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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446786817  16 VIIDEDKCIadkGCTVCVDVCPMDLLAIDPTTQKAfmqfDECWYCM---------PCEKDCPTDAVK 73
Cdd:cd10562   95 VVVDEDKCI---GCGYCVAACPFDVPRYDETTNKI----TKCTLCFdriengmqpACVKTCPTGALT 154

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]

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446786817    7 EVQHRTVApvIIDEDKCIadkGCTVCVDVCPMDLLAIDPTTQKAFMQfDECWYCMPCEKDCPTDAVK 73
Cdd:TIGR01944 101 TIQPPMVA--LIDEDNCI---GCTKCIQACPVDAIVGAAKAMHTVIA-DECTGCDLCVEPCPTDCIE 161

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

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446786817  1 MAFIFKEVQHRTVA-PVIIDEDKCIadkGCTVCVDVCPMDllAIDPTTQKAFMQFDECWYCMPCEKDCPTDAVKV 74
Cdd:COG4231   1 RNITVKILDNRTTAmRYVIDEDKCT---GCGACVKVCPAD--AIEEGDGKAVIDPDLCIGCGSCVQVCPVDAIKL 70

Uncharacterized Fe-S cluster protein [Function unknown];

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446786817 16 VIIDEDKCIadkGCTVCVDVCPMDllAIDPTTQKAFMQFDECWYCMPCEKDCPTDAVKVN 75
Cdd:COG2768   6 PYVDEEKCI---GCGACVKVCPVG--AISIEDGKAVIDPEKCIGCGACIEVCPVGAIKIE 60

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446786817  16 VIIDEDKCIadkGCTVCVDVCPMDLLAIDPTTQKAfmqfDECWYCM---------PCEKDCPTDAVK 73
Cdd:cd10562   95 VVVDEDKCI---GCGYCVAACPFDVPRYDETTNKI----TKCTLCFdriengmqpACVKTCPTGALT 154

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446786817  15 PVIIDEDKCIadkGCTVCVDVCPMDLLAIDPTTQ-------KAFMQFDECWYCMPCEKDCPTDAVKVN 75
Cdd:cd10549   34 GPEIDEDKCV---FCGACVEVCPTGAIELTPEGKeyvpkekEAEIDEEKCIGCGLCVKVCPVDAITLE 98

NADH dehydrogenase subunit I

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446786817  21 DKCIAdkgCTVCVDVCPMDLLAIDPTTQKAF---------MQFDECWYCMPCEKDCPTD 70
Cdd:CHL00014  59 DKCIA---CEVCVRVCPIDLPVVDWKLETDIrkkrllnysIDFGVCIFCGNCVEYCPTN 114

NADH-plastoquinone oxidoreductase subunit; Provisional

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446786817  16 VIIDEDKCIadkGCTVCVDVCPMDLLAIDPTTQKAFMQFDECWYCMPCEKDCPTDAVKVNIPYLL 80
Cdd:PRK08348  37 ILYDVDKCV---GCRMCVTVCPAGVFVYLPEIRKVALWTGRCVFCGQCVDVCPTGALQMSDDFLL 98

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446786817  16 VIIDEDKCIadkGCTVCVDVCPMDllAIDPTTQKAF-MQFDECWYCMPCEKDCPTDAVKVN 75
Cdd:cd10549   73 AEIDEEKCI---GCGLCVKVCPVD--AITLEDELEIvIDKEKCIGCGICAEVCPVNAIKLV 128

ribosome biogenesis/translation initiation ATPase RLI;

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446786817  17 IIDEDKCIADKGCTVCVDVCPM-----DLLAIDPTTQKAFMQFDECWYCMPCEKDCPTDAVK-VNIP 77
Cdd:PRK13409   6 VVDYDRCQPKKCNYECIKYCPVvrtgeETIEIDEDDGKPVISEELCIGCGICVKKCPFDAISiVNLP 72

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
                 ....*....|....*....|....*....|....*....|....*....
gi 446786817  28 GCTVCVDVCPMDLLAIDP-----TTQKAFMQFDECWYCMPCEKDCPTDA 71
Cdd:pfam12838  3 GCGACVAACPVGAITLDEvgekkGTKTVVIDPERCVGCGACVAVCPTGA 51

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446786817  16 VIIDEDKCIA---DKGCTVCVDVCPMDLLAIDPTTQKAFMQFDE--CWYCMPCEKDCPTDAVK 73
Cdd:cd16373   86 AVIDKDRCLAwqgGTDCGVCVEACPTEAIAIVLEDDVLRPVVDEdkCVGCGLCEYVCPVEPPK 148

Fe-S cluster domain-containing protein;

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446786817  16 VIIDEDKCIadkGCTVCVDVCPMDLLAIDPTTQKAFMQFDE--------------CWYCMPCEKDCPTDAVKV 74
Cdd:PRK07118 163 PVVDEDKCT---GCGACVKACPRNVIELIPKSARVFVACNSkdkgkavkkvcevgCIGCGKCVKACPAGAITM 232

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
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446786817  16 VIIDEDKCIadkGCTVCVDVCPMDLLAIDPTTQKAFMqfdeCWYCMPCEKDCPTD 70
Cdd:cd16370   78 VVLDKEKCI---GCGNCVKACIVGAIFWDEETNKPII----CIHCGYCARYCPHD 125

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446786817  16 VIIDEDKCIadkGCTVCVDVCPMDLLAIDPTTQKAFmqfdECWYCM---------PCEKDCPTDAVK 73
Cdd:cd10558   96 VDFQSDKCI---GCGYCIKGCPFDIPRISKDDNKMY----KCTLCSdrvsvglepACVKTCPTGALH 155

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446786817  17 IIDEDKCIadkGCTVCVDVCPMDLLAIDPTTQKAFMQ---FDECWYCMPCEKDCPTDAVKVNIPY 78
Cdd:cd10549    2 KYDPEKCI---GCGICVKACPTDAIELGPNGAIARGPeidEDKCVFCGACVEVCPTGAIELTPEG 63

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

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446786817  17 IIDEDKCIADKGCTVCVDVCPM-----DLLAIDPTTQKAFMQFDECWYCMPCEKDCPTDAVK-VNIP 77
Cdd:COG1245    6 VVDRDRCQPKKCNYECIKYCPVnrtgkEAIEIDEDDGKPVISEELCIGCGICVKKCPFDAISiVNLP 72

tetrathionate reductase subunit TtrB;

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446786817  16 VIIDEDKCIadkGCTVCVDVCPMDLLAIDPTTQKAfmqfDECWYC 60
Cdd:PRK14993 125 VVVDNKRCV---GCAYCVQACPYDARFINHETQTA----DKCTFC 162

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

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446786817  16 VIIDEDKCIadkGCTVCVDVCPMDllAIDPTTQKAFMQFDECWYCMPCEKDCPTDAVKV 74
Cdd:COG4624   86 IIRDKEKCK---NCYPCVRACPVK--AIKVDDGKAEIDEEKCISCGQCVAVCPFGAITE 139

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

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446786817  16 VIIDEDKCIadkGCTVCVDVCPMDLLAIDPTTQKAfmqfDECWYCMP---------CEKDCPTDA 71
Cdd:COG0437   85 VLVDYDKCI---GCRYCVAACPYGAPRFNPETGVV----EKCTFCADrldegllpaCVEACPTGA 142

formate hydrogenlyase complex iron-sulfur subunit; Provisional

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446786817  14 APVIIDE----------DKCIadkGCTVCVDVCPMDLLAI--DPTTQKAFMQFD--ECWYCMPCEKDCPTDAVK 73
Cdd:PRK12387  21 EPIAVDKnfrgkpeynpQQCI---GCAACVNACPSNALTVetDLATGELAWEFNlgRCIFCGRCEEVCPTAAIK 91

photosystem I subunit VII; Provisional

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446786817 21 DKCIadkGCTVCVDVCPMDLLAIDPTTQKAFMQF------DECWYCMPCEKDCPTDAVKVNI 76
Cdd:PLN00071  9 DTCI---GCTQCVRACPTDVLEMIPWDGCKAKQIasaprtEDCVGCKRCESACPTDFLSVRV 67

4Fe-4S dicluster domain;

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446786817  28 GCTVCVDVCPMDLLAIDPTTQKAFMQFDE--CWYCMPCEKDCPTDAV 72
Cdd:pfam13187  4 GCGACVAACPAGAIVPDLVGQTIRGDIAGlaCIGCGACVDACPRGAI 50