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Conserved domains on  [gi|1040425976|gb|OBS99447|]
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4Fe-4S ferredoxin [Vibrio tasmaniensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK14993 super family cl28925
tetrathionate reductase subunit TtrB;
1-251 1.26e-131

tetrathionate reductase subunit TtrB;


The actual alignment was detected with superfamily member PRK14993:

Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 372.67  E-value: 1.26e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976   1 MDSLKRRFLSQFGKVSAGAALIPITGINTAVastairnnnQPDRK-GEVGKRYAMAIDLRKCVGCQACTVGCSVENQAPI 79
Cdd:PRK14993    1 MDSSKRQFLQQLGVLTAGASLVPLAEAKFPF---------SPERHeGSPRHRYAMLIDLRRCIGCQSCTVSCTIENQTPQ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  80 GQFRTTVKQYEVSLddgsTAQQDVKSFMLPRLCNHCDNAPCIKVCPVQATFQREDGIVMVDNERCVACAYCVQACPYDAR 159
Cdd:PRK14993   72 GAFRTTVNQYQVQR----EGSQEVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDAR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 160 FINNDTLTADKCTFCAHRLEDGLLPACVETCVGGARVIGDLKDPNSEINRLLNENQDDIKVLKPEQNTNPHVFYIGMNER 239
Cdd:PRK14993  148 FINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRIATMLHQHRDAIKVLKPENGTSPHVFYLGLDDA 227

                         250
                  ....*....|....
gi 1040425976 240 FVSHIEG--QPAIY 251
Cdd:PRK14993  228 FVTPLMGraQPALW 241
 
Name Accession Description Interval E-value
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
1-251 1.26e-131

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 372.67  E-value: 1.26e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976   1 MDSLKRRFLSQFGKVSAGAALIPITGINTAVastairnnnQPDRK-GEVGKRYAMAIDLRKCVGCQACTVGCSVENQAPI 79
Cdd:PRK14993    1 MDSSKRQFLQQLGVLTAGASLVPLAEAKFPF---------SPERHeGSPRHRYAMLIDLRRCIGCQSCTVSCTIENQTPQ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  80 GQFRTTVKQYEVSLddgsTAQQDVKSFMLPRLCNHCDNAPCIKVCPVQATFQREDGIVMVDNERCVACAYCVQACPYDAR 159
Cdd:PRK14993   72 GAFRTTVNQYQVQR----EGSQEVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDAR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 160 FINNDTLTADKCTFCAHRLEDGLLPACVETCVGGARVIGDLKDPNSEINRLLNENQDDIKVLKPEQNTNPHVFYIGMNER 239
Cdd:PRK14993  148 FINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRIATMLHQHRDAIKVLKPENGTSPHVFYLGLDDA 227

                         250
                  ....*....|....
gi 1040425976 240 FVSHIEG--QPAIY 251
Cdd:PRK14993  228 FVTPLMGraQPALW 241
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 54-234 6.44e-96

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: 279.80  E-value: 6.44e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  54 MAIDLRKCVGCQACTVGCSVENQAPIGQFRTTVKQYEVSLDDgstaqqDVKSFMLPRLCNHCDNAPCIKVCPVQATFQRE 133
Cdd:cd10551     1 MVIDLRKCIGCGACVVACKAENNVPPGVFRNRVLEYEVGEYP------NVKRTFLPVLCNHCENPPCVKVCPTGATYKRE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 134 DGIVMVDNERCVACAYCVQACPYDARFINNDTL------------TADKCTFCAHRLEDGLLPACVETCVGGARVIGDLK 201
Cdd:cd10551    75 DGIVLVDYDKCIGCRYCMAACPYGARYFNPEEPhefgevpvrpkgVVEKCTFCYHRLDEGLLPACVEACPTGARIFGDLD 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1040425976 202 DPNSEINRLLNENQddIKVLKPEQNTNPHVFYI 234
Cdd:cd10551   155 DPNSEVSKLLAERR--AYVLKPELGTKPKVYYI 185
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 49-234 1.65e-84

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 251.02  E-value: 1.65e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  49 GKRYAMAIDLRKCVGCQACTVGCSVENQAPIGQFRTTVKQYEVSLDDgstaqqDVKSFMLPRLCNHCDNAPCIKVCPVQA 128
Cdd:COG0437     3 MKRYGMVIDLTKCIGCRACVVACKEENNLPVGVTWRRVRRYEEGEFP------NVEWLFVPVLCNHCDDPPCVKVCPTGA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 129 TFQREDGIVMVDNERCVACAYCVQACPYDARFINNDTLTADKCTFCAHRLEDGLLPACVETCVGGARVIGDLKDPNSEIN 208
Cdd:COG0437    77 TYKREDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVEACPTGALVFGDLDDPESEVS 156

                         170       180
                  ....*....|....*....|....*.
gi 1040425976 209 RLLNENQDdiKVLKPEQNTNPHVFYI 234
Cdd:COG0437   157 KRLAELPA--YRLLPELGTKPSVYYL 180
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 103-200 9.17e-35

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


Pssm-ID: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 120.82  E-value: 9.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 103 VKSFMLPRLCNHCDNAPCIKVCPVQATFQRE-DGIVMVDNERCVACAYCVQACPYDARFINNDTLTADKCTFCAHRLEDG 181
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPVGAIYKDEeTGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAG 80

                          90
                  ....*....|....*....
gi 1040425976 182 LLPACVETCVGGARVIGDL 200
Cdd:pfam13247  81 LLPACVQTCPTGAMNFGDR 99
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 136-190 9.10e-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: 39.01  E-value: 9.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 136 IVMVDNERCVACAYCVQACPYDA-----RFINndTLTADKCTFCAhrledgllpACVETC 190
Cdd:TIGR01944 107 VALIDEDNCIGCTKCIQACPVDAivgaaKAMH--TVIADECTGCD---------LCVEPC 155
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 112-158 5.48e-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: 37.53  E-value: 5.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1040425976 112 CNHCdnAPCIKVCPVQAtfqredgIVMVDN-----ERCVACAYCVQACPYDA 158
Cdd:NF038196  187 CIGC--GICAKVCPVNN-------IEMEDGkpvwgHNCTHCLACIHRCPKEA 229
 
Name Accession Description Interval E-value
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
1-251 1.26e-131

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 372.67  E-value: 1.26e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976   1 MDSLKRRFLSQFGKVSAGAALIPITGINTAVastairnnnQPDRK-GEVGKRYAMAIDLRKCVGCQACTVGCSVENQAPI 79
Cdd:PRK14993    1 MDSSKRQFLQQLGVLTAGASLVPLAEAKFPF---------SPERHeGSPRHRYAMLIDLRRCIGCQSCTVSCTIENQTPQ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  80 GQFRTTVKQYEVSLddgsTAQQDVKSFMLPRLCNHCDNAPCIKVCPVQATFQREDGIVMVDNERCVACAYCVQACPYDAR 159
Cdd:PRK14993   72 GAFRTTVNQYQVQR----EGSQEVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDAR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 160 FINNDTLTADKCTFCAHRLEDGLLPACVETCVGGARVIGDLKDPNSEINRLLNENQDDIKVLKPEQNTNPHVFYIGMNER 239
Cdd:PRK14993  148 FINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRIATMLHQHRDAIKVLKPENGTSPHVFYLGLDDA 227

                         250
                  ....*....|....
gi 1040425976 240 FVSHIEG--QPAIY 251
Cdd:PRK14993  228 FVTPLMGraQPALW 241
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 54-234 6.44e-96

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: 279.80  E-value: 6.44e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  54 MAIDLRKCVGCQACTVGCSVENQAPIGQFRTTVKQYEVSLDDgstaqqDVKSFMLPRLCNHCDNAPCIKVCPVQATFQRE 133
Cdd:cd10551     1 MVIDLRKCIGCGACVVACKAENNVPPGVFRNRVLEYEVGEYP------NVKRTFLPVLCNHCENPPCVKVCPTGATYKRE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 134 DGIVMVDNERCVACAYCVQACPYDARFINNDTL------------TADKCTFCAHRLEDGLLPACVETCVGGARVIGDLK 201
Cdd:cd10551    75 DGIVLVDYDKCIGCRYCMAACPYGARYFNPEEPhefgevpvrpkgVVEKCTFCYHRLDEGLLPACVEACPTGARIFGDLD 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1040425976 202 DPNSEINRLLNENQddIKVLKPEQNTNPHVFYI 234
Cdd:cd10551   155 DPNSEVSKLLAERR--AYVLKPELGTKPKVYYI 185
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 49-234 1.65e-84

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 251.02  E-value: 1.65e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  49 GKRYAMAIDLRKCVGCQACTVGCSVENQAPIGQFRTTVKQYEVSLDDgstaqqDVKSFMLPRLCNHCDNAPCIKVCPVQA 128
Cdd:COG0437     3 MKRYGMVIDLTKCIGCRACVVACKEENNLPVGVTWRRVRRYEEGEFP------NVEWLFVPVLCNHCDDPPCVKVCPTGA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 129 TFQREDGIVMVDNERCVACAYCVQACPYDARFINNDTLTADKCTFCAHRLEDGLLPACVETCVGGARVIGDLKDPNSEIN 208
Cdd:COG0437    77 TYKREDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVEACPTGALVFGDLDDPESEVS 156

                         170       180
                  ....*....|....*....|....*.
gi 1040425976 209 RLLNENQDdiKVLKPEQNTNPHVFYI 234
Cdd:COG0437   157 KRLAELPA--YRLLPELGTKPSVYYL 180
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 56-198 1.09e-48

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: 158.11  E-value: 1.09e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  56 IDLRKCVGCQACTVGCSVENQAPIGQFRTTVKQYEvsldDGSTaqQDVKSFMLPRLCNHCDNAPCIKVCPVQATFQREDG 135
Cdd:cd16371     4 FDQERCIGCKACEIACKDKNDLPPGVNWRRVYEYE----GGEF--PEVFAYFLSMSCNHCENPACVKVCPTGAITKREDG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040425976 136 IVMVDNERCVACAYCVQACPYDARFINNDTLTADKCTFCAHRLEDGLLPACVETCVGGARVIG 198
Cdd:cd16371    78 IVVVDQDKCIGCGYCVWACPYGAPQYNPETGKMDKCDMCVDRLDEGEKPACVAACPTRALDFG 140
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 54-236 1.13e-46

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


Pssm-ID: 319874 [Multi-domain]  Cd Length: 186  Bit Score: 154.41  E-value: 1.13e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  54 MAIDLRKCVGCQACTVGCSVEN-----------QAPIGQFRTTVKQYEvsldDGSTAQQDVKsfMLPRLCNHCDNAPCIK 122
Cdd:cd10552     1 LVIDVAKCNGCYNCFLACKDEHvgndwpgyaapQPRHGHFWMRILRRE----RGQYPKVDVA--YLPVPCNHCDNAPCIK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 123 VCPVQATFQREDGIVMVDNERCVACAYCVQACPYDARFINNDTLTADKCTFCAHRLEDG-LLPACVETCVGGARVIGDLK 201
Cdd:cd10552    75 AAKDGAVYKRDDGIVIIDPEKAKGQKQLVDACPYGAIYWNEELQVPQKCTFCAHLLDDGwKEPRCVQACPTGALRFGKLE 154

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1040425976 202 DPNSEINRLlnenQDDIKVLKPEQNTNPHVFYIGM 236
Cdd:cd10552   155 DEEMAAKAA----EEGLEVLHPELGTKPRVYYKNL 185
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 54-198 3.56e-46

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: 151.39  E-value: 3.56e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  54 MAIDLRKCVGCQACTVGCSVENQAPIGQFRTTVKQYEVslddgstaqQDVKSFMLPRLCNHCDNAPCIKVCPVQATFQRE 133
Cdd:cd04410     1 LVVDLDRCIGCGTCEVACKQEHGLRPGPDWSRIKVIEG---------GGLERAFLPVSCMHCEDPPCVKACPTGAIYKDE 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040425976 134 DGIVMVDNERCVACAYCVQACPYDARFINNDTLTADKCTFCAHRLEDGLLPACVETCVGGARVIG 198
Cdd:cd04410    72 DGIVLIDEDKCIGCGSCVEACPYGAIVFDPEPGKAVKCDLCGDRLDEGLEPACVKACPTGALTFG 136
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 48-234 1.08e-44

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: 153.23  E-value: 1.08e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  48 VGKRYAMAIDLRKCVGCQACTVGC----------------SVENQAPIGqfrtTVKQYEV-----------------SLD 94
Cdd:cd10555     1 SKRQLAMVMDLNKCIGCQTCTVACktlwtnrngreymywnNVETQPGKG----YPKNWEKkgggfkdkgelkpgiipTLE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  95 D--------------GSTAQQDVKS-------------------------FMLPRLCNHCDNAPCIKVCPVQATFQR-ED 134
Cdd:cd10555    77 DygvpweynheeelfEGKGGRVRPSpkgdptwgpnwdedqgageypnsyyFYLPRICNHCTNPACLAACPRKAIYKReED 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 135 GIVMVDNERCVACAYCVQACPYDARFINNDTLTADKCTFCAHRLEDGLLPACVETCVGGARVIGDLKDPNSEINRLLNEn 214
Cdd:cd10555   157 GIVLVDQDRCRGYRYCVEACPYKKIYFNPVEQKSEKCIFCYPRIEKGVAPACARQCVGRIRFVGYLDDEESPVYKLVKK- 235

                         250       260
                  ....*....|....*....|...
gi 1040425976 215 qddIKV---LKPEQNTNPHVFYI 234
Cdd:cd10555   236 ---WKValpLHPEYGTEPNVFYV 255
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 54-198 2.04e-38

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


Pssm-ID: 319888 [Multi-domain]  Cd Length: 156  Bit Score: 132.14  E-value: 2.04e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  54 MAIDLRKCVGCQACTVGCSVENQAP--IGQFR--------------TTVKQYEVSLDDGstaqqDVKSFMLPRLCNHCDN 117
Cdd:cd16366     1 FLVDTSRCTGCRACQVACKQWNGLPaeKTEFTgsyqnppdltahtwTLVRFYEVEKPGG-----DLSWLFRKDQCMHCTD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 118 APCIKVCPVQATFQREDGIVMVDNERCVACAYCVQACPYDARFINNDTLTADKCTFCAHRLEDGLLPACVETCVGGARVI 197
Cdd:cd16366    76 AGCLAACPTGAIIRTETGTVVVDPETCIGCGYCVNACPFDIPRFDEETGRVAKCTLCYDRISNGLQPACVKTCPTGALTF 155


                  .
gi 1040425976 198 G 198
Cdd:cd16366   156 G 156
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 54-199 9.69e-38

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


Pssm-ID: 319884 [Multi-domain]  Cd Length: 161  Bit Score: 130.50  E-value: 9.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  54 MAIDLRKCVGCQACTVGCSVENQAP------IGQF----------RTTVKQYEVSLDDGstaqqDVKSFMLPRLCNHCDN 117
Cdd:cd10562     1 MLVDTSKCTACRGCQVACKQWNQLPaektpfTGSYqnppdltpntWTLIRFYEHEEDNG-----GIRWLFRKRQCMHCTD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 118 APCIKVCPVQATFQREDGIVMVDNERCVACAYCVQACPYDARFINNDTLTADKCTFCAHRLEDGLLPACVETCVGGARVI 197
Cdd:cd10562    76 AACVKVCPTGALYKTENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCFDRIENGMQPACVKTCPTGALTF 155


                  ..
gi 1040425976 198 GD 199
Cdd:cd10562   156 GD 157
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 50-234 1.53e-37

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: 131.55  E-value: 1.53e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  50 KRYAMAIDLRKCVGCQACTVGCSVENQAPIGQFRTTVKQYEVSLDDGSTAQQDVKS----------FMLPRLCNHCDNAP 119
Cdd:cd16365     1 KQFAAVFNLNKCIGCQTCTVACKNAWTYRKGQEYMWWNNVETKPGGGYPQDWEVKTidnggntrffFYLQRLCNHCTNPA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 120 CIKVCPVQATFQR-EDGIVMVDNERCVACAYCVQACPYDARFINNDTLTADKCTFCAHRLEDGLLPACVETCVGGARVIG 198
Cdd:cd16365    81 CLAACPRGAIYKReEDGIVLIDQKRCRGYRKCVEQCPYKKIYFNGLSRVSEKCIACYPRIEGGDPTRCMSACVGRIRLQG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1040425976 199 DLKD-PNSEINRLLNENQDDIKvLKPEQNTNPHVFYI 234
Cdd:cd16365   161 FLDDnPKSPVTKLIRHWKVALP-LHPEYGTEPNIYYV 196
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 53-199 7.99e-36

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: 126.94  E-value: 7.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  53 AMAIDLRKCVGCQACTVGCSVENQAPIGQF----------------RTTVKQYEVslDDGSTAQQDVKsfmlpRLCNHCD 116
Cdd:cd10561     1 GVLYDTTRCIGCRACEVACKEWNGLPAEDTafgpgwdnprdlsaktYTVIKRYEV--ETGGKGFVFVK-----RQCMHCL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 117 NAPCIKVCPVQATFQREDGIVMVDNERCVACAYCVQACPYDA-RFINNDTL-TADKCTFCAHRLEDGLLPACVETCVGGA 194
Cdd:cd10561    74 DPACVSACPVGALRKTPEGPVTYDEDKCIGCRYCMVACPFNIpKYEWDSANpKIRKCTMCYDRLKEGKQPACVEACPTGA 153


                  ....*
gi 1040425976 195 RVIGD 199
Cdd:cd10561   154 LLFGK 158
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 103-200 9.17e-35

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


Pssm-ID: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 120.82  E-value: 9.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 103 VKSFMLPRLCNHCDNAPCIKVCPVQATFQRE-DGIVMVDNERCVACAYCVQACPYDARFINNDTLTADKCTFCAHRLEDG 181
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPVGAIYKDEeTGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAG 80

                          90
                  ....*....|....*....
gi 1040425976 182 LLPACVETCVGGARVIGDL 200
Cdd:pfam13247  81 LLPACVQTCPTGAMNFGDR 99
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 56-208 4.28e-34

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


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 120.46  E-value: 4.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  56 IDLRKCVGCQACTVGCSVENQapiGQFRTTVKQYEvslddgstaqqdvKSFMLPRLCNHCDNAPCIKVCPVQATFQREDG 135
Cdd:cd16374     3 VDPERCIGCRACEIACAREHS---GKPRISVEVVE-------------DLASVPVRCRHCEDAPCMEVCPTGAIYRDEDG 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040425976 136 IVMVDNERCVACAYCVQACPYDARFINNDTLTADKCTFCAHRLEDGLLPACVETCVGGARVIGDLKDPNSEIN 208
Cdd:cd16374    67 AVLVDPDKCIGCGMCAMACPFGVPRFDPSLKVAVKCDLCIDRRREGKLPACVEACPTGALKFGDIEELLKEKR 139
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 104-198 6.63e-34

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: 126.32  E-value: 6.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 104 KSFM--LPRLCNHCDNAPCIKVCPVQATFQR-EDGIVMVDNERCVACAYCVQACPYDARFINNDTLTADKCTFCAHRLED 180
Cdd:cd10557   169 NTFMfyLPRICNHCLNPACVAACPSGAIYKReEDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSEKCIFCYPRLEA 248

                          90
                  ....*....|....*...
gi 1040425976 181 GLLPACVETCVGGARVIG 198
Cdd:cd10557   249 GQPTVCSETCVGRIRYLG 266
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 53-202 9.56e-33

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


Pssm-ID: 319882 [Multi-domain]  Cd Length: 225  Bit Score: 119.80  E-value: 9.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  53 AMAIDLRKCVGCQACTVGCSVENQAPIGQFRTTVKQYEVSLDDGST------------------AQQDVKSFMLPRLCNH 114
Cdd:cd10560     1 GFFTDTSICIGCKACEVACKQWNQLPADGYDFSGMSYDNTGDLSAStwrhvkfierptedgpanEGGDLQWLFMSDVCKH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 115 CDNAPCIKVCPVQATFQREDGIVMVDNERCVACAYCVQACPYDARFINNDTLTADKCTFCAHRLEDGLLPACVETCVGGA 194
Cdd:cd10560    81 CTDAGCLEACPTGAIFRTEFGTVYIQPDICNGCGYCVAACPFGVIDRNEETGRAHKCTLCYDRLKDGLEPACAKACPTGS 160


                  ....*...
gi 1040425976 195 RVIGDLKD 202
Cdd:cd10560   161 IQFGPLEE 168
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 50-234 2.20e-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: 120.26  E-value: 2.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  50 KRYAMAIDLRKCVGCQACTVGC----------------SVENQaPIGQF------RTTVKQYEVSLDDGST--------- 98
Cdd:cd10556    10 KQFAMVFDTNKCIACQTCTMACkstwtsgkgqeymwwnNVETK-PYGGYplgwdvRLLDEEGGQTWAEGGVyegktifea 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  99 ------------AQQDVKS---------------------------FMLPRLCNHCDNAPCIKVCPVQATFQR-EDGIVM 138
Cdd:cd10556    89 aaageqvlgyrpEDEDWRYpnigedevngertpdtgsslpphpiwfFYLPRICNHCTYPACLAACPRKAIYKReEDGIVL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 139 VDNERCVACAYCVQACPYDARFINNDTLTADKCTFCAHRLEDGLLPACVETCVGGARVIGDLKDPNSEINRLLNENQDDI 218
Cdd:cd10556   169 IDQERCRGYRECVEACPYKKPMYNPTTRVSEKCIGCYPRIEEGDQTQCVSACIGKIRLQGFINTPPDARWADDRDNPIDF 248

                         250       260
                  ....*....|....*....|....
gi 1040425976 219 KV--------LKPEQNTNPHVFYI 234
Cdd:cd10556   249 LVhikkvalpLYPQFGTEPNVYYI 272
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 51-194 3.44e-32

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: 115.92  E-value: 3.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  51 RYAMAIDLRKCVGCQACTVGCSVENQAPIGQFRTTVKQYEVSLDDGstaqqdvksfmLPRL------CNHCDNAPCIKVC 124
Cdd:cd10553     2 KYYLYHDSKRCIGCLACEVHCKVKNNLPVGPRLCRIFAVGPKMVGG-----------KPRLkfvymsCFHCENPWCVKAC 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040425976 125 PVQATFQRE-DGIVMVDNERCVACAYCVQACPYDARFINNDTLTADKCTFCAHRLEDGLLPACVETCVGGA 194
Cdd:cd10553    71 PTGAMQKREkDGIVYVDQELCIGCKACIEACPWGIPQWNPATGKVVKCDYCMDRIDQGLKPACVTGCTTHA 141
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 104-198 2.65e-30

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


Pssm-ID: 440755 [Multi-domain]  Cd Length: 485  Bit Score: 118.37  E-value: 2.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 104 KSFM--LPRLCNHCDNAPCIKVCPVQATFQR-EDGIVMVDNERCVACAYCVQACPYDARFINNDTLTADKCTFCAHRLED 180
Cdd:COG1140   172 NTFMfyLPRICEHCLNPACVASCPSGAIYKReEDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGKAEKCIFCYPRIEA 251

                          90
                  ....*....|....*...
gi 1040425976 181 GLLPACVETCVGGARVIG 198
Cdd:COG1140   252 GQPTVCSETCVGRIRYLG 269
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 53-202 3.35e-30

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: 112.48  E-value: 3.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  53 AMAIDLRKCVGCQACTVGCSV--ENQAPIGQFRTTvkqYEvslddgSTAQQDVKSFMLPRL-----------------CN 113
Cdd:cd10558     1 AKLIDVSKCIGCKACQVACKEwnDLRAEVGHNVGT---YQ------NPADLSPETWTLMKFrevedngklewlirkdgCM 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 114 HCDNAPCIKVCPVQ-ATFQREDGIVMVDNERCVACAYCVQACPYDARFINNDTLTADKCTFCAHRLEDGLLPACVETCVG 192
Cdd:cd10558    72 HCADPGCLKACPSPgAIVQYANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVGLEPACVKTCPT 151

                         170
                  ....*....|
gi 1040425976 193 GARVIGDLKD 202
Cdd:cd10558   152 GALHFGTKED 161
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
5-247 2.80e-29

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 113.23  E-value: 2.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976   5 KRRFLsqfgKVSAGAALipitGINTAVASTAIRNNNQPDRKGEVGkryaMAIDLRKCVGCQACTVGCSVEN--------- 75
Cdd:PRK10882    3 RRNFL----KAASAGAL----LAGALPSVSHAAAENRPPIPGALG----MLYDSTLCVGCQACVTKCQEINfpernpqge 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  76 ---QAPI---GQFRTTVKQYEVSLDDGSTAQQDVKSFMlPRLCNHCDNAPCIKVCPVQA-TFQREDGIVMVDNERCVACA 148
Cdd:PRK10882   71 qtwDNPDklsPYTNNIIKVWKSGTGVNKDQEENGYAYI-KKQCMHCVDPNCVSVCPVSAlTKDPKTGIVHYDKDVCTGCR 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 149 YCVQACPYDA-RFINNDTLTA-DKCTFCAH----RLEDGLLPACVETCVGGARVIGDLKDPNSEINRLLNENQDDiKVLK 222
Cdd:PRK10882  150 YCMVACPFNVpKYDYNNPFGAiHKCELCNQkgveRLDKGGLPGCVEVCPTGAVIFGTREELLAEAKRRLALKPGS-EYHY 228

                         250       260
                  ....*....|....*....|....*
gi 1040425976 223 PEQNTNPHVFYIGMNERFVSHIEGQ 247
Cdd:PRK10882  229 PRQTLKSGDTYLHTVPKYYPHVYGE 253
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 54-194 5.27e-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: 101.88  E-value: 5.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  54 MAIDLRKCVGCQACTVGCSVENQapiGQF-----RTTVKQYEVSLDDgstaqqdvksfmLPRLCNHCDNAPCIKVCPVQA 128
Cdd:cd10550     1 LVVDPEKCTGCRTCELACSLKHE---GVFnpslsRIRVVRFEPEGLD------------VPVVCRQCEDAPCVEACPVGA 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1040425976 129 -TFQREDGIVMVDNERCVACAYCVQACPYDARFINNDTLTADKCTFCahrledGLLPACVETCVGGA 194
Cdd:cd10550    66 iSRDEETGAVVVDEDKCIGCGMCVEACPFGAIRVDPETGKAIKCDLC------GGDPACVKVCPTGA 126
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
56-190 9.91e-24

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 93.57  E-value: 9.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  56 IDLRKCVGCQACTVGCSVENQAPIGQF---RTTVkqyeVSLDDGSTAQQdvksfmlprlCNHCDNAPCIKVCPVQAtFQR 132
Cdd:COG1142     7 ADPEKCIGCRTCEAACAVAHEGEEGEPflpRIRV----VRKAGVSAPVQ----------CRHCEDAPCAEVCPVGA-ITR 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 133 EDGIVMVDNERCVACAYCVQACPYDARFINNDTL--TADKCTFCAHRLEdglLPACVETC 190
Cdd:COG1142    72 DDGAVVVDEEKCIGCGLCVLACPFGAITMVGEKSraVAVKCDLCGGREG---GPACVEAC 128
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 52-199 1.14e-23

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


Pssm-ID: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 94.38  E-value: 1.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  52 YAMAIDLRKCVGCQACTVGCSvENQAPIGQFRTTVKQyevsLDDGSTAQQdvksfmLPRLCNHCDNAPCIKVCPVQATFQ 131
Cdd:cd16369     2 KEFFIDPSRCIGCRACVAACR-ECGTHRGKSMIHVDY----IDRGESTQT------APTVCMHCEDPTCAEVCPADAIKV 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1040425976 132 REDGIVM-VDNERCVACAYCVQACPYDARFINNDTLTADKCTFCAHRLEDGLLPACVETCVGGARVIGD 199
Cdd:cd16369    71 TEDGVVQsALKPRCIGCSNCVNACPFGVPKYDEERNLMMKCDMCYDRTSVGKAPMCASVCPSGALFYGT 139
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 57-190 2.95e-23

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


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 92.71  E-value: 2.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  57 DLRKCVGCQACTVGCSV-ENQAPIGQFRTTVKQYE-----VSLDDGSTAQQdvksfmlprlCNHCDNAPCIKVCPVQATF 130
Cdd:cd10554     5 DPDKCIGCRTCEVACAAaHSGKGIFEAGTDGLPFLprlrvVKTGEVTAPVQ----------CRQCEDAPCANVCPVGAIS 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040425976 131 QrEDGIVMVDNERCVACAYCVQACPYDA-----------RFINNDTLTADKCTFCAHRLEDgllPACVETC 190
Cdd:cd10554    75 Q-EDGVVQVDEERCIGCKLCVLACPFGAiemapttvpgvDWERGPRAVAVKCDLCAGREGG---PACVEAC 141
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 56-194 5.08e-23

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: 91.55  E-value: 5.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  56 IDLRKCVGCQACTVGCSVEN---QAPIGQFRTTVK---QYEVSLDDGStaqqdvkSFMLPrlCNHCDNAPCIKVCPVQA- 128
Cdd:cd10563     4 IDEEKCLGCKLCEVACAVAHsksKDLIKAKLEKERprpRIRVEESGGR-------SFPLQ--CRHCDEPPCVKACMSGAm 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1040425976 129 TFQREDGIVMVDNERCVACAYCVQACPYDARFINNDTLTADKCTFCAHRLEdgllPACVETCVGGA 194
Cdd:cd10563    75 HKDPETGIVIHDEEKCVGCWMCVMVCPYGAIRPDKERKVALKCDLCPDRET----PACVEACPTGA 136
PRK09898 PRK09898
ferredoxin-like protein;
5-202 1.19e-21

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 89.90  E-value: 1.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976   5 KRRFLSQFGKVSAG----AALIPITGI-NTAVASTAIRNNNQPdrKGevgkryAMAIDLRKCVGCQACTVGCSVENQAPI 79
Cdd:PRK09898   15 RLEFLRISGKGLAGltiaPALLSLLGCkQEDIDSGTVGLINTP--KG------VLVTQRARCTGCHRCEISCTNFNDGSV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  80 GQFRTTVK---QYEVSLDDGSTAQQDVKSF-MLPRLCNHCDNAPCIKVCPVQA-TFQREDGIVMVDNERCVACAYCVQAC 154
Cdd:PRK09898   87 GTFFSRIKihrNYFFGDNGVGSGGGLYGDLnYTADTCRQCKEPQCMNVCPIGAiTWQQKEGCITVDHKRCIGCSACTTAC 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1040425976 155 PYDARFINNDTLTADKCTFCAhrledgllpACVETCVGGARVIGDLKD 202
Cdd:PRK09898  167 PWMMATVNTESKKSSKCVLCG---------ECANACPTGALKIIEWKD 205
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 52-210 7.75e-21

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


Pssm-ID: 319890 [Multi-domain]  Cd Length: 200  Bit Score: 87.48  E-value: 7.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  52 YAMAIDLRKCVGCQ-----ACTVGCSVENQA-------PIGQFRTTVKQYE-------------------VSLDDGSTAQ 100
Cdd:cd16368     1 LATLIDLTKCDGCPgesipACVRACREKNQArfpepvsKPIQPYWPRKRIEdwsdkrdvtdrltpynwlyVQKLTVDTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 101 QDVKSFMlPRLCNHCDNAPCIKVCPVQATFQREDGIVMVDNERCVACAYCVQACPY---------------DARFINNDT 165
Cdd:cd16368    81 GEKEVFI-PRRCMHCDNPPCAKLCPFGAARKTPEGAVYIDDDLCFGGAKCRDVCPWhipqrqagvgiylhlAPEYAGGGV 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1040425976 166 LTadKCTFCAHRLEDGLLPACVETCVGGARVIGdlkdPNSEINRL 210
Cdd:cd16368   160 MY--KCDLCKDLLAQGKPPACIEACPKGAQYFG----PRKEMVAL 198
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 51-190 1.20e-19

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 88.27  E-value: 1.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  51 RYAMAiDLRKCVGCQACTVGCSVENQApiGQFRTTVKQYEVSLDDGSTAQQDVKSFmlprlCNHCDNAPCIKVCPVQATF 130
Cdd:PRK12769    3 RFIMA-NSQQCLGCHACEIACVMAHND--EQHVLSQHHFHPRITVIKHQQQRSAVT-----CHHCEDAPCARSCPNGAIS 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1040425976 131 QREDGiVMVDNERCVACAYCVQACPYDARFINNDTL-------TADKCTFCAHRlEDGllPACVETC 190
Cdd:PRK12769   75 HVDDS-IQVNQQKCIGCKSCVVACPFGTMQIVLTPVaagkvkaTAHKCDLCAGR-ENG--PACVENC 137
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 54-229 5.68e-17

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 80.45  E-value: 5.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  54 MAIDLRKCVGCQACTVGCSV-ENQAPIGQFRTTVKQYEVSLDDGSTAQqdvksfmlPRLCNHCDNAPCIKVCPVQA-TFQ 131
Cdd:PRK12809    5 IAAEAAECIGCHACEIACAVaHNQENWPLSHSDFRPRIHVVGKGQAAN--------PVACHHCNNAPCVTACPVNAlTFQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 132 REDgiVMVDNERCVACAYCVQACPYDArfINNDTLTADKCTFCAHRLEDglLPACVETCVGGARVIGDlkdpNSEINRLL 211
Cdd:PRK12809   77 SDS--VQLDEQKCIGCKRCAIACPFGV--VEMVDTIAQKCDLCNQRSSG--TQACIEVCPTQALRLMD----DKGLQQIK 146

                         170
                  ....*....|....*...
gi 1040425976 212 NENQDDIKVLKPEQNTNP 229
Cdd:PRK12809  147 VARQRKTAAGKASSDAQP 164
PRK10330 PRK10330
electron transport protein HydN;
51-190 1.62e-16

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 75.31  E-value: 1.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  51 RYAMAiDLRKCVGCQACTVGCSVENQApigqfrttvkqyevslddgstaQQDVKSF----MLPR-------------LCN 113
Cdd:PRK10330    3 RFIIA-DASKCIGCRTCEVACVVSHQE----------------------NQDCASLtpetFLPRihvikgvnvstatVCR 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 114 HCDNAPCIKVCPVQAtFQREDGIVMVDNERCVACAYCVQACPYDARFI---------------NNDTLTADKCTFCAHRl 178
Cdd:PRK10330   60 QCEDAPCANVCPNGA-ISRDKGFVHVMQERCIGCKTCVVACPYGAMEVvvrpvirnsgaglnvRAEKAEANKCDLCNHR- 137

                         170
                  ....*....|..
gi 1040425976 179 EDGllPACVETC 190
Cdd:PRK10330  138 EDG--PACMAAC 147
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 53-213 1.85e-16

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: 75.55  E-value: 1.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  53 AMAIDLRKCVGCQACTVGCSVENQAPIGQFRTT----------------VKQYEVSLDDGStaqqdVKSFMLPRLCNHCD 116
Cdd:cd10559     1 SFLIDTTRCTACRGCQVACKQWNQLPAEQTKNTgshqnppdlsantyklVRFNEVRNENGK-----PDWLFFPDQCRHCV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 117 NAPCIKVCPVQatfqrEDGIVMVDNERCV--------ACAYCV-QACPYDARFINNDTLTADKCTFCAHRLEDGLLPACV 187
Cdd:cd10559    76 TPPCKDAADMV-----PGAVIQDEATGAVvftektaeLDFDDVlSACPYNIPRKNEATGRIVKCDMCIDRVSNGLQPACV 150

                         170       180
                  ....*....|....*....|....*.
gi 1040425976 188 ETCVGGARVIGDLKDPNSEINRLLNE 213
Cdd:cd10559   151 KACPTGAMNFGDRDEMLAMASKRLEE 176
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 59-194 1.34e-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: 68.52  E-value: 1.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  59 RKCVGCQACTVGCSvenqapigqfRTTVKQyevslDDGSTAQ---QDVKSFMLPRLCNHCDNapCIKVCPVQATFQREDG 135
Cdd:cd16372     8 EKCIGCLQCEEACS----------KTFFKE-----EDREKSCiriTETEGGYAINVCNQCGE--CIDVCPTGAITRDANG 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1040425976 136 IVMVDNERCVACAYCVQACPYDARFINNDTLTADKCTFCAhrledgllpACVETCVGGA 194
Cdd:cd16372    71 VVMINKKLCVGCLMCVGFCPEGAMFKHEDYPEPFKCIACG---------ICVKACPTGA 120
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 51-196 2.24e-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: 319889 [Multi-domain]  Cd Length: 138  Bit Score: 65.79  E-value: 2.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  51 RYAMAIDLRKCVGCQACTVGCSvenQAPIGQFRttvkqyevsLDDGSTAqqdVKSFMLPRLCNHCDNAPCIKVCPVQATF 130
Cdd:cd16367    11 TNLLVIDLDRCIRCDNCEKACA---DTHDGHSR---------LDRNGLR---FGNLLVPTACRHCVDPVCMIGCPTGAIH 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1040425976 131 QREDGIVMVDnERCVACAYCVQACPYDARFInndtLTADKCTFCAHRLEdgllPACVETCVGGARV 196
Cdd:cd16367    76 RDDGGEVVIS-DACCGCGNCASACPYGAIQM----VRAVKCDLCAGYAG----PACVSACPTGAAI 132
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 55-174 2.57e-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: 65.37  E-value: 2.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  55 AIDLRKCVGCQACTVGCSVENQAPIGQFRTTVKqyeVSLDDGstaqqdVKSFMLPRLCNHCDNAPCIKVCPVQATFQRED 134
Cdd:cd16370     5 VKDMERCIGCYSCMLACSRRVHKSASLSKSAIR---VRTRGG------LEGGFTVVVCRACEDPPCAEACPTGALEPRKG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1040425976 135 GIVMVDNERCVACAYCVQACPYDARFINNDTLTADKCTFC 174
Cdd:cd16370    76 GGVVLDKEKCIGCGNCVKACIVGAIFWDEETNKPIICIHC 115
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
109-165 5.22e-09

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 52.04  E-value: 5.22e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1040425976 109 PRLCNHCDNapCIKVCPVQAtFQREDGIVMVDNERCVACAYCVQACPYDARFINNDT 165
Cdd:COG2768    10 EEKCIGCGA--CVKVCPVGA-ISIEDGKAVIDPEKCIGCGACIEVCPVGAIKIEWEE 63
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
54-204 1.40e-08

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 55.03  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  54 MAIDLRKCVGCQACTVGCSVENQAPIGQFRTTVKQYEVSLDDGSTAQQDVKSFMLPRLCNHCDNAPCIKVCPVQATFQRE 133
Cdd:COG4624     3 LLLRACCCCCIEEGDELLLLEEAERVLRIIILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDKR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 134 DGIVMVDNERCVACAYCVQACPYDARFINND--TLTADKCTFCAHrledgllpaCVETCVGGA--------RVIGDLKDP 203
Cdd:COG4624    83 GPSIIRDKEKCKNCYPCVRACPVKAIKVDDGkaEIDEEKCISCGQ---------CVAVCPFGAiteksdieKVKKALKDP 153


                  .
gi 1040425976 204 N 204
Cdd:COG4624   154 E 154
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 56-158 2.96e-08

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: 51.24  E-value: 2.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  56 IDLRKCVGCQACTVGCSVenqapigqfrttvKQYEVSLDDGSTAQQDVKSFMLPRLCNHCDNapCIKVCPVQATFQREDG 135
Cdd:cd10549    37 IDEDKCVFCGACVEVCPT-------------GAIELTPEGKEYVPKEKEAEIDEEKCIGCGL--CVKVCPVDAITLEDEL 101

                          90       100
                  ....*....|....*....|...
gi 1040425976 136 IVMVDNERCVACAYCVQACPYDA 158
Cdd:cd10549   102 EIVIDKEKCIGCGICAEVCPVNA 124
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 111-158 5.99e-08

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 48.89  E-value: 5.99e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1040425976 111 LCNHCDNapCIKVCPVQAtFQREDGIVMVDNERCVACAYCVQACPYDA 158
Cdd:COG2221    16 KCIGCGL--CVAVCPTGA-ISLDDGKLVIDEEKCIGCGACIRVCPTGA 60
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
120-190 1.50e-07

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 51.22  E-value: 1.50e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040425976 120 CIKVCPV---QATFQREDGI-VMVDNERCVACAYCVQACPYDArFINNDTLTADKCTFCAhrledgllpACVETC 190
Cdd:COG0348   184 CRYLCPYgafQGLLSDLSTLrVRYDRGDCIDCGLCVKVCPMGI-DIRKGEINQSECINCG---------RCIDAC 248
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 112-158 3.16e-07

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: 47.35  E-value: 3.16e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1040425976 112 CNHCDNapCIKVCPVQATFQREDGIVMVDNERCVACAYCVQACPYDA 158
Cdd:COG1144    32 CIGCGL--CWIVCPDGAIRVDDGKYYGIDYDYCKGCGICAEVCPVKA 76
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 109-158 3.76e-07

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 46.57  E-value: 3.76e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1040425976 109 PRLCNHCDNapCIKVCPVQAtFQREDGIVMVDNERCVACAYCVQACPYDA 158
Cdd:COG4231    21 EDKCTGCGA--CVKVCPADA-IEEGDGKAVIDPDLCIGCGSCVQVCPVDA 67
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 112-158 7.14e-07

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 45.51  E-value: 7.14e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1040425976 112 CNHCDNapCIKVCPVQA---TFQREDGIVMVDNERCVACAYCVQACPYDA 158
Cdd:COG1143     4 CIGCGL--CVRVCPVDAitiEDGEPGKVYVIDPDKCIGCGLCVEVCPTGA 51
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
109-177 8.73e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 49.81  E-value: 8.73e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1040425976 109 PRLCNHcdnaPCIKVCPVQAT------FQREDGIVMVDNERCVACAYCVQACPYDARFINN--DTLTADkctfCAHR 177
Cdd:PRK13409   14 PKKCNY----ECIKYCPVVRTgeetieIDEDDGKPVISEELCIGCGICVKKCPFDAISIVNlpEELEEE----PVHR 82
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 109-158 8.87e-07

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 45.49  E-value: 8.87e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1040425976 109 PRLCNHCDNapCIKVCPVQATFQREDGIVMVDNERCVACAYCVQACPYDA 158
Cdd:COG1149    10 EEKCIGCGL--CVEVCPEGAIKLDDGGAPVVDPDLCTGCGACVGVCPTGA 57
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 109-158 1.02e-06

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 49.40  E-value: 1.02e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1040425976 109 PRLCNHcdnaPCIKVCPVQAT------FQREDGIVMVDNERCVACAYCVQACPYDA 158
Cdd:COG1245    14 PKKCNY----ECIKYCPVNRTgkeaieIDEDDGKPVISEELCIGCGICVKKCPFDA 65
NapF COG1145
Ferredoxin [Energy production and conversion];
112-158 2.77e-06

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 47.41  E-value: 2.77e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1040425976 112 CNHCDNapCIKVCPVQA-TFQREDGIVMVDNERCVACAYCVQACPYDA 158
Cdd:COG1145   184 CIGCGL--CVKVCPTGAiRLKDGKPQIVVDPDKCIGCGACVKVCPVGA 229
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
132-197 4.62e-06

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 43.57  E-value: 4.62e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040425976 132 REDGIVMVDNERCVACAYCVQACPYDARFINNDTLT--ADKCTFCahrledgllPACVETCVGGARVI 197
Cdd:COG2768     1 HSLGKPYVDEEKCIGCGACVKVCPVGAISIEDGKAVidPEKCIGC---------GACIEVCPVGAIKI 59
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 136-197 6.63e-06

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 43.12  E-value: 6.63e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040425976 136 IVMVDNERCVACAYCVQACPYDARFINNDTLT--ADKCTFCAHrledgllpaCVETCVGGARVI 197
Cdd:COG2221     9 PPKIDEEKCIGCGLCVAVCPTGAISLDDGKLVidEEKCIGCGA---------CIRVCPTGAIKG 63
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 112-158 1.17e-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: 1.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1040425976 112 CNHCDNapCIKVCPVQATFQREDG------IVMVDNERCVACAYCVQACPYDA 158
Cdd:pfam12838   1 CIGCGA--CVAACPVGAITLDEVGekkgtkTVVIDPERCVGCGACVAVCPTGA 51
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
112-158 1.27e-05

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 45.44  E-value: 1.27e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1040425976 112 CNHCDNapCIKVCPVqatfqredGIVM----VDNERCVACAYCVQACPYDA 158
Cdd:COG0348   212 CIDCGL--CVKVCPM--------GIDIrkgeINQSECINCGRCIDACPKDA 252
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 120-155 1.45e-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: 45.37  E-value: 1.45e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1040425976 120 CIKVCPVQATFQREDGIVMVDNERCVACAYCVQACP 155
Cdd:COG2878   145 CIKACPFDAIVGAAKGMHTVDEDKCTGCGLCVEACP 180
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 112-191 3.20e-05

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 43.01  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 112 CNHCDNApCIKVCPVQA----TFQRED---GIVMVDNERCVA------CAYCVQACPYDARFINNDTLT------ADKCT 172
Cdd:cd16373    55 CDLCCDA-CVEVCPTGAlrplDLEEQKvkmGVAVIDKDRCLAwqggtdCGVCVEACPTEAIAIVLEDDVlrpvvdEDKCV 133

                          90
                  ....*....|....*....
gi 1040425976 173 FCahrledGllpACVETCV 191
Cdd:cd16373   134 GC------G---LCEYVCP 143
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
120-158 3.89e-05

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 41.86  E-value: 3.89e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1040425976 120 CIKVCPVQATFQREDGIVMVDNERCVACAYCVQACPYDA 158
Cdd:PRK09623   59 CWKFCPEPAIYIKEDGYVAIDYDYCKGCGICANECPTKA 97
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 109-155 6.37e-05

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


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 39.93  E-value: 6.37e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1040425976 109 PRLCNHCdnAPCIKVCPVQATFQREDGIVMVDN------ERCVACAYCVQACP 155
Cdd:pfam13237   6 PDKCIGC--GRCTAACPAGLTRVGAIVERLEGEavrigvWKCIGCGACVEACP 56
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 109-158 1.01e-04

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: 1.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1040425976 109 PRLCNHCdnAPCIKVCPVQA-TFQREDGIV---MVDNERCVACAYCVQACPYDA 158
Cdd:cd10549     5 PEKCIGC--GICVKACPTDAiELGPNGAIArgpEIDEDKCVFCGACVEVCPTGA 56
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
56-155 1.25e-04

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 42.61  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  56 IDLRKCVGCQACTVGC--SVENQAPIGQfRTTVkqYEVSLDDGstaqQDVKsfmlprlcNHCDNA-----PCIKVCPVQA 128
Cdd:PRK07118  165 VDEDKCTGCGACVKACprNVIELIPKSA-RVFV--ACNSKDKG----KAVK--------KVCEVGcigcgKCVKACPAGA 229

                          90       100
                  ....*....|....*....|....*..
gi 1040425976 129 tFQREDGIVMVDNERCVACAYCVQACP 155
Cdd:PRK07118  230 -ITMENNLAVIDQEKCTSCGKCVEKCP 255
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
109-158 1.75e-04

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 42.54  E-value: 1.75e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1040425976 109 PRLCNHCdnAPCIKVCPVQATFQREDGIVMVDNERCVACAYCVQACPYDA 158
Cdd:COG1148   495 PEKCTGC--GRCVEVCPYGAISIDEKGVAEVNPALCKGCGTCAAACPSGA 542
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 136-194 2.13e-04

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 38.94  E-value: 2.13e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1040425976 136 IVMVDNERCVACAYCVQACPYDA-RFINNDTLT--ADKCTFCAhrledgllpACVETCVGGA 194
Cdd:COG1149     5 IPVIDEEKCIGCGLCVEVCPEGAiKLDDGGAPVvdPDLCTGCG---------ACVGVCPTGA 57
PRK13795 PRK13795
hypothetical protein; Provisional
 111-165 2.38e-04

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 42.29  E-value: 2.38e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1040425976 111 LCNHCDnaPCIKVCPVQAtFQREDG--IVMVDNERCVACAYCVQACPYdARFINNDT 165
Cdd:PRK13795  582 ECVGCG--VCVGACPTGA-IRIEEGkrKISVDEEKCIHCGKCTEVCPV-VKYKDKRN 634
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
120-157 2.51e-04

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 41.84  E-value: 2.51e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1040425976 120 CIKVCPVQAtFQREDGIVMVDNERCVACAYCVQACPYD 157
Cdd:PRK07118  147 CVAACPFDA-IHIENGLPVVDEDKCTGCGACVKACPRN 183
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 139-190 3.30e-04

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: 39.69  E-value: 3.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1040425976 139 VDNERCVACAYCVQACPYDARFINNDTLTA-------DKCTFCAhrledgllpACVETC 190
Cdd:cd10549     3 YDPEKCIGCGICVKACPTDAIELGPNGAIArgpeideDKCVFCG---------ACVEVC 52
NapF COG1145
Ferredoxin [Energy production and conversion];
89-190 3.61e-04

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 41.25  E-value: 3.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976  89 YEVSLDDGSTAQQDVKSFMLPRLCNHCDNAPCIKVCPVQATFQREDGIVMVDNERCVACAYCVQACPYDARFINNDTLTA 168
Cdd:COG1145   129 GEVLLVIAAALAEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVCPTGAIRLKDGKPQI 208

                          90       100
                  ....*....|....*....|....*.
gi 1040425976 169 ----DKCTFCahrledgllPACVETC 190
Cdd:COG1145   209 vvdpDKCIGC---------GACVKVC 225
porD PRK09625
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
 111-155 5.65e-04

pyruvate flavodoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 236596 [Multi-domain]  Cd Length: 133  Bit Score: 38.96  E-value: 5.65e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1040425976 111 LCNHCDNapCIKVCPVQATFQREDGIVMVDNERCVACAYCVQACP 155
Cdd:PRK09625   60 ICINCFN--CWVYCPDAAILSRDKKLKGVDYSHCKGCGVCVEVCP 102
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 142-206 5.75e-04

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: 37.42  E-value: 5.75e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040425976 142 ERCVACAYCVQACPYDARFINND------TLTADKCTFCAhrledgllpACVETCVGGARVIGDLKDPNSE 206
Cdd:COG1143     2 DKCIGCGLCVRVCPVDAITIEDGepgkvyVIDPDKCIGCG---------LCVEVCPTGAISMTPFELAVED 63
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 135-194 6.99e-04

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 37.38  E-value: 6.99e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040425976 135 GIVMVDNERCVACAYCVQACPYDARFINNDTLTA-----DKCTFCAhrledgllpACVETCVGGA 194
Cdd:COG1146     1 MMPVIDTDKCIGCGACVEVCPVDVLELDEEGKKAlvinpEECIGCG---------ACELVCPVGA 56
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
120-158 8.68e-04

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 39.09  E-value: 8.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1040425976 120 CIKVCPVQA----TFQREDGIVMVDN-----ERCVACAYCVQACPYDA 158
Cdd:PRK05888   66 CAAICPADAitieAAEREDGRRRTTRydinfGRCIFCGFCEEACPTDA 113
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 136-190 9.10e-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: 39.01  E-value: 9.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 136 IVMVDNERCVACAYCVQACPYDA-----RFINndTLTADKCTFCAhrledgllpACVETC 190
Cdd:TIGR01944 107 VALIDEDNCIGCTKCIQACPVDAivgaaKAMH--TVIADECTGCD---------LCVEPC 155
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 142-218 1.05e-03

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: 38.17  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 142 ERCVACAYCVQACPYDA------------RFINNDTLTADKCTFCahrledGLlpaCVETCVGGARVIGDLKDPNSEINR 209
Cdd:TIGR01971  43 EKCIGCTLCAAVCPADAirvvpaegedgkRRLKFYEINFGRCIFC------GL---CEEACPTDAIVLTPEFELATYTRS 113


                  ....*....
gi 1040425976 210 LLNENQDDI 218
Cdd:TIGR01971 114 DLVYGKEDL 122
Fer4_9 pfam13187
4Fe-4S dicluster domain;
112-158 1.26e-03

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 35.99  E-value: 1.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1040425976 112 CNHCDNapCIKVCPVQATFQREDGIVMV---DNERCVACAYCVQACPYDA 158
Cdd:pfam13187   2 CTGCGA--CVAACPAGAIVPDLVGQTIRgdiAGLACIGCGACVDACPRGA 49
napG PRK09476
quinol dehydrogenase periplasmic component; Provisional
 112-174 1.54e-03

quinol dehydrogenase periplasmic component; Provisional


Pssm-ID: 236534 [Multi-domain]  Cd Length: 254  Bit Score: 39.22  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425976 112 CNHCDNAPCIKVCPVQA-TFQRED------GI-VMVDNERCVA-----CAYCVQACP-----------------YDARFI 161
Cdd:PRK09476   99 CEMCEDIPCVKACPSGAlDRELVDiddarmGLaVLVDQENCLNfqglrCDVCYRVCPlidkaitlelernertgKHAFFL 178

                          90
                  ....*....|...
gi 1040425976 162 nnDTLTADKCTFC 174
Cdd:PRK09476  179 --PTVHSDACTGC 189
FixX COG2440
Ferredoxin-like protein FixX [Energy production and conversion];
114-158 1.86e-03

Ferredoxin-like protein FixX [Energy production and conversion];


Pssm-ID: 441981 [Multi-domain]  Cd Length: 87  Bit Score: 36.72  E-value: 1.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1040425976 114 HCDNAPCIKVCPVQATFQREDGIVMVDNERCVACAYCVQACPYDA 158
Cdd:COG2440    26 RCLAKPCTRYCPAGVYEIVGDGRLQINYENCLECGTCRIKCPTQN 70
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
141-190 1.86e-03

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 37.94  E-value: 1.86e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1040425976 141 NERCVACAYCVQACPYDARFI----NND----TLTAD----KCTFCahrledGLlpaCVETC 190
Cdd:PRK05888   57 EERCIACKLCAAICPADAITIeaaeREDgrrrTTRYDinfgRCIFC------GF---CEEAC 109
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
139-165 2.56e-03

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 39.07  E-value: 2.56e-03
                          10        20
                  ....*....|....*....|....*..
gi 1040425976 139 VDNERCVACAYCVQACPYDARFINNDT 165
Cdd:COG1148   493 VDPEKCTGCGRCVEVCPYGAISIDEKG 519
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 140-190 2.70e-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: 2.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1040425976 140 DNERCVACAYCVQACPYDARFINND---TLTADKCTFCAhrledgllpACVETC 190
Cdd:COG2878   135 CEYGCIGCGDCIKACPFDAIVGAAKgmhTVDEDKCTGCG---------LCVEAC 179
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 137-190 3.10e-03

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 35.79  E-value: 3.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1040425976 137 VMVDNERCVACAYCVQACPYDARFINNDTLT--ADKCTFCAhrledgllpACVETC 190
Cdd:COG4231    17 YVIDEDKCTGCGACVKVCPADAIEEGDGKAVidPDLCIGCG---------SCVQVC 63
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 137-158 4.33e-03

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


Pssm-ID: 459642 [Multi-domain]  Cd Length: 24  Bit Score: 34.15  E-value: 4.33e-03
                          10        20
                  ....*....|....*....|..
gi 1040425976 137 VMVDNERCVACAYCVQACPYDA 158
Cdd:pfam00037   1 VVIDEEKCIGCGACVEVCPVGA 22
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 111-168 5.01e-03

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 36.35  E-value: 5.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1040425976 111 LCNHCdnAPCIKVCPVQA-TFQREDGIVMVDNERCVACAYCVQACPYDARFINNDTLTA 168
Cdd:PRK08348   43 KCVGC--RMCVTVCPAGVfVYLPEIRKVALWTGRCVFCGQCVDVCPTGALQMSDDFLLA 99
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 112-158 5.48e-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: 37.53  E-value: 5.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1040425976 112 CNHCdnAPCIKVCPVQAtfqredgIVMVDN-----ERCVACAYCVQACPYDA 158
Cdd:NF038196  187 CIGC--GICAKVCPVNN-------IEMEDGkpvwgHNCTHCLACIHRCPKEA 229
PRK06991 PRK06991
electron transport complex subunit RsxB;
136-199 6.54e-03

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 37.47  E-value: 6.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1040425976 136 IVMVDNERCVACAYCVQACPYDARFINND---TLTADKCTFCahrleDGLLPACVETCVGGARVIGD 199
Cdd:PRK06991   79 VAVIDEQLCIGCTLCMQACPVDAIVGAPKqmhTVLADLCTGC-----DLCVPPCPVDCIDMVPVTGE 140
 
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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