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Conserved domains on  [gi|446135243|ref|WP_000213098|]
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MULTISPECIES: dimethylsulfoxide reductase iron-sulfur subunit DmsB [Enterobacteriaceae]

Protein Classification

DmsB/YnfG family anaerobic dimethyl sulfoxide reductase iron-sulfur subunit( domain architecture ID 11496220)

DmsB/YnfG family anaerobic dimethyl sulfoxide reductase iron-sulfur subunit is the electron transfer subunit of the terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds

Gene Ontology:  GO:0051539|GO:0046872|GO:0009061|GO:0009389

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DMSO_dmsB TIGR02951
DMSO reductase, iron-sulfur subunit; This family consists of the iron-sulfur subunit, or chain ...
 4-163 1.67e-99

DMSO reductase, iron-sulfur subunit; This family consists of the iron-sulfur subunit, or chain B, of an enzyme called the anaerobic dimethyl sulfoxide reductase. Chains A and B are catalytic, while chain C is a membrane anchor.


:

Pssm-ID: 131996 [Multi-domain]  Cd Length: 161  Bit Score: 285.09  E-value: 1.67e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243    4 QYGFFIDSSRCTGCKTCELACKDYKDLTPEVSFRRIYEYAGGDWQEDNGVWHQNVFAYYLSISCNHCEDPACTKVCPSGA 83
Cdd:TIGR02951   1 QYGFYVDQTRCSGCKTCQIACKDKNDLEVGVLFRRVYEYEGGGWTEEGEGFHPDVFAYYISISCNHCADPACVKNCPTGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   84 MHKR-EDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVESCPLRALDFGPIDELRKKH 162
Cdd:TIGR02951  81 MYKReEDGLVLVDQDKCIGCRYCVWACPYGAPQYDPQQGVMGKCDGCYDRVEKGLRPACVDACPMRALDFGPIDELRAKY 160


                  .
gi 446135243  163 G 163
Cdd:TIGR02951 161 G 161
 
Name Accession Description Interval E-value
DMSO_dmsB TIGR02951
DMSO reductase, iron-sulfur subunit; This family consists of the iron-sulfur subunit, or chain ...
 4-163 1.67e-99

DMSO reductase, iron-sulfur subunit; This family consists of the iron-sulfur subunit, or chain B, of an enzyme called the anaerobic dimethyl sulfoxide reductase. Chains A and B are catalytic, while chain C is a membrane anchor.


Pssm-ID: 131996 [Multi-domain]  Cd Length: 161  Bit Score: 285.09  E-value: 1.67e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243    4 QYGFFIDSSRCTGCKTCELACKDYKDLTPEVSFRRIYEYAGGDWQEDNGVWHQNVFAYYLSISCNHCEDPACTKVCPSGA 83
Cdd:TIGR02951   1 QYGFYVDQTRCSGCKTCQIACKDKNDLEVGVLFRRVYEYEGGGWTEEGEGFHPDVFAYYISISCNHCADPACVKNCPTGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   84 MHKR-EDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVESCPLRALDFGPIDELRKKH 162
Cdd:TIGR02951  81 MYKReEDGLVLVDQDKCIGCRYCVWACPYGAPQYDPQQGVMGKCDGCYDRVEKGLRPACVDACPMRALDFGPIDELRAKY 160


                  .
gi 446135243  163 G 163
Cdd:TIGR02951 161 G 161
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 6-153 1.23e-83

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: 244.01  E-value: 1.23e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   6 GFFIDSSRCTGCKTCELACKDYKDLTPEVSFRRIYEYAGGDWQedngvwhqNVFAYYLSISCNHCEDPACTKVCPSGAMH 85
Cdd:cd16371    1 GFYFDQERCIGCKACEIACKDKNDLPPGVNWRRVYEYEGGEFP--------EVFAYFLSMSCNHCENPACVKVCPTGAIT 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446135243  86 KREDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVESCPLRALDFG 153
Cdd:cd16371   73 KREDGIVVVDQDKCIGCGYCVWACPYGAPQYNPETGKMDKCDMCVDRLDEGEKPACVAACPTRALDFG 140
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 1-188 2.23e-78

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 232.53  E-value: 2.23e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   1 MTTQYGFFIDSSRCTGCKTCELACKDYKDLTPEVSFRRIYEYAGGDWQedngvwhqNVFAYYLSISCNHCEDPACTKVCP 80
Cdd:COG0437    2 SMKRYGMVIDLTKCIGCRACVVACKEENNLPVGVTWRRVRRYEEGEFP--------NVEWLFVPVLCNHCDDPPCVKVCP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  81 SGAMHKREDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVESCPLRALDFGPIDELRK 160
Cdd:COG0437   74 TGATYKREDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVEACPTGALVFGDLDDPES 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446135243 161 KHGDLAA---VAPLPRAHFTKPNIVIKPNAN 188
Cdd:COG0437  154 EVSKRLAelpAYRLLPELGTKPSVYYLPKRN 184
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 58-153 1.37e-35

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


Pssm-ID: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 120.82  E-value: 1.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   58 VFAYYLSISCNHCEDPACTKVCPSGAMHKRE-DGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEG 136
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPVGAIYKDEeTGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAG 80

                          90
                  ....*....|....*..
gi 446135243  137 KKPICVESCPLRALDFG 153
Cdd:pfam13247  81 LLPACVQTCPTGAMNFG 97
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
6-158 6.32e-33

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 120.54  E-value: 6.32e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   6 GFFIDSSRCTGCKTCELACKDYKDLTPEVSFRRIYE---------------YAGGDWQedNGVWHQNVFAYyLSISCNHC 70
Cdd:PRK10882  39 GMLYDSTLCVGCQACVTKCQEINFPERNPQGEQTWDnpdklspytnniikvWKSGTGV--NKDQEENGYAY-IKKQCMHC 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  71 EDPACTKVCPSGAMHKR-EDGFVVVDEDVCIGCRYCHMACPYGAP--QYNETKGHMTKCDGC----YDRVAEGKKPICVE 143
Cdd:PRK10882 116 VDPNCVSVCPVSALTKDpKTGIVHYDKDVCTGCRYCMVACPFNVPkyDYNNPFGAIHKCELCnqkgVERLDKGGLPGCVE 195

                        170
                 ....*....|....*
gi 446135243 144 SCPLRALDFGPIDEL 158
Cdd:PRK10882 196 VCPTGAVIFGTREEL 210
 
Name Accession Description Interval E-value
DMSO_dmsB TIGR02951
DMSO reductase, iron-sulfur subunit; This family consists of the iron-sulfur subunit, or chain ...
 4-163 1.67e-99

DMSO reductase, iron-sulfur subunit; This family consists of the iron-sulfur subunit, or chain B, of an enzyme called the anaerobic dimethyl sulfoxide reductase. Chains A and B are catalytic, while chain C is a membrane anchor.


Pssm-ID: 131996 [Multi-domain]  Cd Length: 161  Bit Score: 285.09  E-value: 1.67e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243    4 QYGFFIDSSRCTGCKTCELACKDYKDLTPEVSFRRIYEYAGGDWQEDNGVWHQNVFAYYLSISCNHCEDPACTKVCPSGA 83
Cdd:TIGR02951   1 QYGFYVDQTRCSGCKTCQIACKDKNDLEVGVLFRRVYEYEGGGWTEEGEGFHPDVFAYYISISCNHCADPACVKNCPTGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   84 MHKR-EDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVESCPLRALDFGPIDELRKKH 162
Cdd:TIGR02951  81 MYKReEDGLVLVDQDKCIGCRYCVWACPYGAPQYDPQQGVMGKCDGCYDRVEKGLRPACVDACPMRALDFGPIDELRAKY 160


                  .
gi 446135243  163 G 163
Cdd:TIGR02951 161 G 161
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 6-153 1.23e-83

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: 244.01  E-value: 1.23e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   6 GFFIDSSRCTGCKTCELACKDYKDLTPEVSFRRIYEYAGGDWQedngvwhqNVFAYYLSISCNHCEDPACTKVCPSGAMH 85
Cdd:cd16371    1 GFYFDQERCIGCKACEIACKDKNDLPPGVNWRRVYEYEGGEFP--------EVFAYFLSMSCNHCENPACVKVCPTGAIT 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446135243  86 KREDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVESCPLRALDFG 153
Cdd:cd16371   73 KREDGIVVVDQDKCIGCGYCVWACPYGAPQYNPETGKMDKCDMCVDRLDEGEKPACVAACPTRALDFG 140
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 1-188 2.23e-78

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 232.53  E-value: 2.23e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   1 MTTQYGFFIDSSRCTGCKTCELACKDYKDLTPEVSFRRIYEYAGGDWQedngvwhqNVFAYYLSISCNHCEDPACTKVCP 80
Cdd:COG0437    2 SMKRYGMVIDLTKCIGCRACVVACKEENNLPVGVTWRRVRRYEEGEFP--------NVEWLFVPVLCNHCDDPPCVKVCP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  81 SGAMHKREDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVESCPLRALDFGPIDELRK 160
Cdd:COG0437   74 TGATYKREDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVEACPTGALVFGDLDDPES 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446135243 161 KHGDLAA---VAPLPRAHFTKPNIVIKPNAN 188
Cdd:COG0437  154 EVSKRLAelpAYRLLPELGTKPSVYYLPKRN 184
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 9-181 3.22e-56

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: 176.18  E-value: 3.22e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   9 IDSSRCTGCKTCELACKDYKDLTPEVSFRRIYEYAGGdwqedngvWHQNVFAYYLSISCNHCEDPACTKVCPSGAMHKRE 88
Cdd:cd10551    3 IDLRKCIGCGACVVACKAENNVPPGVFRNRVLEYEVG--------EYPNVKRTFLPVLCNHCENPPCVKVCPTGATYKRE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  89 DGFVVVDEDVCIGCRYCHMACPYGAPQYNE------------TKGHMTKCDGCYDRVAEGKKPICVESCPLRALDFG--- 153
Cdd:cd10551   75 DGIVLVDYDKCIGCRYCMAACPYGARYFNPeephefgevpvrPKGVVEKCTFCYHRLDEGLLPACVEACPTGARIFGdld 154

                        170       180
                 ....*....|....*....|....*....
gi 446135243 154 -PIDELRKKHGDLAAVAPLPRAHfTKPNI 181
Cdd:cd10551  155 dPNSEVSKLLAERRAYVLKPELG-TKPKV 182
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 6-160 4.71e-52

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: 165.85  E-value: 4.71e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   6 GFFIDSSRCTGCKTCELACKDYKDLTPEVSfrriyeYAGGDWQEDNGV--------------WHQNVFAYYlSISCNHCE 71
Cdd:cd10561    1 GVLYDTTRCIGCRACEVACKEWNGLPAEDT------AFGPGWDNPRDLsaktytvikryeveTGGKGFVFV-KRQCMHCL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  72 DPACTKVCPSGAMHKREDGFVVVDEDVCIGCRYCHMACPYGAP--QYNETKGHMTKCDGCYDRVAEGKKPICVESCPLRA 149
Cdd:cd10561   74 DPACVSACPVGALRKTPEGPVTYDEDKCIGCRYCMVACPFNIPkyEWDSANPKIRKCTMCYDRLKEGKQPACVEACPTGA 153

                        170
                 ....*....|.
gi 446135243 150 LDFGPIDELRK 160
Cdd:cd10561  154 LLFGKREELLA 164
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 7-153 5.00e-51

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: 161.40  E-value: 5.00e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   7 FFIDSSRCTGCKTCELACKDYKDLTPEVSFRRIYEYAGGDwqedngvwhqnVFAYYLSISCNHCEDPACTKVCPSGAMHK 86
Cdd:cd04410    1 LVVDLDRCIGCGTCEVACKQEHGLRPGPDWSRIKVIEGGG-----------LERAFLPVSCMHCEDPPCVKACPTGAIYK 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446135243  87 REDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVESCPLRALDFG 153
Cdd:cd04410   70 DEDGIVLIDEDKCIGCGSCVEACPYGAIVFDPEPGKAVKCDLCGDRLDEGLEPACVKACPTGALTFG 136
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 8-158 2.76e-49

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: 157.85  E-value: 2.76e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   8 FIDSSRCTGCKTCELACKDYKDLtPEVSFRRIYEY------AGGDW--------QEDNGvwhqNVFAYYLSISCNHCEDP 73
Cdd:cd10562    2 LVDTSKCTACRGCQVACKQWNQL-PAEKTPFTGSYqnppdlTPNTWtlirfyehEEDNG----GIRWLFRKRQCMHCTDA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  74 ACTKVCPSGAMHKREDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVESCPLRALDFG 153
Cdd:cd10562   77 ACVKVCPTGALYKTENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCFDRIENGMQPACVKTCPTGALTFG 156


                 ....*
gi 446135243 154 PIDEL 158
Cdd:cd10562  157 DRDEL 161
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 7-153 5.19e-48

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: 154.48  E-value: 5.19e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   7 FFIDSSRCTGCKTCELACKDYKDLTPEVS-FRRIYEY----AGGDW-------QEDNGVwhqNVFAYYLSISCNHCEDPA 74
Cdd:cd16366    1 FLVDTSRCTGCRACQVACKQWNGLPAEKTeFTGSYQNppdlTAHTWtlvrfyeVEKPGG---DLSWLFRKDQCMHCTDAG 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446135243  75 CTKVCPSGAMHKREDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVESCPLRALDFG 153
Cdd:cd16366   78 CLAACPTGAIIRTETGTVVVDPETCIGCGYCVNACPFDIPRFDEETGRVAKCTLCYDRISNGLQPACVKTCPTGALTFG 156
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 8-161 4.06e-44

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: 143.95  E-value: 4.06e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   8 FIDSSRCTGCKTCELACKDYKDLTPevsfrRIYEYAGGDwqedngvwhqnvfAYYLSISCNHCEDPACTKVCPSGAMHKR 87
Cdd:cd16374    2 YVDPERCIGCRACEIACAREHSGKP-----RISVEVVED-------------LASVPVRCRHCEDAPCMEVCPTGAIYRD 63

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446135243  88 EDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVESCPLRALDFGPIDELRKK 161
Cdd:cd16374   64 EDGAVLVDPDKCIGCGMCAMACPFGVPRFDPSLKVAVKCDLCIDRRREGKLPACVEACPTGALKFGDIEELLKE 137
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 5-153 1.80e-43

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: 142.50  E-value: 1.80e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   5 YGFFIDSSRCTGCKTCELACKDYKDLTPEVSFRRIYEyaggdwqEDNGVWHQNVFAYYLSISCNHCEDPACTKVCPSGAM 84
Cdd:cd10553    3 YYLYHDSKRCIGCLACEVHCKVKNNLPVGPRLCRIFA-------VGPKMVGGKPRLKFVYMSCFHCENPWCVKACPTGAM 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  85 HKRE-DGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVESCPLRALDFG 153
Cdd:cd10553   76 QKREkDGIVYVDQELCIGCKACIEACPWGIPQWNPATGKVVKCDYCMDRIDQGLKPACVTGCTTHALSFV 145
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 6-161 3.60e-43

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: 144.07  E-value: 3.60e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   6 GFFIDSSRCTGCKTCELACKDYKDLTPE----------------------VSFRRIYEYAGGDWQEDNGVWhqnvfaYYL 63
Cdd:cd10560    1 GFFTDTSICIGCKACEVACKQWNQLPADgydfsgmsydntgdlsastwrhVKFIERPTEDGPANEGGDLQW------LFM 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  64 SISCNHCEDPACTKVCPSGAMHKREDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVE 143
Cdd:cd10560   75 SDVCKHCTDAGCLEACPTGAIFRTEFGTVYIQPDICNGCGYCVAACPFGVIDRNEETGRAHKCTLCYDRLKDGLEPACAK 154

                        170
                 ....*....|....*...
gi 446135243 144 SCPLRALDFGPIDELRKK 161
Cdd:cd10560  155 ACPTGSIQFGPLEELRER 172
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 9-160 7.65e-37

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: 127.50  E-value: 7.65e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   9 IDSSRCTGCKTCELACKDYKDLTPEVS---------------------FRRIYEYAGGDWQedngvwhqnvfayYLSISC 67
Cdd:cd10558    4 IDVSKCIGCKACQVACKEWNDLRAEVGhnvgtyqnpadlspetwtlmkFREVEDNGKLEWL-------------IRKDGC 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  68 NHCEDPACTKVCPS-GAMHKREDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVESCP 146
Cdd:cd10558   71 MHCADPGCLKACPSpGAIVQYANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVGLEPACVKTCP 150

                        170
                 ....*....|....
gi 446135243 147 LRALDFGPIDELRK 160
Cdd:cd10558  151 TGALHFGTKEDMLA 164
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 8-153 1.13e-36

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: 124.68  E-value: 1.13e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   8 FIDSSRCTGCKTCELACK----------DYKDLTPEVSFRRIYEYAGGdwqedngvwhqnvfaYYLSISCNHCEDPACTK 77
Cdd:cd10563    3 FIDEEKCLGCKLCEVACAvahskskdliKAKLEKERPRPRIRVEESGG---------------RSFPLQCRHCDEPPCVK 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446135243  78 VCPSGAMHK-REDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRvaegKKPICVESCPLRALDFG 153
Cdd:cd10563   68 ACMSGAMHKdPETGIVIHDEEKCVGCWMCVMVCPYGAIRPDKERKVALKCDLCPDR----ETPACVEACPTGALVLE 140
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 58-153 1.37e-35

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


Pssm-ID: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 120.82  E-value: 1.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   58 VFAYYLSISCNHCEDPACTKVCPSGAMHKRE-DGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEG 136
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPVGAIYKDEeTGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAG 80

                          90
                  ....*....|....*..
gi 446135243  137 KKPICVESCPLRALDFG 153
Cdd:pfam13247  81 LLPACVQTCPTGAMNFG 97
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 4-161 9.72e-35

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: 120.96  E-value: 9.72e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   4 QYGFFIDSSRCTGCKTCELACKDYKDLTPEvsfRRIY-EYAggdwqeDNGVWHQNVfayylSISCNHCEDPACTKVCPSG 82
Cdd:cd16369    1 EKEFFIDPSRCIGCRACVAACRECGTHRGK---SMIHvDYI------DRGESTQTA-----PTVCMHCEDPTCAEVCPAD 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  83 AMHKREDGFVV-VDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVESCPLRALDFGPIDELRKK 161
Cdd:cd16369   67 AIKVTEDGVVQsALKPRCIGCSNCVNACPFGVPKYDEERNLMMKCDMCYDRTSVGKAPMCASVCPSGALFYGTREEIQAL 146
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 9-152 1.20e-34

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


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 119.22  E-value: 1.20e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   9 IDSSRCTGCKTCELAC--KDYKDLTPEVSFRRIYEYaggdwqEDNGVWHQNVfayylsisCNHCEDPACTKVCPSGAMHK 86
Cdd:cd10550    3 VDPEKCTGCRTCELACslKHEGVFNPSLSRIRVVRF------EPEGLDVPVV--------CRQCEDAPCVEACPVGAISR 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446135243  87 -REDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCydrvaeGKKPICVESCPLRALDF 152
Cdd:cd10550   69 dEETGAVVVDEDKCIGCGMCVEACPFGAIRVDPETGKAIKCDLC------GGDPACVKVCPTGALEF 129
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 44-203 6.86e-34

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: 122.80  E-value: 6.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  44 GGDWQEDNGVW-HQNVFAYYLSISCNHCEDPACTKVCPSGAMHKR-EDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKG 121
Cdd:cd10555  109 GPNWDEDQGAGeYPNSYYFYLPRICNHCTNPACLAACPRKAIYKReEDGIVLVDQDRCRGYRYCVEACPYKKIYFNPVEQ 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243 122 HMTKCDGCYDRVAEGKKPICVESCPLRALDFGPIDE-------LRKKHgdlaAVA-PLPRAHFTKPNIVIKPNANSRPTG 193
Cdd:cd10555  189 KSEKCIFCYPRIEKGVAPACARQCVGRIRFVGYLDDeespvykLVKKW----KVAlPLHPEYGTEPNVFYVPPLSPPKLG 264

                        170
                 ....*....|
gi 446135243 194 DTTGYLANPK 203
Cdd:cd10555  265 DDGEPTDEPR 274
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
6-158 6.32e-33

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 120.54  E-value: 6.32e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   6 GFFIDSSRCTGCKTCELACKDYKDLTPEVSFRRIYE---------------YAGGDWQedNGVWHQNVFAYyLSISCNHC 70
Cdd:PRK10882  39 GMLYDSTLCVGCQACVTKCQEINFPERNPQGEQTWDnpdklspytnniikvWKSGTGV--NKDQEENGYAY-IKKQCMHC 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  71 EDPACTKVCPSGAMHKR-EDGFVVVDEDVCIGCRYCHMACPYGAP--QYNETKGHMTKCDGC----YDRVAEGKKPICVE 143
Cdd:PRK10882 116 VDPNCVSVCPVSALTKDpKTGIVHYDKDVCTGCRYCMVACPFNVPkyDYNNPFGAIHKCELCnqkgVERLDKGGLPGCVE 195

                        170
                 ....*....|....*
gi 446135243 144 SCPLRALDFGPIDEL 158
Cdd:PRK10882 196 VCPTGAVIFGTREEL 210
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 7-191 7.24e-32

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: 113.96  E-value: 7.24e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   7 FFIDSSRCTGCKTCELACKDykdltpevsfrriyEYAGGDW------QEDNG-VWHQ----------NVFAYYLSISCNH 69
Cdd:cd10552    1 LVIDVAKCNGCYNCFLACKD--------------EHVGNDWpgyaapQPRHGhFWMRilrrergqypKVDVAYLPVPCNH 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  70 CEDPACTKVCPSGAMHKREDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEG-KKPICVESCPLR 148
Cdd:cd10552   67 CDNAPCIKAAKDGAVYKRDDGIVIIDPEKAKGQKQLVDACPYGAIYWNEELQVPQKCTFCAHLLDDGwKEPRCVQACPTG 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446135243 149 ALDFGPIDELRKKhgDLAAVAPLPrahftkpniVIKPNANSRP 191
Cdd:cd10552  147 ALRFGKLEDEEMA--AKAAEEGLE---------VLHPELGTKP 178
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 4-162 9.29e-32

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: 114.22  E-value: 9.29e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   4 QYGFFIDSSRCTGCKTCELACKD---YKDLTPEVSFRRIYEYAGG----DWQ---EDNGVWHQnvFAYYLSISCNHCEDP 73
Cdd:cd16365    2 QFAAVFNLNKCIGCQTCTVACKNawtYRKGQEYMWWNNVETKPGGgypqDWEvktIDNGGNTR--FFFYLQRLCNHCTNP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  74 ACTKVCPSGAMHKR-EDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVESCPLRALDF 152
Cdd:cd16365   80 ACLAACPRGAIYKReEDGIVLIDQKRCRGYRKCVEQCPYKKIYFNGLSRVSEKCIACYPRIEGGDPTRCMSACVGRIRLQ 159

                        170
                 ....*....|
gi 446135243 153 GPIDELRKKH 162
Cdd:cd16365  160 GFLDDNPKSP 169
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 5-161 2.61e-30

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: 110.20  E-value: 2.61e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   5 YGFFIDSSRCTGCKT-----CELACKDY-KDLTPEVSFRRIYEYAGG----DWQEDNGV------------------WHQ 56
Cdd:cd16368    1 LATLIDLTKCDGCPGesipaCVRACREKnQARFPEPVSKPIQPYWPRkrieDWSDKRDVtdrltpynwlyvqkltvdTAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  57 NVFAYYLSISCNHCEDPACTKVCPSGAMHKREDGFVVVDEDVCIGCRYCHMACPYGAPQYNE-------------TKGHM 123
Cdd:cd16368   81 GEKEVFIPRRCMHCDNPPCAKLCPFGAARKTPEGAVYIDDDLCFGGAKCRDVCPWHIPQRQAgvgiylhlapeyaGGGVM 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446135243 124 TKCDGCYDRVAEGKKPICVESCPLRALDFGPIDELRKK 161
Cdd:cd16368  161 YKCDLCKDLLAQGKPPACIEACPKGAQYFGPRKEMVAL 198
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
9-150 4.32e-30

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 107.82  E-value: 4.32e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   9 IDSSRCTGCKTCELACKD-YKDLTPEVSFRRIYeyaggdwqedngVWHQNVFayYLSISCNHCEDPACTKVCPSGAMHkR 87
Cdd:COG1142    7 ADPEKCIGCRTCEAACAVaHEGEEGEPFLPRIR------------VVRKAGV--SAPVQCRHCEDAPCAEVCPVGAIT-R 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446135243  88 EDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMT--KCDGCYDRvaeGKKPICVESCPLRAL 150
Cdd:COG1142   72 DDGAVVVDEEKCIGCGLCVLACPFGAITMVGEKSRAVavKCDLCGGR---EGGPACVEACPTGAL 133
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
4-191 4.59e-30

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 111.12  E-value: 4.59e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   4 QYGFFIDSSRCTGCKTCELACKdYKDLTPEVSFR---RIYEYAGGDWQEDNGVwhqnvfayYLSISCNHCEDPACTKVCP 80
Cdd:PRK14993  43 RYAMLIDLRRCIGCQSCTVSCT-IENQTPQGAFRttvNQYQVQREGSQEVTNV--------LLPRLCNHCDNPPCVPVCP 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  81 SGAMHKREDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVESCPLRALDFGpidELRK 160
Cdd:PRK14993 114 VQATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIG---DIKD 190

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446135243 161 KHGDLAAVAPLPRAHFTkpniVIKPNANSRP 191
Cdd:PRK14993 191 PHSRIATMLHQHRDAIK----VLKPENGTSP 217
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 6-182 1.37e-29

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: 108.68  E-value: 1.37e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   6 GFFIDSSRCTGCKTCELACKDYKDLTPEVS-FRRIYE----YAGGDW--------QEDNGVwhqnVFAYYLSISCNHCED 72
Cdd:cd10559    1 SFLIDTTRCTACRGCQVACKQWNQLPAEQTkNTGSHQnppdLSANTYklvrfnevRNENGK----PDWLFFPDQCRHCVT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  73 PACTKVC---PSGAMHKREDGFVVVDEDVCIGCRYCHM-ACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVESCPLR 148
Cdd:cd10559   77 PPCKDAAdmvPGAVIQDEATGAVVFTEKTAELDFDDVLsACPYNIPRKNEATGRIVKCDMCIDRVSNGLQPACVKACPTG 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446135243 149 ALDFGPIDE-LRKKHGDLAAVAP-LPRAHFTKPNIV 182
Cdd:cd10559  157 AMNFGDRDEmLAMASKRLEELKKrYPKANLYDPDDV 192
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 10-150 1.55e-27

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: 101.57  E-value: 1.55e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  10 DSSRCTGCKTCELAC------KDYK--DLTPEVSFRRIYEYAGGDwqedngvwhqnvfaYYLSISCNHCEDPACTKVCPS 81
Cdd:cd10554    5 DPDKCIGCRTCEVACaaahsgKGIFeaGTDGLPFLPRLRVVKTGE--------------VTAPVQCRQCEDAPCANVCPV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  82 GAMhKREDGFVVVDEDVCIGCRYCHMACPYGA----PQY-------NETKGHMTKCDGCYDRvAEGkkPICVESCPLRAL 150
Cdd:cd10554   71 GAI-SQEDGVVQVDEERCIGCKLCVLACPFGAiemaPTTvpgvdweRGPRAVAVKCDLCAGR-EGG--PACVEACPTKAL 146
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 56-145 2.06e-27

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: 106.29  E-value: 2.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  56 QNVFAYYLSISCNHCEDPACTKVCPSGAMHKR-EDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVA 134
Cdd:cd10557  168 ENTFMFYLPRICNHCLNPACVAACPSGAIYKReEDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSEKCIFCYPRLE 247

                         90
                 ....*....|.
gi 446135243 135 EGKKPICVESC 145
Cdd:cd10557  248 AGQPTVCSETC 258
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 56-145 2.01e-26

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


Pssm-ID: 440755 [Multi-domain]  Cd Length: 485  Bit Score: 104.89  E-value: 2.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  56 QNVFAYYLSISCNHCEDPACTKVCPSGAMHKR-EDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVA 134
Cdd:COG1140  171 ENTFMFYLPRICEHCLNPACVASCPSGAIYKReEDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGKAEKCIFCYPRIE 250

                         90
                 ....*....|.
gi 446135243 135 EGKKPICVESC 145
Cdd:COG1140  251 AGQPTVCSETC 261
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 4-146 9.08e-26

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: 100.61  E-value: 9.08e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   4 QYGFFIDSSRCTGCKTCELACK-----------------------------DYKDLT----PEVSFRRIYEY-------- 42
Cdd:cd10556   11 QFAMVFDTNKCIACQTCTMACKstwtsgkgqeymwwnnvetkpyggyplgwDVRLLDeeggQTWAEGGVYEGktifeaaa 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  43 ----------AGGDWQEDN--------GVWHQNVFA--------YYLSISCNHCEDPACTKVCPSGAMHKR-EDGFVVVD 95
Cdd:cd10556   91 ageqvlgyrpEDEDWRYPNigedevngERTPDTGSSlpphpiwfFYLPRICNHCTYPACLAACPRKAIYKReEDGIVLID 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446135243  96 EDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVESCP 146
Cdd:cd10556  171 QERCRGYRECVEACPYKKPMYNPTTRVSEKCIGCYPRIEEGDQTQCVSACI 221
PRK10330 PRK10330
electron transport protein HydN;
10-150 5.15e-23

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 91.10  E-value: 5.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  10 DSSRCTGCKTCELAC-------KDYKDLTPEVSFRRIYEYAGgdwqedngvwhQNVFAyylSISCNHCEDPACTKVCPSG 82
Cdd:PRK10330   8 DASKCIGCRTCEVACvvshqenQDCASLTPETFLPRIHVIKG-----------VNVST---ATVCRQCEDAPCANVCPNG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  83 AMhKREDGFVVVDEDVCIGCRYCHMACPYGAPQ---------------YNETKGHMTKCDGCYDRvAEGkkPICVESCPL 147
Cdd:PRK10330  74 AI-SRDKGFVHVMQERCIGCKTCVVACPYGAMEvvvrpvirnsgaglnVRAEKAEANKCDLCNHR-EDG--PACMAACPT 149


                 ...
gi 446135243 148 RAL 150
Cdd:PRK10330 150 HAL 152
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 10-150 1.97e-22

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 94.04  E-value: 1.97e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  10 DSSRCTGCKTCELAC-----KDYKDLTPEVSFRRIYEYAGGdwqedngvwHQNVfayylSISCNHCEDPACTKVCPSGAM 84
Cdd:PRK12769   8 NSQQCLGCHACEIACvmahnDEQHVLSQHHFHPRITVIKHQ---------QQRS-----AVTCHHCEDAPCARSCPNGAI 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446135243  85 HKREDGFVVVDEDvCIGCRYCHMACPYGA------PQYNET-KGHMTKCDGCYDRvAEGkkPICVESCPLRAL 150
Cdd:PRK12769  74 SHVDDSIQVNQQK-CIGCKSCVVACPFGTmqivltPVAAGKvKATAHKCDLCAGR-ENG--PACVENCPADAL 142
PRK09898 PRK09898
ferredoxin-like protein;
12-150 7.81e-19

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 80.65  E-value: 7.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  12 SRCTGCKTCELACKDYKD-----LTPEVSFRRIYEYAGGDWQEDNGVWHQnvfAYYLSISCNHCEDPACTKVCPSGAM-H 85
Cdd:PRK09898  66 ARCTGCHRCEISCTNFNDgsvgtFFSRIKIHRNYFFGDNGVGSGGGLYGD---LNYTADTCRQCKEPQCMNVCPIGAItW 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446135243  86 KREDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDrvaegkkpiCVESCPLRAL 150
Cdd:PRK09898 143 QQKEGCITVDHKRCIGCSACTTACPWMMATVNTESKKSSKCVLCGE---------CANACPTGAL 198
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 9-150 1.51e-17

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: 75.42  E-value: 1.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   9 IDSSRCTGCKTCELACKDYKDLTPEVSFrriyeyaggdwqedNGVWHQNvfaYYLSISCNHCEDPACTKVCPSGAMHKRE 88
Cdd:cd16367   16 IDLDRCIRCDNCEKACADTHDGHSRLDR--------------NGLRFGN---LLVPTACRHCVDPVCMIGCPTGAIHRDD 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446135243  89 DGFVVVDEDvCIGCRYCHMACPYGAPQynetkghM---TKCDGCydrvAEGKKPICVESCPLRAL 150
Cdd:cd16367   79 GGEVVISDA-CCGCGNCASACPYGAIQ-------MvraVKCDLC----AGYAGPACVSACPTGAA 131
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 10-168 2.03e-17

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 79.68  E-value: 2.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  10 DSSRCTGCKTCELAC--KDYKDLTPE--VSFR-RIYEyaggdwqedngVWHQNVFAyylSISCNHCEDPACTKVCPSGAM 84
Cdd:PRK12809   8 EAAECIGCHACEIACavAHNQENWPLshSDFRpRIHV-----------VGKGQAAN---PVACHHCNNAPCVTACPVNAL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  85 HKREDGfVVVDEDVCIGCRYCHMACPYGAPQYNETKGHmtKCDGCYDRvAEGKKPiCVESCPLRAL---DFGPIDELRKK 161
Cdd:PRK12809  74 TFQSDS-VQLDEQKCIGCKRCAIACPFGVVEMVDTIAQ--KCDLCNQR-SSGTQA-CIEVCPTQALrlmDDKGLQQIKVA 148


                 ....*..
gi 446135243 162 HGDLAAV 168
Cdd:PRK12809 149 RQRKTAA 155
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 9-152 6.17e-17

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: 73.46  E-value: 6.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   9 IDSSRCTGCKTCELAC--KDYKDLTPEVSFRRIYEYAGgdwqedngvwHQNVFAyylSISCNHCEDPACTKVCPSGAMHK 86
Cdd:cd16370    6 KDMERCIGCYSCMLACsrRVHKSASLSKSAIRVRTRGG----------LEGGFT---VVVCRACEDPPCAEACPTGALEP 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446135243  87 REDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCydrvaegkkPICVESCPLRALDF 152
Cdd:cd16370   73 RKGGGVVLDKEKCIGCGNCVKACIVGAIFWDEETNKPIICIHC---------GYCARYCPHDVLAM 129
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 9-150 2.49e-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: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 61.20  E-value: 2.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   9 IDSSRCTGCKTCELACKD--YKDLTPEVSFRRIYEYAGGdwqedngvwhqnvfayYLSISCNHCEDpaCTKVCPSGAMHK 86
Cdd:cd16372    5 TDPEKCIGCLQCEEACSKtfFKEEDREKSCIRITETEGG----------------YAINVCNQCGE--CIDVCPTGAITR 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446135243  87 REDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCydrvaegkkPICVESCPLRAL 150
Cdd:cd16372   67 DANGVVMINKKLCVGCLMCVGFCPEGAMFKHEDYPEPFKCIAC---------GICVKACPTGAL 121
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
93-152 2.75e-09

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 56.02  E-value: 2.75e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446135243  93 VVDEDVCIGCRYCHMACPYGAPQYNETKGHM---TKCDGCydrvaeGkkpICVESCPLRALDF 152
Cdd:COG1148  492 EVDPEKCTGCGRCVEVCPYGAISIDEKGVAEvnpALCKGC------G---TCAAACPSGAISL 545
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
67-113 4.73e-08

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 48.57  E-value: 4.73e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446135243  67 CNHCEdpACTKVCPSGAMHKrEDGFVVVDEDVCIGCRYCHMACPYGA 113
Cdd:COG2768   13 CIGCG--ACVKVCPVGAISI-EDGKAVIDPEKCIGCGACIEVCPVGA 56
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 67-113 1.52e-07

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 46.97  E-value: 1.52e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446135243  67 CNHCedPACTKVCPSGAMhKREDGFVVVDEDVCIGCRYCHMACPYGA 113
Cdd:COG2221   17 CIGC--GLCVAVCPTGAI-SLDDGKLVIDEEKCIGCGACIRVCPTGA 60
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 67-113 1.57e-07

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 47.03  E-value: 1.57e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446135243  67 CNHCEdpACTKVCPSGAMHKREDGFVVVDEDVCIGCRYCHMACPYGA 113
Cdd:COG1149   13 CIGCG--LCVEVCPEGAIKLDDGGAPVVDPDLCTGCGACVGVCPTGA 57
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 67-146 3.64e-07

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: 48.02  E-value: 3.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  67 CNHCEDpACTKVCPSGAMHKRED-------GFVVVDEDVCI------GCRYCHMACPYGAPQYNETKGHM------TKCD 127
Cdd:cd16373   55 CDLCCD-ACVEVCPTGALRPLDLeeqkvkmGVAVIDKDRCLawqggtDCGVCVEACPTEAIAIVLEDDVLrpvvdeDKCV 133

                         90
                 ....*....|....*....
gi 446135243 128 GCydrvaeGkkpICVESCP 146
Cdd:cd16373  134 GC------G---LCEYVCP 143
NapF COG1145
Ferredoxin [Energy production and conversion];
67-113 6.49e-07

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 48.18  E-value: 6.49e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 446135243  67 CNHCEdpACTKVCPSGAMHKREDGF-VVVDEDVCIGCRYCHMACPYGA 113
Cdd:COG1145  184 CIGCG--LCVKVCPTGAIRLKDGKPqIVVDPDKCIGCGACVKVCPVGA 229
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 67-113 9.08e-07

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 45.03  E-value: 9.08e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446135243  67 CNHCEDpaCTKVCPSGAMHKrEDGFVVVDEDVCIGCRYCHMACPYGA 113
Cdd:COG4231   24 CTGCGA--CVKVCPADAIEE-GDGKAVIDPDLCIGCGSCVQVCPVDA 67
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 9-113 1.36e-06

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: 45.85  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   9 IDSSRCTGCKTCELAC-KDYKDLTPEVsfrriyeyaggdwqEDNGVWHQNVFAY-YLSISCNhcedpACTKVCPSGAMHK 86
Cdd:cd10549   37 IDEDKCVFCGACVEVCpTGAIELTPEG--------------KEYVPKEKEAEIDeEKCIGCG-----LCVKVCPVDAITL 97

                         90       100
                 ....*....|....*....|....*..
gi 446135243  87 REDGFVVVDEDVCIGCRYCHMACPYGA 113
Cdd:cd10549   98 EDELEIVIDKEKCIGCGICAEVCPVNA 124
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 74-152 1.46e-06

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: 45.85  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  74 ACTKVCPSGA--------MHKREDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGH---MTKCDGCydrvaegkkPICV 142
Cdd:cd10549   47 ACVEVCPTGAieltpegkEYVPKEKEAEIDEEKCIGCGLCVKVCPVDAITLEDELEIvidKEKCIGC---------GICA 117

                         90
                 ....*....|
gi 446135243 143 ESCPLRALDF 152
Cdd:cd10549  118 EVCPVNAIKL 127
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 41-113 1.69e-06

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: 44.66  E-value: 1.69e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446135243  41 EYAGGDWQEDNGVWHQNVfayylsisCNHCEdpACTKVCPSGAMHKREDGFVVVDEDVCIGCRYCHMACPYGA 113
Cdd:COG1144   14 AYKTGGWRVERPVVDEDK--------CIGCG--LCWIVCPDGAIRVDDGKYYGIDYDYCKGCGICAEVCPVKA 76
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
75-153 1.90e-06

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 46.98  E-value: 1.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  75 CTKVCPSGAMH---KREDGFVV-VDEDVCIGCRYCHMACPYGAPQYNETKGHMTkCDGCYDrvaegkkpiCVESCPLRAL 150
Cdd:COG0348  184 CRYLCPYGAFQgllSDLSTLRVrYDRGDCIDCGLCVKVCPMGIDIRKGEINQSE-CINCGR---------CIDACPKDAI 253


                 ...
gi 446135243 151 DFG 153
Cdd:COG0348  254 RFS 256
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 92-154 2.51e-06

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 43.56  E-value: 2.51e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446135243  92 VVVDEDVCIGCRYCHMACPYGAPQYNETKGHM---TKCDGCYdrvaegkkpICVESCPLRALDFGP 154
Cdd:COG1149    6 PVIDEEKCIGCGLCVEVCPEGAIKLDDGGAPVvdpDLCTGCG---------ACVGVCPTGAITLEE 62
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
75-113 3.34e-06

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 44.17  E-value: 3.34e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 446135243  75 CTKVCPSGAMHKREDGFVVVDEDVCIGCRYCHMACPYGA 113
Cdd:PRK09623  59 CWKFCPEPAIYIKEDGYVAIDYDYCKGCGICANECPTKA 97
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 67-113 3.48e-06

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: 43.20  E-value: 3.48e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446135243  67 CNHCEdpACTKVCPSGAMH---KREDGFVVVDEDVCIGCRYCHMACPYGA 113
Cdd:COG1143    4 CIGCG--LCVRVCPVDAITiedGEPGKVYVIDPDKCIGCGLCVEVCPTGA 51
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
67-113 6.85e-06

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 45.79  E-value: 6.85e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446135243  67 CNHCEdpACTKVCPSGAMhKREDGFVVVDEDVCIGCRYCHMACPYGA 113
Cdd:COG4624   93 CKNCY--PCVRACPVKAI-KVDDGKAEIDEEKCISCGQCVAVCPFGA 136
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
67-176 7.87e-06

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 45.40  E-value: 7.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  67 CNHCEDPACTKVCPSGAMHKREDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHM--TKCDGCydrvaeGKkpiCVES 144
Cdd:COG4624   61 CCRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCYPCVRACPVKAIKVDDGKAEIdeEKCISC------GQ---CVAV 131

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446135243 145 CPLRAL----DFGP-IDELRKKHGDLAAVAPLPRAHF 176
Cdd:COG4624  132 CPFGAIteksDIEKvKKALKDPEKVVAQVAPAVRGQF 168
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
67-113 8.07e-06

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 45.62  E-value: 8.07e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446135243  67 CNHCEdpACTKVCPSGAMHKREDGFVVVDEDVCIGCRYCHMACPYGA 113
Cdd:COG1148  498 CTGCG--RCVEVCPYGAISIDEKGVAEVNPALCKGCGTCAAACPSGA 542
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 93-157 8.09e-06

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: 42.73  E-value: 8.09e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446135243  93 VVDEDVCIGCRYCHMACPYGAPQYNETKGH---MTKCDGCYdrvaegkkpICVESCPLRALDFGPIDE 157
Cdd:COG1144   26 VVDEDKCIGCGLCWIVCPDGAIRVDDGKYYgidYDYCKGCG---------ICAEVCPVKAIEMVPEEK 84
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 75-110 1.87e-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: 44.21  E-value: 1.87e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 446135243  75 CTKVCPSGAMHKREDGFVVVDEDVCIGCRYCHMACP 110
Cdd:COG2878  145 CIKACPFDAIVGAAKGMHTVDEDKCTGCGLCVEACP 180
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 67-146 2.46e-05

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: 42.38  E-value: 2.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  67 CNHCEdpACTKVCPSGAMHKREDG----FVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGcyDRVAEGKKPI-- 140
Cdd:cd10549    8 CIGCG--ICVKACPTDAIELGPNGaiarGPEIDEDKCVFCGACVEVCPTGAIELTPEGKEYVPKEK--EAEIDEEKCIgc 83


                 ....*...
gi 446135243 141 --CVESCP 146
Cdd:cd10549   84 glCVKVCP 91
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 67-113 2.50e-05

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 44.00  E-value: 2.50e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446135243  67 CNHcedpACTKVCP---SG--AMHKRE-DGFVVVDEDVCIGCRYCHMACPYGA 113
Cdd:COG1245   17 CNY----ECIKYCPvnrTGkeAIEIDEdDGKPVISEELCIGCGICVKKCPFDA 65
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
75-112 5.64e-05

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 42.61  E-value: 5.64e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446135243  75 CTKVCPSGAMHKrEDGFVVVDEDVCIGCRYCHMACPYG 112
Cdd:PRK07118 147 CVAACPFDAIHI-ENGLPVVDEDKCTGCGACVKACPRN 183
NapF COG1145
Ferredoxin [Energy production and conversion];
14-156 8.50e-05

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 42.02  E-value: 8.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  14 CTGCKTCELACKDYKDLTPEVSFRRIYEYAGGDWQEDNGVWHQNVFAYYLSISCNHCEDPACTKVCPSGAMHKREDGFVV 93
Cdd:COG1145   99 VLLLALAVAGAAKRLIISAVKLVAGLVVAAGEVLLVIAAALAEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAV 178

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446135243  94 VDEDVCIGCRYCHMACPYGAPQYNETKGHMT----KCDGCYdrvaegkkpICVESCPLRALDFGPID 156
Cdd:COG1145  179 IDAEKCIGCGLCVKVCPTGAIRLKDGKPQIVvdpdKCIGCG---------ACVKVCPVGAISLEPKE 236
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 66-113 8.62e-05

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 42.55  E-value: 8.62e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446135243  66 SCNHC-EDPACTKVCPSGAMHK-REDGFVVVDEDVCIGCRYCHMACPYGA 113
Cdd:PRK12771 508 SCGNCfECDNCYGACPQDAIIKlGPGRRYHFDYDKCTGCHICADVCPCGA 557
methan_mark_16 TIGR03287
putative methanogenesis marker 16 metalloprotein; Members of this protein family, to date, are ...
 67-117 9.89e-05

putative methanogenesis marker 16 metalloprotein; Members of this protein family, to date, are found in a completed prokaryotic genome if and only if the species is one of the archaeal methanogens. The exact function is unknown, but likely is linked to methanogenesis or a process closely connected to it. This protein is a predicted to bind FeS clusters, based on the presence of two copies of the Fer4 domain (pfam00037), with each copy having four Cys residues invariant across all members. [Energy metabolism, Methanogenesis]


Pssm-ID: 274501 [Multi-domain]  Cd Length: 391  Bit Score: 42.06  E-value: 9.89e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446135243   67 CNHCEDPACTKVCPSGAMhkREDGfvVVDEDVCIGCRYCHMACPYGAPQYN 117
Cdd:TIGR03287 304 CENCDPCLVEEACPVPAI--KKDG--TLNTEDCFGCGYCAEICPGGAFEVN 350
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
9-113 1.45e-04

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 41.46  E-value: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243   9 IDSSRCTGCKTCELAC-KDYKDLTPEVsfRRIYEYAGgdwQEDNGVWHQNVfayyLSISCNHCEdpACTKVCPSGAMhKR 87
Cdd:PRK07118 165 VDEDKCTGCGACVKACpRNVIELIPKS--ARVFVACN---SKDKGKAVKKV----CEVGCIGCG--KCVKACPAGAI-TM 232

                         90       100
                 ....*....|....*....|....*.
gi 446135243  88 EDGFVVVDEDVCIGCRYCHMACPYGA 113
Cdd:PRK07118 233 ENNLAVIDQEKCTSCGKCVEKCPTKA 258
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
67-113 1.60e-04

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 41.72  E-value: 1.60e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446135243  67 CNHcedpACTKVCPSGAMHKR------EDGFVVVDEDVCIGCRYCHMACPYGA 113
Cdd:PRK13409  17 CNY----ECIKYCPVVRTGEEtieideDDGKPVISEELCIGCGICVKKCPFDA 65
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 90-160 1.70e-04

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 38.54  E-value: 1.70e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446135243  90 GFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMT-----KCDGCYdrvaegkkpICVESCPLRALDFGPIDELRK 160
Cdd:COG1146    1 MMPVIDTDKCIGCGACVEVCPVDVLELDEEGKKALvinpeECIGCG---------ACELVCPVGAITVEDDEPEEQ 67
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 67-113 5.31e-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: 36.74  E-value: 5.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446135243   67 CNHCEdpACTKVCPSGAM------HKREDGFVVVDEDVCIGCRYCHMACPYGA 113
Cdd:pfam12838   1 CIGCG--ACVAACPVGAItldevgEKKGTKTVVIDPERCVGCGACVAVCPTGA 51
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
87-154 5.79e-04

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 37.40  E-value: 5.79e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  87 REDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMT--KCDGCYdrvaegkkpICVESCPLRALDFGP 154
Cdd:COG2768    1 HSLGKPYVDEEKCIGCGACVKVCPVGAISIEDGKAVIDpeKCIGCG---------ACIEVCPVGAIKIEW 61
Fer4_6 pfam12837
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 91-114 6.28e-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: 36.05  E-value: 6.28e-04
                          10        20
                  ....*....|....*....|....
gi 446135243   91 FVVVDEDVCIGCRYCHMACPYGAP 114
Cdd:pfam12837   1 VVEVDPDKCIGCGRCVVVCPYGAI 24
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 96-156 7.11e-04

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 36.65  E-value: 7.11e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446135243  96 EDVCIGCRYCHMACPYGAPQYNETKGH------MTKCDGCYdrvaegkkpICVESCPLRALDFGPID 156
Cdd:COG1143    1 EDKCIGCGLCVRVCPVDAITIEDGEPGkvyvidPDKCIGCG---------LCVEVCPTGAISMTPFE 58
napG PRK09476
quinol dehydrogenase periplasmic component; Provisional
 64-110 7.14e-04

quinol dehydrogenase periplasmic component; Provisional


Pssm-ID: 236534 [Multi-domain]  Cd Length: 254  Bit Score: 39.22  E-value: 7.14e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  64 SISCNHCEDPACTKVCPSGAM-HKRED------GF-VVVDEDVCIG-----CRYCHMACP 110
Cdd:PRK09476  96 DIPCEMCEDIPCVKACPSGALdRELVDiddarmGLaVLVDQENCLNfqglrCDVCYRVCP 155
PRK06991 PRK06991
electron transport complex subunit RsxB;
93-155 7.83e-04

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 39.39  E-value: 7.83e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446135243  93 VVDEDVCIGCRYCHMACPY----GAPQYNETKgHMTKCDGCydrvaegkkPICVESCPLRALDFGPI 155
Cdd:PRK06991  81 VIDEQLCIGCTLCMQACPVdaivGAPKQMHTV-LADLCTGC---------DLCVPPCPVDCIDMVPV 137
PRK13795 PRK13795
hypothetical protein; Provisional
 75-110 1.23e-03

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 39.21  E-value: 1.23e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446135243  75 CTKVCPSGAMhKREDG--FVVVDEDVCIGCRYCHMACP 110
Cdd:PRK13795 589 CVGACPTGAI-RIEEGkrKISVDEEKCIHCGKCTEVCP 625
oorD PRK09626
2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed
 67-110 1.31e-03

2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed


Pssm-ID: 236597 [Multi-domain]  Cd Length: 103  Bit Score: 37.01  E-value: 1.31e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446135243  67 CNHCEdpACTKVCPSGAMHKRED-----GFV--VVDEDVCIGCRYCHMACP 110
Cdd:PRK09626  18 CKACD--ICVSVCPAGVLAMRIDphavlGKMikVVHPESCIGCRECELHCP 66
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 92-113 2.02e-03

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


Pssm-ID: 459642 [Multi-domain]  Cd Length: 24  Bit Score: 34.53  E-value: 2.02e-03
                          10        20
                  ....*....|....*....|..
gi 446135243   92 VVVDEDVCIGCRYCHMACPYGA 113
Cdd:pfam00037   1 VVIDEEKCIGCGACVEVCPVGA 22
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 92-149 2.14e-03

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 35.79  E-value: 2.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446135243  92 VVVDEDVCIGCRYCHMACPYGAPQYNETKG--HMTKCDGCYdrvaegkkpICVESCPLRA 149
Cdd:COG4231   17 YVIDEDKCTGCGACVKVCPADAIEEGDGKAviDPDLCIGCG---------SCVQVCPVDA 67
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 92-155 2.65e-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: 2.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446135243   92 VVVDEDVCIGCRYCHMACP----YGAPQYNETKgHMTKCDGCydrvaegkkPICVESCPLRALDFGPI 155
Cdd:TIGR01944 108 ALIDEDNCIGCTKCIQACPvdaiVGAAKAMHTV-IADECTGC---------DLCVEPCPTDCIEMIPV 165
PRK00783 PRK00783
DNA-directed RNA polymerase subunit D; Provisional
 67-113 2.81e-03

DNA-directed RNA polymerase subunit D; Provisional


Pssm-ID: 234837 [Multi-domain]  Cd Length: 263  Bit Score: 37.56  E-value: 2.81e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446135243  67 CNHCEDpaCTKVCPSGAMHKREDGFVVVDEDVCIGCRYCHMACPYGA 113
Cdd:PRK00783 171 CDECEK--CVEACPRGVLELKEGKLVVTDLLNCSLCKLCERACPGKA 215
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 93-161 3.59e-03

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: 36.22  E-value: 3.59e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446135243  93 VVDEDVCIGCRYCHMACPYGAPQYNETKG-------HMTKCDGCYdrvaegkkpICVESCPLRALDFGPIDELRKK 161
Cdd:cd10549    2 KYDPEKCIGCGICVKACPTDAIELGPNGAiargpeiDEDKCVFCG---------ACVEVCPTGAIELTPEGKEYVP 68
PRK13795 PRK13795
hypothetical protein; Provisional
 99-147 3.79e-03

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 37.67  E-value: 3.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446135243  99 CIGCRYCHMACPYGAPQYNETKGHMT----KCDGCydrvaeGKkpiCVESCPL 147
Cdd:PRK13795 583 CVGCGVCVGACPTGAIRIEEGKRKISvdeeKCIHC------GK---CTEVCPV 626
PRK06273 PRK06273
ferredoxin; Provisional
 66-110 4.67e-03

ferredoxin; Provisional


Pssm-ID: 235764 [Multi-domain]  Cd Length: 165  Bit Score: 36.23  E-value: 4.67e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446135243  66 SCNHCEdpACTKVCPSGA--MHKRE-----DGFV-----VVDEDVCIGCRYCHMACP 110
Cdd:PRK06273  50 LCIGCG--GCANVCPTKAieMIPVEpvkitEGYVktkipKIDYEKCVYCLYCHDFCP 104
ACS_1 cd01916
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
 59-114 5.29e-03

Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.


Pssm-ID: 238897 [Multi-domain]  Cd Length: 731  Bit Score: 37.39  E-value: 5.29e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446135243  59 FAYYLSiSCNHCEDpaCTKVCPSG-----AMHKREDG---FVVVDEDVCIGCRYCHMACPYGAP 114
Cdd:cd01916  360 FQELAA-KCTDCGW--CTRACPNSlrikeAMEAAKEGdfsGLADLFDQCVGCGRCEQECPKEIP 420
porD PRK09624
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
 75-113 6.62e-03

pyruvate ferredoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 170017 [Multi-domain]  Cd Length: 105  Bit Score: 35.00  E-value: 6.62e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 446135243  75 CTKVCPSGAMHKREDGFVVVDEDVCIGCRYCHMACPYGA 113
Cdd:PRK09624  59 CYIYCPEPAIYLDEEGYPVFDYDYCKGCGICANECPTKA 97
 
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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