Domain of unknown function (DUF3470); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 50 amino acids in length. This domain is found associated with pfam00037. This domain has a single completely conserved residue N that may be functionally important.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
1FD2_A         65 QEFIQLNAELAEVWPNITEKKDPLPDAEDWDGVKGKLQHLER 106
Cdd:pfam11953   1 EKFIELNAELAKIWPNITEKKDPLPDADEWKGVPDKLELLER 42

Domain of unknown function (DUF3470); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 50 amino acids in length. This domain is found associated with pfam00037. This domain has a single completely conserved residue N that may be functionally important.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
1FD2_A         65 QEFIQLNAELAEVWPNITEKKDPLPDAEDWDGVKGKLQHLER 106
Cdd:pfam11953   1 EKFIELNAELAKIWPNITEKKDPLPDADEWKGVPDKLELLER 42

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
                  ....*....|....*....|....*....|....*....|....*....|....*
1FD2_A          1 AFVVTDNCIKCkyTDCVEVAPVDCFYEGPNFL-VIHPDECIDCALCEPECPAQAI 54
Cdd:TIGR01944 108 ALIDEDNCIGC--TKCIQACPVDAIVGAAKAMhTVIADECTGCDLCVEPCPTDCI 160

bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
1FD2_A        1 AFVVTDNCIKCKytDCVEVAPVDCFYEGPNFLVIHPDECIDCALCEPECPAQAIFSEDEV 60
Cdd:cd03110  59 AFIDQEKCIRCG--NCERVCKFGAILEFFQKLIVDESLCEGCGACVIICPRGAIYLKDRD 116

Rnf electron transport complex subunit RnfB;

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
1FD2_A         1 AFVVTDNCIKCkyTDCVEVAPVDCFYEGPNFL--VIHPdECIDCALCEPECPAQAI 54
Cdd:PRK08764  80 AWIVEADCIGC--TKCIQACPVDAIVGGAKHMhtVIAP-LCTGCELCVPACPVDCI 132

Domain of unknown function (DUF3470); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 50 amino acids in length. This domain is found associated with pfam00037. This domain has a single completely conserved residue N that may be functionally important.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
1FD2_A         65 QEFIQLNAELAEVWPNITEKKDPLPDAEDWDGVKGKLQHLER 106
Cdd:pfam11953   1 EKFIELNAELAKIWPNITEKKDPLPDADEWKGVPDKLELLER 42

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

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
1FD2_A        1 AFVVTDNCIKCKytDCVEVAPVDCFYEGPNFLVIHPDECIDCALCEPECPAQAIFSEDEVPE 62
Cdd:COG4231  17 YVIDEDKCTGCG--ACVKVCPADAIEEGDGKAVIDPDLCIGCGSCVQVCPVDAIKLEKRVPE 76

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
                  ....*....|....*....|....*....|....*....|....*....|....*
1FD2_A          1 AFVVTDNCIKCkyTDCVEVAPVDCFYEGPNFL-VIHPDECIDCALCEPECPAQAI 54
Cdd:TIGR01944 108 ALIDEDNCIGC--TKCIQACPVDAIVGAAKAMhTVIADECTGCDLCVEPCPTDCI 160

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

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
1FD2_A        1 AFVVTDNCIKCKytDCVEVAPVDCFY-EGPNFLVIHPDECIDCALCEPECPAQAI 54
Cdd:COG1149   6 PVIDEEKCIGCG--LCVEVCPEGAIKlDDGGAPVVDPDLCTGCGACVGVCPTGAI 58

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

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
1FD2_A        5 TDNCIKCkyTDCVEVAPVDCFYEGPNFL-VIHPDECIDCALCEPECPAQAI 54
Cdd:COG2878 136 EYGCIGC--GDCIKACPFDAIVGAAKGMhTVDEDKCTGCGLCVEACPVDCI 184

YfhL family 4Fe-4S dicluster ferredoxin;

                         10        20
                 ....*....|....*....|....
1FD2_A        37 DECIDCALCEPECPAQAIFSEDEV 60
Cdd:NF033683   7 DECINCDVCEPECPNEAISMGDEI 30

Ferredoxin [Energy production and conversion];

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
1FD2_A        3 VVTDNCIKCKYtdCVEVAPVDCFY--EGPNFLVIHPDECIDCALCEPECPAQAI 54
Cdd:COG1145 179 IDAEKCIGCGL--CVKVCPTGAIRlkDGKPQIVVDPDKCIGCGACVKVCPVGAI 230

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).

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
1FD2_A         2 FVVTDNCIKCKYtdCVEVAPVDC--FYEG-PNFLvihpDECIDCALCEPECPAQAI 54
Cdd:NF038196 181 FHVTDKCIGCGI--CAKVCPVNNieMEDGkPVWG----HNCTHCLACIHRCPKEAI 230

Polyferredoxin NapH [Energy production and conversion];

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
1FD2_A        2 FVVT---DNCIKCKytDCVEVAPVDCFyegPNFLVIHPDECIDCALCEPECPAQAI 54
Cdd:COG0348 203 LRVRydrGDCIDCG--LCVKVCPMGID---IRKGEINQSECINCGRCIDACPKDAI 253

electron transport complex subunit RsxB;

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
1FD2_A         1 AFVVTDNCIKCkyTDCVEVAPVDCFYEGPNFL-VIHPDECIDCALCEPECPAQAIfseDEVP 61
Cdd:PRK06991  80 AVIDEQLCIGC--TLCMQACPVDAIVGAPKQMhTVLADLCTGCDLCVPPCPVDCI---DMVP 136

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.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
1FD2_A        2 FVVTDNCIKCKYTDCVEVAPVDCFYEGPN-FLVIHPDECIDCALCEPECPAQAIF 55
Cdd:cd04410  44 AFLPVSCMHCEDPPCVKACPTGAIYKDEDgIVLIDEDKCIGCGSCVEACPYGAIV 98

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

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
1FD2_A        6 DNCIKCkyTDCVEVAPVDCFYEGPNFLVIHPDECIDCALCEPECPAQAIFSEDEVPE 62
Cdd:COG4624  91 EKCKNC--YPCVRACPVKAIKVDDGKAEIDEEKCISCGQCVAVCPFGAITEKSDIEK 145

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
                ....*....|....*....|....*....|....*....|....
1FD2_A        8 CIKCKYTDCVEVAPVDCFYEGPN-FLVIHPDECIDCALCEPECP 50
Cdd:cd10562  70 CMHCTDAACVKVCPTGALYKTENgAVVVDEDKCIGCGYCVAACP 113

electron transport complex protein RnfB; Provisional

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
1FD2_A         1 AFVVTDNCIKCkyTDCVEVAPVDCFYEGPNFL--VIhPDECIDCALCEPECPAQAI 54
Cdd:PRK05113 109 AFIDEDNCIGC--TKCIQACPVDAIVGATKAMhtVI-SDLCTGCDLCVAPCPTDCI 161

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
                ....*....|....*....|....*..
1FD2_A       33 VIHPDECIDCALCEPECPAQAIFSEDE 59
Cdd:COG1144  26 VVDEDKCIGCGLCWIVCPDGAIRVDDG 52

Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];

                        10        20        30
                ....*....|....*....|....*....|....*.
1FD2_A       35 HPDECIDCALCEPECPaQAIfsedEVPEDMQEFIQL 70
Cdd:COG1453 329 KASACIECGACEERCP-QGL----DIPELLKEAHEL 359