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Conserved domains on  [gi|409105620|gb|AFV11745|]
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formate dehydrogenase iron-sulfur subunit FdxH [Thermacetogenium phaeum DSM 12270]

Protein Classification

4Fe-4S dicluster domain-containing protein( domain architecture ID 11586846)

4Fe-4S dicluster domain-containing protein similar to Escherichia coli hydrogenase-4 component A, a probable electron transfer protein for hydrogenase 4

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 7-166 8.75e-97

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: 280.73  E-value: 8.75e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   7 YLVDTTKCIACRGCVVACKQWNQLPAEQTRFTGSYQTVPDLTGNTFTIISFHEYEED-GRIRWYFAKRQCMHCLEPVCMK 85
Cdd:cd10562    1 MLVDTSKCTACRGCQVACKQWNQLPAEKTPFTGSYQNPPDLTPNTWTLIRFYEHEEDnGGIRWLFRKRQCMHCTDAACVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  86 VCPQKAISITDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAEGDLPACVKACITGALEYGNRDE 165
Cdd:cd10562   81 VCPTGALYKTENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCFDRIENGMQPACVKTCPTGALTFGDRDE 160


                 .
gi 409105620 166 L 166
Cdd:cd10562  161 L 161
 
Name Accession Description Interval E-value
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 7-166 8.75e-97

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: 280.73  E-value: 8.75e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   7 YLVDTTKCIACRGCVVACKQWNQLPAEQTRFTGSYQTVPDLTGNTFTIISFHEYEED-GRIRWYFAKRQCMHCLEPVCMK 85
Cdd:cd10562    1 MLVDTSKCTACRGCQVACKQWNQLPAEKTPFTGSYQNPPDLTPNTWTLIRFYEHEEDnGGIRWLFRKRQCMHCTDAACVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  86 VCPQKAISITDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAEGDLPACVKACITGALEYGNRDE 165
Cdd:cd10562   81 VCPTGALYKTENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCFDRIENGMQPACVKTCPTGALTFGDRDE 160


                 .
gi 409105620 166 L 166
Cdd:cd10562  161 L 161
FDH-beta TIGR01582
formate dehydrogenase, beta subunit, Fe-S containing; This model represents the beta subunit ...
 8-260 4.64e-71

formate dehydrogenase, beta subunit, Fe-S containing; This model represents the beta subunit of the gamma-proteobacterial formate dehydrogenase. This subunit contains four 4Fe-4S clusters and is involved in transmitting electrons from the alpha subunit (TIGR01553) at the periplasmic space to the gamma subunit which spans the cytoplasmic membrane. In addition to the gamma proteobacteria, a sequence from Aquifex aolicus falls within the scope of this model. This appears to be the case for the alpha, gamma and epsilon (accessory protein TIGR01562) chains as well. [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]


Pssm-ID: 273705 [Multi-domain]  Cd Length: 283  Bit Score: 219.78  E-value: 4.64e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620    8 LVDTTKCIACRGCVVACKQWNQL-PAEQTRFTGSYQTVPDLTGNTFTIISFHEYEEDGRIRWYFAKRQCMHCLEPVCMKV 86
Cdd:TIGR01582  25 LIDVSSCIGCKACQAACQEWNDTtPPILSRKVGGYQNPPDLLPETFTLMRFKEGEESDGLEWLIRKDGCMHCREPGCLKA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   87 CPQKAISITDTGAVVR-DNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAEGDLPACVKACITGALEYGNRDE 165
Cdd:TIGR01582 105 CPAPGAIIQYQNGIVDfDHSKCIGCGYCIVGCPFNIPRYDKVDNRPYKCTLCIDRVSVGQEPACVKTCPTNAISFGFKED 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  166 LLAKAKERVNNLIG-DYPNANVYGETQAGGTNILYVL--ADVPGKY-GFEEDPKVSTAITAWQNVIKPYFPWLIALTAAG 241
Cdd:TIGR01582 185 MKERAEKRVADLKSrGYPNAGLYDPPGVGGTHVMYVLhhGDKPKDYqDLPEDPRIDASVGLWKGVLKTIGSIAMGGTALG 264

                         250
                  ....*....|....*....
gi 409105620  242 SIFSFFSTRLLKVGKEAHE 260
Cdd:TIGR01582 265 VFLHLILWGPNKVLGGKEE 283
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 1-200 1.06e-70

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 215.20  E-value: 1.06e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   1 MAKTKGYLVDTTKCIACRGCVVACKQWNQLPAeqtrftgsyqtvpdltGNTFTIISFHEYEEDGRIRWYFAKRQCMHCLE 80
Cdd:COG0437    2 SMKRYGMVIDLTKCIGCRACVVACKEENNLPV----------------GVTWRRVRRYEEGEFPNVEWLFVPVLCNHCDD 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  81 PVCMKVCPQKAISITDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAEGDLPACVKACITGALEY 160
Cdd:COG0437   66 PPCVKVCPTGATYKREDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVEACPTGALVF 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 409105620 161 GNRDELLAKAKERVNNLigdypNANVYGETQAGGTNILYV 200
Cdd:COG0437  146 GDLDDPESEVSKRLAEL-----PAYRLLPELGTKPSVYYL 180
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
6-262 2.80e-57

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 186.03  E-value: 2.80e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   6 GYLVDTTKCIACRGCVVACKQWNqLPAEQTRFTGSYQTVPDLTGNTFTIISFH-----EYEEDGRIRWYFAKRQCMHCLE 80
Cdd:PRK10882  39 GMLYDSTLCVGCQACVTKCQEIN-FPERNPQGEQTWDNPDKLSPYTNNIIKVWksgtgVNKDQEENGYAYIKKQCMHCVD 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  81 PVCMKVCPQKAISITD-TGAVVRDNDKCVGCQYCAAACPFHIPR--YNPTTDKETKCSLC----AERTAEGDLPACVKAC 153
Cdd:PRK10882 118 PNCVSVCPVSALTKDPkTGIVHYDKDVCTGCRYCMVACPFNVPKydYNNPFGAIHKCELCnqkgVERLDKGGLPGCVEVC 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620 154 ITGALEYGNRDELLAKAKERVN---NLIGDYP-----------------NANVYGETQAGGTNILYvLADVP-GKYGFEE 212
Cdd:PRK10882 198 PTGAVIFGTREELLAEAKRRLAlkpGSEYHYPrqtlksgdtylhtvpkyYPHVYGEKEGGGTQVLV-LSGVPfENLGLPK 276

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 409105620 213 DPKVSTAITA--WQNVIKPYFPWLIALTAAgsiFSFFSTRLLKvgKEAHEGE 262
Cdd:PRK10882 277 LDDLSTGARSehIQHTLYKGMILPLAVLAG---LTVLVRRNTK--NDHHDGG 323
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 66-163 1.22e-30

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: 110.03  E-value: 1.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   66 IRWYFAKRQCMHCLEPVCMKVCPQKAIsITD--TGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAE 143
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPVGAI-YKDeeTGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEA 79

                          90       100
                  ....*....|....*....|
gi 409105620  144 GDLPACVKACITGALEYGNR 163
Cdd:pfam13247  80 GLLPACVQTCPTGAMNFGDR 99
FDH3_beta NF038355
formate dehydrogenase FDH3 subunit beta; Members of this family are the beta subunit of the ...
 7-174 8.16e-29

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


Pssm-ID: 439648 [Multi-domain]  Cd Length: 180  Bit Score: 107.84  E-value: 8.16e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   7 YLVDTTKCIACRGCVVACKQWNQLPaeqtrftgsyqtvpdLTGNTFTIISFHEYEEdGRIRWYFAkrqCMHCLEPVCMKV 86
Cdd:NF038355   5 FLCDTERCIECNGCVVACKNAHELP---------------WGINRRRVVTLNDGVP-GEKSISVA---CMHCTDAPCAAV 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  87 CPQKAISITDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTD-----KETKCSLCA-----------------ERTAEG 144
Cdd:NF038355  66 CPVDCFYIRADGIVLHDKDKCIGCGYCLYACPFGAPQFPKDGAfgargKMDKCTFCAggpeetnseaerekygqNRIAEG 145

                        170       180       190
                 ....*....|....*....|....*....|
gi 409105620 145 DLPACVKACITGALEYGNRDELLAKAKERV 174
Cdd:NF038355 146 KLPLCAEMCSTKALLAGDAEVVADIYRERV 175
 
Name Accession Description Interval E-value
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 7-166 8.75e-97

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: 280.73  E-value: 8.75e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   7 YLVDTTKCIACRGCVVACKQWNQLPAEQTRFTGSYQTVPDLTGNTFTIISFHEYEED-GRIRWYFAKRQCMHCLEPVCMK 85
Cdd:cd10562    1 MLVDTSKCTACRGCQVACKQWNQLPAEKTPFTGSYQNPPDLTPNTWTLIRFYEHEEDnGGIRWLFRKRQCMHCTDAACVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  86 VCPQKAISITDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAEGDLPACVKACITGALEYGNRDE 165
Cdd:cd10562   81 VCPTGALYKTENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCFDRIENGMQPACVKTCPTGALTFGDRDE 160


                 .
gi 409105620 166 L 166
Cdd:cd10562  161 L 161
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 6-199 4.63e-87

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: 257.14  E-value: 4.63e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   6 GYLVDTTKCIACRGCVVACKQWNQLPAEQTRFTGSYQTVPDLTGNTFTIISFHEyEEDGRIRWYFAKRQCMHCLEPVCMK 85
Cdd:cd10561    1 GVLYDTTRCIGCRACEVACKEWNGLPAEDTAFGPGWDNPRDLSAKTYTVIKRYE-VETGGKGFVFVKRQCMHCLDPACVS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  86 VCPQKAISITDTGAVVRDNDKCVGCQYCAAACPFHIPRY--NPTTDKETKCSLCAERTAEGDLPACVKACITGALEYGNR 163
Cdd:cd10561   80 ACPVGALRKTPEGPVTYDEDKCIGCRYCMVACPFNIPKYewDSANPKIRKCTMCYDRLKEGKQPACVEACPTGALLFGKR 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 409105620 164 DELLAKAKERVNNLIGDYpNANVYGETQAGGTNILY 199
Cdd:cd10561  160 EELLAEAKRRIAANPGRY-VDHVYGEKEAGGTSVLY 194
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 8-211 8.94e-83

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: 246.92  E-value: 8.94e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   8 LVDTTKCIACRGCVVACKQWNQLPAEQTRFTGSYQTVPDLTGNTFTIISFHEYEEDGRIRWYFAKRQCMHCLEPVCMKVC 87
Cdd:cd10558    3 LIDVSKCIGCKACQVACKEWNDLRAEVGHNVGTYQNPADLSPETWTLMKFREVEDNGKLEWLIRKDGCMHCADPGCLKAC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  88 P-QKAISITDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAEGDLPACVKACITGALEYGNRDEL 166
Cdd:cd10558   83 PsPGAIVQYANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVGLEPACVKTCPTGALHFGTKEDM 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 409105620 167 LAKAKERVNNLIGD-YPNANVYGETQAGGTNILYVLADVPGKYGFE 211
Cdd:cd10558  163 LALAEKRVAALKERgYTNAGLYDPKGVGGTHVMYVLHHADKPEGYP 208
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 7-161 6.72e-74

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: 222.66  E-value: 6.72e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   7 YLVDTTKCIACRGCVVACKQWNQLPAEQTRFTGSYQTVPDLTGNTFTIISFHEYEED-GRIRWYFAKRQCMHCLEPVCMK 85
Cdd:cd16366    1 FLVDTSRCTGCRACQVACKQWNGLPAEKTEFTGSYQNPPDLTAHTWTLVRFYEVEKPgGDLSWLFRKDQCMHCTDAGCLA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 409105620  86 VCPQKAISITDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAEGDLPACVKACITGALEYG 161
Cdd:cd16366   81 ACPTGAIIRTETGTVVVDPETCIGCGYCVNACPFDIPRFDEETGRVAKCTLCYDRISNGLQPACVKTCPTGALTFG 156
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 6-218 1.30e-72

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: 221.88  E-value: 1.30e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   6 GYLVDTTKCIACRGCVVACKQWNQLPAEQTRFTG-SYQTVPDLTGNTFTIISFHE-------YEEDGRIRWYFAKRQCMH 77
Cdd:cd10560    1 GFFTDTSICIGCKACEVACKQWNQLPADGYDFSGmSYDNTGDLSASTWRHVKFIErptedgpANEGGDLQWLFMSDVCKH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  78 CLEPVCMKVCPQKAISITDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAEGDLPACVKACITGA 157
Cdd:cd10560   81 CTDAGCLEACPTGAIFRTEFGTVYIQPDICNGCGYCVAACPFGVIDRNEETGRAHKCTLCYDRLKDGLEPACAKACPTGS 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 409105620 158 LEYGNRDELLAKAKERVNNLIGD-YPNANVYG---ETQAGGTNILYVLADVPGKYGFEEDPKVST 218
Cdd:cd10560  161 IQFGPLEELRERARARVEQLHEQgVVEAYLYGadpTEGYGGLNAFFLLLDKPEVYGLPADPLLPT 225
FDH-beta TIGR01582
formate dehydrogenase, beta subunit, Fe-S containing; This model represents the beta subunit ...
 8-260 4.64e-71

formate dehydrogenase, beta subunit, Fe-S containing; This model represents the beta subunit of the gamma-proteobacterial formate dehydrogenase. This subunit contains four 4Fe-4S clusters and is involved in transmitting electrons from the alpha subunit (TIGR01553) at the periplasmic space to the gamma subunit which spans the cytoplasmic membrane. In addition to the gamma proteobacteria, a sequence from Aquifex aolicus falls within the scope of this model. This appears to be the case for the alpha, gamma and epsilon (accessory protein TIGR01562) chains as well. [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]


Pssm-ID: 273705 [Multi-domain]  Cd Length: 283  Bit Score: 219.78  E-value: 4.64e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620    8 LVDTTKCIACRGCVVACKQWNQL-PAEQTRFTGSYQTVPDLTGNTFTIISFHEYEEDGRIRWYFAKRQCMHCLEPVCMKV 86
Cdd:TIGR01582  25 LIDVSSCIGCKACQAACQEWNDTtPPILSRKVGGYQNPPDLLPETFTLMRFKEGEESDGLEWLIRKDGCMHCREPGCLKA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   87 CPQKAISITDTGAVVR-DNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAEGDLPACVKACITGALEYGNRDE 165
Cdd:TIGR01582 105 CPAPGAIIQYQNGIVDfDHSKCIGCGYCIVGCPFNIPRYDKVDNRPYKCTLCIDRVSVGQEPACVKTCPTNAISFGFKED 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  166 LLAKAKERVNNLIG-DYPNANVYGETQAGGTNILYVL--ADVPGKY-GFEEDPKVSTAITAWQNVIKPYFPWLIALTAAG 241
Cdd:TIGR01582 185 MKERAEKRVADLKSrGYPNAGLYDPPGVGGTHVMYVLhhGDKPKDYqDLPEDPRIDASVGLWKGVLKTIGSIAMGGTALG 264

                         250
                  ....*....|....*....
gi 409105620  242 SIFSFFSTRLLKVGKEAHE 260
Cdd:TIGR01582 265 VFLHLILWGPNKVLGGKEE 283
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 6-203 5.84e-71

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: 216.53  E-value: 5.84e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   6 GYLVDTTKCIACRGCVVACKQWNQLPAEQTRFTGSYQTVPDLTGNTFTIISFHEYE-EDGRIRWYFAKRQCMHCLEPVCM 84
Cdd:cd10559    1 SFLIDTTRCTACRGCQVACKQWNQLPAEQTKNTGSHQNPPDLSANTYKLVRFNEVRnENGKPDWLFFPDQCRHCVTPPCK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  85 KVCPQK--AISITD-TGAVV-----RDNDKCVgcqyCAAACPFHIPRYNPTTDKETKCSLCAERTAEGDLPACVKACITG 156
Cdd:cd10559   81 DAADMVpgAVIQDEaTGAVVftektAELDFDD----VLSACPYNIPRKNEATGRIVKCDMCIDRVSNGLQPACVKACPTG 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 409105620 157 ALEYGNRDELLAKAKERVNNLIGDYPNANVYgetQAGGTNILYVLAD 203
Cdd:cd10559  157 AMNFGDRDEMLAMASKRLEELKKRYPKANLY---DPDDVRVIWLLAE 200
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 1-200 1.06e-70

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 215.20  E-value: 1.06e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   1 MAKTKGYLVDTTKCIACRGCVVACKQWNQLPAeqtrftgsyqtvpdltGNTFTIISFHEYEEDGRIRWYFAKRQCMHCLE 80
Cdd:COG0437    2 SMKRYGMVIDLTKCIGCRACVVACKEENNLPV----------------GVTWRRVRRYEEGEFPNVEWLFVPVLCNHCDD 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  81 PVCMKVCPQKAISITDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAEGDLPACVKACITGALEY 160
Cdd:COG0437   66 PPCVKVCPTGATYKREDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVEACPTGALVF 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 409105620 161 GNRDELLAKAKERVNNLigdypNANVYGETQAGGTNILYV 200
Cdd:COG0437  146 GDLDDPESEVSKRLAEL-----PAYRLLPELGTKPSVYYL 180
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
6-262 2.80e-57

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 186.03  E-value: 2.80e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   6 GYLVDTTKCIACRGCVVACKQWNqLPAEQTRFTGSYQTVPDLTGNTFTIISFH-----EYEEDGRIRWYFAKRQCMHCLE 80
Cdd:PRK10882  39 GMLYDSTLCVGCQACVTKCQEIN-FPERNPQGEQTWDNPDKLSPYTNNIIKVWksgtgVNKDQEENGYAYIKKQCMHCVD 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  81 PVCMKVCPQKAISITD-TGAVVRDNDKCVGCQYCAAACPFHIPR--YNPTTDKETKCSLC----AERTAEGDLPACVKAC 153
Cdd:PRK10882 118 PNCVSVCPVSALTKDPkTGIVHYDKDVCTGCRYCMVACPFNVPKydYNNPFGAIHKCELCnqkgVERLDKGGLPGCVEVC 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620 154 ITGALEYGNRDELLAKAKERVN---NLIGDYP-----------------NANVYGETQAGGTNILYvLADVP-GKYGFEE 212
Cdd:PRK10882 198 PTGAVIFGTREELLAEAKRRLAlkpGSEYHYPrqtlksgdtylhtvpkyYPHVYGEKEGGGTQVLV-LSGVPfENLGLPK 276

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 409105620 213 DPKVSTAITA--WQNVIKPYFPWLIALTAAgsiFSFFSTRLLKvgKEAHEGE 262
Cdd:PRK10882 277 LDDLSTGARSehIQHTLYKGMILPLAVLAG---LTVLVRRNTK--NDHHDGG 323
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 6-161 5.14e-55

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: 173.90  E-value: 5.14e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   6 GYLVDTTKCIACRGCVVACKQWNQLPAEQTRftgsyqtvpdltgntftiISFHEYEED--GRIRWYFAKRQCMHCLEPVC 83
Cdd:cd16371    1 GFYFDQERCIGCKACEIACKDKNDLPPGVNW------------------RRVYEYEGGefPEVFAYFLSMSCNHCENPAC 62

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 409105620  84 MKVCPQKAISITDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAEGDLPACVKACITGALEYG 161
Cdd:cd16371   63 VKVCPTGAITKREDGIVVVDQDKCIGCGYCVWACPYGAPQYNPETGKMDKCDMCVDRLDEGEKPACVAACPTRALDFG 140
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 8-161 1.02e-50

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: 162.56  E-value: 1.02e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   8 LVDTTKCIACRGCVVACKQWNQLPaeqtrftgsyqtvpdlTGNTFTIIsfhEYEEDGRIRWYFAKRQCMHCLEPVCMKVC 87
Cdd:cd04410    2 VVDLDRCIGCGTCEVACKQEHGLR----------------PGPDWSRI---KVIEGGGLERAFLPVSCMHCEDPPCVKAC 62

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 409105620  88 PQKAISITDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAEGDLPACVKACITGALEYG 161
Cdd:cd04410   63 PTGAIYKDEDGIVLIDEDKCIGCGSCVEACPYGAIVFDPEPGKAVKCDLCGDRLDEGLEPACVKACPTGALTFG 136
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 7-164 1.09e-44

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: 148.83  E-value: 1.09e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   7 YLVDTTKCIACRGCVVACKQWNQLPAEQTRftgsyqtvpdltgntfTIISFHEYEEDGRIRWYFAKRQCMHCLEPVCMKV 86
Cdd:cd10551    1 MVIDLRKCIGCGACVVACKAENNVPPGVFR----------------NRVLEYEVGEYPNVKRTFLPVLCNHCENPPCVKV 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  87 CPQKAISITDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKET------------KCSLCAERTAEGDLPACVKACI 154
Cdd:cd10551   65 CPTGATYKREDGIVLVDYDKCIGCRYCMAACPYGARYFNPEEPHEFgevpvrpkgvveKCTFCYHRLDEGLLPACVEACP 144

                        170
                 ....*....|
gi 409105620 155 TGALEYGNRD 164
Cdd:cd10551  145 TGARIFGDLD 154
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 8-171 3.53e-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: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 122.77  E-value: 3.53e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   8 LVDTTKCIACRGCVVACKQWNqlpAEQTRftgsyqtvpdltgntftiISFHEYEEDGRIRWyfakrQCMHCLEPVCMKVC 87
Cdd:cd16374    2 YVDPERCIGCRACEIACAREH---SGKPR------------------ISVEVVEDLASVPV-----RCRHCEDAPCMEVC 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  88 PQKAISITDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAEGDLPACVKACITGALEYGNRDELL 167
Cdd:cd16374   56 PTGAIYRDEDGAVLVDPDKCIGCGMCAMACPFGVPRFDPSLKVAVKCDLCIDRRREGKLPACVEACPTGALKFGDIEELL 135


                 ....
gi 409105620 168 AKAK 171
Cdd:cd16374  136 KEKR 139
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 9-176 6.15e-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: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 120.96  E-value: 6.15e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   9 VDTTKCIACRGCVVAC------KQWNQLPAEQTRFTGSYQTVPDLtgntftiisfheyeedgrirwyfakrqCMHCLEPV 82
Cdd:cd16369    6 IDPSRCIGCRACVAACrecgthRGKSMIHVDYIDRGESTQTAPTV---------------------------CMHCEDPT 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  83 CMKVCPQKAISITDTGAVVRDND-KCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAEGDLPACVKACITGALEYG 161
Cdd:cd16369   59 CAEVCPADAIKVTEDGVVQSALKpRCIGCSNCVNACPFGVPKYDEERNLMMKCDMCYDRTSVGKAPMCASVCPSGALFYG 138

                        170
                 ....*....|....*
gi 409105620 162 NRDELLAKAKERVNN 176
Cdd:cd16369  139 TREEIQALRPGSTPV 153
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 10-161 2.76e-32

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: 115.54  E-value: 2.76e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  10 DTTKCIACRGCVVACKQWNQLPAeQTRFTGSYQTVPDLTgntftiisfheyeeDGRIRWYFAKRQCMHCLEPVCMKVCPQ 89
Cdd:cd10553    8 DSKRCIGCLACEVHCKVKNNLPV-GPRLCRIFAVGPKMV--------------GGKPRLKFVYMSCFHCENPWCVKACPT 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 409105620  90 KAISITDT-GAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAEGDLPACVKACITGALEYG 161
Cdd:cd10553   73 GAMQKREKdGIVYVDQELCIGCKACIEACPWGIPQWNPATGKVVKCDYCMDRIDQGLKPACVTGCTTHALSFV 145
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 8-160 2.97e-31

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


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 112.67  E-value: 2.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   8 LVDTTKCIACRGCVVACKQWNqlpaeqtrfTGSYQtvPDLTGntftiISFHEYEEDGRIRWYFakrqCMHCLEPVCMKVC 87
Cdd:cd10550    2 VVDPEKCTGCRTCELACSLKH---------EGVFN--PSLSR-----IRVVRFEPEGLDVPVV----CRQCEDAPCVEAC 61

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 409105620  88 PQKAISI-TDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCaertaEGDlPACVKACITGALEY 160
Cdd:cd10550   62 PVGAISRdEETGAVVVDEDKCIGCGMCVEACPFGAIRVDPETGKAIKCDLC-----GGD-PACVKVCPTGALEF 129
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 66-163 1.22e-30

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: 110.03  E-value: 1.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   66 IRWYFAKRQCMHCLEPVCMKVCPQKAIsITD--TGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAE 143
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPVGAI-YKDeeTGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEA 79

                          90       100
                  ....*....|....*....|
gi 409105620  144 GDLPACVKACITGALEYGNR 163
Cdd:pfam13247  80 GLLPACVQTCPTGAMNFGDR 99
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
2-157 2.37e-29

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 111.12  E-value: 2.37e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   2 AKTKGYLVDTTKCIACRGCVVACKQWNQLPAEQTRFT-GSYQTVPDLTGNTFTIIsfheyeedgrirwyfAKRQCMHCLE 80
Cdd:PRK14993  41 RHRYAMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTvNQYQVQREGSQEVTNVL---------------LPRLCNHCDN 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 409105620  81 PVCMKVCPQKAISITDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAEGDLPACVKACITGA 157
Cdd:PRK14993 106 PPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGA 182
FDH3_beta NF038355
formate dehydrogenase FDH3 subunit beta; Members of this family are the beta subunit of the ...
 7-174 8.16e-29

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


Pssm-ID: 439648 [Multi-domain]  Cd Length: 180  Bit Score: 107.84  E-value: 8.16e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   7 YLVDTTKCIACRGCVVACKQWNQLPaeqtrftgsyqtvpdLTGNTFTIISFHEYEEdGRIRWYFAkrqCMHCLEPVCMKV 86
Cdd:NF038355   5 FLCDTERCIECNGCVVACKNAHELP---------------WGINRRRVVTLNDGVP-GEKSISVA---CMHCTDAPCAAV 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  87 CPQKAISITDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTD-----KETKCSLCA-----------------ERTAEG 144
Cdd:NF038355  66 CPVDCFYIRADGIVLHDKDKCIGCGYCLYACPFGAPQFPKDGAfgargKMDKCTFCAggpeetnseaerekygqNRIAEG 145

                        170       180       190
                 ....*....|....*....|....*....|
gi 409105620 145 DLPACVKACITGALEYGNRDELLAKAKERV 174
Cdd:NF038355 146 KLPLCAEMCSTKALLAGDAEVVADIYRERV 175
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 8-171 1.04e-27

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: 105.58  E-value: 1.04e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   8 LVDTTKCIACRG-----CVVACKQWNQ--LPAEQTRFTGSY---QTVPD----------LTGNTFTIISFHEYEEDGRIR 67
Cdd:cd16368    4 LIDLTKCDGCPGesipaCVRACREKNQarFPEPVSKPIQPYwprKRIEDwsdkrdvtdrLTPYNWLYVQKLTVDTAGGEK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  68 WYFAKRQCMHCLEPVCMKVCPQKAISITDTGAVVRDNDKCVGCQYCAAACPFHIPR-------YNPTTDKET------KC 134
Cdd:cd16368   84 EVFIPRRCMHCDNPPCAKLCPFGAARKTPEGAVYIDDDLCFGGAKCRDVCPWHIPQrqagvgiYLHLAPEYAgggvmyKC 163

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 409105620 135 SLCAERTAEGDLPACVKACITGALEYGNRDELLAKAK 171
Cdd:cd16368  164 DLCKDLLAQGKPPACIEACPKGAQYFGPRKEMVALAR 200
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 8-161 2.25e-24

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: 95.02  E-value: 2.25e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   8 LVDTTKCIACRGCVVACKqwnqlpAEQTrftgSYQTVPDLTGNTFTIISFHEYEEDGRIrwYFAKrQCMHCLEPVCMKVC 87
Cdd:cd10563    3 FIDEEKCLGCKLCEVACA------VAHS----KSKDLIKAKLEKERPRPRIRVEESGGR--SFPL-QCRHCDEPPCVKAC 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 409105620  88 PQKAISITD-TGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERtaegDLPACVKACITGALEYG 161
Cdd:cd10563   70 MSGAMHKDPeTGIVIHDEEKCVGCWMCVMVCPYGAIRPDKERKVALKCDLCPDR----ETPACVEACPTGALVLE 140
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
4-160 1.85e-23

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 92.41  E-value: 1.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   4 TKGYLVDTTKCIACRGCVVACkqwnqlpAEQTRFTGSYQTVPDLT---GNTFTIISfheyeedgrirwyfakrQCMHCLE 80
Cdd:COG1142    2 NKFIIADPEKCIGCRTCEAAC-------AVAHEGEEGEPFLPRIRvvrKAGVSAPV-----------------QCRHCED 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  81 PVCMKVCPQKAISItDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKET--KCSLCAERTaegDLPACVKACITGAL 158
Cdd:COG1142   58 APCAEVCPVGAITR-DDGAVVVDEEKCIGCGLCVLACPFGAITMVGEKSRAVavKCDLCGGRE---GGPACVEACPTGAL 133


                 ..
gi 409105620 159 EY 160
Cdd:COG1142  134 RL 135
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 6-154 3.04e-23

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: 93.80  E-value: 3.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   6 GYLVDTTKCIACRGCVVACKQ-WNQLPAEQTRFTGSYQTVPdlTGNTFTIISFHEYEEDGRIRWYF-AKRQCMHCLEPVC 83
Cdd:cd16365    4 AAVFNLNKCIGCQTCTVACKNaWTYRKGQEYMWWNNVETKP--GGGYPQDWEVKTIDNGGNTRFFFyLQRLCNHCTNPAC 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 409105620  84 MKVCPQKAI-SITDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAEGDLPACVKACI 154
Cdd:cd16365   82 LAACPRGAIyKREEDGIVLIDQKRCRGYRKCVEQCPYKKIYFNGLSRVSEKCIACYPRIEGGDPTRCMSACV 153
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 8-158 5.57e-23

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: 91.55  E-value: 5.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   8 LVDTTKCIACRGCVVACKQWNQLPAEQTRFTGSYQTVPdltgntftiisfheyeedgRIRWYFAKR-----QCMHCLEPV 82
Cdd:cd10554    3 IADPDKCIGCRTCEVACAAAHSGKGIFEAGTDGLPFLP-------------------RLRVVKTGEvtapvQCRQCEDAP 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  83 CMKVCPQKAISITDtGAVVRDNDKCVGCQYCAAACPFH----IPRYNPTTDKET-------KCSLCAERtAEGdlPACVK 151
Cdd:cd10554   64 CANVCPVGAISQED-GVVQVDEERCIGCKLCVLACPFGaiemAPTTVPGVDWERgpravavKCDLCAGR-EGG--PACVE 139


                 ....*..
gi 409105620 152 ACITGAL 158
Cdd:cd10554  140 ACPTKAL 146
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 6-154 1.41e-22

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: 94.06  E-value: 1.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   6 GYLVDTTKCIACRGCVVACKQ------------WN-------------------QLPAEQTRFTG---SYQTVPDLTGNT 51
Cdd:cd10556   13 AMVFDTNKCIACQTCTMACKStwtsgkgqeymwWNnvetkpyggyplgwdvrllDEEGGQTWAEGgvyEGKTIFEAAAAG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  52 FTIISFHEYEEDGR------------------------IRWYF-AKRQCMHCLEPVCMKVCPQKAI-SITDTGAVVRDND 105
Cdd:cd10556   93 EQVLGYRPEDEDWRypnigedevngertpdtgsslpphPIWFFyLPRICNHCTYPACLAACPRKAIyKREEDGIVLIDQE 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 409105620 106 KCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAEGDLPACVKACI 154
Cdd:cd10556  173 RCRGYRECVEACPYKKPMYNPTTRVSEKCIGCYPRIEEGDQTQCVSACI 221
PRK09898 PRK09898
ferredoxin-like protein;
5-159 9.32e-22

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 89.90  E-value: 9.32e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   5 KGYLV-DTTKCIACRGCVVACKQWNQlpaeqtRFTGSYQTVPDLTGNTFTIISFHEYEEDGRIRWYFAKRQCMHCLEPVC 83
Cdd:PRK09898  58 KGVLVtQRARCTGCHRCEISCTNFND------GSVGTFFSRIKIHRNYFFGDNGVGSGGGLYGDLNYTADTCRQCKEPQC 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 409105620  84 MKVCPQKAISIT-DTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAErtaegdlpaCVKACITGALE 159
Cdd:PRK09898 132 MNVCPIGAITWQqKEGCITVDHKRCIGCSACTTACPWMMATVNTESKKSSKCVLCGE---------CANACPTGALK 199
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 8-171 1.03e-20

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: 86.61  E-value: 1.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   8 LVDTTKCIACRGCVVACKQwnqlPAEQTRFTGSYQTVPDlTGNTFTIISFHEYEEDGRIRWYFAKRQCMHCLEPVCMKVC 87
Cdd:cd10552    2 VIDVAKCNGCYNCFLACKD----EHVGNDWPGYAAPQPR-HGHFWMRILRRERGQYPKVDVAYLPVPCNHCDNAPCIKAA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  88 PQKAISITDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAEG-DLPACVKACITGALEYGNRDEL 166
Cdd:cd10552   77 KDGAVYKRDDGIVIIDPEKAKGQKQLVDACPYGAIYWNEELQVPQKCTFCAHLLDDGwKEPRCVQACPTGALRFGKLEDE 156


                 ....*
gi 409105620 167 LAKAK 171
Cdd:cd10552  157 EMAAK 161
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 6-153 1.41e-19

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: 86.20  E-value: 1.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   6 GYLVDTTKCIACRGCVVACKQ------------WNQL--------PAEQTRFTGSYQTVPDLT-GNTFTIISF-----HE 59
Cdd:cd10555    6 AMVMDLNKCIGCQTCTVACKTlwtnrngreymyWNNVetqpgkgyPKNWEKKGGGFKDKGELKpGIIPTLEDYgvpweYN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  60 YEE------DGRIR-------------------------WYF-AKRQCMHCLEPVCMKVCPQKAISITDT-GAVVRDNDK 106
Cdd:cd10555   86 HEEelfegkGGRVRpspkgdptwgpnwdedqgageypnsYYFyLPRICNHCTNPACLAACPRKAIYKREEdGIVLVDQDR 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 409105620 107 CVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAEGDLPACVKAC 153
Cdd:cd10555  166 CRGYRYCVEACPYKKIYFNPVEQKSEKCIFCYPRIEKGVAPACARQC 212
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 8-158 4.15e-19

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: 80.81  E-value: 4.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   8 LVDTTKCIACRGCVVACKQwnqlpaeqtrftgSYQTVPDLTGNTFTIISFHeyeedgrirwyFAKrQCMHCLEPVCMKVC 87
Cdd:cd16367   15 VIDLDRCIRCDNCEKACAD-------------THDGHSRLDRNGLRFGNLL-----------VPT-ACRHCVDPVCMIGC 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 409105620  88 PQKAISITDTGAvVRDNDKCVGCQYCAAACPFHipryNPTTDKETKCSLCAERTAegdlPACVKACITGAL 158
Cdd:cd16367   70 PTGAIHRDDGGE-VVISDACCGCGNCASACPYG----AIQMVRAVKCDLCAGYAG----PACVSACPTGAA 131
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 8-173 5.40e-17

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 80.18  E-value: 5.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   8 LVDTTKCIACRGCVVAC---KQWNQLPAEQTRFTgsyqtvPdltgntftiisfheyeedgRIRWYFAKRQ-----CMHCL 79
Cdd:PRK12769   6 MANSQQCLGCHACEIACvmaHNDEQHVLSQHHFH------P-------------------RITVIKHQQQrsavtCHHCE 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  80 EPVCMKVCPQKAISITDTGAVVRdNDKCVGCQYCAAACPFH-----IPRYNPTTDKET--KCSLCAERtAEGdlPACVKA 152
Cdd:PRK12769  61 DAPCARSCPNGAISHVDDSIQVN-QQKCIGCKSCVVACPFGtmqivLTPVAAGKVKATahKCDLCAGR-ENG--PACVEN 136

                        170       180
                 ....*....|....*....|.
gi 409105620 153 CITGALEYGNRDELLAKAKER 173
Cdd:PRK12769 137 CPADALQLVTEQALSGMAKSR 157
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 73-160 2.82e-16

beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes nitrate reductase A, a member of the DMSO reductase family. The respiratory nitrate reductase complex (NarGHI) from E. coli is a heterotrimer, with the catalytic subunit (NarG) with a molybdo-bis (molybdopterin guanine dinucleotide) cofactor and an [Fe-S] cluster, the electron transfer subunit (NarH) with four [Fe-S] clusters, and the integral membrane subunit (NarI) with two b-type hemes. Nitrate reductase A often forms a respiratory chain with the formate dehydrogenase via the lipid soluble quinol pool. Electron transfer from formate to nitrate is coupled to proton translocation across the cytoplasmic membrane generating proton motive force by a redox loop mechanism. Demethylmenaquinol (DMKH2) has been shown to be a good substrate for NarGHI in nitrate respiration in E. coli.


Pssm-ID: 319879 [Multi-domain]  Cd Length: 363  Bit Score: 77.40  E-value: 2.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  73 RQCMHCLEPVCMKVCPQKAISITDT-GAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAEGDLPACVK 151
Cdd:cd10557  177 RICNHCLNPACVAACPSGAIYKREEdGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSEKCIFCYPRLEAGQPTVCSE 256


                 ....*....
gi 409105620 152 ACItGALEY 160
Cdd:cd10557  257 TCV-GRIRY 264
PRK10330 PRK10330
electron transport protein HydN;
8-173 2.06e-12

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 64.14  E-value: 2.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   8 LVDTTKCIACRGCVVAC---KQWNQLPAEQT--RFTGSYQTVPDLTGNTFTIisfheyeedgrirwyfakrqCMHCLEPV 82
Cdd:PRK10330   6 IADASKCIGCRTCEVACvvsHQENQDCASLTpeTFLPRIHVIKGVNVSTATV--------------------CRQCEDAP 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  83 CMKVCPQKAISiTDTGAVVRDNDKCVGCQYCAAACPF-------------HIPRYNPTTDK--ETKCSLCAERtAEGdlP 147
Cdd:PRK10330  66 CANVCPNGAIS-RDKGFVHVMQERCIGCKTCVVACPYgamevvvrpvirnSGAGLNVRAEKaeANKCDLCNHR-EDG--P 141

                        170       180
                 ....*....|....*....|....*.
gi 409105620 148 ACVKACITGALEYGNRDELLAKAKER 173
Cdd:PRK10330 142 ACMAACPTHALICVDRNKLEQLSAEK 167
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 73-160 3.14e-12

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


Pssm-ID: 440755 [Multi-domain]  Cd Length: 485  Bit Score: 65.98  E-value: 3.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  73 RQCMHCLEPVCMKVCPQKAI-SITDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAEGDLPACVK 151
Cdd:COG1140  180 RICEHCLNPACVASCPSGAIyKREEDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGKAEKCIFCYPRIEAGQPTVCSE 259


                 ....*....
gi 409105620 152 ACItGALEY 160
Cdd:COG1140  260 TCV-GRIRY 267
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 10-209 8.82e-12

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 64.66  E-value: 8.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  10 DTTKCIACRGCVVAC---KQWNQLPAEQTRFTGSYQTVpdLTGNTFTIISfheyeedgrirwyfakrqCMHCLEPVCMKV 86
Cdd:PRK12809   8 EAAECIGCHACEIACavaHNQENWPLSHSDFRPRIHVV--GKGQAANPVA------------------CHHCNNAPCVTA 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  87 CPQKAIsITDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKetKCSLCAERTAEGDlpACVKACITGALEYGNRDEL 166
Cdd:PRK12809  68 CPVNAL-TFQSDSVQLDEQKCIGCKRCAIACPFGVVEMVDTIAQ--KCDLCNQRSSGTQ--ACIEVCPTQALRLMDDKGL 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 409105620 167 LAKAKERVNNLIGDYPNANVYGETQAGgtnilyvLADVPGKYG 209
Cdd:PRK12809 143 QQIKVARQRKTAAGKASSDAQPSRSAA-------LLPVNSRKG 178
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 9-160 1.06e-11

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


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 60.75  E-value: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   9 VDTTKCIACRGCVVACkqwnqlpaeQTRFTGSYqtvpdltGNTFTIISFHEYeedGRIRWYFAKRQCMHCLEPVCMKVCP 88
Cdd:cd16370    6 KDMERCIGCYSCMLAC---------SRRVHKSA-------SLSKSAIRVRTR---GGLEGGFTVVVCRACEDPPCAEACP 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 409105620  89 QKAISITDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAertaegdlpACVKACITGALEY 160
Cdd:cd16370   67 TGALEPRKGGGVVLDKEKCIGCGNCVKACIVGAIFWDEETNKPIICIHCG---------YCARYCPHDVLAM 129
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 75-159 2.87e-11

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


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 59.27  E-value: 2.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  75 CMHCLEpvCMKVCPQKAISITDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAertaegdlpACVKACI 154
Cdd:cd16372   49 CNQCGE--CIDVCPTGAITRDANGVVMINKKLCVGCLMCVGFCPEGAMFKHEDYPEPFKCIACG---------ICVKACP 117


                 ....*
gi 409105620 155 TGALE 159
Cdd:cd16372  118 TGALE 122
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 2-118 5.94e-10

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: 55.87  E-value: 5.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620   2 AKTKGYLVDTTKCIACRGCVVACkqwnqlPAEQTRFTGSYQTVPDLTGNTftiisfhEYEEDGrirwyfakrqCMHCLep 81
Cdd:cd10549   30 AIARGPEIDEDKCVFCGACVEVC------PTGAIELTPEGKEYVPKEKEA-------EIDEEK----------CIGCG-- 84

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 409105620  82 VCMKVCPQKAISITDTGAVVRDNDKCVGCQYCAAACP 118
Cdd:cd10549   85 LCVKVCPVDAITLEDELEIVIDKEKCIGCGICAEVCP 121
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 64-120 8.66e-10

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 53.90  E-value: 8.66e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 409105620  64 GRIRWYFAKRQCMHClePVCMKVCPQKAISITDTGAVVrDNDKCVGCQYCAAACPFH 120
Cdd:COG2221    6 GTWPPKIDEEKCIGC--GLCVAVCPTGAISLDDGKLVI-DEEKCIGCGACIRVCPTG 59
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
82-120 1.78e-09

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 53.20  E-value: 1.78e-09
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 409105620  82 VCMKVCPQKAISITDTGAVVrDNDKCVGCQYCAAACPFH 120
Cdd:COG2768   18 ACVKVCPVGAISIEDGKAVI-DPEKCIGCGACIEVCPVG 55
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
80-165 4.92e-09

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 55.45  E-value: 4.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  80 EPVCMKVCP----QKAISITDTGAVVRDNDKCVGCQYCAAACPFHI-PRYNPTTDKEtkCSLCAertaegdlpACVKACI 154
Cdd:COG0348  181 RQWCRYLCPygafQGLLSDLSTLRVRYDRGDCIDCGLCVKVCPMGIdIRKGEINQSE--CINCG---------RCIDACP 249

                         90
                 ....*....|.
gi 409105620 155 TGALEYGNRDE 165
Cdd:COG0348  250 KDAIRFSSRGE 260
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 75-120 3.13e-08

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: 50.05  E-value: 3.13e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 409105620  75 CMHCLepVCMKVCPQKAISITDTGAVVRDNDKCVGCQYCAAACPFH 120
Cdd:COG1144   32 CIGCG--LCWIVCPDGAIRVDDGKYYGIDYDYCKGCGICAEVCPVK 75
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 83-160 3.21e-08

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 50.86  E-value: 3.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  83 CMKVCPQKAISITDTGAVVR----DNDKCVGCQYCAAACPFHIPRYnpTTDKETKCSLCAERTAEGDLP----ACVKACI 154
Cdd:cd10549   14 CVKACPTDAIELGPNGAIARgpeiDEDKCVFCGACVEVCPTGAIEL--TPEGKEYVPKEKEAEIDEEKCigcgLCVKVCP 91


                 ....*.
gi 409105620 155 TGALEY 160
Cdd:cd10549   92 VDAITL 97
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 75-120 7.03e-08

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 48.57  E-value: 7.03e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 409105620  75 CMHCLepVCMKVCPQKAISITDTGAVVRDNDKCVGCQYCAAACPFH 120
Cdd:COG1149   13 CIGCG--LCVEVCPEGAIKLDDGGAPVVDPDLCTGCGACVGVCPTG 56
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 75-120 1.06e-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: 45.12  E-value: 1.06e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 409105620  75 CMHCLepVCMKVCPQKAISITDTGAVVR---DNDKCVGCQYCAAACPFH 120
Cdd:COG1143    4 CIGCG--LCVRVCPVDAITIEDGEPGKVyviDPDKCIGCGLCVEVCPTG 50
NapF COG1145
Ferredoxin [Energy production and conversion];
44-120 1.39e-06

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 48.18  E-value: 1.39e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 409105620  44 VPDLTGNTFTIISFHEYEEDGRIRWYFAKRQCMHCLepVCMKVCPQKAISITDTGAVVR-DNDKCVGCQYCAAACPFH 120
Cdd:COG1145  153 VDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCG--LCVKVCPTGAIRLKDGKPQIVvDPDKCIGCGACVKVCPVG 228
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
72-160 1.43e-06

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 48.87  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409105620  72 KRQCMHCLEPVCMKVCPQKAIsITDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDK--ETKCSLCAertaegdlpAC 149
Cdd:COG4624   59 CCCCRCCVAISCIQVRGIIII-DKRGPSIIRDKEKCKNCYPCVRACPVKAIKVDDGKAEidEEKCISCG---------QC 128

                         90
                 ....*....|.
gi 409105620 150 VKACITGALEY 160
Cdd:COG4624  129 VAVCPFGAITE 139
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
75-143 2.90e-06

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 47.24  E-value: 2.90e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 409105620  75 CMHCLepVCMKVCPQKAISITDTGAVVrDNDKCVGCQYCAAACPFHIPRYNPTTDKETKCSLCAERTAE 143
Cdd:PRK07118 215 CIGCG--KCVKACPAGAITMENNLAVI-DQEKCTSCGKCVEKCPTKAIRILNKPPKVKEPKKAAAEAAA 280
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
75-118 3.23e-06

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 47.93  E-value: 3.23e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 409105620  75 CMHCLepVCMKVCPQKAISITDTGAVVRDNDKCVGCQYCAAACP 118
Cdd:COG1148  498 CTGCG--RCVEVCPYGAISIDEKGVAEVNPALCKGCGTCAAACP 539
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 83-120 3.79e-06

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 43.88  E-value: 3.79e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 409105620  83 CMKVCPQKAISITDTGAVVrDNDKCVGCQYCAAACPFH 120
Cdd:COG4231   30 CVKVCPADAIEEGDGKAVI-DPDLCIGCGSCVQVCPVD 66
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
74-118 6.42e-06

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 44.17  E-value: 6.42e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 409105620  74 QCMHCLepVCMKVCPQKAISITDTGAVVRDNDKCVGCQYCAAACP 118
Cdd:PRK09623  52 KCVKCY--ICWKFCPEPAIYIKEDGYVAIDYDYCKGCGICANECP 94
porD PRK09624
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
 70-118 9.51e-06

pyruvate ferredoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 170017 [Multi-domain]  Cd Length: 105  Bit Score: 43.48  E-value: 9.51e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 409105620  70 FAKRQCMHCLepVCMKVCPQKAISITDTGAVVRDNDKCVGCQYCAAACP 118
Cdd:PRK09624  48 FNRDKCVRCY--LCYIYCPEPAIYLDEEGYPVFDYDYCKGCGICANECP 94
PRK13795 PRK13795
hypothetical protein; Provisional
 75-118 1.07e-05

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 46.14  E-value: 1.07e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 409105620  75 CMHCLepVCMKVCPQKAISITD-TGAVVRDNDKCVGCQYCAAACP 118
Cdd:PRK13795 583 CVGCG--VCVGACPTGAIRIEEgKRKISVDEEKCIHCGKCTEVCP 625
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 83-121 1.10e-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: 45.37  E-value: 1.10e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 409105620  83 CMKVCPQKAISITDTGAVVRDNDKCVGCQYCAAACPFHI 121
Cdd:COG2878  145 CIKACPFDAIVGAAKGMHTVDEDKCTGCGLCVEACPVDC 183
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 71-120 1.13e-05

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 46.02  E-value: 1.13e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 409105620  71 AKRqCMHCLEPV----CMKVCPQKAISITDTGAVVR-DNDKCVGCQYCAAACPFH 120
Cdd:PRK12771 503 AAR-CLSCGNCFecdnCYGACPQDAIIKLGPGRRYHfDYDKCTGCHICADVCPCG 556
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 82-118 1.37e-05

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 42.00  E-value: 1.37e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 409105620  82 VCMKVCPQKAISITDTG--AVVRDNDKCVGCQYCAAACP 118
Cdd:COG1146   15 ACVEVCPVDVLELDEEGkkALVINPEECIGCGACELVCP 53
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 98-168 1.99e-05

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 42.90  E-value: 1.99e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 409105620  98 GAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDK----ETKCSLCAErtaegdlpaCVKACITGALEYgNRDELLA 168
Cdd:PRK08348  35 GKILYDVDKCVGCRMCVTVCPAGVFVYLPEIRKvalwTGRCVFCGQ---------CVDVCPTGALQM-SDDFLLA 99
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 75-119 6.69e-05

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 39.82  E-value: 6.69e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 409105620   75 CMHCLepVCMKVCPQKAISITD------TGAVVRDNDKCVGCQYCAAACPF 119
Cdd:pfam12838   1 CIGCG--ACVAACPVGAITLDEvgekkgTKTVVIDPERCVGCGACVAVCPT 49
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 103-174 7.14e-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: 41.61  E-value: 7.14e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 409105620 103 DNDKCVGCQYCAAACPFHIPRYNPTTDK-------ETKCSLCAertaegdlpACVKACITGALEYGNRDELLAKAKERV 174
Cdd:cd10549    4 DPEKCIGCGICVKACPTDAIELGPNGAIargpeidEDKCVFCG---------ACVEVCPTGAIELTPEGKEYVPKEKEA 73
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
83-121 1.00e-04

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 42.61  E-value: 1.00e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 409105620  83 CMKVCPQKAISITDTGAVVrDNDKCVGCQYCAAACPFHI 121
Cdd:PRK07118 147 CVAACPFDAIHIENGLPVV-DEDKCTGCGACVKACPRNV 184
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 75-118 1.21e-04

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


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 39.16  E-value: 1.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 409105620   75 CMHCLEpvCMKVCPQKAIS------ITDTGAVVRDNDKCVGCQYCAAACP 118
Cdd:pfam13237   9 CIGCGR--CTAACPAGLTRvgaiveRLEGEAVRIGVWKCIGCGACVEACP 56
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 71-118 4.13e-04

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: 39.93  E-value: 4.13e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 409105620  71 AKRQCMHCLepVCMKVCPQKAISITDTGAVVR---DNDKCVGCQYCAAACP 118
Cdd:cd16373   95 AWQGGTDCG--VCVEACPTEAIAIVLEDDVLRpvvDEDKCVGCGLCEYVCP 143
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 93-162 4.30e-04

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 37.72  E-value: 4.30e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 409105620  93 SITDTGAVVRDNDKCVGCQYCAAACPFHIPRYN---PTTDKEtKCSLCAertaegdlpACVKACITGALEYGN 162
Cdd:COG2221    3 GIIGTWPPKIDEEKCIGCGLCVAVCPTGAISLDdgkLVIDEE-KCIGCG---------ACIRVCPTGAIKGEK 65
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 103-165 4.76e-04

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 37.79  E-value: 4.76e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 409105620 103 DNDKCVGCQYCAAACPFH----IPRYNPTTDKEtKCSLCAertaegdlpACVKACITGALEYGNRDE 165
Cdd:COG1149    9 DEEKCIGCGLCVEVCPEGaiklDDGGAPVVDPD-LCTGCG---------ACVGVCPTGAITLEEREA 65
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
97-159 1.04e-03

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 37.02  E-value: 1.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 409105620  97 TGAVVRDNDKCVGCQYCAAACPFH---IPRYNPTTDKEtKCSLCaertaegdlPACVKACITGALE 159
Cdd:COG2768    3 LGKPYVDEEKCIGCGACVKVCPVGaisIEDGKAVIDPE-KCIGC---------GACIEVCPVGAIK 58
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
83-119 1.75e-03

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 39.41  E-value: 1.75e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 409105620  83 CMKVCP-----QKAISI-TDTGAVVRDNDKCVGCQYCAAACPF 119
Cdd:PRK13409  21 CIKYCPvvrtgEETIEIdEDDGKPVISEELCIGCGICVKKCPF 63
Fer4_9 pfam13187
4Fe-4S dicluster domain;
83-121 2.64e-03

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 35.22  E-value: 2.64e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 409105620   83 CMKVCPQKAISITDTG---AVVRDNDKCVGCQYCAAACPFHI 121
Cdd:pfam13187   8 CVAACPAGAIVPDLVGqtiRGDIAGLACIGCGACVDACPRGA 49
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
99-172 3.08e-03

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 38.69  E-value: 3.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 409105620  99 AVVrDNDKCVGCQYCAAACPFHIPRYNPTTD---KETKCSLCAertaegdlpACVKACITGALEYGN--RDELLAKAKE 172
Cdd:COG1148  491 AEV-DPEKCTGCGRCVEVCPYGAISIDEKGVaevNPALCKGCG---------TCAAACPSGAISLKGftDDQILAQIDA 559
RNAP_D cd07030
D subunit of Archaeal RNA polymerase; The D subunit of archaeal RNA polymerase (RNAP) is ...
 104-159 3.18e-03

D subunit of Archaeal RNA polymerase; The D subunit of archaeal RNA polymerase (RNAP) is involved in the assembly of RNAP subunits. RNAP is a large multi-subunit complex responsible for the synthesis of RNA. It is the principal enzyme of the transcription process, and is a final target in many regulatory pathways that control gene expression in all living cells. A single distinct RNAP complex is found in archaea, which may be responsible for the synthesis of all RNAs. The archaeal RNAP harbors homologues of all eukaryotic RNAP II subunits with two exceptions (RPB8 and RPB9). The 12 archaeal subunits are designated by letters and can be divided into three functional groups that are engaged in: (I) catalysis (A'/A", B'/B" or B); (II) assembly (L, N, D and P); and (III) auxiliary functions (F, E, H and K). The D subunit is equivalent to the RPB3 subunit of eukaryotic RNAP II. It contains two subdomains: one subdomain is similar the eukaryotic Rpb11/AC19/archaeal L subunit which is involved in dimerization, and the other is an inserted beta sheet subdomain. The assembly of the two largest archaeal RNAP subunits that provide most of the enzyme's catalytic functions depends on the presence of the archaeal D/L heterodimer.


Pssm-ID: 132908 [Multi-domain]  Cd Length: 259  Bit Score: 38.02  E-value: 3.18e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 409105620 104 NDKCVGCQYCAAACP---FHIPRYNPTTDKETKCSLCAErtaegdlpaCVKACITGALE 159
Cdd:cd07030  168 DEDCDGCGKCVEECPrgvLELEEGKVVVEDLEDCSLCKL---------CERACDAGAIR 217
NapF COG1145
Ferredoxin [Energy production and conversion];
90-164 3.91e-03

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 37.78  E-value: 3.91e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 409105620  90 KAISITDTGAVVRDNDKCVGCQYCAAACPFHIPRYNPTTDK----ETKCSLCaertaegdlPACVKACITGALEYGNRD 164
Cdd:COG1145  167 ELKIAIKKAKAVIDAEKCIGCGLCVKVCPTGAIRLKDGKPQivvdPDKCIGC---------GACVKVCPVGAISLEPKE 236
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 100-160 6.17e-03

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 34.69  E-value: 6.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 409105620 100 VVRDNDKCVGCQYCAAACP---FHIP--RYNPTTDKETKCSLCAertaegdlpACVKACITGALEY 160
Cdd:COG1146    3 PVIDTDKCIGCGACVEVCPvdvLELDeeGKKALVINPEECIGCG---------ACELVCPVGAITV 59
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 105-164 6.62e-03

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: 34.34  E-value: 6.62e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 409105620 105 DKCVGCQYCAAACPFHIPRYNPTTDKET------KCSLCAertaegdlpACVKACITGALEYGNRD 164
Cdd:COG1143    2 DKCIGCGLCVRVCPVDAITIEDGEPGKVyvidpdKCIGCG---------LCVEVCPTGAISMTPFE 58
 
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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