LCNQCDSppCVQVCPVGATFKTRDGV-ILVDSKRCIGCRYCLQACPYGA 174
Cdd:PRK12771  511 NCFECDN--CYGACPQDAIIKLGPGRrYHFDYDKCTGCHICADVCPCGA 557
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 159-210 7.82e-04

NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes "I" subunits from the closely related F420H2 dehydrogenase and formate hydrogenlyase complexes. [Energy metabolism, Electron transport]


Pssm-ID: 273902 [Multi-domain]  Cd Length: 122  Bit Score: 38.55  E-value: 7.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1083021138 159 RCIGCRYCLQACPYGARFIDPRSRTAEK------------CTFCyhrivkGLvpaCVEVCPSQA 210
Cdd:TIGR01971  44 KCIGCTLCAAVCPADAIRVVPAEGEDGKrrlkfyeinfgrCIFC------GL---CEEACPTDA 98
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 158-210 1.00e-03

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 38.78  E-value: 1.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1083021138 158 KRCIGCRYCLQACPYGARF---------------IDPRSRtaeKCTFCYHrivkglvpACVEVCPSQA 210
Cdd:cd16373    14 ALCIRCGLCVEACPTGVIQpagledgleggrtpyLDPREG---PCDLCCD--------ACVEVCPTGA 70
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
153-210 1.33e-03

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 38.10  E-value: 1.33e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083021138 153 ILVDSKRCIGCRYCLQACPY---GARFIDPRSR----------TAEKCTFCYHRivkglvpACVEVCPSQA 210
Cdd:COG1142     5 IIADPEKCIGCRTCEAACAVaheGEEGEPFLPRirvvrkagvsAPVQCRHCEDA-------PCAEVCPVGA 68
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
159-207 2.07e-03

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 37.94  E-value: 2.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1083021138 159 RCIGCRYCLQACPYGARFIDPRSRTA------------EKCTFCyhrivkGLvpaCVEVCP 207
Cdd:PRK05888   59 RCIACKLCAAICPADAITIEAAEREDgrrrttrydinfGRCIFC------GF---CEEACP 110
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 160-207 2.53e-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: 38.44  E-value: 2.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1083021138 160 CIGCRYCLQACPYGARFIDPRSRT---AEKCTFCyhrivkGLvpaCVEVCP 207
Cdd:COG2878   139 CIGCGDCIKACPFDAIVGAAKGMHtvdEDKCTGC------GL---CVEACP 180
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 153-210 2.56e-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: 36.99  E-value: 2.56e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138 153 ILVDSKRCIGCRYCLQACPYGA------------RFIDPrsrtaEKCTFCYhrivkglvpACVEVCPSQA 210
Cdd:cd10549     1 LKYDPEKCIGCGICVKACPTDAielgpngaiargPEIDE-----DKCVFCG---------ACVEVCPTGA 56
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 99-171 2.91e-03

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: 37.47  E-value: 2.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1083021138  99 VDSPNGGLDGFKLQPQEKTVirSFFVPKLCNQCDSppCVQVCPVGATFKTRDGVILVDSKRCIGCRYCLQACP 171
Cdd:TIGR01944  88 VEPIPQPLDADAGTIQPPMV--ALIDEDNCIGCTK--CIQACPVDAIVGAAKAMHTVIADECTGCDLCVEPCP 156
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 125-174 3.06e-03

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 38.61  E-value: 3.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1083021138 125 PKLCNQcdspPCVQVCPV---GA---TFKTRDGVILVDSKRCIGCRYCLQACPYGA 174
Cdd:COG1245    14 PKKCNY----ECIKYCPVnrtGKeaiEIDEDDGKPVISEELCIGCGICVKKCPFDA 65
PRK06991 PRK06991
electron transport complex subunit RsxB;
152-207 5.82e-03

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 37.08  E-value: 5.82e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1083021138 152 VILVDSKRCIGCRYCLQACPYGARFIDPRSR---TAEKCTFCyhrivkglvPACVEVCP 207
Cdd:PRK06991   79 VAVIDEQLCIGCTLCMQACPVDAIVGAPKQMhtvLADLCTGC---------DLCVPPCP 128
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 157-210 6.61e-03

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


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 37.15  E-value: 6.61e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1083021138 157 SKRCIGCRYCLQACPYGA-RFIDPRSRTAEKCTFCYhrivkglvpACVEVCPSQA 210
Cdd:NF038196  184 TDKCIGCGICAKVCPVNNiEMEDGKPVWGHNCTHCL---------ACIHRCPKEA 229
Fer4_9 pfam13187
4Fe-4S dicluster domain;
128-174 7.57e-03

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 33.68  E-value: 7.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1083021138 128 CNQCDSppCVQVCPVGATFKTRDGVILV---DSKRCIGCRYCLQACPYGA 174
Cdd:pfam13187   2 CTGCGA--CVAACPAGAIVPDLVGQTIRgdiAGLACIGCGACVDACPRGA 49
PRK00783 PRK00783
DNA-directed RNA polymerase subunit D; Provisional
 124-174 8.02e-03

DNA-directed RNA polymerase subunit D; Provisional


Pssm-ID: 234837 [Multi-domain]  Cd Length: 263  Bit Score: 36.79  E-value: 8.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1083021138 124 VPKLCNQCDSppCVQVCPVGATFKTRDGVILVDSKRCIGCRYCLQACPYGA 174
Cdd:PRK00783  167 VSEDCDECEK--CVEACPRGVLELKEGKLVVTDLLNCSLCKLCERACPGKA 215
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 57-144 8.36e-03

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 34.25  E-value: 8.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083021138  57 DKCIGCGRCADACKKEndvptgpfffrtwierYVILEGGEVVVDspnggldgfklqpqektvirsffvPKLCNQCDSppC 136
Cdd:COG4231    22 DKCTGCGACVKVCPAD----------------AIEEGDGKAVID------------------------PDLCIGCGS--C 59


                  ....*...
gi 1083021138 137 VQVCPVGA 144
Cdd:COG4231    60 VQVCPVDA 67
PRK06273 PRK06273
ferredoxin; Provisional
 155-215 9.41e-03

ferredoxin; Provisional


Pssm-ID: 235764 [Multi-domain]  Cd Length: 165  Bit Score: 35.84  E-value: 9.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1083021138 155 VDSKRCIGCRYCLQACPYGA---------RFIDPRSRT------AEKCTFCYHrivkglvpaCVEVCPSQArIFGE 215
Cdd:PRK06273   46 VFEELCIGCGGCANVCPTKAiemipvepvKITEGYVKTkipkidYEKCVYCLY---------CHDFCPVFA-LFNE 111
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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