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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692191181   1 VFAYYLSIACNHCEDPACTKVCPSGAMHKRDDGFVVVDEDVCIGCRYCHMACPYGAPQYNAAKGHMTKCDGCHSRVADGK 80
Cdd:cd16371   45 VFAYFLSMSCNHCENPACVKVCPTGAITKREDGIVVVDQDKCIGCGYCVWACPYGAPQYNPETGKMDKCDMCVDRLDEGE 124

                         90
                 ....*....|....*.
gi 692191181  81 KPICVESCPLRALDFG 96
Cdd:cd16371  125 KPACVAACPTRALDFG 140

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692191181    1 VFAYYLSIACNHCEDPACTKVCPSGAMHKR-DDGFVVVDEDVCIGCRYCHMACPYGAPQYNAAKGHMTKCDGCHSRVADG 79
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPVGAIYKDeETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAG 80

                          90
                  ....*....|....*..
gi 692191181   80 KKPICVESCPLRALDFG 96
Cdd:pfam13247  81 LLPACVQTCPTGAMNFG 97

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692191181   1 VFAYYLSIACNHCEDPACTKVCPSGAMHKRDDGFVVVDEDVCIGCRYCHMACPYGAPQYNAAKGHMTKCDGCHSRVADGK 80
Cdd:cd16371   45 VFAYFLSMSCNHCENPACVKVCPTGAITKREDGIVVVDQDKCIGCGYCVWACPYGAPQYNPETGKMDKCDMCVDRLDEGE 124

                         90
                 ....*....|....*.
gi 692191181  81 KPICVESCPLRALDFG 96
Cdd:cd16371  125 KPACVAACPTRALDFG 140

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692191181   4 YYLSIACNHCEDPACTKVCPSGAMHKRDDGFVVVDEDVCIGCRYCHMACPYGAPQYNA------------AKGHMTKCDG 71
Cdd:cd10551   47 TFLPVLCNHCENPPCVKVCPTGATYKREDGIVLVDYDKCIGCRYCMAACPYGARYFNPeephefgevpvrPKGVVEKCTF 126

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 692191181  72 CHSRVADGKKPICVESCPLRALDFG----PIEELRKKHGQLAAVAPLPSAHfTKPSI 124
Cdd:cd10551  127 CYHRLDEGLLPACVEACPTGARIFGdlddPNSEVSKLLAERRAYVLKPELG-TKPKV 182

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692191181   4 YYLSIACNHCEDPACTKVCPSGAMHKRDDGFVVVDEDVCIGCRYCHMACPYGAPQYNAAKGHMTKCDGCHSRVADGKKPI 83
Cdd:cd10562   64 LFRKRQCMHCTDAACVKVCPTGALYKTENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCFDRIENGMQPA 143

                         90
                 ....*....|....*...
gi 692191181  84 CVESCPLRALDFGPIEEL 101
Cdd:cd10562  144 CVKTCPTGALTFGDRDEL 161

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692191181   5 YLSIACNHCEDPACTKVCPSGAMHKRDDGFVVVDEDVCIGCRYCHMACPYGAPQYNAAKGHMTKCDGCHSRVADGKKPIC 84
Cdd:cd16366   65 FRKDQCMHCTDAGCLAACPTGAIIRTETGTVVVDPETCIGCGYCVNACPFDIPRFDEETGRVAKCTLCYDRISNGLQPAC 144

                         90
                 ....*....|..
gi 692191181  85 VESCPLRALDFG 96
Cdd:cd16366  145 VKTCPTGALTFG 156

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692191181    1 VFAYYLSIACNHCEDPACTKVCPSGAMHKR-DDGFVVVDEDVCIGCRYCHMACPYGAPQYNAAKGHMTKCDGCHSRVADG 79
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPVGAIYKDeETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAG 80

                          90
                  ....*....|....*..
gi 692191181   80 KKPICVESCPLRALDFG 96
Cdd:pfam13247  81 LLPACVQTCPTGAMNFG 97

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692191181   5 YLSIACNHCEDPACTKVCPSGAMHKRDDGFVVVDEDVCIGCRYCHMACPYGAPQYNAAKGHMTKCDGCHSRVADGKKPIC 84
Cdd:cd10560   73 FMSDVCKHCTDAGCLEACPTGAIFRTEFGTVYIQPDICNGCGYCVAACPFGVIDRNEETGRAHKCTLCYDRLKDGLEPAC 152

                         90       100
                 ....*....|....*....|
gi 692191181  85 VESCPLRALDFGPIEELRKK 104
Cdd:cd10560  153 AKACPTGSIQFGPLEELRER 172

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692191181   9 ACNHCEDPACTKVCPS-GAMHKRDDGFVVVDEDVCIGCRYCHMACPYGAPQYNAAKGHMTKCDGCHSRVADGKKPICVES 87
Cdd:cd10558   69 GCMHCADPGCLKACPSpGAIVQYANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVGLEPACVKT 148

                         90       100       110
                 ....*....|....*....|....*....|....
gi 692191181  88 CPLRALDFGPIEELRKKHGQlaAVAPLPSAHFTK 121
Cdd:cd10558  149 CPTGALHFGTKEDMLALAEK--RVAALKERGYTN 180

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692191181   4 YYLSIACNHCEDPACTKVCPSGAMHKRD-DGFVVVDEDVCIGCRYCHMACPYGAPQYNAAKGHMTKCDGCHSRvadgKKP 82
Cdd:cd10563   51 RSFPLQCRHCDEPPCVKACMSGAMHKDPeTGIVIHDEEKCVGCWMCVMVCPYGAIRPDKERKVALKCDLCPDR----ETP 126

                         90
                 ....*....|....
gi 692191181  83 ICVESCPLRALDFG 96
Cdd:cd10563  127 ACVEACPTGALVLE 140

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692191181   4 YYLSIACNHCEDPACTKVCPSGAMHK-RDDGFVVVDEDVCIGCRYCHMACPYGAPQYNAAKGHMTKCDGChsrvadGKKP 82
Cdd:cd10550   43 LDVPVVCRQCEDAPCVEACPVGAISRdEETGAVVVDEDKCIGCGMCVEACPFGAIRVDPETGKAIKCDLC------GGDP 116

                         90
                 ....*....|...
gi 692191181  83 ICVESCPLRALDF 95
Cdd:cd10550  117 ACVKVCPTGALEF 129

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692191181   1 VFAYYLSIACNHCEDPACTKVCPSGAMHKRD-DGFVVVDEDVCIGCRYCHMACPYGAPQYNAAKGHMTKCDGCHSRVADG 79
Cdd:cd10557  170 TFMFYLPRICNHCLNPACVAACPSGAIYKREeDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSEKCIFCYPRLEAG 249

                 ....*....
gi 692191181  80 KKPICVESC 88
Cdd:cd10557  250 QPTVCSETC 258

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692191181   1 VFAYYLSIACNHCEDPACTKVCPSGAMHKRD-DGFVVVDEDVCIGCRYCHMACPYGAPQYNAAKGHMTKCDGCHSRVADG 79
Cdd:COG1140  173 TFMFYLPRICEHCLNPACVASCPSGAIYKREeDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGKAEKCIFCYPRIEAG 252

                 ....*....
gi 692191181  80 KKPICVESC 88
Cdd:COG1140  253 QPTVCSETC 261

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692191181   2 FAYYLSIACNHCEDPACTKVCPSGAMHKR-DDGFVVVDEDVCIGCRYCHMACPYGAPQYNAAKGHMTKCDGCHSRVADGK 80
Cdd:cd16365   65 FFFYLQRLCNHCTNPACLAACPRGAIYKReEDGIVLIDQKRCRGYRKCVEQCPYKKIYFNGLSRVSEKCIACYPRIEGGD 144

                         90       100
                 ....*....|....*....|....*
gi 692191181  81 KPICVESCPLRALDFGPIEELRKKH 105
Cdd:cd16365  145 PTRCMSACVGRIRLQGFLDDNPKSP 169

tetrathionate reductase subunit TtrB;

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 692191181  10 CNHCEDPACTKVCPSGAMHKRDDGFVVVDEDVCIGCRYCHMACPYGAPQYNAAKGHMTKCDGCHSRVADGKKPICVESC 88
Cdd:PRK14993 100 CNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESC 178

putative oxidoreductase Fe-S binding subunit; Reviewed

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692191181   7 SIACNHCEDPACTKVCPSGAMHKRDDGFVVVDEDvCIGCRYCHMACPYGAPQ-------YNAAKGHMTKCDGCHSRvADG 79
Cdd:PRK12769  53 AVTCHHCEDAPCARSCPNGAISHVDDSIQVNQQK-CIGCKSCVVACPFGTMQivltpvaAGKVKATAHKCDLCAGR-ENG 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 692191181  80 kkPICVESCPLRAL---DFGPIEELRKKHGQLAAVAPLPSAHFTKP 122
Cdd:PRK12769 131 --PACVENCPADALqlvTEQALSGMAKSRRLRTARQEHQPWHASTA 174

electron transport protein HydN;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692191181   7 SIACNHCEDPACTKVCPSGAMhKRDDGFVVVDEDVCIGCRYCHMACPYGAPQ---------------YNAAKGHMTKCDG 71
Cdd:PRK10330  55 ATVCRQCEDAPCANVCPNGAI-SRDKGFVHVMQERCIGCKTCVVACPYGAMEvvvrpvirnsgaglnVRAEKAEANKCDL 133

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 692191181  72 CHSRVADgkkPICVESCPLRAL---DFGPIEELRKKHGQLAAVAPLPSAHF 119
Cdd:PRK10330 134 CNHREDG---PACMAACPTHALicvDRNKLEQLSAEKRRRAALDSTASLMF 181

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692191181   9 ACNHCEDPACTKVCPSGAMHKRDDGFVVVDEDvCIGCRYCHMACPYGAPQYNAAkghmTKCDGChsrvADGKKPICVESC 88
Cdd:cd16367   56 ACRHCVDPVCMIGCPTGAIHRDDGGEVVISDA-CCGCGNCASACPYGAIQMVRA----VKCDLC----AGYAGPACVSAC 126

                 ....*
gi 692191181  89 PLRAL 93
Cdd:cd16367  127 PTGAA 131

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692191181   8 IACNHCEDPACTKVCPSGAMHKRDDGFVVVDEDVCIGCRYCHMACPYGAPQYNAAKGHMTKCDGCHsrvadgkkpICVES 87
Cdd:cd16370   51 VVCRACEDPPCAEACPTGALEPRKGGGVVLDKEKCIGCGNCVKACIVGAIFWDEETNKPIICIHCG---------YCARY 121

                 ....*...
gi 692191181  88 CPLRALDF 95
Cdd:cd16370  122 CPHDVLAM 129

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692191181  10 CNHCEDpaCTKVCPSGAMHKRDDGFVVVDEDVCIGCRYCHMACPYGAPQYNAAKGHMTKCDGCHsrvadgkkpICVESCP 89
Cdd:cd16372   49 CNQCGE--CIDVCPTGAITRDANGVVMINKKLCVGCLMCVGFCPEGAMFKHEDYPEPFKCIACG---------ICVKACP 117

                 ....
gi 692191181  90 LRAL 93
Cdd:cd16372  118 TGAL 121

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

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 692191181  10 CNHCEdpACTKVCPSGAMHKRDDGFVVVDEDVCIGCRYCHMACPYGA 56
Cdd:COG1149   13 CIGCG--LCVEVCPEGAIKLDDGGAPVVDPDLCTGCGACVGVCPTGA 57

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692191181   8 IACNHCEDpACTKVCPSGAMHKRDD-------GFVVVDEDVCI------GCRYCHMACPYGAPQYNAAKGHM------TK 68
Cdd:cd16373   53 GPCDLCCD-ACVEVCPTGALRPLDLeeqkvkmGVAVIDKDRCLawqggtDCGVCVEACPTEAIAIVLEDDVLrpvvdeDK 131

                         90       100
                 ....*....|....*....|.
gi 692191181  69 CDGChsrvadGkkpICVESCP 89
Cdd:cd16373  132 CVGC------G---LCEYVCP 143

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

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 692191181  10 CNHCEdpACTKVCPSGAMHKRDDGFVVVDEDVCIGCRYCHMACPYGA 56
Cdd:COG1144   32 CIGCG--LCWIVCPDGAIRVDDGKYYGIDYDYCKGCGICAEVCPVKA 76

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

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 692191181   9 ACNHCEdpACTKVCPSGAMhKRDDGFVVVDEDVCIGCRYCHMACPYGA 56
Cdd:COG4624   92 KCKNCY--PCVRACPVKAI-KVDDGKAEIDEEKCISCGQCVAVCPFGA 136

Polyferredoxin NapH [Energy production and conversion];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692191181  18 CTKVCPSGAMH---KRDDGFVV-VDEDVCIGCRYCHMACPYGAPQYNAAKGHMTkCDGCHSrvadgkkpiCVESCPLRAL 93
Cdd:COG0348  184 CRYLCPYGAFQgllSDLSTLRVrYDRGDCIDCGLCVKVCPMGIDIRKGEINQSE-CINCGR---------CIDACPKDAI 253

                 ...
gi 692191181  94 DFG 96
Cdd:COG0348  254 RFS 256

3-methyl-2-oxobutanoate dehydrogenase subunit delta;

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 692191181  18 CTKVCPSGAMHKRDDGFVVVDEDVCIGCRYCHMACPYGA 56
Cdd:PRK09623  59 CWKFCPEPAIYIKEDGYVAIDYDYCKGCGICANECPTKA 97

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692191181   5 YLSIACNHCEdpACTKVCPSGAMHKRDDG----FVVVDEDVCIGCRYCHMACPYGAPQYNAAKGHMTKCDGchSRVADGK 80
Cdd:cd10549    3 YDPEKCIGCG--ICVKACPTDAIELGPNGaiarGPEIDEDKCVFCGACVEVCPTGAIELTPEGKEYVPKEK--EAEIDEE 78

                         90
                 ....*....|...
gi 692191181  81 KPI----CVESCP 89
Cdd:cd10549   79 KCIgcglCVKVCP 91

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692191181  17 ACTKVCPSGAMHKRDDGF--------VVVDEDVCIGCRYCHMACPYGAPQYNAAKGH---MTKCDGCHsrvadgkkpICV 85
Cdd:cd10549   47 ACVEVCPTGAIELTPEGKeyvpkekeAEIDEEKCIGCGLCVKVCPVDAITLEDELEIvidKEKCIGCG---------ICA 117

                         90
                 ....*....|
gi 692191181  86 ESCPLRALDF 95
Cdd:cd10549  118 EVCPVNAIKL 127

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