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Conserved domains on  [gi|2238914871|ref|WP_249245787|]
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formate dehydrogenase subunit beta [Brenneria tiliae]

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 ...
 7-282 3.24e-161

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: 449.74  E-value: 3.24e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871   7 DIIKRSATNDftPPPQVRSDKSEVAKLIDVTTCIGCKACQVACSEWNDIRDEVG-HNAGVYDNPADLSAKSWTLMRFSEV 85
Cdd:TIGR01582   1 DIKRLSATKE--PDPSVKTYPTELAKLIDVSSCIGCKACQAACQEWNDTTPPILsRKVGGYQNPPDLLPETFTLMRFKEG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  86 EENDRLEWLIRKDGCMHCSDPGCLKACPSAGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVD 165
Cdd:TIGR01582  79 EESDGLEWLIRKDGCMHCREPGCLKACPAPGAIIQYQNGIVDFDHSKCIGCGYCIVGCPFNIPRYDKVDNRPYKCTLCID 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 166 RVSVGQEPACVKTCPTGAIRFGTKAEMKHLAEERLIDLKKRGYAHAGLYDPQGVGGTHVMYVLHHADRPSLYHNLPDNPQ 245
Cdd:TIGR01582 159 RVSVGQEPACVKTCPTNAISFGFKEDMKERAEKRVADLKSRGYPNAGLYDPPGVGGTHVMYVLHHGDKPKDYQDLPEDPR 238

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2238914871 246 ISTPVDLWKGILKPLSALGFVATFAGLIFHYVGIGPN 282
Cdd:TIGR01582 239 IDASVGLWKGVLKTIGSIAMGGTALGVFLHLILWGPN 275
 
Name Accession Description Interval E-value
FDH-beta TIGR01582
formate dehydrogenase, beta subunit, Fe-S containing; This model represents the beta subunit ...
 7-282 3.24e-161

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: 449.74  E-value: 3.24e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871   7 DIIKRSATNDftPPPQVRSDKSEVAKLIDVTTCIGCKACQVACSEWNDIRDEVG-HNAGVYDNPADLSAKSWTLMRFSEV 85
Cdd:TIGR01582   1 DIKRLSATKE--PDPSVKTYPTELAKLIDVSSCIGCKACQAACQEWNDTTPPILsRKVGGYQNPPDLLPETFTLMRFKEG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  86 EENDRLEWLIRKDGCMHCSDPGCLKACPSAGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVD 165
Cdd:TIGR01582  79 EESDGLEWLIRKDGCMHCREPGCLKACPAPGAIIQYQNGIVDFDHSKCIGCGYCIVGCPFNIPRYDKVDNRPYKCTLCID 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 166 RVSVGQEPACVKTCPTGAIRFGTKAEMKHLAEERLIDLKKRGYAHAGLYDPQGVGGTHVMYVLHHADRPSLYHNLPDNPQ 245
Cdd:TIGR01582 159 RVSVGQEPACVKTCPTNAISFGFKEDMKERAEKRVADLKSRGYPNAGLYDPPGVGGTHVMYVLHHGDKPKDYQDLPEDPR 238

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2238914871 246 ISTPVDLWKGILKPLSALGFVATFAGLIFHYVGIGPN 282
Cdd:TIGR01582 239 IDASVGLWKGVLKTIGSIAMGGTALGVFLHLILWGPN 275
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 31-238 3.14e-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: 419.10  E-value: 3.14e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  31 AKLIDVTTCIGCKACQVACSEWNDIRDEVGHNAGVYDNPADLSAKSWTLMRFSEVEENDRLEWLIRKDGCMHCSDPGCLK 110
Cdd:cd10558     1 AKLIDVSKCIGCKACQVACKEWNDLRAEVGHNVGTYQNPADLSPETWTLMKFREVEDNGKLEWLIRKDGCMHCADPGCLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 111 ACPSAGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVDRVSVGQEPACVKTCPTGAIRFGTKA 190
Cdd:cd10558    81 ACPSPGAIVQYANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVGLEPACVKTCPTGALHFGTKE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2238914871 191 EMKHLAEERLIDLKKRGYAHAGLYDPQGVGGTHVMYVLHHADRPSLYH 238
Cdd:cd10558   161 DMLALAEKRVAALKERGYTNAGLYDPKGVGGTHVMYVLHHADKPEGYP 208
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 25-227 9.23e-69

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 211.73  E-value: 9.23e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  25 SDKSEVAKLIDVTTCIGCKACQVACSEWNDIRDEVghnagvydnpadlsakSWTLMRFSEVEENDRLEWLIRKDGCMHCS 104
Cdd:COG0437     1 LSMKRYGMVIDLTKCIGCRACVVACKEENNLPVGV----------------TWRRVRRYEEGEFPNVEWLFVPVLCNHCD 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 105 DPGCLKACPSaGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVDRVSVGQEPACVKTCPTGAI 184
Cdd:COG0437    65 DPPCVKVCPT-GATYKREDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVEACPTGAL 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2238914871 185 RFGTKAEMKHLAEERLIDLKKRGyahaglYDPQGVGGTHVMYV 227
Cdd:COG0437   144 VFGDLDDPESEVSKRLAELPAYR------LLPELGTKPSVYYL 180
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
30-270 4.19e-44

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 152.90  E-value: 4.19e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  30 VAKLIDVTTCIGCKACQVACSEWNDIRDEVGHNaGVYDNPADLSAKSWTLM---RFSEVEENDRLE--WLIRKDGCMHCS 104
Cdd:PRK10882   38 LGMLYDSTLCVGCQACVTKCQEINFPERNPQGE-QTWDNPDKLSPYTNNIIkvwKSGTGVNKDQEEngYAYIKKQCMHCV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 105 DPGCLKACPsAGAIIQYA-NGIVDFQSENCIGCGYCIAGCPFDIPRLNKDD--NRVYKCTLC----VDRVSVGQEPACVK 177
Cdd:PRK10882  117 DPNCVSVCP-VSALTKDPkTGIVHYDKDVCTGCRYCMVACPFNVPKYDYNNpfGAIHKCELCnqkgVERLDKGGLPGCVE 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 178 TCPTGAIRFGTKAEMKHLAEERL-------------------IDLKKRGYAHAGLYDPQGVGGTHVMYVLHHAdrpslYH 238
Cdd:PRK10882  196 VCPTGAVIFGTREELLAEAKRRLalkpgseyhyprqtlksgdTYLHTVPKYYPHVYGEKEGGGTQVLVLSGVP-----FE 270

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2238914871 239 NL--PDNPQISTPVD-------LWKGILKPLSALGFVATFA 270
Cdd:PRK10882  271 NLglPKLDDLSTGARsehiqhtLYKGMILPLAVLAGLTVLV 311
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 91-187 3.79e-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: 106.95  E-value: 3.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  91 LEWLIRKDGCMHCSDPGCLKACPSaGAIIQ-YANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVDRVSV 169
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPV-GAIYKdEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEA 79

                          90
                  ....*....|....*...
gi 2238914871 170 GQEPACVKTCPTGAIRFG 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 2.17e-21

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: 88.97  E-value: 2.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  33 LIDVTTCIGCKACQVACSEWNDIrdevghnagvydnpadlsakSWTLMRFSEVEENDRLEWLIRKD-GCMHCSDPGCLKA 111
Cdd:NF038355    6 LCDTERCIECNGCVVACKNAHEL--------------------PWGINRRRVVTLNDGVPGEKSISvACMHCTDAPCAAV 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 112 CPsAGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDN-----RVYKCTLC-----------------VDRVSV 169
Cdd:NF038355   66 CP-VDCFYIRADGIVLHDKDKCIGCGYCLYACPFGAPQFPKDGAfgargKMDKCTFCaggpeetnseaerekygQNRIAE 144

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2238914871 170 GQEPACVKTCPTGAIRFGTKAEMKHLAEERLIdlkKRGY 208
Cdd:NF038355  145 GKLPLCAEMCSTKALLAGDAEVVADIYRERVV---ARGA 180
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 130-189 9.50e-06

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: 46.01  E-value: 9.50e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2238914871 130 SENCIGCGYCIAGCPFDIPRLnkDDNRVY---KCTLCVdrvsvgqepACVKTCPTGAIRFGTK 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 ...
 7-282 3.24e-161

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: 449.74  E-value: 3.24e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871   7 DIIKRSATNDftPPPQVRSDKSEVAKLIDVTTCIGCKACQVACSEWNDIRDEVG-HNAGVYDNPADLSAKSWTLMRFSEV 85
Cdd:TIGR01582   1 DIKRLSATKE--PDPSVKTYPTELAKLIDVSSCIGCKACQAACQEWNDTTPPILsRKVGGYQNPPDLLPETFTLMRFKEG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  86 EENDRLEWLIRKDGCMHCSDPGCLKACPSAGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVD 165
Cdd:TIGR01582  79 EESDGLEWLIRKDGCMHCREPGCLKACPAPGAIIQYQNGIVDFDHSKCIGCGYCIVGCPFNIPRYDKVDNRPYKCTLCID 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 166 RVSVGQEPACVKTCPTGAIRFGTKAEMKHLAEERLIDLKKRGYAHAGLYDPQGVGGTHVMYVLHHADRPSLYHNLPDNPQ 245
Cdd:TIGR01582 159 RVSVGQEPACVKTCPTNAISFGFKEDMKERAEKRVADLKSRGYPNAGLYDPPGVGGTHVMYVLHHGDKPKDYQDLPEDPR 238

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2238914871 246 ISTPVDLWKGILKPLSALGFVATFAGLIFHYVGIGPN 282
Cdd:TIGR01582 239 IDASVGLWKGVLKTIGSIAMGGTALGVFLHLILWGPN 275
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 31-238 3.14e-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: 419.10  E-value: 3.14e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  31 AKLIDVTTCIGCKACQVACSEWNDIRDEVGHNAGVYDNPADLSAKSWTLMRFSEVEENDRLEWLIRKDGCMHCSDPGCLK 110
Cdd:cd10558     1 AKLIDVSKCIGCKACQVACKEWNDLRAEVGHNVGTYQNPADLSPETWTLMKFREVEDNGKLEWLIRKDGCMHCADPGCLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 111 ACPSAGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVDRVSVGQEPACVKTCPTGAIRFGTKA 190
Cdd:cd10558    81 ACPSPGAIVQYANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVGLEPACVKTCPTGALHFGTKE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2238914871 191 EMKHLAEERLIDLKKRGYAHAGLYDPQGVGGTHVMYVLHHADRPSLYH 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 1.29e-89

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: 263.49  E-value: 1.29e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  32 KLIDVTTCIGCKACQVACSEWNDIRDEVGHNAGVYDNPADLSAKSWTLMRFSEVEEND-RLEWLIRKDGCMHCSDPGCLK 110
Cdd:cd16366     1 FLVDTSRCTGCRACQVACKQWNGLPAEKTEFTGSYQNPPDLTAHTWTLVRFYEVEKPGgDLSWLFRKDQCMHCTDAGCLA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2238914871 111 ACPSaGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVDRVSVGQEPACVKTCPTGAIRFG 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 ...
 33-248 2.13e-82

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: 247.68  E-value: 2.13e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  33 LIDVTTCIGCKACQVACSEWNDIRDEVGHNAG-VYDNPADLSAKSWTLMRFSEV-------EENDRLEWLIRKDGCMHCS 104
Cdd:cd10560     3 FTDTSICIGCKACEVACKQWNQLPADGYDFSGmSYDNTGDLSASTWRHVKFIERptedgpaNEGGDLQWLFMSDVCKHCT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 105 DPGCLKACPSaGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVDRVSVGQEPACVKTCPTGAI 184
Cdd:cd10560    83 DAGCLEACPT-GAIFRTEFGTVYIQPDICNGCGYCVAACPFGVIDRNEETGRAHKCTLCYDRLKDGLEPACAKACPTGSI 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2238914871 185 RFGTKAEMKHLAEERLIDLKKRGYAHAGLY--DP-QGVGGTHVMYVLhhADRPSLYhNLPDNPQIST 248
Cdd:cd10560   162 QFGPLEELRERARARVEQLHEQGVVEAYLYgaDPtEGYGGLNAFFLL--LDKPEVY-GLPADPLLPT 225
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 32-192 4.62e-76

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: 229.50  E-value: 4.62e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  32 KLIDVTTCIGCKACQVACSEWNDIRDEVGHNAGVYDNPADLSAKSWTLMRFSEVEE-NDRLEWLIRKDGCMHCSDPGCLK 110
Cdd:cd10562     1 MLVDTSKCTACRGCQVACKQWNQLPAEKTPFTGSYQNPPDLTPNTWTLIRFYEHEEdNGGIRWLFRKRQCMHCTDAACVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 111 ACPSaGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVDRVSVGQEPACVKTCPTGAIRFGTKA 190
Cdd:cd10562    81 VCPT-GALYKTENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCFDRIENGMQPACVKTCPTGALTFGDRD 159


                  ..
gi 2238914871 191 EM 192
Cdd:cd10562   160 EL 161
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 25-227 9.23e-69

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 211.73  E-value: 9.23e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  25 SDKSEVAKLIDVTTCIGCKACQVACSEWNDIRDEVghnagvydnpadlsakSWTLMRFSEVEENDRLEWLIRKDGCMHCS 104
Cdd:COG0437     1 LSMKRYGMVIDLTKCIGCRACVVACKEENNLPVGV----------------TWRRVRRYEEGEFPNVEWLFVPVLCNHCD 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 105 DPGCLKACPSaGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVDRVSVGQEPACVKTCPTGAI 184
Cdd:COG0437    65 DPPCVKVCPT-GATYKREDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVEACPTGAL 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2238914871 185 RFGTKAEMKHLAEERLIDLKKRGyahaglYDPQGVGGTHVMYV 227
Cdd:COG0437   144 VFGDLDDPESEVSKRLAELPAYR------LLPELGTKPSVYYL 180
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 31-226 1.53e-68

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: 211.30  E-value: 1.53e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  31 AKLIDVTTCIGCKACQVACSEWNDIRDEVGHNAGVYDNPADLSAKSWTLMRFSEVeENDRLEWLIRKDGCMHCSDPGCLK 110
Cdd:cd10561     1 GVLYDTTRCIGCRACEVACKEWNGLPAEDTAFGPGWDNPRDLSAKTYTVIKRYEV-ETGGKGFVFVKRQCMHCLDPACVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 111 ACPsAGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRL--NKDDNRVYKCTLCVDRVSVGQEPACVKTCPTGAIRFGT 188
Cdd:cd10561    80 ACP-VGALRKTPEGPVTYDEDKCIGCRYCMVACPFNIPKYewDSANPKIRKCTMCYDRLKEGKQPACVEACPTGALLFGK 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2238914871 189 KAEMKHLAEERLIDLKKRGYAHagLYDPQGVGGTHVMY 226
Cdd:cd10561   159 REELLAEAKRRIAANPGRYVDH--VYGEKEAGGTSVLY 194
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 33-230 8.60e-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: 8.60e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  33 LIDVTTCIGCKACQVACSEWNDIRDEVGHNAGVYDNPADLSAKSWTLMRFSEVE-ENDRLEWLIRKDGCMHCSDPGCLKA 111
Cdd:cd10559     3 LIDTTRCTACRGCQVACKQWNQLPAEQTKNTGSHQNPPDLSANTYKLVRFNEVRnENGKPDWLFFPDQCRHCVTPPCKDA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 112 CPSA-GAIIQ-YANGIVDFQSENCIGC-GYCIAGCPFDIPRLNKDDNRVYKCTLCVDRVSVGQEPACVKTCPTGAIRFGT 188
Cdd:cd10559    83 ADMVpGAVIQdEATGAVVFTEKTAELDfDDVLSACPYNIPRKNEATGRIVKCDMCIDRVSNGLQPACVKACPTGAMNFGD 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2238914871 189 KAEMKHLAEERLIDLKKRgYAHAGLYDPQGVggtHVMYVLHH 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 9.16e-50

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


Pssm-ID: 319870 [Multi-domain]  Cd Length: 136  Bit Score: 161.40  E-value: 9.16e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  33 LIDVTTCIGCKACQVACSEWNDIRDEVGhnagvydnpadlsaksWTLMRFSEVEEndrLEWLIRKDGCMHCSDPGCLKAC 112
Cdd:cd04410     2 VVDLDRCIGCGTCEVACKQEHGLRPGPD----------------WSRIKVIEGGG---LERAFLPVSCMHCEDPPCVKAC 62

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2238914871 113 PSaGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVDRVSVGQEPACVKTCPTGAIRFG 187
Cdd:cd04410    63 PT-GAIYKDEDGIVLIDEDKCIGCGSCVEACPYGAIVFDPEPGKAVKCDLCGDRLDEGLEPACVKACPTGALTFG 136
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 33-187 5.65e-49

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: 159.26  E-value: 5.65e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  33 LIDVTTCIGCKACQVACSEWNDIRDEVghnagvydnpadlsakswtlmRFSEVEENDRLEWLIRKD-----GCMHCSDPG 107
Cdd:cd16371     3 YFDQERCIGCKACEIACKDKNDLPPGV---------------------NWRRVYEYEGGEFPEVFAyflsmSCNHCENPA 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 108 CLKACPsAGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVDRVSVGQEPACVKTCPTGAIRFG 187
Cdd:cd16371    62 CVKVCP-TGAITKREDGIVVVDQDKCIGCGYCVWACPYGAPQYNPETGKMDKCDMCVDRLDEGEKPACVAACPTRALDFG 140
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
30-270 4.19e-44

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 152.90  E-value: 4.19e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  30 VAKLIDVTTCIGCKACQVACSEWNDIRDEVGHNaGVYDNPADLSAKSWTLM---RFSEVEENDRLE--WLIRKDGCMHCS 104
Cdd:PRK10882   38 LGMLYDSTLCVGCQACVTKCQEINFPERNPQGE-QTWDNPDKLSPYTNNIIkvwKSGTGVNKDQEEngYAYIKKQCMHCV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 105 DPGCLKACPsAGAIIQYA-NGIVDFQSENCIGCGYCIAGCPFDIPRLNKDD--NRVYKCTLC----VDRVSVGQEPACVK 177
Cdd:PRK10882  117 DPNCVSVCP-VSALTKDPkTGIVHYDKDVCTGCRYCMVACPFNVPKYDYNNpfGAIHKCELCnqkgVERLDKGGLPGCVE 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 178 TCPTGAIRFGTKAEMKHLAEERL-------------------IDLKKRGYAHAGLYDPQGVGGTHVMYVLHHAdrpslYH 238
Cdd:PRK10882  196 VCPTGAVIFGTREELLAEAKRRLalkpgseyhyprqtlksgdTYLHTVPKYYPHVYGEKEGGGTQVLVLSGVP-----FE 270

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2238914871 239 NL--PDNPQISTPVD-------LWKGILKPLSALGFVATFA 270
Cdd:PRK10882  271 NLglPKLDDLSTGARsehiqhtLYKGMILPLAVLAGLTVLV 311
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 33-187 4.09e-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: 145.75  E-value: 4.09e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  33 LIDVTTCIGCKACQVACSEWNDIRDEVGHNagvydnpadlsaksWTLMRFSEVEENDRLEWLIRkdGCMHCSDPGCLKAC 112
Cdd:cd10551     2 VIDLRKCIGCGACVVACKAENNVPPGVFRN--------------RVLEYEVGEYPNVKRTFLPV--LCNHCENPPCVKVC 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 113 PSaGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVY------------KCTLCVDRVSVGQEPACVKTCP 180
Cdd:cd10551    66 PT-GATYKREDGIVLVDYDKCIGCRYCMAACPYGARYFNPEEPHEFgevpvrpkgvveKCTFCYHRLDEGLLPACVEACP 144


                  ....*..
gi 2238914871 181 TGAIRFG 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 9.24e-35

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


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 122.77  E-value: 9.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  33 LIDVTTCIGCKACQVACSEWNdirdevghnagvydnpadlSAKSwtlmRFSEVEENDRLEWLIRkdgCMHCSDPGCLKAC 112
Cdd:cd16374     2 YVDPERCIGCRACEIACAREH-------------------SGKP----RISVEVVEDLASVPVR---CRHCEDAPCMEVC 55

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2238914871 113 PSaGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVDRVSVGQEPACVKTCPTGAIRFGTKAE 191
Cdd:cd16374    56 PT-GAIYRDEDGAVLVDPDKCIGCGMCAMACPFGVPRFDPSLKVAVKCDLCIDRRREGKLPACVEACPTGALKFGDIEE 133
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 34-200 1.30e-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: 123.65  E-value: 1.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  34 IDVTTCIGCKACQVACSEWnDIRDEVGHNAGVYDNPADLSAKSWTLmrfseveendrlewlirkdgCMHCSDPGCLKACP 113
Cdd:cd16369     6 IDPSRCIGCRACVAACREC-GTHRGKSMIHVDYIDRGESTQTAPTV--------------------CMHCEDPTCAEVCP 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 114 sAGAIIQYANGIV-DFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVDRVSVGQEPACVKTCPTGAIRFGTKAEM 192
Cdd:cd16369    65 -ADAIKVTEDGVVqSALKPRCIGCSNCVNACPFGVPKYDEERNLMMKCDMCYDRTSVGKAPMCASVCPSGALFYGTREEI 143


                  ....*...
gi 2238914871 193 KHLAEERL 200
Cdd:cd16369   144 QALRPGST 151
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 35-188 7.26e-32

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


Pssm-ID: 319875 [Multi-domain]  Cd Length: 146  Bit Score: 115.54  E-value: 7.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  35 DVTTCIGCKACQVACSEWNdirdevghNAGVYDNPADLSAKSWTLmrfseVEENDRLEWLIRKdgCMHCSDPGCLKACPS 114
Cdd:cd10553     8 DSKRCIGCLACEVHCKVKN--------NLPVGPRLCRIFAVGPKM-----VGGKPRLKFVYMS--CFHCENPWCVKACPT 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2238914871 115 AGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVDRVSVGQEPACVKTCPTGAIRFGT 188
Cdd:cd10553    73 GAMQKREKDGIVYVDQELCIGCKACIEACPWGIPQWNPATGKVVKCDYCMDRIDQGLKPACVTGCTTHALSFVR 146
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 91-187 3.79e-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: 106.95  E-value: 3.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  91 LEWLIRKDGCMHCSDPGCLKACPSaGAIIQ-YANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVDRVSV 169
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPV-GAIYKdEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEA 79

                          90
                  ....*....|....*...
gi 2238914871 170 GQEPACVKTCPTGAIRFG 187
Cdd:pfam13247  80 GLLPACVQTCPTGAMNFG 97
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 30-197 5.54e-29

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: 109.82  E-value: 5.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  30 VAKLIDVTTCIGCK-----ACQVACSE-------------------------WNDIRDevghnagVYDNpadLSAKSWTL 79
Cdd:cd16368     1 LATLIDLTKCDGCPgesipACVRACREknqarfpepvskpiqpywprkriedWSDKRD-------VTDR---LTPYNWLY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  80 MRFSEVEENDRLEWLIRKDGCMHCSDPGCLKACPSaGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKD------ 153
Cdd:cd16368    71 VQKLTVDTAGGEKEVFIPRRCMHCDNPPCAKLCPF-GAARKTPEGAVYIDDDLCFGGAKCRDVCPWHIPQRQAGvgiylh 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2238914871 154 -------DNRVYKCTLCVDRVSVGQEPACVKTCPTGAIRFGTKAEMKHLAE 197
Cdd:cd16368   150 lapeyagGGVMYKCDLCKDLLAQGKPPACIEACPKGAQYFGPRKEMVALAR 200
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 33-186 1.33e-27

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


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 103.81  E-value: 1.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  33 LIDVTTCIGCKACQVACSEwndirdevgHNAGVYdNPAdLSAkswtlMRFSEVEENDrlewLIRKDGCMHCSDPGCLKAC 112
Cdd:cd10550     2 VVDPEKCTGCRTCELACSL---------KHEGVF-NPS-LSR-----IRVVRFEPEG----LDVPVVCRQCEDAPCVEAC 61

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2238914871 113 PsAGAIIQ-YANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCvdrvsvGQEPACVKTCPTGAIRF 186
Cdd:cd10550    62 P-VGAISRdEETGAVVVDEDKCIGCGMCVEACPFGAIRVDPETGKAIKCDLC------GGDPACVKVCPTGALEF 129
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 33-187 1.50e-27

CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the iron-sulfur subunit of carbon monoxide dehydrogenase (CODH), found in anaerobic bacteria and archaea. Carbon monoxide dehydrogenase is a key enzyme for carbon monoxide (CO) metabolism, where CooF is the proposed mediator of electron transfer between CODH and the CO-induced hydrogenase, catalyzing the reaction that uses CO as a single carbon and energy source, and producing only H2 and CO2. The ion-sulfur subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons in the protein complex during reaction.


Pssm-ID: 319885 [Multi-domain]  Cd Length: 140  Bit Score: 103.87  E-value: 1.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  33 LIDVTTCIGCKACQVACSewndirdeVGHNAgvYDNPADLSAKSWTLMRFSEVEENDRLEWLIRkdgCMHCSDPGCLKAC 112
Cdd:cd10563     3 FIDEEKCLGCKLCEVACA--------VAHSK--SKDLIKAKLEKERPRPRIRVEESGGRSFPLQ---CRHCDEPPCVKAC 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2238914871 113 PSaGAIIQY-ANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVDRvsvgQEPACVKTCPTGAIRFG 187
Cdd:cd10563    70 MS-GAMHKDpETGIVIHDEEKCVGCWMCVMVCPYGAIRPDKERKVALKCDLCPDR----ETPACVEACPTGALVLE 140
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
13-183 1.63e-24

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 98.79  E-value: 1.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  13 ATNDFTPPPQVRSDKSEVAKLIDVTTCIGCKACQVACSewndirdevghnagvYDNPADLSAKSWTLMRF------SEVE 86
Cdd:PRK14993   27 AKFPFSPERHEGSPRHRYAMLIDLRRCIGCQSCTVSCT---------------IENQTPQGAFRTTVNQYqvqregSQEV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  87 ENDRLEWLirkdgCMHCSDPGCLKACPsAGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVDR 166
Cdd:PRK14993   92 TNVLLPRL-----CNHCDNPPCVPVCP-VQATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHR 165

                         170
                  ....*....|....*..
gi 2238914871 167 VSVGQEPACVKTCPTGA 183
Cdd:PRK14993  166 LEAGLLPACVESCVGGA 182
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
33-186 4.40e-24

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 94.72  E-value: 4.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  33 LIDVTTCIGCKACQVACSewndirdeVGHNAGVYDNPADlsakswtlmrfseveendRLEwLIRKDG------CMHCSDP 106
Cdd:COG1142     6 IADPEKCIGCRTCEAACA--------VAHEGEEGEPFLP------------------RIR-VVRKAGvsapvqCRHCEDA 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 107 GCLKACPsAGAIIQyANGIVDFQSENCIGCGYCIAGCPFDI--PRLNKDDNRVYKCTLCVDRvsvGQEPACVKTCPTGAI 184
Cdd:COG1142    59 PCAEVCP-VGAITR-DDGAVVVDEEKCIGCGLCVLACPFGAitMVGEKSRAVAVKCDLCGGR---EGGPACVEACPTGAL 133


                  ..
gi 2238914871 185 RF 186
Cdd:COG1142   134 RL 135
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 39-186 1.19e-23

HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 93.86  E-value: 1.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  39 CIGCKACQVACSEWNdiRDEVGHNAGVYDNPAdlsakswtlmrfseveeNDRLeWLIRKDG------CMHCSDPGCLKAC 112
Cdd:cd10554     9 CIGCRTCEVACAAAH--SGKGIFEAGTDGLPF-----------------LPRL-RVVKTGEvtapvqCRQCEDAPCANVC 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 113 PsAGAIIQyANGIVDFQSENCIGCGYCIAGCPF---------DIPRLNKDDNR--VYKCTLCVDRvsvGQEPACVKTCPT 181
Cdd:cd10554    69 P-VGAISQ-EDGVVQVDEERCIGCKLCVLACPFgaiemapttVPGVDWERGPRavAVKCDLCAGR---EGGPACVEACPT 143


                  ....*
gi 2238914871 182 GAIRF 186
Cdd:cd10554   144 KALTL 148
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 33-198 1.37e-23

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: 95.09  E-value: 1.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  33 LIDVTTCIGCKACQVACsewndiRDE-VGHNAGVYDNPADLSAKSWtlMRFSEVE--ENDRLEWLIRKDGCMHCSDPGCL 109
Cdd:cd10552     2 VIDVAKCNGCYNCFLAC------KDEhVGNDWPGYAAPQPRHGHFW--MRILRRErgQYPKVDVAYLPVPCNHCDNAPCI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 110 KACPSaGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVDRVSVG-QEPACVKTCPTGAIRFG- 187
Cdd:cd10552    74 KAAKD-GAVYKRDDGIVIIDPEKAKGQKQLVDACPYGAIYWNEELQVPQKCTFCAHLLDDGwKEPRCVQACPTGALRFGk 152

                         170
                  ....*....|..
gi 2238914871 188 -TKAEMKHLAEE 198
Cdd:cd10552   153 lEDEEMAAKAAE 164
FDH3_beta NF038355
formate dehydrogenase FDH3 subunit beta; Members of this family are the beta subunit of the ...
 33-208 2.17e-21

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: 88.97  E-value: 2.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  33 LIDVTTCIGCKACQVACSEWNDIrdevghnagvydnpadlsakSWTLMRFSEVEENDRLEWLIRKD-GCMHCSDPGCLKA 111
Cdd:NF038355    6 LCDTERCIECNGCVVACKNAHEL--------------------PWGINRRRVVTLNDGVPGEKSISvACMHCTDAPCAAV 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 112 CPsAGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDN-----RVYKCTLC-----------------VDRVSV 169
Cdd:NF038355   66 CP-VDCFYIRADGIVLHDKDKCIGCGYCLYACPFGAPQFPKDGAfgargKMDKCTFCaggpeetnseaerekygQNRIAE 144

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2238914871 170 GQEPACVKTCPTGAIRFGTKAEMKHLAEERLIdlkKRGY 208
Cdd:NF038355  145 GKLPLCAEMCSTKALLAGDAEVVADIYRERVV---ARGA 180
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 28-186 7.30e-20

beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several DMSO reductase superfamily, including nitrate reductase A, ethylbenzene dehydrogenase and selenate reductase. DMSO Reductase (DMSOR) family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. . The beta subunits of DMSOR contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system. Nitrate reductase A contains three subunits (the catalytic subunit NarG, the catalytic subunit NarH with four [Fe-S] clusters, and integral membrane subunit NarI) and often forms a respiratory chain with the formate dehydrogenase via the lipid soluble quinol pool. Ethylbenzene dehydrogenase oxidizes the hydrocarbon ethylbenzene to (S)-1-phenylethanol. Selenate reductase catalyzes reduction of selenate to selenite in bacterial species that can obtain energy by respiring anaerobically with selenate as the terminal electron acceptor.


Pssm-ID: 319887 [Multi-domain]  Cd Length: 201  Bit Score: 85.33  E-value: 7.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  28 SEVAKLIDVTTCIGCKACQVACSEWNDIRDEVGHN--AGVYDNPADLSAKSWtlmrfsEVEENDRLEWL----IRKDGCM 101
Cdd:cd16365     1 KQFAAVFNLNKCIGCQTCTVACKNAWTYRKGQEYMwwNNVETKPGGGYPQDW------EVKTIDNGGNTrfffYLQRLCN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 102 HCSDPGCLKACPSAGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVDRVSVGQEPACVKTCPt 181
Cdd:cd16365    75 HCTNPACLAACPRGAIYKREEDGIVLIDQKRCRGYRKCVEQCPYKKIYFNGLSRVSEKCIACYPRIEGGDPTRCMSACV- 153


                  ....*
gi 2238914871 182 GAIRF 186
Cdd:cd16365   154 GRIRL 158
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 39-199 1.13e-19

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 89.04  E-value: 1.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  39 CIGCKACQVACSewndirdeVGHNAGVY-DNPADLSAkswtlmRFSEVEENDRLEWLIrkdgCMHCSDPGCLKACPSaGA 117
Cdd:PRK12769   12 CLGCHACEIACV--------MAHNDEQHvLSQHHFHP------RITVIKHQQQRSAVT----CHHCEDAPCARSCPN-GA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 118 IIQYANGIVDFQsENCIGCGYCIAGCPFDIPRL-------NKDDNRVYKCTLCVDRvsvGQEPACVKTCPTGAIRFGTKA 190
Cdd:PRK12769   73 ISHVDDSIQVNQ-QKCIGCKSCVVACPFGTMQIvltpvaaGKVKATAHKCDLCAGR---ENGPACVENCPADALQLVTEQ 148


                  ....*....
gi 2238914871 191 EMKHLAEER 199
Cdd:PRK12769  149 ALSGMAKSR 157
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 35-201 2.40e-18

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 85.08  E-value: 2.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  35 DVTTCIGCKACQVACSewndirdeVGHNAgvydnpadlsaKSWTLMRfseVEENDRLEWLIRKDG-----CMHCSDPGCL 109
Cdd:PRK12809    8 EAAECIGCHACEIACA--------VAHNQ-----------ENWPLSH---SDFRPRIHVVGKGQAanpvaCHHCNNAPCV 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 110 KACPSAGAIiqYANGIVDFQSENCIGCGYCIAGCPFDIPRLNkdDNRVYKCTLCVDRVSvGQEpACVKTCPTGAIRFGTK 189
Cdd:PRK12809   66 TACPVNALT--FQSDSVQLDEQKCIGCKRCAIACPFGVVEMV--DTIAQKCDLCNQRSS-GTQ-ACIEVCPTQALRLMDD 139

                         170
                  ....*....|..
gi 2238914871 190 AEMKHLAEERLI 201
Cdd:PRK12809  140 KGLQQIKVARQR 151
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 33-185 1.13e-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: 77.73  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  33 LIDVTTCIGCKACQVACSEWNDIRDEVGHNAGVYDNpadlsakswtlmrfseveendrleWLIrKDGCMHCSDPGCLKAC 112
Cdd:cd16367    15 VIDLDRCIRCDNCEKACADTHDGHSRLDRNGLRFGN------------------------LLV-PTACRHCVDPVCMIGC 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2238914871 113 PsAGAIIQYANGIVdFQSENCIGCGYCIAGCPFDIPRLNKDDnrvyKCTLCVDrvsvGQEPACVKTCPTGAIR 185
Cdd:cd16367    70 P-TGAIHRDDGGEV-VISDACCGCGNCASACPYGAIQMVRAV----KCDLCAG----YAGPACVSACPTGAAI 132
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 100-186 3.29e-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: 80.04  E-value: 3.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 100 CMHCSDPGCLKACPSaGAIIQYA-NGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVDRVSVGQEPACVKT 178
Cdd:cd10555   133 CNHCTNPACLAACPR-KAIYKREeDGIVLVDQDRCRGYRYCVEACPYKKIYFNPVEQKSEKCIFCYPRIEKGVAPACARQ 211


                  ....*...
gi 2238914871 179 CPtGAIRF 186
Cdd:cd10555   212 CV-GRIRF 218
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 100-186 5.25e-17

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: 80.10  E-value: 5.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 100 CMHCSDPGCLKACPSaGAIIQYA-NGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVDRVSVGQEPACVKT 178
Cdd:cd10557   179 CNHCLNPACVAACPS-GAIYKREeDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSEKCIFCYPRLEAGQPTVCSET 257


                  ....*...
gi 2238914871 179 CpTGAIRF 186
Cdd:cd10557   258 C-VGRIRY 264
PRK09898 PRK09898
ferredoxin-like protein;
39-185 2.15e-16

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 76.03  E-value: 2.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  39 CIGCKACQVACSEWNDIR------------------DEVGHNAGVYDNpadlsakswtlmrfseveendrleWLIRKDGC 100
Cdd:PRK09898   68 CTGCHRCEISCTNFNDGSvgtffsrikihrnyffgdNGVGSGGGLYGD------------------------LNYTADTC 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 101 MHCSDPGCLKACPSAGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCvdrvsvgqePACVKTCP 180
Cdd:PRK09898  124 RQCKEPQCMNVCPIGAITWQQKEGCITVDHKRCIGCSACTTACPWMMATVNTESKKSSKCVLC---------GECANACP 194


                  ....*
gi 2238914871 181 TGAIR 185
Cdd:PRK09898  195 TGALK 199
Form-deh_trans pfam09163
Formate dehydrogenase N, transmembrane; Members of this family are predominantly found in the ...
 246-282 1.97e-15

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: 68.80  E-value: 1.97e-15
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2238914871 246 ISTPVDLWKGILKPLSALGFVATFAGLIFHYVGIGPN 282
Cdd:pfam09163   1 ISPSVELWKGVLKPLGAAGMGAAALAGFFHYITVGPN 37
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 100-186 3.25e-13

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


Pssm-ID: 440755 [Multi-domain]  Cd Length: 485  Bit Score: 69.45  E-value: 3.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 100 CMHCSDPGCLKACPSaGAIIQYA-NGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVDRVSVGQEPACVKT 178
Cdd:COG1140   182 CEHCLNPACVASCPS-GAIYKREeDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGKAEKCIFCYPRIEAGQPTVCSET 260


                  ....*...
gi 2238914871 179 CpTGAIRF 186
Cdd:COG1140   261 C-VGRIRY 267
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 32-186 1.30e-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: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 63.83  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  32 KLIDVTTCIGCKACQVACSEwndirdEVGHNAGVYDNPADLSAKSWTLMRFSEVEendrlewlirkdgCMHCSDPGCLKA 111
Cdd:cd16370     4 RVKDMERCIGCYSCMLACSR------RVHKSASLSKSAIRVRTRGGLEGGFTVVV-------------CRACEDPPCAEA 64

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2238914871 112 CPSaGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCvdrvsvgqePACVKTCPTGAIRF 186
Cdd:cd16370    65 CPT-GALEPRKGGGVVLDKEKCIGCGNCVKACIVGAIFWDEETNKPIICIHC---------GYCARYCPHDVLAM 129
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 34-185 5.31e-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: 61.97  E-value: 5.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  34 IDVTTCIGCKACQVACSE-WNDIRDevghnagvydnpADLSAkswtlMRFSEVEENDRLewlirkDGCMHCSDpgCLKAC 112
Cdd:cd16372     5 TDPEKCIGCLQCEEACSKtFFKEED------------REKSC-----IRITETEGGYAI------NVCNQCGE--CIDVC 59

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2238914871 113 PsAGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCvdrvsvgqePACVKTCPTGAIR 185
Cdd:cd16372    60 P-TGAITRDANGVVMINKKLCVGCLMCVGFCPEGAMFKHEDYPEPFKCIAC---------GICVKACPTGALE 122
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 100-185 6.92e-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: 64.40  E-value: 6.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 100 CMHCSDPGCLKACPSAGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVDRVSVGQEPACVKTC 179
Cdd:cd10556   141 CNHCTYPACLAACPRKAIYKREEDGIVLIDQERCRGYRECVEACPYKKPMYNPTTRVSEKCIGCYPRIEEGDQTQCVSAC 220


                  ....*.
gi 2238914871 180 PtGAIR 185
Cdd:cd10556   221 I-GKIR 225
PRK10330 PRK10330
electron transport protein HydN;
33-184 5.53e-11

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 60.29  E-value: 5.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  33 LIDVTTCIGCKACQVACSewndirdeVGHNAGvyDNPADLSAKSWtLMRFSEVEENDRLEWLIrkdgCMHCSDPGCLKAC 112
Cdd:PRK10330    6 IADASKCIGCRTCEVACV--------VSHQEN--QDCASLTPETF-LPRIHVIKGVNVSTATV----CRQCEDAPCANVC 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 113 PSaGAIIQyANGIVDFQSENCIGCGYCIAGCPF-------------DIPRLN--KDDNRVYKCTLCVDRVSvgqEPACVK 177
Cdd:PRK10330   71 PN-GAISR-DKGFVHVMQERCIGCKTCVVACPYgamevvvrpvirnSGAGLNvrAEKAEANKCDLCNHRED---GPACMA 145


                  ....*..
gi 2238914871 178 TCPTGAI 184
Cdd:PRK10330  146 ACPTHAL 152
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 96-185 1.22e-07

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: 51.53  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  96 RKDGCMHCSDpgCLKACPSaGAIIQYANGI--VDfqSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTL---CVDRVSVG 170
Cdd:COG2878   135 CEYGCIGCGD--CIKACPF-DAIVGAAKGMhtVD--EDKCTGCGLCVEACPVDCIEMVPVSPTVVVSSWdkgKAVRKVVG 209

                          90
                  ....*....|....*
gi 2238914871 171 QEPACVKTCPTGAIR 185
Cdd:COG2878   210 CIGLCCKKCCPAAAI 224
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
125-193 1.23e-07

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 51.60  E-value: 1.23e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 125 IVDFQSENCIGCGYCIAGCPFDI-PRLNKDDNrvYKCTLCVDrvsvgqepaCVKTCPTGAIRFGTKAEMK 193
Cdd:COG0348   204 RVRYDRGDCIDCGLCVKVCPMGIdIRKGEINQ--SECINCGR---------CIDACPKDAIRFSSRGEKT 262
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 127-202 1.44e-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: 49.32  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 127 DFQSENCIGCGYCIAGCPFDIPRLNKDDNRVY-------KCTLCvdrvsvGqepACVKTCPTGAIRFGT-KAEMKHLAEE 198
Cdd:cd10549     2 KYDPEKCIGCGICVKACPTDAIELGPNGAIARgpeidedKCVFC------G---ACVEVCPTGAIELTPeGKEYVPKEKE 72


                  ....
gi 2238914871 199 RLID 202
Cdd:cd10549    73 AEID 76
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
95-184 2.17e-07

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 51.57  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  95 IRKDGCMHCSDPGCLKACP----SAGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRlnKDDNRVY----KCTLCvdr 166
Cdd:COG4624    51 CPRCCLCCCCCCRCCVAISciqvRGIIIIDKRGPSIIRDKEKCKNCYPCVRACPVKAIK--VDDGKAEideeKCISC--- 125

                          90
                  ....*....|....*...
gi 2238914871 167 vsvGQepaCVKTCPTGAI 184
Cdd:COG4624   126 ---GQ---CVAVCPFGAI 137
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 121-189 2.99e-07

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 47.03  E-value: 2.99e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2238914871 121 YANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRV---YKCTLCVdrvsvgqepACVKTCPTGAIRFGTK 189
Cdd:COG1149     1 VKRKIPVIDEEKCIGCGLCVEVCPEGAIKLDDGGAPVvdpDLCTGCG---------ACVGVCPTGAITLEER 63
NapF COG1145
Ferredoxin [Energy production and conversion];
125-190 4.21e-07

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 50.11  E-value: 4.21e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 125 IVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVY----KCTLCvdrvsvgqePACVKTCPTGAIRFGTKA 190
Cdd:COG1145   176 KAVIDAEKCIGCGLCVKVCPTGAIRLKDGKPQIVvdpdKCIGC---------GACVKVCPVGAISLEPKE 236
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 131-194 5.50e-07

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 46.24  E-value: 5.50e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2238914871 131 ENCIGCGYCIAGCPFDIPRLNKDDNRVY-----KCTLCvdrvsvgqePACVKTCPTGAIRFGTKAEMKH 194
Cdd:COG1146     8 DKCIGCGACVEVCPVDVLELDEEGKKALvinpeECIGC---------GACELVCPVGAITVEDDEPEEQ 67
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
131-186 1.03e-06

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 45.49  E-value: 1.03e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2238914871 131 ENCIGCGYCIAGCPFDIPRLNKDDNRV--YKCTLCvdrvsvgqePACVKTCPTGAIRF 186
Cdd:COG2768    11 EKCIGCGACVKVCPVGAISIEDGKAVIdpEKCIGC---------GACIEVCPVGAIKI 59
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
99-185 3.58e-06

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 47.62  E-value: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  99 GCMHCSDpgCLKACPsAGAI-IQyaNGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVY------------------- 158
Cdd:PRK07118  140 GCLGLGS--CVAACP-FDAIhIE--NGLPVVDEDKCTGCGACVKACPRNVIELIPKSARVFvacnskdkgkavkkvcevg 214

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2238914871 159 --KCTLCV------------DRVSVGQEP-----ACVKTCPTGAIR 185
Cdd:PRK07118  215 ciGCGKCVkacpagaitmenNLAVIDQEKctscgKCVEKCPTKAIR 260
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 23-146 4.71e-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: 45.08  E-value: 4.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  23 VRSDKSEVAKLIDVTTCIGCKACQVACSeWNDIrdevghnagvydnpadlsakswTLMRFSEVEENDRLEWLIRKDGCMH 102
Cdd:cd10549    26 GPNGAIARGPEIDEDKCVFCGACVEVCP-TGAI----------------------ELTPEGKEYVPKEKEAEIDEEKCIG 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2238914871 103 CSDpgCLKACPSaGAIIQYANGIVDFQSENCIGCGYCIAGCPFD 146
Cdd:cd10549    83 CGL--CVKVCPV-DAITLEDELEIVIDKEKCIGCGICAEVCPVN 123
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
94-146 5.26e-06

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 43.57  E-value: 5.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2238914871  94 LIRKDGCMHCSDpgCLKACPsAGAIIQyANGIVDFQSENCIGCGYCIAGCPFD 146
Cdd:COG2768     7 YVDEEKCIGCGA--CVKVCP-VGAISI-EDGKAVIDPEKCIGCGACIEVCPVG 55
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 95-146 6.13e-06

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 43.12  E-value: 6.13e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2238914871  95 IRKDGCMHCSDpgCLKACPSaGAIiQYANGIVDFQSENCIGCGYCIAGCPFD 146
Cdd:COG2221    12 IDEEKCIGCGL--CVAVCPT-GAI-SLDDGKLVIDEEKCIGCGACIRVCPTG 59
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 131-188 7.77e-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: 7.77e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2238914871 131 ENCIGCGYCIAGCPFDIPRLNKDDNRVY------KCTLCVdrvsvgqepACVKTCPTGAIRFGT 188
Cdd:COG1143     2 DKCIGCGLCVRVCPVDAITIEDGEPGKVyvidpdKCIGCG---------LCVEVCPTGAISMTP 56
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 130-189 9.50e-06

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: 46.01  E-value: 9.50e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2238914871 130 SENCIGCGYCIAGCPFDIPRLnkDDNRVY---KCTLCVdrvsvgqepACVKTCPTGAIRFGTK 189
Cdd:NF038196  184 TDKCIGCGICAKVCPVNNIEM--EDGKPVwghNCTHCL---------ACIHRCPKEAIEYGKK 235
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 117-185 1.22e-05

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 42.35  E-value: 1.22e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2238914871 117 AIIQYANGIVDfqSENCIGCGYCIAGCPFDIPRLnkDDNRVY----KCTLCvdrvsvgqePACVKTCPTGAIR 185
Cdd:COG2221     3 GIIGTWPPKID--EEKCIGCGLCVAVCPTGAISL--DDGKLVideeKCIGC---------GACIRVCPTGAIK 62
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
133-191 1.83e-05

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 45.31  E-value: 1.83e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2238914871 133 CIGCGYCIAGCPFD-------IPRLNKDdnrvyKCTLCvdrvsvgqePACVKTCPTGAIRFGTKAE 191
Cdd:PRK07118  141 CLGLGSCVAACPFDaihiengLPVVDED-----KCTGC---------GACVKACPRNVIELIPKSA 192
Fer4_9 pfam13187
4Fe-4S dicluster domain;
132-184 1.97e-05

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 41.39  E-value: 1.97e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2238914871 132 NCIGCGYCIAGCPFDI------PRLNKDDNRVYKCTLCVdrvsvgqepACVKTCPTGAI 184
Cdd:pfam13187   1 KCTGCGACVAACPAGAivpdlvGQTIRGDIAGLACIGCG---------ACVDACPRGAI 50
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 97-193 2.05e-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: 43.15  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  97 KDGCMHCSDpgCLKACPsAGAIIQYANGIV----DFQSENCIGCGYCIAGCPFDIPRLNKDdnrvYKCTLCVDRVSVGQE 172
Cdd:cd10549     5 PEKCIGCGI--CVKACP-TDAIELGPNGAIargpEIDEDKCVFCGACVEVCPTGAIELTPE----GKEYVPKEKEAEIDE 77

                          90       100
                  ....*....|....*....|....*..
gi 2238914871 173 P------ACVKTCPTGAIRFGTKAEMK 193
Cdd:cd10549    78 EkcigcgLCVKVCPVDAITLEDELEIV 104
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 93-144 2.14e-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: 41.47  E-value: 2.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2238914871  93 WLIRKDGCMHCsdPGCLKACPSAGAI-----IQYANGIVDFQSENCIGCGYCIAGCP 144
Cdd:pfam13237   2 VVIDPDKCIGC--GRCTAACPAGLTRvgaivERLEGEAVRIGVWKCIGCGACVEACP 56
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
131-186 4.04e-05

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 44.85  E-value: 4.04e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2238914871 131 ENCIGCGYCIAGCPFDIPRLNKDDNRVY---KCTLCvdrvsvGqepACVKTCPTGAIRF 186
Cdd:COG1148   496 EKCTGCGRCVEVCPYGAISIDEKGVAEVnpaLCKGC------G---TCAAACPSGAISL 545
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 131-185 4.56e-05

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 40.80  E-value: 4.56e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2238914871 131 ENCIGCGYCIAGCPFDIprLNKDDNRVY----KCTLCVdrvsvgqepACVKTCPTGAIR 185
Cdd:COG4231    22 DKCTGCGACVKVCPADA--IEEGDGKAVidpdLCIGCG---------SCVQVCPVDAIK 69
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 95-146 1.05e-04

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 39.71  E-value: 1.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2238914871  95 IRKDGCMHCSDpgCLKACPsAGAIIQYANGIVDFQSENCIGCGYCIAGCPFD 146
Cdd:COG1149     8 IDEEKCIGCGL--CVEVCP-EGAIKLDDGGAPVVDPDLCTGCGACVGVCPTG 56
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 84-186 1.14e-04

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 41.23  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  84 EVEEND--RLEWLIRKDGCMHCsdpG-CLKACPSaGAIIQYANGIVDF--------QSENCIGCGYCIAGCPFDIPRLNK 152
Cdd:cd10549    24 ELGPNGaiARGPEIDEDKCVFC---GaCVEVCPT-GAIELTPEGKEYVpkekeaeiDEEKCIGCGLCVKVCPVDAITLED 99

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2238914871 153 DDNRVY---KCTLCvdrvsvgqePACVKTCPTGAIRF 186
Cdd:cd10549   100 ELEIVIdkeKCIGC---------GICAEVCPVNAIKL 127
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 100-147 1.67e-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: 38.66  E-value: 1.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2238914871 100 CMHCSDpgCLKACPSA-----GAIIQYANGIVDFQSENCIGCGYCIAGCPFDI 147
Cdd:pfam12838   1 CIGCGA--CVAACPVGaitldEVGEKKGTKTVVIDPERCVGCGACVAVCPTGA 51
Fer COG1141
Ferredoxin [Energy production and conversion];
131-185 4.81e-04

Ferredoxin [Energy production and conversion];


Pssm-ID: 440756 [Multi-domain]  Cd Length: 63  Bit Score: 37.55  E-value: 4.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2238914871 131 ENCIGCGYCIAGCPfDIPRLNKDDnrvyKCTLCVDRVSVGQEPAC---VKTCPTGAIR 185
Cdd:COG1141     8 DTCIGCGLCVALAP-EVFELDDDG----KAVVLDEEVPEELEEDVreaADACPVGAIT 60
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 133-193 5.64e-04

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 39.55  E-value: 5.64e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2238914871 133 CIGCGYCIAGCPFDI---------------PRLnkdDNRVYKCTLCVDrvsvgqepACVKTCPTGAIRFGTKAEMK 193
Cdd:cd16373    16 CIRCGLCVEACPTGViqpagledgleggrtPYL---DPREGPCDLCCD--------ACVEVCPTGALRPLDLEEQK 80
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 133-183 7.63e-04

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 36.74  E-value: 7.63e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 133 CIGCGYCIAGCPFDIPRLNKDDN---------RVYKCTLCvdrvsvgqePACVKTCPTGA 183
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEkkgtktvviDPERCVGC---------GACVAVCPTGA 51
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
95-151 1.40e-03

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 39.84  E-value: 1.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2238914871  95 IRKDGCMHCSdpGCLKACPsAGAIIQYANGIVDFQSENCIGCGYCIAGCPFDIPRLN 151
Cdd:COG1148   493 VDPEKCTGCG--RCVEVCP-YGAISIDEKGVAEVNPALCKGCGTCAAACPSGAISLK 546
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 131-227 1.57e-03

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


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 39.68  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 131 ENCIGCGYCIAGCPF--------DIPR-----------------LNKDDNRV-YKCTLCvdRvsvgqepACVKTCPTGaI 184
Cdd:COG0247    78 DACVGCGFCRAMCPSykatgdekDSPRgrinllrevlegelpldLSEEVYEVlDLCLTC--K-------ACETACPSG-V 147

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2238914871 185 RFGT-KAEMK-HLAEERLIDLKKRGYAH-AGLYDPQGVGGTHVMYV 227
Cdd:COG0247   148 DIADlIAEARaQLVERGGRPLRDRLLRTfPDRVPAADKEGAEVLLF 193
PRK13795 PRK13795
hypothetical protein; Provisional
 83-144 1.58e-03

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 39.98  E-value: 1.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2238914871  83 SEVEENDRLewLIRKDGCMHCsdpG-CLKACPSAGAIIQYANGIVDFQSENCIGCGYCIAGCP 144
Cdd:PRK13795  568 SLFKDAARL--LRRAAECVGC---GvCVGACPTGAIRIEEGKRKISVDEEKCIHCGKCTEVCP 625
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
 131-207 1.83e-03

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 38.47  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871 131 ENCIGCGYCIAGCPFDIPRLNKDD---NRVY-----KCTLCvdrvsvGQepaCVKTCPTGAIRFGTKAEmkhLAEERLID 202
Cdd:PRK12387   38 QQCIGCAACVNACPSNALTVETDLatgELAWefnlgRCIFC------GR---CEEVCPTAAIKLSQEFE---LAVWKKED 105


                  ....*
gi 2238914871 203 LKKRG 207
Cdd:PRK12387  106 LLQQS 110
flavo_MJ0208 TIGR02700
archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of ...
 91-146 2.13e-03

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: 38.70  E-value: 2.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2238914871  91 LEWLIRKDGCMHCSDpgCLKACPSaGAIIQyANGIVDFQSENCIGCGYCIAGCPFD 146
Cdd:TIGR02700 141 TPYMIDRKRCKGCGI--CVDACPR-SAIDM-VDGKAFIRLLKCVGCGKCKEACPYN 192
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 97-146 2.36e-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: 35.88  E-value: 2.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2238914871  97 KDGCMHCSDpgCLKACPsAGAIIQYANG---IVDFQSENCIGCGYCIAGCPFD 146
Cdd:COG1143     1 EDKCIGCGL--CVRVCP-VDAITIEDGEpgkVYVIDPDKCIGCGLCVEVCPTG 50
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 128-184 2.88e-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: 36.18  E-value: 2.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2238914871 128 FQSENCIGCGYCIAGCPFDIprLNKDDNRVY-----KCTLCvdrvsvgqePACVKTCPTGAI 184
Cdd:COG1144    27 VDEDKCIGCGLCWIVCPDGA--IRVDDGKYYgidydYCKGC---------GICAEVCPVKAI 77
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 131-197 4.37e-03

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: 36.84  E-value: 4.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2238914871 131 ENCIGCGYCIAGCPFDI--------PRLNKDDNrvyKCTLCvdrvsvgqePACVKTCPTGAIRFGTKAEMKHLAE 197
Cdd:cd10564    13 DLCTRCGDCVEACPEGIivrgdggfPELDFSRG---ECTFC---------GACAEACPEGALDPAREAPWPLRAE 75
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
123-188 4.80e-03

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 36.56  E-value: 4.80e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2238914871 123 NGIVDFQSENCIGCGYCIAGCPF---------DIPRL----NKDDNRVYKCTLCVDRvsvgqepACVKTCPTGAIRFGT 188
Cdd:COG1142     2 NKFIIADPEKCIGCRTCEAACAVahegeegepFLPRIrvvrKAGVSAPVQCRHCEDA-------PCAEVCPVGAITRDD 73
PRK00783 PRK00783
DNA-directed RNA polymerase subunit D; Provisional
 130-185 6.17e-03

DNA-directed RNA polymerase subunit D; Provisional


Pssm-ID: 234837 [Multi-domain]  Cd Length: 263  Bit Score: 37.56  E-value: 6.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2238914871 130 SENCIGCGYCIAGCPFDIPRLNKDDNRV---YKCTLCvdrvsvgqePACVKTCPTGAIR 185
Cdd:PRK00783  168 SEDCDECEKCVEACPRGVLELKEGKLVVtdlLNCSLC---------KLCERACPGKAIR 217
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 98-186 7.60e-03

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: 36.07  E-value: 7.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  98 DGCMHCSDpgCLKACPSaGAIIQYANGI--VDFQSENCIGCGYCIAGCP---FDIPR--------------LNKddNRVY 158
Cdd:cd10564    13 DLCTRCGD--CVEACPE-GIIVRGDGGFpeLDFSRGECTFCGACAEACPegaLDPAReapwplraeigdscLAL--QGVE 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2238914871 159 kCTLCVD-----------RVSVGQEP-----------ACVKTCPTGAIRF 186
Cdd:cd10564    88 -CRSCQDacptqairfrpRLGGIALPeldadactgcgACVSVCPVGAITL 136
Fer4_9 pfam13187
4Fe-4S dicluster domain;
100-147 9.50e-03

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 33.68  E-value: 9.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2238914871 100 CMHCSDpgCLKACPsAGAIIQYANG---IVDFQSENCIGCGYCIAGCPFDI 147
Cdd:pfam13187   2 CTGCGA--CVAACP-AGAIVPDLVGqtiRGDIAGLACIGCGACVDACPRGA 49
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
99-168 9.50e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 36.83  E-value: 9.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2238914871  99 GCMHCSDpgCLKACPsAGAIIQyANGIVDFQSENCIGCGYCIAGCPFDIPRLNKDDNRVYKCTLCVDRVS 168
Cdd:PRK07118  214 GCIGCGK--CVKACP-AGAITM-ENNLAVIDQEKCTSCGKCVEKCPTKAIRILNKPPKVKEPKKAAAEAA 279
 
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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