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Conserved domains on  [gi|1997329585|ref|WP_206056922|]
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MULTISPECIES: hydrogenase 2 operon protein HybA [Escherichia]

Protein Classification

hydrogenase 2 operon protein HybA( domain architecture ID 11485058)

hydrogenase 2 operon protein HybA participates in the periplasmic electron-transferring activity of hydrogenase 2 during its catalytic turnover

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
1-328 0e+00

hydrogenase 2 operon protein HybA;


:

Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 640.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585   1 MNRRNFIKAASCGALLTGALPSVSHAAAENRPLIPGSLGMLYDSTLCVGCQACVTKCQDINFPERNPQGEQTWSNNDKLS 80
Cdd:PRK10882    1 MNRRNFLKAASAGALLAGALPSVSHAAAENRPPIPGALGMLYDSTLCVGCQACVTKCQEINFPERNPQGEQTWDNPDKLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  81 PYTNNIIQVWTSGTGVNKDQEENGYAYIKKQCMHCVDPNCVSVCPVSALKKDPKTGIVHYDKDVCTGCRYCMVACPYNVP 160
Cdd:PRK10882   81 PYTNNIIKVWKSGTGVNKDQEENGYAYIKKQCMHCVDPNCVSVCPVSALTKDPKTGIVHYDKDVCTGCRYCMVACPFNVP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 161 KYDYNNPFGALHKCELCNQKGVERLDKGGLPGCVEVCPAGAVIFGTREELMAEAKKRLALKPGSEYHYPRQTLKSGDTYL 240
Cdd:PRK10882  161 KYDYNNPFGAIHKCELCNQKGVERLDKGGLPGCVEVCPTGAVIFGTREELLAEAKRRLALKPGSEYHYPRQTLKSGDTYL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 241 HTVPKYYPHLYGEKEGGGTQVLVLTGVPYENLDLPKLDDLSTGARSENIQHTLYKGMMLPLAVLAGLTVLVRRNTKNDHH 320
Cdd:PRK10882  241 HTVPKYYPHVYGEKEGGGTQVLVLSGVPFENLGLPKLDDLSTGARSEHIQHTLYKGMILPLAVLAGLTVLVRRNTKNDHH 320


                  ....*...
gi 1997329585 321 DGGDDHES 328
Cdd:PRK10882  321 DGGDDHES 328
 
Name Accession Description Interval E-value
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
1-328 0e+00

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 640.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585   1 MNRRNFIKAASCGALLTGALPSVSHAAAENRPLIPGSLGMLYDSTLCVGCQACVTKCQDINFPERNPQGEQTWSNNDKLS 80
Cdd:PRK10882    1 MNRRNFLKAASAGALLAGALPSVSHAAAENRPPIPGALGMLYDSTLCVGCQACVTKCQEINFPERNPQGEQTWDNPDKLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  81 PYTNNIIQVWTSGTGVNKDQEENGYAYIKKQCMHCVDPNCVSVCPVSALKKDPKTGIVHYDKDVCTGCRYCMVACPYNVP 160
Cdd:PRK10882   81 PYTNNIIKVWKSGTGVNKDQEENGYAYIKKQCMHCVDPNCVSVCPVSALTKDPKTGIVHYDKDVCTGCRYCMVACPFNVP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 161 KYDYNNPFGALHKCELCNQKGVERLDKGGLPGCVEVCPAGAVIFGTREELMAEAKKRLALKPGSEYHYPRQTLKSGDTYL 240
Cdd:PRK10882  161 KYDYNNPFGAIHKCELCNQKGVERLDKGGLPGCVEVCPTGAVIFGTREELLAEAKRRLALKPGSEYHYPRQTLKSGDTYL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 241 HTVPKYYPHLYGEKEGGGTQVLVLTGVPYENLDLPKLDDLSTGARSENIQHTLYKGMMLPLAVLAGLTVLVRRNTKNDHH 320
Cdd:PRK10882  241 HTVPKYYPHVYGEKEGGGTQVLVLSGVPFENLGLPKLDDLSTGARSEHIQHTLYKGMILPLAVLAGLTVLVRRNTKNDHH 320


                  ....*...
gi 1997329585 321 DGGDDHES 328
Cdd:PRK10882  321 DGGDDHES 328
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 39-265 4.05e-104

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: 302.98  E-value: 4.05e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  39 GMLYDSTLCVGCQACVTKCQDINFPERNPQGE-QTWSNNDKLSPYTNNIIQVWTSGTGvnkdqeENGYAYIKKQCMHCVD 117
Cdd:cd10561     1 GVLYDTTRCIGCRACEVACKEWNGLPAEDTAFgPGWDNPRDLSAKTYTVIKRYEVETG------GKGFVFVKRQCMHCLD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 118 PNCVSVCPVSALKKDPkTGIVHYDKDVCTGCRYCMVACPYNVPKYDYNNPFGALHKCELCNqkgvERLDKGGLPGCVEVC 197
Cdd:cd10561    75 PACVSACPVGALRKTP-EGPVTYDEDKCIGCRYCMVACPFNIPKYEWDSANPKIRKCTMCY----DRLKEGKQPACVEAC 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1997329585 198 PAGAVIFGTREELMAEAKKRLALKPGseyhyprqtlksgdtylhtvpKYYPHLYGEKEGGGTQVLVLT 265
Cdd:cd10561   150 PTGALLFGKREELLAEAKRRIAANPG---------------------RYVDHVYGEKEAGGTSVLYLS 196
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 38-223 4.10e-58

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 185.54  E-value: 4.10e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  38 LGMLYDSTLCVGCQACVTKCQDINFPERNPqgeqtwsnndklspyTNNIIQVWTSGTGvnkdqEENGYAYIKKQCMHCVD 117
Cdd:COG0437     6 YGMVIDLTKCIGCRACVVACKEENNLPVGV---------------TWRRVRRYEEGEF-----PNVEWLFVPVLCNHCDD 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 118 PNCVSVCPVSALKKDpKTGIVHYDKDVCTGCRYCMVACPYNVPKYDYNNpfGALHKCELCnqkgVERLDKGGLPGCVEVC 197
Cdd:COG0437    66 PPCVKVCPTGATYKR-EDGIVLVDYDKCIGCRYCVAACPYGAPRFNPET--GVVEKCTFC----ADRLDEGLLPACVEAC 138

                         170       180
                  ....*....|....*....|....*.
gi 1997329585 198 PAGAVIFGTREELMAEAKKRLALKPG 223
Cdd:COG0437   139 PTGALVFGDLDDPESEVSKRLAELPA 164
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 111-207 1.09e-26

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: 101.17  E-value: 1.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 111 QCMHCVDPNCVSVCPVSALKKDPKTGIVHYDKDVCTGCRYCMVACPYNVPKYDYNNpfGALHKCELCNqkgvERLDKGGL 190
Cdd:pfam13247   9 QCRHCLNPPCKASCPVGAIYKDEETGAVLLDEKTCRGWRECVSACPYNIPRYNDET--GKAEKCDMCY----DRVEAGLL 82

                          90
                  ....*....|....*..
gi 1997329585 191 PGCVEVCPAGAVIFGTR 207
Cdd:pfam13247  83 PACVQTCPTGAMNFGDR 99
FDH3_beta NF038355
formate dehydrogenase FDH3 subunit beta; Members of this family are the beta subunit of the ...
 43-221 1.05e-24

formate dehydrogenase FDH3 subunit beta; Members of this family are the beta subunit of the FDH3 type of formate dehydrogenase as found in Methylorubrum (Methylobacterium) extorquens.


Pssm-ID: 439648 [Multi-domain]  Cd Length: 180  Bit Score: 98.21  E-value: 1.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  43 DSTLCVGCQACVTKCQDINfpernpqgEQTWSNNDKlspytnniiQVWTSGTGVNkdqeenGYAYIKKQCMHCVDPNCVS 122
Cdd:NF038355    8 DTERCIECNGCVVACKNAH--------ELPWGINRR---------RVVTLNDGVP------GEKSISVACMHCTDAPCAA 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 123 VCPVSALKKDpKTGIVHYDKDVCTGCRYCMVACPYNVPKYDYNNPFGA---LHKCELC-------------NQKGVERLD 186
Cdd:NF038355   65 VCPVDCFYIR-ADGIVLHDKDKCIGCGYCLYACPFGAPQFPKDGAFGArgkMDKCTFCaggpeetnseaerEKYGQNRIA 143

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1997329585 187 KGGLPGCVEVCPAGAVIFGTREELMAEAKKRLALK 221
Cdd:NF038355  144 EGKLPLCAEMCSTKALLAGDAEVVADIYRERVVAR 178
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 106-158 5.91e-03

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


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 37.08  E-value: 5.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1997329585 106 AYI-KKQCMHCVdpNCVSVCPVSALKKDPKTgiVH-YDKDVCTGCRYCMVACPYN 158
Cdd:TIGR01944 108 ALIdEDNCIGCT--KCIQACPVDAIVGAAKA--MHtVIADECTGCDLCVEPCPTD 158
 
Name Accession Description Interval E-value
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
1-328 0e+00

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 640.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585   1 MNRRNFIKAASCGALLTGALPSVSHAAAENRPLIPGSLGMLYDSTLCVGCQACVTKCQDINFPERNPQGEQTWSNNDKLS 80
Cdd:PRK10882    1 MNRRNFLKAASAGALLAGALPSVSHAAAENRPPIPGALGMLYDSTLCVGCQACVTKCQEINFPERNPQGEQTWDNPDKLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  81 PYTNNIIQVWTSGTGVNKDQEENGYAYIKKQCMHCVDPNCVSVCPVSALKKDPKTGIVHYDKDVCTGCRYCMVACPYNVP 160
Cdd:PRK10882   81 PYTNNIIKVWKSGTGVNKDQEENGYAYIKKQCMHCVDPNCVSVCPVSALTKDPKTGIVHYDKDVCTGCRYCMVACPFNVP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 161 KYDYNNPFGALHKCELCNQKGVERLDKGGLPGCVEVCPAGAVIFGTREELMAEAKKRLALKPGSEYHYPRQTLKSGDTYL 240
Cdd:PRK10882  161 KYDYNNPFGAIHKCELCNQKGVERLDKGGLPGCVEVCPTGAVIFGTREELLAEAKRRLALKPGSEYHYPRQTLKSGDTYL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 241 HTVPKYYPHLYGEKEGGGTQVLVLTGVPYENLDLPKLDDLSTGARSENIQHTLYKGMMLPLAVLAGLTVLVRRNTKNDHH 320
Cdd:PRK10882  241 HTVPKYYPHVYGEKEGGGTQVLVLSGVPFENLGLPKLDDLSTGARSEHIQHTLYKGMILPLAVLAGLTVLVRRNTKNDHH 320


                  ....*...
gi 1997329585 321 DGGDDHES 328
Cdd:PRK10882  321 DGGDDHES 328
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 39-265 4.05e-104

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: 302.98  E-value: 4.05e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  39 GMLYDSTLCVGCQACVTKCQDINFPERNPQGE-QTWSNNDKLSPYTNNIIQVWTSGTGvnkdqeENGYAYIKKQCMHCVD 117
Cdd:cd10561     1 GVLYDTTRCIGCRACEVACKEWNGLPAEDTAFgPGWDNPRDLSAKTYTVIKRYEVETG------GKGFVFVKRQCMHCLD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 118 PNCVSVCPVSALKKDPkTGIVHYDKDVCTGCRYCMVACPYNVPKYDYNNPFGALHKCELCNqkgvERLDKGGLPGCVEVC 197
Cdd:cd10561    75 PACVSACPVGALRKTP-EGPVTYDEDKCIGCRYCMVACPFNIPKYEWDSANPKIRKCTMCY----DRLKEGKQPACVEAC 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1997329585 198 PAGAVIFGTREELMAEAKKRLALKPGseyhyprqtlksgdtylhtvpKYYPHLYGEKEGGGTQVLVLT 265
Cdd:cd10561   150 PTGALLFGKREELLAEAKRRIAANPG---------------------RYVDHVYGEKEAGGTSVLYLS 196
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 38-223 4.10e-58

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 185.54  E-value: 4.10e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  38 LGMLYDSTLCVGCQACVTKCQDINFPERNPqgeqtwsnndklspyTNNIIQVWTSGTGvnkdqEENGYAYIKKQCMHCVD 117
Cdd:COG0437     6 YGMVIDLTKCIGCRACVVACKEENNLPVGV---------------TWRRVRRYEEGEF-----PNVEWLFVPVLCNHCDD 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 118 PNCVSVCPVSALKKDpKTGIVHYDKDVCTGCRYCMVACPYNVPKYDYNNpfGALHKCELCnqkgVERLDKGGLPGCVEVC 197
Cdd:COG0437    66 PPCVKVCPTGATYKR-EDGIVLVDYDKCIGCRYCVAACPYGAPRFNPET--GVVEKCTFC----ADRLDEGLLPACVEAC 138

                         170       180
                  ....*....|....*....|....*.
gi 1997329585 198 PAGAVIFGTREELMAEAKKRLALKPG 223
Cdd:COG0437   139 PTGALVFGDLDDPESEVSKRLAELPA 164
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 40-210 1.15e-42

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: 144.75  E-value: 1.15e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  40 MLYDSTLCVGCQACVTKCQDIN-FPERNPQGEQTWSNNDKLSPYTNNIIQVWTSGTGVNKDQeengYAYIKKQCMHCVDP 118
Cdd:cd10562     1 MLVDTSKCTACRGCQVACKQWNqLPAEKTPFTGSYQNPPDLTPNTWTLIRFYEHEEDNGGIR----WLFRKRQCMHCTDA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 119 NCVSVCPVSALKKDpKTGIVHYDKDVCTGCRYCMVACPYNVPKYDYNNpfGALHKCELCnqkgVERLDKGGLPGCVEVCP 198
Cdd:cd10562    77 ACVKVCPTGALYKT-ENGAVVVDEDKCIGCGYCVAACPFDVPRYDETT--NKITKCTLC----FDRIENGMQPACVKTCP 149

                         170
                  ....*....|..
gi 1997329585 199 AGAVIFGTREEL 210
Cdd:cd10562   150 TGALTFGDRDEL 161
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 41-268 2.00e-41

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: 143.30  E-value: 2.00e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  41 LYDSTLCVGCQACVTKCQ---DINFPERNPQGeqTWSNNDKLSPYTNNIIQVwtsgtgvnKDQEENG---YAYIKKQCMH 114
Cdd:cd10558     3 LIDVSKCIGCKACQVACKewnDLRAEVGHNVG--TYQNPADLSPETWTLMKF--------REVEDNGkleWLIRKDGCMH 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 115 CVDPNCVSVCPVSALKKDPKTGIVHYDKDVCTGCRYCMVACPYNVPKYDYNNpfGALHKCELCNQKGVERLDkgglPGCV 194
Cdd:cd10558    73 CADPGCLKACPSPGAIVQYANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDD--NKMYKCTLCSDRVSVGLE----PACV 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1997329585 195 EVCPAGAVIFGTREELMAEAKKRLA-LKpgsEYHYPRQTlksgdtylhtvpkyyphLYGEKEGGGTQVL-VLTGVP 268
Cdd:cd10558   147 KTCPTGALHFGTKEDMLALAEKRVAaLK---ERGYTNAG-----------------LYDPKGVGGTHVMyVLHHAD 202
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 40-205 4.86e-41

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: 141.52  E-value: 4.86e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  40 MLYDSTLCVGCQACVTKCQDINfperNPQGEQTWsnndklspytnniIQVWTSGTGvnkDQEENGYAYIKKQCMHCVDPN 119
Cdd:cd10551     1 MVIDLRKCIGCGACVVACKAEN----NVPPGVFR-------------NRVLEYEVG---EYPNVKRTFLPVLCNHCENPP 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 120 CVSVCPVSALKKDPkTGIVHYDKDVCTGCRYCMVACPYNVPKYDYNNPFGALH----------KCELCnqkgVERLDKGG 189
Cdd:cd10551    61 CVKVCPTGATYKRE-DGIVLVDYDKCIGCRYCMAACPYGARYFNPEEPHEFGEvpvrpkgvveKCTFC----YHRLDEGL 135

                         170
                  ....*....|....*.
gi 1997329585 190 LPGCVEVCPAGAVIFG 205
Cdd:cd10551   136 LPACVEACPTGARIFG 151
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 39-205 8.74e-40

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: 136.54  E-value: 8.74e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  39 GMLYDSTLCVGCQACVTKCQDINfperNPQGEQTWsnndklspytnniIQVWTSGTGVNKDQEEngyAYIKKQCMHCVDP 118
Cdd:cd16371     1 GFYFDQERCIGCKACEIACKDKN----DLPPGVNW-------------RRVYEYEGGEFPEVFA---YFLSMSCNHCENP 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 119 NCVSVCPVSALKKDPkTGIVHYDKDVCTGCRYCMVACPYNVPKYDYNNpfGALHKCELCnqkgVERLDKGGLPGCVEVCP 198
Cdd:cd16371    61 ACVKVCPTGAITKRE-DGIVVVDQDKCIGCGYCVWACPYGAPQYNPET--GKMDKCDMC----VDRLDEGEKPACVAACP 133


                  ....*..
gi 1997329585 199 AGAVIFG 205
Cdd:cd16371   134 TRALDFG 140
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 40-205 1.49e-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: 134.06  E-value: 1.49e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  40 MLYDSTLCVGCQACVTKCQDIN-FPERNPQGEQTWSNNDKLSPYTNNIIQVwtsgtgvnKDQEENG----YAYIKKQCMH 114
Cdd:cd16366     1 FLVDTSRCTGCRACQVACKQWNgLPAEKTEFTGSYQNPPDLTAHTWTLVRF--------YEVEKPGgdlsWLFRKDQCMH 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 115 CVDPNCVSVCPVSALKKDPkTGIVHYDKDVCTGCRYCMVACPYNVPKYDYNnpFGALHKCELCnqkgVERLDKGGLPGCV 194
Cdd:cd16366    73 CTDAGCLAACPTGAIIRTE-TGTVVVDPETCIGCGYCVNACPFDIPRFDEE--TGRVAKCTLC----YDRISNGLQPACV 145

                         170
                  ....*....|.
gi 1997329585 195 EVCPAGAVIFG 205
Cdd:cd16366   146 KTCPTGALTFG 156
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 40-205 3.64e-38

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: 132.51  E-value: 3.64e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  40 MLYDSTLCVGCQACVTKCQDINFPERNPQgeqtwsnndklspyTNNIIQVWTsgtgvnkdqEENGYAYIKKQCMHCVDPN 119
Cdd:cd04410     1 LVVDLDRCIGCGTCEVACKQEHGLRPGPD--------------WSRIKVIEG---------GGLERAFLPVSCMHCEDPP 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 120 CVSVCPVSALKKDPkTGIVHYDKDVCTGCRYCMVACPYNVPKYDYNNpfGALHKCELCnqkgVERLDKGGLPGCVEVCPA 199
Cdd:cd04410    58 CVKACPTGAIYKDE-DGIVLIDEDKCIGCGSCVEACPYGAIVFDPEP--GKAVKCDLC----GDRLDEGLEPACVKACPT 130


                  ....*.
gi 1997329585 200 GAVIFG 205
Cdd:cd04410   131 GALTFG 136
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 39-277 7.92e-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: 121.34  E-value: 7.92e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  39 GMLYDSTLCVGCQACVTKCQDINFPERNPQGEQTWS--NNDKLSPYTNNII----QVWTSGTGVNKDQEEngYAYIKKQC 112
Cdd:cd10560     1 GFFTDTSICIGCKACEVACKQWNQLPADGYDFSGMSydNTGDLSASTWRHVkfieRPTEDGPANEGGDLQ--WLFMSDVC 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 113 MHCVDPNCVSVCPVSALKKDPkTGIVHYDKDVCTGCRYCMVACPYNVPkyDYNNPFGALHKCELCNqkgvERLDKGGLPG 192
Cdd:cd10560    79 KHCTDAGCLEACPTGAIFRTE-FGTVYIQPDICNGCGYCVAACPFGVI--DRNEETGRAHKCTLCY----DRLKDGLEPA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 193 CVEVCPAGAVIFGTREELMAEAKKRLAlkpgseyhyprqtlksgdtYLHTVPKYYPHLYGEKEGGGTQVLVLtgvPYENL 272
Cdd:cd10560   152 CAKACPTGSIQFGPLEELRERARARVE-------------------QLHEQGVVEAYLYGADPTEGYGGLNA---FFLLL 209


                  ....*
gi 1997329585 273 DLPKL 277
Cdd:cd10560   210 DKPEV 214
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 43-215 5.57e-32

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: 116.22  E-value: 5.57e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  43 DSTLCVGCQACVTKCQDINFPERNpqgeqtwsnndklspytnniIQVWTSGTGvnkdqeengyAYIKKQCMHCVDPNCVS 122
Cdd:cd16374     4 DPERCIGCRACEIACAREHSGKPR--------------------ISVEVVEDL----------ASVPVRCRHCEDAPCME 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 123 VCPVSALKKDPkTGIVHYDKDVCTGCRYCMVACPYNVPKYDYNNpfGALHKCELCnqkgVERLDKGGLPGCVEVCPAGAV 202
Cdd:cd16374    54 VCPTGAIYRDE-DGAVLVDPDKCIGCGMCAMACPFGVPRFDPSL--KVAVKCDLC----IDRRREGKLPACVEACPTGAL 126

                         170
                  ....*....|...
gi 1997329585 203 IFGTREELMAEAK 215
Cdd:cd16374   127 KFGDIEELLKEKR 139
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 38-215 1.40e-31

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: 117.14  E-value: 1.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  38 LGMLYDSTLCVGCQ-----ACVTKCQDIN---FPERNPQGEQT---------WSNN----DKLSPYTnniiqvWTSGTGV 96
Cdd:cd16368     1 LATLIDLTKCDGCPgesipACVRACREKNqarFPEPVSKPIQPywprkriedWSDKrdvtDRLTPYN------WLYVQKL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  97 NKDQEENGY-AYIKKQCMHCVDPNCVSVCPVSALKKDPkTGIVHYDKDVCTGCRYCMVACPYNVPK-------YDYNNP- 167
Cdd:cd16368    75 TVDTAGGEKeVFIPRRCMHCDNPPCAKLCPFGAARKTP-EGAVYIDDDLCFGGAKCRDVCPWHIPQrqagvgiYLHLAPe 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1997329585 168 ---FGALHKCELCnqkgVERLDKGGLPGCVEVCPAGAVIFGTREELMAEAK 215
Cdd:cd16368   154 yagGGVMYKCDLC----KDLLAQGKPPACIEACPKGAQYFGPRKEMVALAR 200
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 43-201 1.14e-28

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: 107.28  E-value: 1.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  43 DSTLCVGCQACVTKCqdinfpernpqgeqTWSNNDKLSPYTNNIiQVWtsgtgvnkdQEENGYAYIKKQCMHCVDPNCVS 122
Cdd:cd10550     4 DPEKCTGCRTCELAC--------------SLKHEGVFNPSLSRI-RVV---------RFEPEGLDVPVVCRQCEDAPCVE 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 123 VCPVSALKKDPKTGIVHYDKDVCTGCRYCMVACPYNVPKYDYNN--PFgalhKCELCnqkgverldkGGLPGCVEVCPAG 200
Cdd:cd10550    60 ACPVGAISRDEETGAVVVDEDKCIGCGMCVEACPFGAIRVDPETgkAI----KCDLC----------GGDPACVKVCPTG 125


                  .
gi 1997329585 201 A 201
Cdd:cd10550   126 A 126
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 40-206 1.91e-28

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: 107.45  E-value: 1.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  40 MLY-DSTLCVGCQACVTKCQDINfpeRNPQGeqtwsnndklsPYTNNIIqvwTSGTGVNKDQEENGYAYIKkqCMHCVDP 118
Cdd:cd10553     4 YLYhDSKRCIGCLACEVHCKVKN---NLPVG-----------PRLCRIF---AVGPKMVGGKPRLKFVYMS--CFHCENP 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 119 NCVSVCPVSALKKDPKTGIVHYDKDVCTGCRYCMVACPYNVPKydYNNPFGALHKCELCnqkgVERLDKGGLPGCVEVCP 198
Cdd:cd10553    65 WCVKACPTGAMQKREKDGIVYVDQELCIGCKACIEACPWGIPQ--WNPATGKVVKCDYC----MDRIDQGLKPACVTGCT 138


                  ....*...
gi 1997329585 199 AGAVIFGT 206
Cdd:cd10553   139 THALSFVR 146
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 39-239 3.66e-28

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: 108.29  E-value: 3.66e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  39 GMLYDSTLCVGCQACVTKCQDINfpeRNPqGEQT-----WSNNDKLSPYTNNIIQVwtsgtgvNKDQEENG---YAYIKK 110
Cdd:cd10559     1 SFLIDTTRCTACRGCQVACKQWN---QLP-AEQTkntgsHQNPPDLSANTYKLVRF-------NEVRNENGkpdWLFFPD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 111 QCMHCVDPNCVSVCPV--SALKKDPKTGIVHYDKDVCTGCRYCMV-ACPYNVPKYdyNNPFGALHKCELCNqkgvERLDK 187
Cdd:cd10559    70 QCRHCVTPPCKDAADMvpGAVIQDEATGAVVFTEKTAELDFDDVLsACPYNIPRK--NEATGRIVKCDMCI----DRVSN 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1997329585 188 GGLPGCVEVCPAGAVIFGTREELMAEAKKRLA-LKPgseyHYPRQTLKSGDTY 239
Cdd:cd10559   144 GLQPACVKACPTGAMNFGDRDEMLAMASKRLEeLKK----RYPKANLYDPDDV 192
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 43-205 4.40e-27

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: 103.49  E-value: 4.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  43 DSTLCVGCQACVTKCQDinfpERNPQGEQTWSNNDKLSPyTNNIIQvwtsgtgvnkdqEENGYAYIKKQCMHCVDPNCVS 122
Cdd:cd10563     5 DEEKCLGCKLCEVACAV----AHSKSKDLIKAKLEKERP-RPRIRV------------EESGGRSFPLQCRHCDEPPCVK 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 123 VCPVSALKKDPKTGIVHYDKDVCTGCRYCMVACPYNVPKYDYNNpfGALHKCELCNQKGVerldkgglPGCVEVCPAGAV 202
Cdd:cd10563    68 ACMSGAMHKDPETGIVIHDEEKCVGCWMCVMVCPYGAIRPDKER--KVALKCDLCPDRET--------PACVEACPTGAL 137


                  ...
gi 1997329585 203 IFG 205
Cdd:cd10563   138 VLE 140
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 111-207 1.09e-26

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: 101.17  E-value: 1.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 111 QCMHCVDPNCVSVCPVSALKKDPKTGIVHYDKDVCTGCRYCMVACPYNVPKYDYNNpfGALHKCELCNqkgvERLDKGGL 190
Cdd:pfam13247   9 QCRHCLNPPCKASCPVGAIYKDEETGAVLLDEKTCRGWRECVSACPYNIPRYNDET--GKAEKCDMCY----DRVEAGLL 82

                          90
                  ....*....|....*..
gi 1997329585 191 PGCVEVCPAGAVIFGTR 207
Cdd:pfam13247  83 PACVQTCPTGAMNFGDR 99
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 40-213 2.03e-26

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: 102.85  E-value: 2.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  40 MLYDSTLCVGCQACVTKCQdinfpERNPQGEQTWSNNDKLSPYTNniiqVWTSGTgvnkdqeengyayikkQCMHCVDPN 119
Cdd:cd16369     4 FFIDPSRCIGCRACVAACR-----ECGTHRGKSMIHVDYIDRGES----TQTAPT----------------VCMHCEDPT 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 120 CVSVCPVSALKKDPKtGIVHY-DKDVCTGCRYCMVACPYNVPKYDYNNPFgaLHKCELCnqkgVERLDKGGLPGCVEVCP 198
Cdd:cd16369    59 CAEVCPADAIKVTED-GVVQSaLKPRCIGCSNCVNACPFGVPKYDEERNL--MMKCDMC----YDRTSVGKAPMCASVCP 131

                         170
                  ....*....|....*
gi 1997329585 199 AGAVIFGTREELMAE 213
Cdd:cd16369   132 SGALFYGTREEIQAL 146
FDH3_beta NF038355
formate dehydrogenase FDH3 subunit beta; Members of this family are the beta subunit of the ...
 43-221 1.05e-24

formate dehydrogenase FDH3 subunit beta; Members of this family are the beta subunit of the FDH3 type of formate dehydrogenase as found in Methylorubrum (Methylobacterium) extorquens.


Pssm-ID: 439648 [Multi-domain]  Cd Length: 180  Bit Score: 98.21  E-value: 1.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  43 DSTLCVGCQACVTKCQDINfpernpqgEQTWSNNDKlspytnniiQVWTSGTGVNkdqeenGYAYIKKQCMHCVDPNCVS 122
Cdd:NF038355    8 DTERCIECNGCVVACKNAH--------ELPWGINRR---------RVVTLNDGVP------GEKSISVACMHCTDAPCAA 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 123 VCPVSALKKDpKTGIVHYDKDVCTGCRYCMVACPYNVPKYDYNNPFGA---LHKCELC-------------NQKGVERLD 186
Cdd:NF038355   65 VCPVDCFYIR-ADGIVLHDKDKCIGCGYCLYACPFGAPQFPKDGAFGArgkMDKCTFCaggpeetnseaerEKYGQNRIA 143

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1997329585 187 KGGLPGCVEVCPAGAVIFGTREELMAEAKKRLALK 221
Cdd:NF038355  144 EGKLPLCAEMCSTKALLAGDAEVVADIYRERVVAR 178
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
39-205 2.34e-23

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 96.48  E-value: 2.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  39 GMLYDSTLCVGCQACVTKCQDINfpeRNPQGEqtwsnndklspYTNNIIQVWTSGTGvnkdQEENGYAYIKKQCMHCVDP 118
Cdd:PRK14993   45 AMLIDLRRCIGCQSCTVSCTIEN---QTPQGA-----------FRTTVNQYQVQREG----SQEVTNVLLPRLCNHCDNP 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 119 NCVSVCPVSALKKDpKTGIVHYDKDVCTGCRYCMVACPYNVpkYDYNNPFGALHKCELCnqkgVERLDKGGLPGCVEVCP 198
Cdd:PRK14993  107 PCVPVCPVQATFQR-EDGIVVVDNKRCVGCAYCVQACPYDA--RFINHETQTADKCTFC----VHRLEAGLLPACVESCV 179


                  ....*..
gi 1997329585 199 AGAVIFG 205
Cdd:PRK14993  180 GGARIIG 186
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
43-204 1.27e-20

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 86.25  E-value: 1.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  43 DSTLCVGCQACVTKCQDINFPERNPQgEQTWsnndklspytnniIQVwtsgtgvnkdqEENGYAYIKKQCMHCVDPNCVS 122
Cdd:COG1142     8 DPEKCIGCRTCEAACAVAHEGEEGEP-FLPR-------------IRV-----------VRKAGVSAPVQCRHCEDAPCAE 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 123 VCPVSALKKDpkTGIVHYDKDVCTGCRYCMVACPYNVPKYDYNNPFGALHKCELCnqkgverLDKGGLPGCVEVCPAGAV 202
Cdd:COG1142    63 VCPVGAITRD--DGAVVVDEEKCIGCGLCVLACPFGAITMVGEKSRAVAVKCDLC-------GGREGGPACVEACPTGAL 133


                  ..
gi 1997329585 203 IF 204
Cdd:COG1142   134 RL 135
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 38-205 2.93e-20

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: 86.87  E-value: 2.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  38 LGMLYDSTLCVGCQACVTKCQdiNFPERNPQGEQTWSNNDKLSPYtNNIIQVWTsgtgvNKDQEENGYA----YIKKQCM 113
Cdd:cd16365     3 FAAVFNLNKCIGCQTCTVACK--NAWTYRKGQEYMWWNNVETKPG-GGYPQDWE-----VKTIDNGGNTrfffYLQRLCN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 114 HCVDPNCVSVCPVSALKKDPKTGIVHYDKDVCTGCRYCMVACPYNVPKydYNNPFGALHKCELCnqkgVERLDKGGLPGC 193
Cdd:cd16365    75 HCTNPACLAACPRGAIYKREEDGIVLIDQKRCRGYRKCVEQCPYKKIY--FNGLSRVSEKCIAC----YPRIEGGDPTRC 148

                         170
                  ....*....|..
gi 1997329585 194 VEVCPAGAVIFG 205
Cdd:cd16365   149 MSACVGRIRLQG 160
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 43-201 8.06e-20

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: 84.23  E-value: 8.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  43 DSTLCVGCQ----ACVTKCQDINFPERNPQGEQtwsnndkLSPyTNNIIQVwtsgtgvnkdqeENGYAYIkkQCMHCVDP 118
Cdd:cd10554     5 DPDKCIGCRtcevACAAAHSGKGIFEAGTDGLP-------FLP-RLRVVKT------------GEVTAPV--QCRQCEDA 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 119 NCVSVCPVSALKKDPktGIVHYDKDVCTGCRYCMVACPY---NVPKYDYNNPFGAL------HKCELCNqkgverlDKGG 189
Cdd:cd10554    63 PCANVCPVGAISQED--GVVQVDEERCIGCKLCVLACPFgaiEMAPTTVPGVDWERgpravaVKCDLCA-------GREG 133

                         170
                  ....*....|..
gi 1997329585 190 LPGCVEVCPAGA 201
Cdd:cd10554   134 GPACVEACPTKA 145
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 40-215 3.88e-17

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: 78.14  E-value: 3.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  40 MLYDSTLCVGCQACVTKCQDinfpernpqgeqTWSNNDkLSPYTNNiiQVWTSGTGVNKDQEENG------YAYIKKQCM 113
Cdd:cd10552     1 LVIDVAKCNGCYNCFLACKD------------EHVGND-WPGYAAP--QPRHGHFWMRILRRERGqypkvdVAYLPVPCN 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 114 HCVDPNCVSVCPVSALKKDPKtGIVHYDKDVCTGCRYCMVACPYNVpkYDYNNPFGALHKCELCnqkgVERLDKG-GLPG 192
Cdd:cd10552    66 HCDNAPCIKAAKDGAVYKRDD-GIVIIDPEKAKGQKQLVDACPYGA--IYWNEELQVPQKCTFC----AHLLDDGwKEPR 138

                         170       180
                  ....*....|....*....|...
gi 1997329585 193 CVEVCPAGAVIFGTREELMAEAK 215
Cdd:cd10552   139 CVQACPTGALRFGKLEDEEMAAK 161
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 59-209 5.40e-16

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: 77.34  E-value: 5.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  59 DINFPERNPQGEQTWSN-NDKLSPytnniiqVWtsgtGVNKDQEE-------NGYAYIKKQCMHCVDPNCVSVCPVSALK 130
Cdd:cd10555    83 EYNHEEELFEGKGGRVRpSPKGDP-------TW----GPNWDEDQgageypnSYYFYLPRICNHCTNPACLAACPRKAIY 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 131 KDPKTGIVHYDKDVCTGCRYCMVACPYNVPkydYNNPF-GALHKCELCnqkgVERLDKGGLPGCVEVCPAGAVIFGTREE 209
Cdd:cd10555   152 KREEDGIVLVDQDRCRGYRYCVEACPYKKI---YFNPVeQKSEKCIFC----YPRIEKGVAPACARQCVGRIRFVGYLDD 224
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 107-197 1.06e-15

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: 77.02  E-value: 1.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 107 YIKKQCMHCVDPNCVSVCPVSALKKDPKTGIVHYDKDVCTGCRYCMVACPYNvpKYDYNNPFGALHKCELCnqkgVERLD 186
Cdd:cd10557   174 YLPRICNHCLNPACVAACPSGAIYKREEDGIVLIDQDRCRGWRMCVSACPYK--KVYYNWKTGKSEKCIFC----YPRLE 247

                          90
                  ....*....|.
gi 1997329585 187 KGGLPGCVEVC 197
Cdd:cd10557   248 AGQPTVCSETC 258
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 43-202 1.78e-14

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 73.91  E-value: 1.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  43 DSTLCVGCQACVTKCQDINFPERNPQgeqtwSNNDKLSPytnniIQVWTSGTGVNKdqeengyayikKQCMHCVDPNCVS 122
Cdd:PRK12809    8 EAAECIGCHACEIACAVAHNQENWPL-----SHSDFRPR-----IHVVGKGQAANP-----------VACHHCNNAPCVT 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 123 VCPVSALKKDPKTgiVHYDKDVCTGCRYCMVACPYNVPKYDYNnpfgALHKCELCNQKgverldKGGLPGCVEVCPAGAV 202
Cdd:PRK12809   67 ACPVNALTFQSDS--VQLDEQKCIGCKRCAIACPFGVVEMVDT----IAQKCDLCNQR------SSGTQACIEVCPTQAL 134
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 43-202 1.94e-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: 68.90  E-value: 1.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  43 DSTLCVGCQACVTKCQDINFPERNPqgeqtwsnndklspyTNNIIQVwtsgtgvnkDQEENGYAYIkkQCMHCvdPNCVS 122
Cdd:cd16372     6 DPEKCIGCLQCEEACSKTFFKEEDR---------------EKSCIRI---------TETEGGYAIN--VCNQC--GECID 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 123 VCPVSALKKDPKtGIVHYDKDVCTGCRYCMVACPYNVPKY--DYNNPFgalhKCELCNQkgverldkgglpgCVEVCPAG 200
Cdd:cd16372    58 VCPTGAITRDAN-GVVMINKKLCVGCLMCVGFCPEGAMFKheDYPEPF----KCIACGI-------------CVKACPTG 119


                  ..
gi 1997329585 201 AV 202
Cdd:cd16372   120 AL 121
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 43-217 4.93e-14

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 72.86  E-value: 4.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  43 DSTLCVGCQACVTKCQDINFPERNPqgeqtwsnndkLSPytnniiQVWTSGTGVNKDQEENGYAYikkqCMHCVDPNCVS 122
Cdd:PRK12769    8 NSQQCLGCHACEIACVMAHNDEQHV-----------LSQ------HHFHPRITVIKHQQQRSAVT----CHHCEDAPCAR 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 123 VCPVSALKKdpKTGIVHYDKDVCTGCRYCMVACPYN----VPKYDYNNPFGA-LHKCELCnqkgverLDKGGLPGCVEVC 197
Cdd:PRK12769   67 SCPNGAISH--VDDSIQVNQQKCIGCKSCVVACPFGtmqiVLTPVAAGKVKAtAHKCDLC-------AGRENGPACVENC 137

                         170       180
                  ....*....|....*....|
gi 1997329585 198 PAGAVIFGTREELMAEAKKR 217
Cdd:PRK12769  138 PADALQLVTEQALSGMAKSR 157
PRK10330 PRK10330
electron transport protein HydN;
112-220 2.63e-13

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 67.22  E-value: 2.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 112 CMHCVDPNCVSVCPVSALKKDpkTGIVHYDKDVCTGCRYCMVACPYN----VPKYDYNNPFGAL---------HKCELCN 178
Cdd:PRK10330   58 CRQCEDAPCANVCPNGAISRD--KGFVHVMQERCIGCKTCVVACPYGamevVVRPVIRNSGAGLnvraekaeaNKCDLCN 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1997329585 179 QKgverlDKGglPGCVEVCPAGAVIFGTR---EELMAEAKKRLAL 220
Cdd:PRK10330  136 HR-----EDG--PACMAACPTHALICVDRnklEQLSAEKRRRAAL 173
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 107-198 1.64e-12

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: 66.71  E-value: 1.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 107 YIKKQCMHCVDPNCVSVCPVSALKKDPKTGIVHYDKDVCTGCRYCMVACPYNVPKydYNNPFGALHKCELCnqkgVERLD 186
Cdd:cd10556   136 YLPRICNHCTYPACLAACPRKAIYKREEDGIVLIDQERCRGYRECVEACPYKKPM--YNPTTRVSEKCIGC----YPRIE 209

                          90
                  ....*....|..
gi 1997329585 187 KGGLPGCVEVCP 198
Cdd:cd10556   210 EGDQTQCVSACI 221
PRK09898 PRK09898
ferredoxin-like protein;
47-202 1.96e-12

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 65.24  E-value: 1.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  47 CVGCQACVTKCqdinfpernpqgeqTWSNNDKLSPYTNNIIQVWTSGTGVNKDQEENGY----AYIKKQCMHCVDPNCVS 122
Cdd:PRK09898   68 CTGCHRCEISC--------------TNFNDGSVGTFFSRIKIHRNYFFGDNGVGSGGGLygdlNYTADTCRQCKEPQCMN 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 123 VCPVSALKKDPKTGIVHYDKDVCTGCRYCMVACPYNVPKYDYNNPFGAlhKCELCNQkgverldkgglpgCVEVCPAGAV 202
Cdd:PRK09898  134 VCPIGAITWQQKEGCITVDHKRCIGCSACTTACPWMMATVNTESKKSS--KCVLCGE-------------CANACPTGAL 198
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 112-203 4.64e-12

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


Pssm-ID: 319889 [Multi-domain]  Cd Length: 138  Bit Score: 62.71  E-value: 4.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 112 CMHCVDPNCVSVCPVSALKKDPkTGIVHYDkDVCTGCRYCMVACPYNVPKYDYNNpfgalhKCELCNQkgverldkGGLP 191
Cdd:cd16367    57 CRHCVDPVCMIGCPTGAIHRDD-GGEVVIS-DACCGCGNCASACPYGAIQMVRAV------KCDLCAG--------YAGP 120

                          90
                  ....*....|..
gi 1997329585 192 GCVEVCPAGAVI 203
Cdd:cd16367   121 ACVSACPTGAAI 132
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 112-197 2.94e-11

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


Pssm-ID: 440755 [Multi-domain]  Cd Length: 485  Bit Score: 64.06  E-value: 2.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 112 CMHCVDPNCVSVCPVSALKKDPKTGIVHYDKDVCTGCRYCMVACPYNvpKYDYNNPFGALHKCELCnqkgVERLDKGGLP 191
Cdd:COG1140   182 CEHCLNPACVASCPSGAIYKREEDGIVLVDQDKCRGWRMCVSGCPYK--KVYFNWKTGKAEKCIFC----YPRIEAGQPT 255


                  ....*.
gi 1997329585 192 GCVEVC 197
Cdd:COG1140   256 VCSETC 261
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 47-198 4.45e-11

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: 59.59  E-value: 4.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  47 CVGCQACVTKCQdinfpernpqgeQTWSNNDKLSpytNNIIQVWTSGtGVnkdqeENGYAYIKkqCMHCVDPNCVSVCPV 126
Cdd:cd16370    11 CIGCYSCMLACS------------RRVHKSASLS---KSAIRVRTRG-GL-----EGGFTVVV--CRACEDPPCAEACPT 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1997329585 127 SALKKDPKTGiVHYDKDVCTGCRYCMVACPYNVPKYDYNnpfgaLHKCELCNQKGVerldkgglpgCVEVCP 198
Cdd:cd16370    68 GALEPRKGGG-VVLDKEKCIGCGNCVKACIVGAIFWDEE-----TNKPIICIHCGY----------CARYCP 123
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 42-202 2.46e-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: 51.63  E-value: 2.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  42 YDSTLCVGCQACVTKCqdinfpernpqgeqtwsnndklsPYtnNIIQVwtsgtgVNKDQEENGYAYIKKQCMHCvdPNCV 121
Cdd:cd10549     3 YDPEKCIGCGICVKAC-----------------------PT--DAIEL------GPNGAIARGPEIDEDKCVFC--GACV 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 122 SVCPVSALK-------KDPKTGIVHYDKDVCTGCRYCMVACPYNV--------PKYDYNnpfgalhKCELCNQkgverld 186
Cdd:cd10549    50 EVCPTGAIEltpegkeYVPKEKEAEIDEEKCIGCGLCVKVCPVDAitledeleIVIDKE-------KCIGCGI------- 115

                         170
                  ....*....|....*.
gi 1997329585 187 kgglpgCVEVCPAGAV 202
Cdd:cd10549   116 ------CAEVCPVNAI 125
NapF COG1145
Ferredoxin [Energy production and conversion];
101-159 2.62e-08

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 53.96  E-value: 2.62e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1997329585 101 EENGYAYIKKQCMHCvdPNCVSVCPVSALKKDPKTGIVHYDKDVCTGCRYCMVACPYNV 159
Cdd:COG1145   173 KKAKAVIDAEKCIGC--GLCVKVCPTGAIRLKDGKPQIVVDPDKCIGCGACVKVCPVGA 229
PRK13795 PRK13795
hypothetical protein; Provisional
 120-167 3.65e-07

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 51.53  E-value: 3.65e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1997329585 120 CVSVCPVSALKKDPKTGIVHYDKDVCTGCRYCMVACPynVPKY-DYNNP 167
Cdd:PRK13795  589 CVGACPTGAIRIEEGKRKISVDEEKCIHCGKCTEVCP--VVKYkDKRNG 635
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
108-167 4.09e-07

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 47.03  E-value: 4.09e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 108 IKKQCMHCVdpNCVSVCPVSALKKDpkTGIVHYDKDVCTGCRYCMVACPYNVPKYDYNNP 167
Cdd:COG2768     9 DEEKCIGCG--ACVKVCPVGAISIE--DGKAVIDPEKCIGCGACIEVCPVGAIKIEWEED 64
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
120-209 6.10e-07

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 50.06  E-value: 6.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 120 CVSVCPVSALK---KDPKTGIVHYDKDVCTGCRYCMVACPYNVPkyDYNNPFGALHkCELCnqkgverldkgGLpgCVEV 196
Cdd:COG0348   184 CRYLCPYGAFQgllSDLSTLRVRYDRGDCIDCGLCVKVCPMGID--IRKGEINQSE-CINC-----------GR--CIDA 247

                          90
                  ....*....|...
gi 1997329585 197 CPAGAVIFGTREE 209
Cdd:COG0348   248 CPKDAIRFSSRGE 260
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 110-156 9.26e-07

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 50.26  E-value: 9.26e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1997329585 110 KQCMHCVD----PNCVSVCPVSALKKDPKTGIVHYDKDVCTGCRYCMVACP 156
Cdd:PRK12771  504 ARCLSCGNcfecDNCYGACPQDAIIKLGPGRRYHFDYDKCTGCHICADVCP 554
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
99-201 3.33e-06

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 48.48  E-value: 3.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  99 DQEENGYAYIKKQCMHCVDPNCVSVCPVSAlkKDPKTGIVHYDKDVCTGCRYCMVACPYNVPKYDYNNPFGALHKCELCN 178
Cdd:COG4624    49 SCCPRCCLCCCCCCRCCVAISCIQVRGIII--IDKRGPSIIRDKEKCKNCYPCVRACPVKAIKVDDGKAEIDEEKCISCG 126

                          90       100
                  ....*....|....*....|...
gi 1997329585 179 QkgverldkgglpgCVEVCPAGA 201
Cdd:COG4624   127 Q-------------CVAVCPFGA 136
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 107-156 7.87e-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: 7.87e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1997329585 107 YIKKQCMHCvdPNCVSVCPVSALKkdPKTGIVHYDKDVCTGCRYCMVACP 156
Cdd:COG2221    12 IDEEKCIGC--GLCVAVCPTGAIS--LDDGKLVIDEEKCIGCGACIRVCP 57
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 112-159 1.24e-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: 42.13  E-value: 1.24e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1997329585 112 CMHCvdPNCVSVCPVSALKKDPK-----TGIVHYDKDVCTGCRYCMVACPYNV 159
Cdd:pfam12838   1 CIGC--GACVAACPVGAITLDEVgekkgTKTVVIDPERCVGCGACVAVCPTGA 51
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 134-209 2.39e-05

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 41.64  E-value: 2.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1997329585 134 KTGIVHYDKDVCTGCRYCMVACPYNVPKYDynNPFGALHKCELCNqkgverldkgGLPGCVEVCPAGAVIFGTREE 209
Cdd:COG1149     2 KRKIPVIDEEKCIGCGLCVEVCPEGAIKLD--DGGAPVVDPDLCT----------GCGACVGVCPTGAITLEEREA 65
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 120-158 3.43e-05

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 41.27  E-value: 3.43e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1997329585 120 CVSVCPVSALK--KDPKTGIVHYDKDVCTGCRYCMVACPYN 158
Cdd:COG1143    10 CVRVCPVDAITieDGEPGKVYVIDPDKCIGCGLCVEVCPTG 50
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 112-158 3.64e-05

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 41.25  E-value: 3.64e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1997329585 112 CMHCvdPNCVSVCPVSALKKDpKTGIVHYDKDVCTGCRYCMVACPYN 158
Cdd:COG1149    13 CIGC--GLCVEVCPEGAIKLD-DGGAPVVDPDLCTGCGACVGVCPTG 56
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 142-208 3.90e-05

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 40.88  E-value: 3.90e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1997329585 142 KDVCTGCRYCMVACPYNVPKYDYNNPFGALH----KCELCNQkgverldkgglpgCVEVCPAGAVIFGTRE 208
Cdd:COG1143     1 EDKCIGCGLCVRVCPVDAITIEDGEPGKVYVidpdKCIGCGL-------------CVEVCPTGAISMTPFE 58
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
141-215 4.15e-05

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 45.24  E-value: 4.15e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1997329585 141 DKDVCTGCRYCMVACPYNVPKYDYNNPfgALHKCELCNQKGVerldkgglpgCVEVCPAGAVIFG--TREELMAEAK 215
Cdd:COG1148   494 DPEKCTGCGRCVEVCPYGAISIDEKGV--AEVNPALCKGCGT----------CAAACPSGAISLKgfTDDQILAQID 558
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 112-199 8.44e-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: 42.24  E-value: 8.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 112 CMHCVDpNCVSVCPVSALK------KDPKTGIVHYDKDVC------TGCRYCMVACPYN----VPKYDYNNPFgaLHKcE 175
Cdd:cd16373    55 CDLCCD-ACVEVCPTGALRpldleeQKVKMGVAVIDKDRClawqggTDCGVCVEACPTEaiaiVLEDDVLRPV--VDE-D 130

                          90       100
                  ....*....|....*....|....
gi 1997329585 176 LCNQKGVerldkgglpgCVEVCPA 199
Cdd:cd16373   131 KCVGCGL----------CEYVCPV 144
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 136-202 8.64e-05

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 41.36  E-value: 8.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1997329585 136 GIVHYDKDVCTGCRYCMVACPYNVPKYDYNNPFGALH--KCELCNQkgverldkgglpgCVEVCPAGAV 202
Cdd:PRK08348   35 GKILYDVDKCVGCRMCVTVCPAGVFVYLPEIRKVALWtgRCVFCGQ-------------CVDVCPTGAL 90
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 112-156 9.26e-05

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


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 43.06  E-value: 9.26e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1997329585 112 CMHCVDpnCVSVCPVSALKKDPKtGIVHYDKDVCTGCRYCMVACP 156
Cdd:COG2878   139 CIGCGD--CIKACPFDAIVGAAK-GMHTVDEDKCTGCGLCVEACP 180
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 107-156 1.01e-04

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


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 40.42  E-value: 1.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1997329585 107 YIKKQCMHCVdpNCVSVCPVSALKKDPKTGI-VHYDKdvCTGCRYCMVACP 156
Cdd:COG1144    27 VDEDKCIGCG--LCWIVCPDGAIRVDDGKYYgIDYDY--CKGCGICAEVCP 73
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
112-156 1.05e-04

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 43.70  E-value: 1.05e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1997329585 112 CMHCVdpNCVSVCPVSALKKDPKtGIVHYDKDVCTGCRYCMVACP 156
Cdd:COG1148   498 CTGCG--RCVEVCPYGAISIDEK-GVAEVNPALCKGCGTCAAACP 539
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 120-156 1.14e-04

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 39.69  E-value: 1.14e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1997329585 120 CVSVCPVSALKKDPKTG-IVHYDKDVCTGCRYCMVACP 156
Cdd:COG1146    16 CVEVCPVDVLELDEEGKkALVINPEECIGCGACELVCP 53
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
112-159 1.32e-04

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 43.00  E-value: 1.32e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1997329585 112 CMHCVDpnCVSVCPVSALKKDPktGIVHYDKDVCTGCRYCMVACPYNV 159
Cdd:PRK07118  141 CLGLGS--CVAACPFDAIHIEN--GLPVVDEDKCTGCGACVKACPRNV 184
Fer4_6 pfam12837
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 137-160 2.45e-04

4Fe-4S binding domain; This 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: 432822 [Multi-domain]  Cd Length: 24  Bit Score: 37.59  E-value: 2.45e-04
                          10        20
                  ....*....|....*....|....
gi 1997329585 137 IVHYDKDVCTGCRYCMVACPYNVP 160
Cdd:pfam12837   1 VVEVDPDKCIGCGRCVVVCPYGAI 24
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 112-158 2.55e-04

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.


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 41.99  E-value: 2.55e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1997329585 112 CMHCvdPNCVSVCPVSALKKDPKTGIVhyDKDVCTGCRYCMVACPYN 158
Cdd:cd03110    66 CIRC--GNCERVCKFGAILEFFQKLIV--DESLCEGCGACVIICPRG 108
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 130-201 3.26e-04

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


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 38.88  E-value: 3.26e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1997329585 130 KKDPKTGIVHYDKDVCTGCRYCMVACPYNVPKYDYNNPFG-ALHKCELCnqkGVerldkgglpgCVEVCPAGA 201
Cdd:COG1144    17 TGGWRVERPVVDEDKCIGCGLCWIVCPDGAIRVDDGKYYGiDYDYCKGC---GI----------CAEVCPVKA 76
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 120-158 3.29e-04

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 38.87  E-value: 3.29e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1997329585 120 CVSVCPVSALKKDPKTgiVHYDKDVCTGCRYCMVACPYN 158
Cdd:COG4231    30 CVKVCPADAIEEGDGK--AVIDPDLCIGCGSCVQVCPVD 66
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 111-160 4.47e-04

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


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 41.60  E-value: 4.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1997329585 111 QCMHCvdPNCVSVCPV-------------------SALKKDPKTGIVHYDKDV---CTGCRYCMVACPYNVP 160
Cdd:COG0247    79 ACVGC--GFCRAMCPSykatgdekdsprgrinllrEVLEGELPLDLSEEVYEVldlCLTCKACETACPSGVD 148
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
141-214 4.47e-04

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 38.17  E-value: 4.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1997329585 141 DKDVCTGCRYCMVACPYNVPKYDYNNPFGALHKCELCNQkgverldkgglpgCVEVCPAGAVIFGTRE-----ELMAEA 214
Cdd:COG2768     9 DEEKCIGCGACVKVCPVGAISIEDGKAVIDPEKCIGCGA-------------CIEVCPVGAIKIEWEEdeefqEKMAEY 74
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 145-201 4.97e-04

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 37.51  E-value: 4.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1997329585 145 CTGCRYCMVACPYNVPKYDYNNPFGALHK-------CELCNQkgverldkgglpgCVEVCPAGA 201
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKKGTKTvvidperCVGCGA-------------CVAVCPTGA 51
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 138-202 5.48e-04

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 38.10  E-value: 5.48e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1997329585 138 VHYDKDVCTGCRYCMVACPYNVPKYD----YNNPfgalhkcELCNQKGVerldkgglpgCVEVCPAGAV 202
Cdd:COG4231    17 YVIDEDKCTGCGACVKVCPADAIEEGdgkaVIDP-------DLCIGCGS----------CVQVCPVDAI 68
NapF COG1145
Ferredoxin [Energy production and conversion];
128-208 5.48e-04

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 40.86  E-value: 5.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 128 ALKKDPKTGIVHYDKDVCTGCRYCMVACPYNVPKYDyNNPFGALHKCELCNqkgverldkgGLPGCVEVCPAGAVIFGTR 207
Cdd:COG1145   167 ELKIAIKKAKAVIDAEKCIGCGLCVKVCPTGAIRLK-DGKPQIVVDPDKCI----------GCGACVKVCPVGAISLEPK 235


                  .
gi 1997329585 208 E 208
Cdd:COG1145   236 E 236
oorD PRK09626
2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed
 120-156 7.71e-04

2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed


Pssm-ID: 236597 [Multi-domain]  Cd Length: 103  Bit Score: 38.55  E-value: 7.71e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1997329585 120 CVSVCP--VSALKKDPKT------GIVHydKDVCTGCRYCMVACP 156
Cdd:PRK09626   24 CVSVCPagVLAMRIDPHAvlgkmiKVVH--PESCIGCRECELHCP 66
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 112-156 1.37e-03

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: 36.46  E-value: 1.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1997329585 112 CMHCvdPNCVSVCP-----VSALKKDPKTGIVHYDKDVCTGCRYCMVACP 156
Cdd:pfam13237   9 CIGC--GRCTAACPagltrVGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
141-206 1.65e-03

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 38.10  E-value: 1.65e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1997329585 141 DKDVCTGCRYCMVACPYNVPKYDYNNPFGALHkcelcnqkgVERLDKGGLPG---------CVEVCPAGAVIFGT 206
Cdd:COG1142     8 DPEKCIGCRTCEAACAVAHEGEEGEPFLPRIR---------VVRKAGVSAPVqcrhcedapCAEVCPVGAITRDD 73
Fer4_9 pfam13187
4Fe-4S dicluster domain;
145-202 1.95e-03

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 35.61  E-value: 1.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1997329585 145 CTGCRYCMVACPYNVPKYD----YNNPFGALHKCELCNQkgverldkgglpgCVEVCPAGAV 202
Cdd:pfam13187   2 CTGCGACVAACPAGAIVPDlvgqTIRGDIAGLACIGCGA-------------CVDACPRGAI 50
COG1453 COG1453
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
142-222 2.77e-03

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


Pssm-ID: 441062 [Multi-domain]  Cd Length: 365  Bit Score: 39.03  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 142 KDVCTGCRYCMvACPYNVP--------------------KYDYNNpFGALHKCELCNQKGVerldkgglpgCVEVCPAGA 201
Cdd:COG1453   280 KDFCTGCGYCM-PCPQGINipevfrlynlaraygmreyaKERYNA-LGPGAKASACIECGA----------CEERCPQGL 347

                          90       100
                  ....*....|....*....|.
gi 1997329585 202 VIfgtrEELMAEAKKRLALKP 222
Cdd:COG1453   348 DI----PELLKEAHELLGGLP 364
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 136-209 2.95e-03

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 35.84  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585 136 GIVHYDKDVCTGCRYCMVACPYNV-------PKYDYNNPfgalHKCELCNQkgverldkgglpgCVEVCPAGAVIFGTRE 208
Cdd:COG1146     1 MMPVIDTDKCIGCGACVEVCPVDVleldeegKKALVINP----EECIGCGA-------------CELVCPVGAITVEDDE 63


                  .
gi 1997329585 209 E 209
Cdd:COG1146    64 P 64
Fer4_2 pfam12797
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 136-157 3.72e-03

4Fe-4S binding domain; This 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: 463711 [Multi-domain]  Cd Length: 22  Bit Score: 34.30  E-value: 3.72e-03
                          10        20
                  ....*....|....*....|..
gi 1997329585 136 GIVHYDKDVCTGCRYCMVACPY 157
Cdd:pfam12797   1 WKPLIDADKCIGCGACVSACPA 22
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
43-159 3.94e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 38.38  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997329585  43 DSTLCVGCQACVTKC-QDInfPERNPQGEQTW---SNNDKlspytnniiqvwtsGTGVNKdqeengyaYIKKQCMHCvdP 118
Cdd:PRK07118  166 DEDKCTGCGACVKACpRNV--IELIPKSARVFvacNSKDK--------------GKAVKK--------VCEVGCIGC--G 219

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1997329585 119 NCVSVCPVSALKKDpkTGIVHYDKDVCTGCRYCMVACPYNV 159
Cdd:PRK07118  220 KCVKACPAGAITME--NNLAVIDQEKCTSCGKCVEKCPTKA 258
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 106-158 5.91e-03

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


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 37.08  E-value: 5.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1997329585 106 AYI-KKQCMHCVdpNCVSVCPVSALKKDPKTgiVH-YDKDVCTGCRYCMVACPYN 158
Cdd:TIGR01944 108 ALIdEDNCIGCT--KCIQACPVDAIVGAAKA--MHtVIADECTGCDLCVEPCPTD 158
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 145-201 9.15e-03

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 36.08  E-value: 9.15e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1997329585 145 CTGCRYCMVACPYNV---------------PKYDYNNPFgalhkCELCNQKgverldkgglpgCVEVCPAGA 201
Cdd:cd16373    16 CIRCGLCVEACPTGViqpagledgleggrtPYLDPREGP-----CDLCCDA------------CVEVCPTGA 70
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 138-161 9.79e-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: 32.99  E-value: 9.79e-03
                          10        20
                  ....*....|....*....|....
gi 1997329585 138 VHYDKDVCTGCRYCMVACPYNVPK 161
Cdd:pfam00037   1 VVIDEEKCIGCGACVEVCPVGAIT 24
 
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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