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Conserved domains on  [gi|304997|gb|AAB03026|]
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formate dehydrogenase-O beta subunit [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FDH-beta super family cl36936
formate dehydrogenase, beta subunit, Fe-S containing; This model represents the beta subunit ...
 7-288 1.61e-164

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]


The actual alignment was detected with superfamily member TIGR01582:

Pssm-ID: 273705 [Multi-domain]  Cd Length: 283  Bit Score: 458.22  E-value: 1.61e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997       7 DIIRRSATNGltPAPQARDFQEEVAKLIDVTTCIGCKACQVACSEWNDIRDTVGN-NIGVYDNPNDLSAKSWTVMRFSEV 85
Cdd:TIGR01582   1 DIKRLSATKE--PDPSVKTYPTELAKLIDVSSCIGCKACQAACQEWNDTTPPILSrKVGGYQNPPDLLPETFTLMRFKEG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997      86 EQNDKLEWLIRKDGCMHCSDPGCLKACPAEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVD 165
Cdd:TIGR01582  79 EESDGLEWLIRKDGCMHCREPGCLKACPAPGAIIQYQNGIVDFDHSKCIGCGYCIVGCPFNIPRYDKVDNRPYKCTLCID 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997     166 RVVVGQEPACVKTCPTGAIHFGTKESMKTLASERVAELKTRGYDNAGLYDPAGVGGTHVMYVLHHADKPNLYHGLPENPE 245
Cdd:TIGR01582 159 RVSVGQEPACVKTCPTNAISFGFKEDMKERAEKRVADLKSRGYPNAGLYDPPGVGGTHVMYVLHHGDKPKDYQDLPEDPR 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 304997     246 ISETVKFWKGIWKPLAAVGFAATFAASIFHYVGVGPNRADEEE 288
Cdd:TIGR01582 239 IDASVGLWKGVLKTIGSIAMGGTALGVFLHLILWGPNKVLGGK 281
 
Name Accession Description Interval E-value
FDH-beta TIGR01582
formate dehydrogenase, beta subunit, Fe-S containing; This model represents the beta subunit ...
 7-288 1.61e-164

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: 458.22  E-value: 1.61e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997       7 DIIRRSATNGltPAPQARDFQEEVAKLIDVTTCIGCKACQVACSEWNDIRDTVGN-NIGVYDNPNDLSAKSWTVMRFSEV 85
Cdd:TIGR01582   1 DIKRLSATKE--PDPSVKTYPTELAKLIDVSSCIGCKACQAACQEWNDTTPPILSrKVGGYQNPPDLLPETFTLMRFKEG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997      86 EQNDKLEWLIRKDGCMHCSDPGCLKACPAEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVD 165
Cdd:TIGR01582  79 EESDGLEWLIRKDGCMHCREPGCLKACPAPGAIIQYQNGIVDFDHSKCIGCGYCIVGCPFNIPRYDKVDNRPYKCTLCID 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997     166 RVVVGQEPACVKTCPTGAIHFGTKESMKTLASERVAELKTRGYDNAGLYDPAGVGGTHVMYVLHHADKPNLYHGLPENPE 245
Cdd:TIGR01582 159 RVSVGQEPACVKTCPTNAISFGFKEDMKERAEKRVADLKSRGYPNAGLYDPPGVGGTHVMYVLHHGDKPKDYQDLPEDPR 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 304997     246 ISETVKFWKGIWKPLAAVGFAATFAASIFHYVGVGPNRADEEE 288
Cdd:TIGR01582 239 IDASVGLWKGVLKTIGSIAMGGTALGVFLHLILWGPNKVLGGK 281
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 31-238 6.59e-150

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: 418.33  E-value: 6.59e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    31 AKLIDVTTCIGCKACQVACSEWNDIRDTVGNNIGVYDNPNDLSAKSWTVMRFSEVEQNDKLEWLIRKDGCMHCSDPGCLK 110
Cdd:cd10558   1 AKLIDVSKCIGCKACQVACKEWNDLRAEVGHNVGTYQNPADLSPETWTLMKFREVEDNGKLEWLIRKDGCMHCADPGCLK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997   111 ACPAEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVDRVVVGQEPACVKTCPTGAIHFGTKE 190
Cdd:cd10558  81 ACPSPGAIVQYANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVGLEPACVKTCPTGALHFGTKE 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 304997   191 SMKTLASERVAELKTRGYDNAGLYDPAGVGGTHVMYVLHHADKPNLYH 238
Cdd:cd10558 161 DMLALAEKRVAALKERGYTNAGLYDPKGVGGTHVMYVLHHADKPEGYP 208
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 31-227 1.22e-70

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 216.35  E-value: 1.22e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    31 AKLIDVTTCIGCKACQVACSEWNDIRDTVgnnigvydnpndlsakSWTVMRFSEVEQNDKLEWLIRKDGCMHCSDPGCLK 110
Cdd:COG0437   7 GMVIDLTKCIGCRACVVACKEENNLPVGV----------------TWRRVRRYEEGEFPNVEWLFVPVLCNHCDDPPCVK 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997   111 ACPAeGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVDRVVVGQEPACVKTCPTGAIHFGTKE 190
Cdd:COG0437  71 VCPT-GATYKREDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVEACPTGALVFGDLD 149

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 304997   191 SMKTLASERVAELKTRgydnaGLYDPAGvGGTHVMYV 227
Cdd:COG0437 150 DPESEVSKRLAELPAY-----RLLPELG-TKPSVYYL 180
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
13-300 1.43e-46

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 159.45  E-value: 1.43e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997     13 ATNGLTPAPQARD------FQEEVAKLIDVTTCIGCKACQVACSEWNDI-RDTVGNniGVYDNPNDLSAKSWTVM---RF 82
Cdd:PRK10882  15 LLAGALPSVSHAAaenrppIPGALGMLYDSTLCVGCQACVTKCQEINFPeRNPQGE--QTWDNPDKLSPYTNNIIkvwKS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997     83 SEVEQNDKLE--WLIRKDGCMHCSDPGCLKACPAEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPED--NRVY 158
Cdd:PRK10882  93 GTGVNKDQEEngYAYIKKQCMHCVDPNCVSVCPVSALTKDPKTGIVHYDKDVCTGCRYCMVACPFNVPKYDYNNpfGAIH 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    159 KCTLC----VDRVVVGQEPACVKTCPTGAIHFGTKESMKTLASERVAE-------------------LKTRGYDNAGLYD 215
Cdd:PRK10882 173 KCELCnqkgVERLDKGGLPGCVEVCPTGAVIFGTREELLAEAKRRLALkpgseyhyprqtlksgdtyLHTVPKYYPHVYG 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    216 PAGVGGTHVMYvLHHADKPNLyhGLPE-----NPEISETVK--FWKGIWKPLAAVGFAATFAASifhyvgvgpNRADEEe 288
Cdd:PRK10882 253 EKEGGGTQVLV-LSGVPFENL--GLPKlddlsTGARSEHIQhtLYKGMILPLAVLAGLTVLVRR---------NTKNDH- 319

                        330
                 ....*....|..
gi 304997    289 nnlHEEKDEERK 300
Cdd:PRK10882 320 ---HDGGDDHES 328
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 91-187 2.67e-29

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: 107.33  E-value: 2.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997      91 LEWLIRKDGCMHCSDPGCLKACPAeGAIIQ-YANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVDRVVV 169
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPV-GAIYKdEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEA 79

                          90
                  ....*....|....*...
gi 304997     170 GQEPACVKTCPTGAIHFG 187
Cdd:pfam13247  80 GLLPACVQTCPTGAMNFG 97
FDH3_beta NF038355
formate dehydrogenase FDH3 subunit beta; Members of this family are the beta subunit of the ...
 33-208 5.48e-22

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: 90.51  E-value: 5.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997     33 LIDVTTCIGCKACQVACSEWNDIrdtvgnnigvydnpndlsakSWTVMRFSEVEQNDKLEWLIRKD-GCMHCSDPGCLKA 111
Cdd:NF038355   6 LCDTERCIECNGCVVACKNAHEL--------------------PWGINRRRVVTLNDGVPGEKSISvACMHCTDAPCAAV 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    112 CPAEgAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLnPEDN------RVYKCTLC-----------------VDRVV 168
Cdd:NF038355  66 CPVD-CFYIRADGIVLHDKDKCIGCGYCLYACPFGAPQF-PKDGafgargKMDKCTFCaggpeetnseaerekygQNRIA 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 304997    169 VGQEPACVKTCPTGAIHFGTKESMKTLASERVAelkTRGY 208
Cdd:NF038355 144 EGKLPLCAEMCSTKALLAGDAEVVADIYRERVV---ARGA 180
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 130-189 2.02e-05

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 44.85  E-value: 2.02e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 304997    130 SEQCIGCGYCIAGCPFDIPRLnpEDNRVY---KCTLCVdrvvvgqepACVKTCPTGAIHFGTK 189
Cdd:NF038196 184 TDKCIGCGICAKVCPVNNIEM--EDGKPVwghNCTHCL---------ACIHRCPKEAIEYGKK 235
 
Name Accession Description Interval E-value
FDH-beta TIGR01582
formate dehydrogenase, beta subunit, Fe-S containing; This model represents the beta subunit ...
 7-288 1.61e-164

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: 458.22  E-value: 1.61e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997       7 DIIRRSATNGltPAPQARDFQEEVAKLIDVTTCIGCKACQVACSEWNDIRDTVGN-NIGVYDNPNDLSAKSWTVMRFSEV 85
Cdd:TIGR01582   1 DIKRLSATKE--PDPSVKTYPTELAKLIDVSSCIGCKACQAACQEWNDTTPPILSrKVGGYQNPPDLLPETFTLMRFKEG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997      86 EQNDKLEWLIRKDGCMHCSDPGCLKACPAEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVD 165
Cdd:TIGR01582  79 EESDGLEWLIRKDGCMHCREPGCLKACPAPGAIIQYQNGIVDFDHSKCIGCGYCIVGCPFNIPRYDKVDNRPYKCTLCID 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997     166 RVVVGQEPACVKTCPTGAIHFGTKESMKTLASERVAELKTRGYDNAGLYDPAGVGGTHVMYVLHHADKPNLYHGLPENPE 245
Cdd:TIGR01582 159 RVSVGQEPACVKTCPTNAISFGFKEDMKERAEKRVADLKSRGYPNAGLYDPPGVGGTHVMYVLHHGDKPKDYQDLPEDPR 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 304997     246 ISETVKFWKGIWKPLAAVGFAATFAASIFHYVGVGPNRADEEE 288
Cdd:TIGR01582 239 IDASVGLWKGVLKTIGSIAMGGTALGVFLHLILWGPNKVLGGK 281
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 31-238 6.59e-150

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: 418.33  E-value: 6.59e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    31 AKLIDVTTCIGCKACQVACSEWNDIRDTVGNNIGVYDNPNDLSAKSWTVMRFSEVEQNDKLEWLIRKDGCMHCSDPGCLK 110
Cdd:cd10558   1 AKLIDVSKCIGCKACQVACKEWNDLRAEVGHNVGTYQNPADLSPETWTLMKFREVEDNGKLEWLIRKDGCMHCADPGCLK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997   111 ACPAEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVDRVVVGQEPACVKTCPTGAIHFGTKE 190
Cdd:cd10558  81 ACPSPGAIVQYANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVGLEPACVKTCPTGALHFGTKE 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 304997   191 SMKTLASERVAELKTRGYDNAGLYDPAGVGGTHVMYVLHHADKPNLYH 238
Cdd:cd10558 161 DMLALAEKRVAALKERGYTNAGLYDPKGVGGTHVMYVLHHADKPEGYP 208
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 32-187 2.36e-86

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: 255.40  E-value: 2.36e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    32 KLIDVTTCIGCKACQVACSEWNDIRDTVGNNIGVYDNPNDLSAKSWTVMRFSEVEQND-KLEWLIRKDGCMHCSDPGCLK 110
Cdd:cd16366   1 FLVDTSRCTGCRACQVACKQWNGLPAEKTEFTGSYQNPPDLTAHTWTLVRFYEVEKPGgDLSWLFRKDQCMHCTDAGCLA 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 304997   111 ACPAeGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVDRVVVGQEPACVKTCPTGAIHFG 187
Cdd:cd16366  81 ACPT-GAIIRTETGTVVVDPETCIGCGYCVNACPFDIPRFDEETGRVAKCTLCYDRISNGLQPACVKTCPTGALTFG 156
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 33-245 7.06e-79

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: 238.82  E-value: 7.06e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    33 LIDVTTCIGCKACQVACSEWNDIRDTVGNNIG-VYDNPNDLSAKSWTVMRFSEVEQNDK-------LEWLIRKDGCMHCS 104
Cdd:cd10560   3 FTDTSICIGCKACEVACKQWNQLPADGYDFSGmSYDNTGDLSASTWRHVKFIERPTEDGpaneggdLQWLFMSDVCKHCT 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997   105 DPGCLKACPAeGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVDRVVVGQEPACVKTCPTGAI 184
Cdd:cd10560  83 DAGCLEACPT-GAIFRTEFGTVYIQPDICNGCGYCVAACPFGVIDRNEETGRAHKCTLCYDRLKDGLEPACAKACPTGSI 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 304997   185 HFGTKESMKTLASERVAELKTRGYDNAGLY--DP-AGVGGTHVMYVLhhADKPNLYhGLPENPE 245
Cdd:cd10560 162 QFGPLEELRERARARVEQLHEQGVVEAYLYgaDPtEGYGGLNAFFLL--LDKPEVY-GLPADPL 222
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 32-192 8.89e-75

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: 226.03  E-value: 8.89e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    32 KLIDVTTCIGCKACQVACSEWNDIRDTVGNNIGVYDNPNDLSAKSWTVMRFSEVE-QNDKLEWLIRKDGCMHCSDPGCLK 110
Cdd:cd10562   1 MLVDTSKCTACRGCQVACKQWNQLPAEKTPFTGSYQNPPDLTPNTWTLIRFYEHEeDNGGIRWLFRKRQCMHCTDAACVK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997   111 ACPaEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVDRVVVGQEPACVKTCPTGAIHFGTKE 190
Cdd:cd10562  81 VCP-TGALYKTENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCFDRIENGMQPACVKTCPTGALTFGDRD 159


                ..
gi 304997   191 SM 192
Cdd:cd10562 160 EL 161
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 31-227 1.22e-70

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 216.35  E-value: 1.22e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    31 AKLIDVTTCIGCKACQVACSEWNDIRDTVgnnigvydnpndlsakSWTVMRFSEVEQNDKLEWLIRKDGCMHCSDPGCLK 110
Cdd:COG0437   7 GMVIDLTKCIGCRACVVACKEENNLPVGV----------------TWRRVRRYEEGEFPNVEWLFVPVLCNHCDDPPCVK 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997   111 ACPAeGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVDRVVVGQEPACVKTCPTGAIHFGTKE 190
Cdd:COG0437  71 VCPT-GATYKREDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVEACPTGALVFGDLD 149

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 304997   191 SMKTLASERVAELKTRgydnaGLYDPAGvGGTHVMYV 227
Cdd:COG0437 150 DPESEVSKRLAELPAY-----RLLPELG-TKPSVYYL 180
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 31-226 7.93e-66

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: 204.75  E-value: 7.93e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    31 AKLIDVTTCIGCKACQVACSEWNDIRDTVGNNIGVYDNPNDLSAKSWTVMRFSEVEqNDKLEWLIRKDGCMHCSDPGCLK 110
Cdd:cd10561   1 GVLYDTTRCIGCRACEVACKEWNGLPAEDTAFGPGWDNPRDLSAKTYTVIKRYEVE-TGGKGFVFVKRQCMHCLDPACVS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997   111 ACPAeGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPR-----LNPednRVYKCTLCVDRVVVGQEPACVKTCPTGAIH 185
Cdd:cd10561  80 ACPV-GALRKTPEGPVTYDEDKCIGCRYCMVACPFNIPKyewdsANP---KIRKCTMCYDRLKEGKQPACVEACPTGALL 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 304997   186 FGTKESMKTLASERVAELKTRGYDNA-GLYDpagVGGTHVMY 226
Cdd:cd10561 156 FGKREELLAEAKRRIAANPGRYVDHVyGEKE---AGGTSVLY 194
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 33-230 7.54e-64

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: 199.58  E-value: 7.54e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    33 LIDVTTCIGCKACQVACSEWNDIRDTVGNNIGVYDNPNDLSAKSWTVMRFSEVE-QNDKLEWLIRKDGCMHCSDPGCLKA 111
Cdd:cd10559   3 LIDTTRCTACRGCQVACKQWNQLPAEQTKNTGSHQNPPDLSANTYKLVRFNEVRnENGKPDWLFFPDQCRHCVTPPCKDA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997   112 CP-AEGAIIQ-YANGIVDFQSEQCIGC-GYCIAGCPFDIPRLNPEDNRVYKCTLCVDRVVVGQEPACVKTCPTGAIHFGT 188
Cdd:cd10559  83 ADmVPGAVIQdEATGAVVFTEKTAELDfDDVLSACPYNIPRKNEATGRIVKCDMCIDRVSNGLQPACVKACPTGAMNFGD 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 304997   189 KESMKTLASERVAELKTRgYDNAGLYDPAGVggtHVMYVLHH 230
Cdd:cd10559 163 RDEMLAMASKRLEELKKR-YPKANLYDPDDV---RVIWLLAE 200
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 33-187 1.00e-49

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


Pssm-ID: 319870 [Multi-domain]  Cd Length: 136  Bit Score: 161.40  E-value: 1.00e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    33 LIDVTTCIGCKACQVACSEWNDIRdtvgnnigvydnpndlSAKSWTVMRFSEVEqndKLEWLIRKDGCMHCSDPGCLKAC 112
Cdd:cd04410   2 VVDLDRCIGCGTCEVACKQEHGLR----------------PGPDWSRIKVIEGG---GLERAFLPVSCMHCEDPPCVKAC 62

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 304997   113 PaEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVDRVVVGQEPACVKTCPTGAIHFG 187
Cdd:cd04410  63 P-TGAIYKDEDGIVLIDEDKCIGCGSCVEACPYGAIVFDPEPGKAVKCDLCGDRLDEGLEPACVKACPTGALTFG 136
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 33-187 1.15e-48

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: 158.88  E-value: 1.15e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    33 LIDVTTCIGCKACQVACSEWNDIRDTVgnnigvydnpndlsakswtvmRFSEVEQNDKLEWLIRKD-----GCMHCSDPG 107
Cdd:cd16371   3 YFDQERCIGCKACEIACKDKNDLPPGV---------------------NWRRVYEYEGGEFPEVFAyflsmSCNHCENPA 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997   108 CLKACPAeGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVDRVVVGQEPACVKTCPTGAIHFG 187
Cdd:cd16371  62 CVKVCPT-GAITKREDGIVVVDQDKCIGCGYCVWACPYGAPQYNPETGKMDKCDMCVDRLDEGEKPACVAACPTRALDFG 140
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
13-300 1.43e-46

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 159.45  E-value: 1.43e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997     13 ATNGLTPAPQARD------FQEEVAKLIDVTTCIGCKACQVACSEWNDI-RDTVGNniGVYDNPNDLSAKSWTVM---RF 82
Cdd:PRK10882  15 LLAGALPSVSHAAaenrppIPGALGMLYDSTLCVGCQACVTKCQEINFPeRNPQGE--QTWDNPDKLSPYTNNIIkvwKS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997     83 SEVEQNDKLE--WLIRKDGCMHCSDPGCLKACPAEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPED--NRVY 158
Cdd:PRK10882  93 GTGVNKDQEEngYAYIKKQCMHCVDPNCVSVCPVSALTKDPKTGIVHYDKDVCTGCRYCMVACPFNVPKYDYNNpfGAIH 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    159 KCTLC----VDRVVVGQEPACVKTCPTGAIHFGTKESMKTLASERVAE-------------------LKTRGYDNAGLYD 215
Cdd:PRK10882 173 KCELCnqkgVERLDKGGLPGCVEVCPTGAVIFGTREELLAEAKRRLALkpgseyhyprqtlksgdtyLHTVPKYYPHVYG 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    216 PAGVGGTHVMYvLHHADKPNLyhGLPE-----NPEISETVK--FWKGIWKPLAAVGFAATFAASifhyvgvgpNRADEEe 288
Cdd:PRK10882 253 EKEGGGTQVLV-LSGVPFENL--GLPKlddlsTGARSEHIQhtLYKGMILPLAVLAGLTVLVRR---------NTKNDH- 319

                        330
                 ....*....|..
gi 304997    289 nnlHEEKDEERK 300
Cdd:PRK10882 320 ---HDGGDDHES 328
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 33-187 3.55e-43

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: 146.14  E-value: 3.55e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    33 LIDVTTCIGCKACQVACSEWNDIRDtvgnniGVYdnpndlsaksWTVMRFSEVEQNDKLEWLIRKDGCMHCSDPGCLKAC 112
Cdd:cd10551   2 VIDLRKCIGCGACVVACKAENNVPP------GVF----------RNRVLEYEVGEYPNVKRTFLPVLCNHCENPPCVKVC 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997   113 PAeGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVY------------KCTLCVDRVVVGQEPACVKTCP 180
Cdd:cd10551  66 PT-GATYKREDGIVLVDYDKCIGCRYCMAACPYGARYFNPEEPHEFgevpvrpkgvveKCTFCYHRLDEGLLPACVEACP 144


                ....*..
gi 304997   181 TGAIHFG 187
Cdd:cd10551 145 TGARIFG 151
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 33-191 3.17e-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: 123.92  E-value: 3.17e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    33 LIDVTTCIGCKACQVACSEWNDIRdtvgNNIGVYDNPNDLSAKswtvMRfseveqndklewlirkdgCMHCSDPGCLKAC 112
Cdd:cd16374   2 YVDPERCIGCRACEIACAREHSGK----PRISVEVVEDLASVP----VR------------------CRHCEDAPCMEVC 55

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 304997   113 PaEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVDRVVVGQEPACVKTCPTGAIHFGTKES 191
Cdd:cd16374  56 P-TGAIYRDEDGAVLVDPDKCIGCGMCAMACPFGVPRFDPSLKVAVKCDLCIDRRREGKLPACVEACPTGALKFGDIEE 133
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 34-192 5.31e-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: 122.11  E-value: 5.31e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    34 IDVTTCIGCKACQVACSEWNDIRDTvgNNIGVYDNPNDLSAKSWTVMrfseveqndklewlirkdgCMHCSDPGCLKACP 113
Cdd:cd16369   6 IDPSRCIGCRACVAACRECGTHRGK--SMIHVDYIDRGESTQTAPTV-------------------CMHCEDPTCAEVCP 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997   114 AEgAIIQYANGIV-DFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVDRVVVGQEPACVKTCPTGAIHFGTKESM 192
Cdd:cd16369  65 AD-AIKVTEDGVVqSALKPRCIGCSNCVNACPFGVPKYDEERNLMMKCDMCYDRTSVGKAPMCASVCPSGALFYGTREEI 143
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 35-188 1.35e-33

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: 120.16  E-value: 1.35e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    35 DVTTCIGCKACQVACSEWNdirdtvgnNIGVYDNPNDLSAKSwtvmrFSEVEQNDKLEWLIRKdgCMHCSDPGCLKACPA 114
Cdd:cd10553   8 DSKRCIGCLACEVHCKVKN--------NLPVGPRLCRIFAVG-----PKMVGGKPRLKFVYMS--CFHCENPWCVKACPT 72

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 304997   115 eGAIIQY-ANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVDRVVVGQEPACVKTCPTGAIHFGT 188
Cdd:cd10553  73 -GAMQKReKDGIVYVDQELCIGCKACIEACPWGIPQWNPATGKVVKCDYCMDRIDQGLKPACVTGCTTHALSFVR 146
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 30-196 6.98e-30

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


Pssm-ID: 319890 [Multi-domain]  Cd Length: 200  Bit Score: 112.13  E-value: 6.98e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    30 VAKLIDVTTCIGCK-----ACQVACSEWNDIR--DTVGNNIGVY-------------DNPNDLSAKSWTVMRFSEVEQND 89
Cdd:cd16368   1 LATLIDLTKCDGCPgesipACVRACREKNQARfpEPVSKPIQPYwprkriedwsdkrDVTDRLTPYNWLYVQKLTVDTAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    90 KLEWLIRKDGCMHCSDPGCLKACPAeGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPR----------LNPE---DNR 156
Cdd:cd16368  81 GEKEVFIPRRCMHCDNPPCAKLCPF-GAARKTPEGAVYIDDDLCFGGAKCRDVCPWHIPQrqagvgiylhLAPEyagGGV 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 304997   157 VYKCTLCVDRVVVGQEPACVKTCPTGAIHFGTKESMKTLA 196
Cdd:cd16368 160 MYKCDLCKDLLAQGKPPACIEACPKGAQYFGPRKEMVALA 199
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 91-187 2.67e-29

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: 107.33  E-value: 2.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997      91 LEWLIRKDGCMHCSDPGCLKACPAeGAIIQ-YANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVDRVVV 169
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPV-GAIYKdEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEA 79

                          90
                  ....*....|....*...
gi 304997     170 GQEPACVKTCPTGAIHFG 187
Cdd:pfam13247  80 GLLPACVQTCPTGAMNFG 97
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 33-187 9.91e-29

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: 107.34  E-value: 9.91e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    33 LIDVTTCIGCKACQVACSEwndiRDTVGNNIGVYDNPNDLSakswtvMRFSEVEQNDKLEWLIRkdgCMHCSDPGCLKAC 112
Cdd:cd10563   3 FIDEEKCLGCKLCEVACAV----AHSKSKDLIKAKLEKERP------RPRIRVEESGGRSFPLQ---CRHCDEPPCVKAC 69

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 304997   113 PAeGAIIQY-ANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVDRvvvgQEPACVKTCPTGAIHFG 187
Cdd:cd10563  70 MS-GAMHKDpETGIVIHDEEKCVGCWMCVMVCPYGAIRPDKERKVALKCDLCPDR----ETPACVEACPTGALVLE 140
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 33-186 3.36e-28

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


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 105.35  E-value: 3.36e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    33 LIDVTTCIGCKACQVACSEWNDirdtvgnniGVYdNPndlsAKS-WTVMRFSEVEqndklewLIRKDGCMHCSDPGCLKA 111
Cdd:cd10550   2 VVDPEKCTGCRTCELACSLKHE---------GVF-NP----SLSrIRVVRFEPEG-------LDVPVVCRQCEDAPCVEA 60

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 304997   112 CPaEGAIIQ-YANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCvdrvvvGQEPACVKTCPTGAIHF 186
Cdd:cd10550  61 CP-VGAISRdEETGAVVVDEDKCIGCGMCVEACPFGAIRVDPETGKAIKCDLC------GGDPACVKVCPTGALEF 129
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
13-204 5.69e-26

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 103.03  E-value: 5.69e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997     13 ATNGLTPAPQARDFQEEVAKLIDVTTCIGCKACQVACSEWN-----DIRDTVgNNIGVYDNPndlsakswtvmrfSEVEQ 87
Cdd:PRK14993  27 AKFPFSPERHEGSPRHRYAMLIDLRRCIGCQSCTVSCTIENqtpqgAFRTTV-NQYQVQREG-------------SQEVT 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997     88 NDKLEWLirkdgCMHCSDPGCLKACPAEgAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVDRV 167
Cdd:PRK14993  93 NVLLPRL-----CNHCDNPPCVPVCPVQ-ATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRL 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 304997    168 VVGQEPACVKTCPTGAIHFGT----KESMKTLASERVAELK 204
Cdd:PRK14993 167 EAGLLPACVESCVGGARIIGDikdpHSRIATMLHQHRDAIK 207
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
33-186 3.40e-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: 3.40e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    33 LIDVTTCIGCKACQVACSEwndirdtvgnnigVYDNPNDLSAKSW-TVMRFSEVeqndklewlIRKDGCMHCSDPGCLKA 111
Cdd:COG1142   6 IADPEKCIGCRTCEAACAV-------------AHEGEEGEPFLPRiRVVRKAGV---------SAPVQCRHCEDAPCAEV 63

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 304997   112 CPAeGAIIQyANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNR--VYKCTLCVDRvvvGQEPACVKTCPTGAIHF 186
Cdd:COG1142  64 CPV-GAITR-DDGAVVVDEEKCIGCGLCVLACPFGAITMVGEKSRavAVKCDLCGGR---EGGPACVEACPTGALRL 135
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 39-186 1.54e-22

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: 91.17  E-value: 1.54e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    39 CIGCKACQVACSEWNdirdTVGNNIGVYDNPNDLSAKSWtvmrfseveqndklewLIRKDG------CMHCSDPGCLKAC 112
Cdd:cd10554   9 CIGCRTCEVACAAAH----SGKGIFEAGTDGLPFLPRLR----------------VVKTGEvtapvqCRQCEDAPCANVC 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997   113 PAeGAIIQyANGIVDFQSEQCIGCGYCIAGCPF-----------DIPRLNPEDNRVYKCTLCVDRvvvGQEPACVKTCPT 181
Cdd:cd10554  69 PV-GAISQ-EDGVVQVDEERCIGCKLCVLACPFgaiemapttvpGVDWERGPRAVAVKCDLCAGR---EGGPACVEACPT 143


                ....*
gi 304997   182 GAIHF 186
Cdd:cd10554 144 KALTL 148
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 33-203 2.91e-22

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: 91.62  E-value: 2.91e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    33 LIDVTTCIGCKACQVACsewndiRDT-VGNNIGVYDNPNDLSAKSWtvMRFSEVEQND--KLEWLIRKDGCMHCSDPGCL 109
Cdd:cd10552   2 VIDVAKCNGCYNCFLAC------KDEhVGNDWPGYAAPQPRHGHFW--MRILRRERGQypKVDVAYLPVPCNHCDNAPCI 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997   110 KACPAeGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVDRVVVG-QEPACVKTCPTGAIHFG- 187
Cdd:cd10552  74 KAAKD-GAVYKRDDGIVIIDPEKAKGQKQLVDACPYGAIYWNEELQVPQKCTFCAHLLDDGwKEPRCVQACPTGALRFGk 152

                       170
                ....*....|....*..
gi 304997   188 -TKESMKTLASERVAEL 203
Cdd:cd10552 153 lEDEEMAAKAAEEGLEV 169
FDH3_beta NF038355
formate dehydrogenase FDH3 subunit beta; Members of this family are the beta subunit of the ...
 33-208 5.48e-22

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: 90.51  E-value: 5.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997     33 LIDVTTCIGCKACQVACSEWNDIrdtvgnnigvydnpndlsakSWTVMRFSEVEQNDKLEWLIRKD-GCMHCSDPGCLKA 111
Cdd:NF038355   6 LCDTERCIECNGCVVACKNAHEL--------------------PWGINRRRVVTLNDGVPGEKSISvACMHCTDAPCAAV 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    112 CPAEgAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLnPEDN------RVYKCTLC-----------------VDRVV 168
Cdd:NF038355  66 CPVD-CFYIRADGIVLHDKDKCIGCGYCLYACPFGAPQF-PKDGafgargKMDKCTFCaggpeetnseaerekygQNRIA 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 304997    169 VGQEPACVKTCPTGAIHFGTKESMKTLASERVAelkTRGY 208
Cdd:NF038355 144 EGKLPLCAEMCSTKALLAGDAEVVADIYRERVV---ARGA 180
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 39-199 8.51e-20

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 89.42  E-value: 8.51e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997     39 CIGCKACQVACsewndirdTVGNNIGVY-DNPNDLSAKswtVMRFSEVEQNDKLEwlirkdgCMHCSDPGCLKACPaEGA 117
Cdd:PRK12769  12 CLGCHACEIAC--------VMAHNDEQHvLSQHHFHPR---ITVIKHQQQRSAVT-------CHHCEDAPCARSCP-NGA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    118 IIQYANGIVDFQsEQCIGCGYCIAGCPFDIPR--LNPEDN-----RVYKCTLCVDRvvvGQEPACVKTCPTGAIHFGTKE 190
Cdd:PRK12769  73 ISHVDDSIQVNQ-QKCIGCKSCVVACPFGTMQivLTPVAAgkvkaTAHKCDLCAGR---ENGPACVENCPADALQLVTEQ 148


                 ....*....
gi 304997    191 SMKTLASER 199
Cdd:PRK12769 149 ALSGMAKSR 157
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 29-180 1.86e-19

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: 84.17  E-value: 1.86e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    29 EVAKLIDVTTCIGCKACQVACSEWNDIRDTVG----NNIGVYdnPNDLSAKSWtvmrfsEVEQNDKLEWL----IRKDGC 100
Cdd:cd16365   2 QFAAVFNLNKCIGCQTCTVACKNAWTYRKGQEymwwNNVETK--PGGGYPQDW------EVKTIDNGGNTrfffYLQRLC 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997   101 MHCSDPGCLKACPAEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVDRVVVGQEPACVKTCP 180
Cdd:cd16365  74 NHCTNPACLAACPRGAIYKREEDGIVLIDQKRCRGYRKCVEQCPYKKIYFNGLSRVSEKCIACYPRIEGGDPTRCMSACV 153
Form-deh_trans pfam09163
Formate dehydrogenase N, transmembrane; Members of this family are predominantly found in the ...
 246-288 5.87e-19

Formate dehydrogenase N, transmembrane; Members of this family are predominantly found in the beta subunit of formate dehydrogenase, and consist of a single transmembrane helix. They act as a transmembrane anchor, and allow for conduction of electrons within the protein.


Pssm-ID: 430440  Cd Length: 43  Bit Score: 78.43  E-value: 5.87e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 304997     246 ISETVKFWKGIWKPLAAVGFAATFAASIFHYVGVGPNRADEEE 288
Cdd:pfam09163   1 ISPSVELWKGVLKPLGAAGMGAAALAGFFHYITVGPNKVEEEE 43
PRK09898 PRK09898
ferredoxin-like protein;
39-185 7.99e-19

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 82.96  E-value: 7.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997     39 CIGCKACQVACSEWND-------IRDTVGNNIGVYDNpndlsakswtvmrfsEVEQNDKL--EWLIRKDGCMHCSDPGCL 109
Cdd:PRK09898  68 CTGCHRCEISCTNFNDgsvgtffSRIKIHRNYFFGDN---------------GVGSGGGLygDLNYTADTCRQCKEPQCM 132

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 304997    110 KACPAEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCvdrvvvgqePACVKTCPTGAIH 185
Cdd:PRK09898 133 NVCPIGAITWQQKEGCITVDHKRCIGCSACTTACPWMMATVNTESKKSSKCVLC---------GECANACPTGALK 199
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 33-185 2.11e-17

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


Pssm-ID: 319889 [Multi-domain]  Cd Length: 138  Bit Score: 76.96  E-value: 2.11e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    33 LIDVTTCIGCKACQVACSEWNDIRDTVGNNIGVYDNpndlsakswtvmrfseveqndkleWLIrKDGCMHCSDPGCLKAC 112
Cdd:cd16367  15 VIDLDRCIRCDNCEKACADTHDGHSRLDRNGLRFGN------------------------LLV-PTACRHCVDPVCMIGC 69

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 304997   113 PaEGAIIQYANGIVdFQSEQCIGCGYCIAGCPFDIPRLnpedNRVYKCTLCVDrvvvGQEPACVKTCPTGAIH 185
Cdd:cd16367  70 P-TGAIHRDDGGEV-VISDACCGCGNCASACPYGAIQM----VRAVKCDLCAG----YAGPACVSACPTGAAI 132
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 100-187 2.24e-17

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: 80.81  E-value: 2.24e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997   100 CMHCSDPGCLKACPaEGAIIQYA-NGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVDRVVVGQEPACVKT 178
Cdd:cd10555 133 CNHCTNPACLAACP-RKAIYKREeDGIVLVDQDRCRGYRYCVEACPYKKIYFNPVEQKSEKCIFCYPRIEKGVAPACARQ 211


                ....*....
gi 304997   179 CPTGAIHFG 187
Cdd:cd10555 212 CVGRIRFVG 220
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 35-199 1.55e-16

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 79.68  E-value: 1.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997     35 DVTTCIGCKACQVACS------EWNDIRDTVGNNIGVYDNPNDLSAKSwtvmrfseveqndklewlirkdgCMHCSDPGC 108
Cdd:PRK12809   8 EAAECIGCHACEIACAvahnqeNWPLSHSDFRPRIHVVGKGQAANPVA-----------------------CHHCNNAPC 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    109 LKACPAEGAIiqYANGIVDFQSEQCIGCGYCIAGCPFDIPRLnpEDNRVYKCTLCVDRvVVGQEpACVKTCPTGAIHFGT 188
Cdd:PRK12809  65 VTACPVNALT--FQSDSVQLDEQKCIGCKRCAIACPFGVVEM--VDTIAQKCDLCNQR-SSGTQ-ACIEVCPTQALRLMD 138

                        170
                 ....*....|.
gi 304997    189 KESMKTLASER 199
Cdd:PRK12809 139 DKGLQQIKVAR 149
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 100-179 8.33e-15

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


Pssm-ID: 319879 [Multi-domain]  Cd Length: 363  Bit Score: 73.93  E-value: 8.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997   100 CMHCSDPGCLKACPAeGAIIQYA-NGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVDRVVVGQEPACVKT 178
Cdd:cd10557 179 CNHCLNPACVAACPS-GAIYKREeDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSEKCIFCYPRLEAGQPTVCSET 257


                .
gi 304997   179 C 179
Cdd:cd10557 258 C 258
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 32-184 2.00e-13

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: 65.76  E-value: 2.00e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    32 KLIDVTTCIGCKACQVACSEwndirdTVGNNIGVydnpndlsAKSwtVMRfseVEQNDKLEWLIRKDGCMHCSDPGCLKA 111
Cdd:cd16370   4 RVKDMERCIGCYSCMLACSR------RVHKSASL--------SKS--AIR---VRTRGGLEGGFTVVVCRACEDPPCAEA 64

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 304997   112 CPaEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCvdrvvvgqePACVKTCPTGAI 184
Cdd:cd16370  65 CP-TGALEPRKGGGVVLDKEKCIGCGNCVKACIVGAIFWDEETNKPIICIHC---------GYCARYCPHDVL 127
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 100-180 2.61e-12

Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate reductase (SER), a member of the DMSO reductase family. SER catalyzes the reduction of selenate to selenite in bacterial species that can obtain energy by respiring anaerobically with selenate as the terminal electron acceptor. The enzyme comprises three subunits SerABC, forming a heterotrimer, with the catalytic component (alpha-subunit), iron-sulfur protein (beta-subunit) and monomeric b-type heme-containing gamma subunit. Beta subunit contains coordinating one [3Fe-4S] cluster and three [4Fe-4S] clusters and functions as electron carrier.


Pssm-ID: 319878 [Multi-domain]  Cd Length: 287  Bit Score: 65.94  E-value: 2.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997   100 CMHCSDPGCLKACPAEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVDRVVVGQEPACVKTC 179
Cdd:cd10556 141 CNHCTYPACLAACPRKAIYKREEDGIVLIDQERCRGYRECVEACPYKKPMYNPTTRVSEKCIGCYPRIEEGDQTQCVSAC 220


                .
gi 304997   180 P 180
Cdd:cd10556 221 I 221
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 34-184 6.08e-12

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


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 61.58  E-value: 6.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    34 IDVTTCIGCKACQVACSE-WNDIRDTvgnnigvydnpnDLSAkswtvMRFSEVEQNDKLewlirkDGCMHCSDpgCLKAC 112
Cdd:cd16372   5 TDPEKCIGCLQCEEACSKtFFKEEDR------------EKSC-----IRITETEGGYAI------NVCNQCGE--CIDVC 59

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 304997   113 PaEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCvdrvvvgqePACVKTCPTGAI 184
Cdd:cd16372  60 P-TGAITRDANGVVMINKKLCVGCLMCVGFCPEGAMFKHEDYPEPFKCIAC---------GICVKACPTGAL 121
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 100-179 7.95e-12

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


Pssm-ID: 440755 [Multi-domain]  Cd Length: 485  Bit Score: 65.21  E-value: 7.95e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997   100 CMHCSDPGCLKACPAeGAIIQYA-NGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLCVDRVVVGQEPACVKT 178
Cdd:COG1140 182 CEHCLNPACVASCPS-GAIYKREeDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGKAEKCIFCYPRIEAGQPTVCSET 260


                .
gi 304997   179 C 179
Cdd:COG1140 261 C 261
PRK10330 PRK10330
electron transport protein HydN;
33-199 6.76e-11

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 60.29  E-value: 6.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997     33 LIDVTTCIGCKACQVAC----SEWNDI----RDTVGNNIGVYDNPNDLSAKSwtvmrfseveqndklewlirkdgCMHCS 104
Cdd:PRK10330   6 IADASKCIGCRTCEVACvvshQENQDCasltPETFLPRIHVIKGVNVSTATV-----------------------CRQCE 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    105 DPGCLKACPaEGAIIQyANGIVDFQSEQCIGCGYCIAGCPF-------------DIPRLN--PEDNRVYKCTLCVDRvvv 169
Cdd:PRK10330  63 DAPCANVCP-NGAISR-DKGFVHVMQERCIGCKTCVVACPYgamevvvrpvirnSGAGLNvrAEKAEANKCDLCNHR--- 137

                        170       180       190
                 ....*....|....*....|....*....|
gi 304997    170 GQEPACVKTCPTGAIHFGTKESMKTLASER 199
Cdd:PRK10330 138 EDGPACMAACPTHALICVDRNKLEQLSAEK 167
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 96-185 2.59e-09

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: 56.54  E-value: 2.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    96 RKDGCMHCSDpgCLKACPAeGAIIQYANGI--VDfqSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTL---CVDRVVVG 170
Cdd:COG2878 135 CEYGCIGCGD--CIKACPF-DAIVGAAKGMhtVD--EDKCTGCGLCVEACPVDCIEMVPVSPTVVVSSWdkgKAVRKVVG 209

                        90
                ....*....|....*
gi 304997   171 QEPACVKTCPTGAIH 185
Cdd:COG2878 210 CIGLCCKKCCPAAAI 224
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
131-202 4.13e-07

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 46.65  E-value: 4.13e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 304997   131 EQCIGCGYCIAGCPFDIPRLnpEDNRVY----KCTLCvdrvvvgqePACVKTCPTGAIHFGTKESMKTlaSERVAE 202
Cdd:COG2768  11 EKCIGCGACVKVCPVGAISI--EDGKAVidpeKCIGC---------GACIEVCPVGAIKIEWEEDEEF--QEKMAE 73
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
33-185 5.90e-07

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 50.41  E-value: 5.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    33 LIDVTTCIGCKACQVACSEWNDIRDTVGNNIGVYDNPNDLSAKSwtvmrFSEVEQNDKLEWLIRKDGCMHCSDPGCLKAc 112
Cdd:COG4624   3 LLLRACCCCCIEEGDELLLLEEAERVLRIIILEALLPEHVDDDS-----ACSCCPRCCLCCCCCCRCCVAISCIQVRGI- 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 304997   113 paegAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNpeDNRVY----KCTLCvdrvvvGQepaCVKTCPTGAIH 185
Cdd:COG4624  77 ----IIIDKRGPSIIRDKEKCKNCYPCVRACPVKAIKVD--DGKAEideeKCISC------GQ---CVAVCPFGAIT 138
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 127-188 6.30e-07

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: 47.78  E-value: 6.30e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 304997   127 DFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVY-------KCTLCvdrvvvGqepACVKTCPTGAIHFGT 188
Cdd:cd10549   2 KYDPEKCIGCGICVKACPTDAIELGPNGAIARgpeidedKCVFC------G---ACVEVCPTGAIELTP 61
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
125-193 6.68e-07

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 49.68  E-value: 6.68e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 304997   125 IVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRvYKCTLCVDrvvvgqepaCVKTCPTGAIHFGTKESMK 193
Cdd:COG0348 204 RVRYDRGDCIDCGLCVKVCPMGIDIRKGEINQ-SECINCGR---------CIDACPKDAIRFSSRGEKT 262
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 121-190 7.50e-07

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 45.87  E-value: 7.50e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 304997   121 YANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRV---YKCTLCVdrvvvgqepACVKTCPTGAIHFGTKE 190
Cdd:COG1149   1 VKRKIPVIDEEKCIGCGLCVEVCPEGAIKLDDGGAPVvdpDLCTGCG---------ACVGVCPTGAITLEERE 64
NapF COG1145
Ferredoxin [Energy production and conversion];
89-190 9.35e-07

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 48.95  E-value: 9.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    89 DKLEWLIRKDGCMHCSDPGCLKACPAEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVY----KCTLCv 164
Cdd:COG1145 140 AEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVCPTGAIRLKDGKPQIVvdpdKCIGC- 218

                        90       100
                ....*....|....*....|....*.
gi 304997   165 drvvvgqePACVKTCPTGAIHFGTKE 190
Cdd:COG1145 219 --------GACVKVCPVGAISLEPKE 236
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
99-202 9.97e-07

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 49.16  E-value: 9.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997     99 GCMHCSDpgCLKACPAEGAIIQyaNGIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVY-------------------- 158
Cdd:PRK07118 140 GCLGLGS--CVAACPFDAIHIE--NGLPVVDEDKCTGCGACVKACPRNVIELIPKSARVFvacnskdkgkavkkvcevgc 215

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 304997    159 -KCTLCV------------DRVVVGQEP-----ACVKTCPTGAIHFGTKESMKTLASERVAE 202
Cdd:PRK07118 216 iGCGKCVkacpagaitmenNLAVIDQEKctscgKCVEKCPTKAIRILNKPPKVKEPKKAAAE 277
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 131-184 2.83e-06

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 44.31  E-value: 2.83e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 304997   131 EQCIGCGYCIAGCPFDIPRLNPEDNRVY-----KCTLCvdrvvvgqePACVKTCPTGAI 184
Cdd:COG1146   8 DKCIGCGACVEVCPVDVLELDEEGKKALvinpeECIGC---------GACELVCPVGAI 57
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 97-185 3.12e-06

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 45.47  E-value: 3.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    97 KDGCMHCSDpgCLKACPAeGAIIQYANGIV----DFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVYKCTLcvdRVVVGQE 172
Cdd:cd10549   5 PEKCIGCGI--CVKACPT-DAIELGPNGAIargpEIDEDKCVFCGACVEVCPTGAIELTPEGKEYVPKEK---EAEIDEE 78

                        90
                ....*....|....*...
gi 304997   173 P-----ACVKTCPTGAIH 185
Cdd:cd10549  79 KcigcgLCVKVCPVDAIT 96
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 131-190 8.76e-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: 42.81  E-value: 8.76e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 304997   131 EQCIGCGYCIAGCPFDIPRLNPEDNRVY------KCTLCVdrvvvgqepACVKTCPTGAIHFGTKE 190
Cdd:COG1143   2 DKCIGCGLCVRVCPVDAITIEDGEPGKVyvidpdKCIGCG---------LCVEVCPTGAISMTPFE 58
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
94-154 1.10e-05

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 42.80  E-value: 1.10e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 304997    94 LIRKDGCMHCSDpgCLKACPAEgaIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPED 154
Cdd:COG2768   7 YVDEEKCIGCGA--CVKVCPVG--AISIEDGKAVIDPEKCIGCGACIEVCPVGAIKIEWEE 63
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 95-146 1.83e-05

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 41.96  E-value: 1.83e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 304997    95 IRKDGCMHCSDpgCLKACPaEGAIiQYANGIVDFQSEQCIGCGYCIAGCPFD 146
Cdd:COG2221  12 IDEEKCIGCGL--CVAVCP-TGAI-SLDDGKLVIDEEKCIGCGACIRVCPTG 59
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 130-189 2.02e-05

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 44.85  E-value: 2.02e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 304997    130 SEQCIGCGYCIAGCPFDIPRLnpEDNRVY---KCTLCVdrvvvgqepACVKTCPTGAIHFGTK 189
Cdd:NF038196 184 TDKCIGCGICAKVCPVNNIEM--EDGKPVwghNCTHCL---------ACIHRCPKEAIEYGKK 235
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 93-144 2.64e-05

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: 41.08  E-value: 2.64e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 304997      93 WLIRKDGCMHCsdPGCLKACPAEGAI-----IQYANGIVDFQSEQCIGCGYCIAGCP 144
Cdd:pfam13237   2 VVIDPDKCIGC--GRCTAACPAGLTRvgaivERLEGEAVRIGVWKCIGCGACVEACP 56
Fer4_9 pfam13187
4Fe-4S dicluster domain;
132-184 2.81e-05

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 41.00  E-value: 2.81e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 304997     132 QCIGCGYCIAGCPFDI------PRLNPEDNRVYKCTLCVdrvvvgqepACVKTCPTGAI 184
Cdd:pfam13187   1 KCTGCGACVAACPAGAivpdlvGQTIRGDIAGLACIGCG---------ACVDACPRGAI 50
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 34-146 2.89e-05

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 42.77  E-value: 2.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    34 IDVTTCIGCKACQVACSewndiRDTVgnnigvydnpndlsakswTVMRFSEVEQNDKLEWLIRKDGCMHCSDpgCLKACP 113
Cdd:cd10549  37 IDEDKCVFCGACVEVCP-----TGAI------------------ELTPEGKEYVPKEKEAEIDEEKCIGCGL--CVKVCP 91

                        90       100       110
                ....*....|....*....|....*....|...
gi 304997   114 aEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFD 146
Cdd:cd10549  92 -VDAITLEDELEIVIDKEKCIGCGICAEVCPVN 123
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 95-146 4.18e-05

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 40.87  E-value: 4.18e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 304997    95 IRKDGCMHCSDpgCLKACPaEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFD 146
Cdd:COG1149   8 IDEEKCIGCGL--CVEVCP-EGAIKLDDGGAPVVDPDLCTGCGACVGVCPTG 56
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
131-186 4.90e-05

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 44.47  E-value: 4.90e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997   131 EQCIGCGYCIAGCPFDIPRLNpEDNRVY----KCTLCvdrvvvGqepACVKTCPTGAIHF 186
Cdd:COG1148 496 EKCTGCGRCVEVCPYGAISID-EKGVAEvnpaLCKGC------G---TCAAACPSGAISL 545
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 117-185 6.25e-05

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 40.42  E-value: 6.25e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 304997   117 AIIQYANGIVDfqSEQCIGCGYCIAGCPFDIprLNPEDNRVY----KCTLCvdrvvvgqePACVKTCPTGAIH 185
Cdd:COG2221   3 GIIGTWPPKID--EEKCIGCGLCVAVCPTGA--ISLDDGKLVideeKCIGC---------GACIRVCPTGAIK 62
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 98-186 1.07e-04

NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. 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 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: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 41.46  E-value: 1.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    98 DGCMHCSDpgCLKACPaEGAIIQYANGI--VDFQSEQCIGCGYCIAGCP---FDIPRLNPED------------NRVYkC 160
Cdd:cd10564  13 DLCTRCGD--CVEACP-EGIIVRGDGGFpeLDFSRGECTFCGACAEACPegaLDPAREAPWPlraeigdsclalQGVE-C 88

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 304997   161 TLCVD-----------RVVVGQEP-----------ACVKTCPTGAIHF 186
Cdd:cd10564  89 RSCQDacptqairfrpRLGGIALPeldadactgcgACVSVCPVGAITL 136
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 133-194 1.20e-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: 41.47  E-value: 1.20e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 304997   133 CIGCGYCIAGCPFDI---------------PRLNPEDNrvyKCTLCVDrvvvgqepACVKTCPTGAIHFGTKESMKT 194
Cdd:cd16373  16 CIRCGLCVEACPTGViqpagledgleggrtPYLDPREG---PCDLCCD--------ACVEVCPTGALRPLDLEEQKV 81
napG PRK09476
quinol dehydrogenase periplasmic component; Provisional
 127-183 1.40e-04

quinol dehydrogenase periplasmic component; Provisional


Pssm-ID: 236534 [Multi-domain]  Cd Length: 254  Bit Score: 42.69  E-value: 1.40e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 304997    127 DFQSeQCIGCGYCIAGCPFDIPRL-NPEDN----------RVYKCTLCVDrvvvgqePACVKTCPTGA 183
Cdd:PRK09476  56 DFLS-ACIRCGLCVQACPYDTLKLaTLASGlsagtpyfvaRDIPCEMCED-------IPCVKACPSGA 115
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 131-184 1.50e-04

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 39.64  E-value: 1.50e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 304997   131 EQCIGCGYCIAGCPFDIprLNPEDNRVY----KCTLCVdrvvvgqepACVKTCPTGAI 184
Cdd:COG4231  22 DKCTGCGACVKVCPADA--IEEGDGKAVidpdLCIGCG---------SCVQVCPVDAI 68
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 94-153 2.18e-04

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


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 40.94  E-value: 2.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997      94 LIRKDGCMHCSDpgCLKACPAEgAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLNPE 153
Cdd:TIGR01944 109 LIDEDNCIGCTK--CIQACPVD-AIVGAAKAMHTVIADECTGCDLCVEPCPTDCIEMIPV 165
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 124-204 3.20e-04

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 39.82  E-value: 3.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997    124 GIVDFQSEQCIGCGYCIAGCPFDIPRLNPEDNRVY----KCTLCvdrvvvGQepaCVKTCPTGAIHFGTK---------- 189
Cdd:PRK08348  35 GKILYDVDKCVGCRMCVTVCPAGVFVYLPEIRKVAlwtgRCVFC------GQ---CVDVCPTGALQMSDDfllasydrfd 105

                         90
                 ....*....|....*
gi 304997    190 ESMKTLASERVAELK 204
Cdd:PRK08348 106 EKFIPLKPEKVEEIK 120
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 133-183 4.27e-04

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 37.51  E-value: 4.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997     133 CIGCGYCIAGCPFDIPRLNPEDN---------RVYKCTLCvdrvvvgqePACVKTCPTGA 183
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEkkgtktvviDPERCVGC---------GACVAVCPTGA 51
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 95-146 4.59e-04

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 38.10  E-value: 4.59e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 304997    95 IRKDGCMHCSDpgCLKACPAEgaIIQYANGIVDFQSEQCIGCGYCIAGCPFD 146
Cdd:COG4231  19 IDEDKCTGCGA--CVKVCPAD--AIEEGDGKAVIDPDLCIGCGSCVQVCPVD 66
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 100-147 5.25e-04

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 37.12  E-value: 5.25e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 304997     100 CMHCSDpgCLKACPA-----EGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDI 147
Cdd:pfam12838   1 CIGCGA--CVAACPVgaitlDEVGEKKGTKTVVIDPERCVGCGACVAVCPTGA 51
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
95-151 5.38e-04

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 41.38  E-value: 5.38e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 304997    95 IRKDGCMHCSdpGCLKACPAeGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDIPRLN 151
Cdd:COG1148 493 VDPEKCTGCG--RCVEVCPY-GAISIDEKGVAEVNPALCKGCGTCAAACPSGAISLK 546
flavo_MJ0208 TIGR02700
archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of ...
 90-146 7.24e-04

archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of archaealflavoprotein. The other, described by TIGR02699 and typified by the partially characterized AF1518 of Archaeoglobus fulgidus, is a homodimeric FMN-containing flavoprotein that accepts electrons from ferredoxin and can transfer them to various oxidoreductases. The function of this protein family is unknown. [Unknown function, General]


Pssm-ID: 131747 [Multi-domain]  Cd Length: 234  Bit Score: 40.24  E-value: 7.24e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 304997      90 KLEWLIRKDGCMHCSDpgCLKACPAEGaiIQYANGIVDFQSEQCIGCGYCIAGCPFD 146
Cdd:TIGR02700 140 ITPYMIDRKRCKGCGI--CVDACPRSA--IDMVDGKAFIRLLKCVGCGKCKEACPYN 192
Fer4_13 pfam13370
4Fe-4S single cluster domain of Ferredoxin I; Fer4_13 is a ferredoxin I from sulfate-reducing ...
 131-185 1.07e-03

4Fe-4S single cluster domain of Ferredoxin I; Fer4_13 is a ferredoxin I from sulfate-reducing bacteria. Chemical sequence analysis suggests that this characteriztic [4Fe-4S] cluster sulfur environment is widely distributed among ferredoxins.


Pssm-ID: 433153 [Multi-domain]  Cd Length: 58  Bit Score: 36.52  E-value: 1.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997     131 EQCIGCGYCIAGCPfDIPRLNPEDNRVYkctlcVDRVVVGQ-EPACVK----TCPTGAIH 185
Cdd:pfam13370   4 DTCIDCGTCRELAP-EVFKYDDDGGASF-----VHDQPVNEeEEDLAEealdSCPVEAIG 57
PRK13795 PRK13795
hypothetical protein; Provisional
 94-144 1.56e-03

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 39.98  E-value: 1.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 304997     94 LIRKDGCMHCsdpG-CLKACPaEGAI-IQYANGIVDFQSEQCIGCGYCIAGCP 144
Cdd:PRK13795 577 LRRAAECVGC---GvCVGACP-TGAIrIEEGKRKISVDEEKCIHCGKCTEVCP 625
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
123-188 2.99e-03

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 37.33  E-value: 2.99e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 304997   123 NGIVDFQSEQCIGCGYCIAGCPF---------DIPRL----NPEDNRVYKCTLCVDRvvvgqepACVKTCPTGAIHFGT 188
Cdd:COG1142   2 NKFIIADPEKCIGCRTCEAACAVahegeegepFLPRIrvvrKAGVSAPVQCRHCEDA-------PCAEVCPVGAITRDD 73
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
34-144 3.31e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 38.38  E-value: 3.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304997     34 IDVTTCIGCKACQVACSewNDIRDTV--GNNIGVYDNPNDlsaKSWTVMRFSEVeqndklewlirkdGCMHCSDpgCLKA 111
Cdd:PRK07118 165 VDEDKCTGCGACVKACP--RNVIELIpkSARVFVACNSKD---KGKAVKKVCEV-------------GCIGCGK--CVKA 224

                         90       100       110
                 ....*....|....*....|....*....|...
gi 304997    112 CPAeGAIIQyANGIVDFQSEQCIGCGYCIAGCP 144
Cdd:PRK07118 225 CPA-GAITM-ENNLAVIDQEKCTSCGKCVEKCP 255
Fer COG1141
Ferredoxin [Energy production and conversion];
131-185 3.35e-03

Ferredoxin [Energy production and conversion];


Pssm-ID: 440756 [Multi-domain]  Cd Length: 63  Bit Score: 35.24  E-value: 3.35e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 304997   131 EQCIGCGYCIAGCPfDIPRLNPEDnrvyKCTLCVDRVVVGQEPAC---VKTCPTGAIH 185
Cdd:COG1141   8 DTCIGCGLCVALAP-EVFELDDDG----KAVVLDEEVPEELEEDVreaADACPVGAIT 60
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 95-146 4.07e-03

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: 35.80  E-value: 4.07e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 304997    95 IRKDGCMHCSDpgCLKACPaEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFD 146
Cdd:COG1144  27 VDEDKCIGCGL--CWIVCP-DGAIRVDDGKYYGIDYDYCKGCGICAEVCPVK 75
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 97-146 5.34e-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: 34.72  E-value: 5.34e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 304997    97 KDGCMHCSDpgCLKACPAeGAIIQYANG---IVDFQSEQCIGCGYCIAGCPFD 146
Cdd:COG1143   1 EDKCIGCGL--CVRVCPV-DAITIEDGEpgkVYVIDPDKCIGCGLCVEVCPTG 50
Fer4_9 pfam13187
4Fe-4S dicluster domain;
100-147 6.53e-03

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 34.07  E-value: 6.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 304997     100 CMHCSDpgCLKACPAeGAIIQYANG---IVDFQSEQCIGCGYCIAGCPFDI 147
Cdd:pfam13187   2 CTGCGA--CVAACPA-GAIVPDLVGqtiRGDIAGLACIGCGACVDACPRGA 49
PRK08764 PRK08764
Rnf electron transport complex subunit RnfB;
90-146 9.01e-03

Rnf electron transport complex subunit RnfB;


Pssm-ID: 181550 [Multi-domain]  Cd Length: 135  Bit Score: 35.67  E-value: 9.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 304997     90 KLEWLIRKDgCMHCSDpgCLKACPAEgAIIQYANGIVDFQSEQCIGCGYCIAGCPFD 146
Cdd:PRK08764  78 QVAWIVEAD-CIGCTK--CIQACPVD-AIVGGAKHMHTVIAPLCTGCELCVPACPVD 130
 
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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