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Conserved domains on  [gi|498485091|ref|WP_010786847|]
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formate dehydrogenase subunit beta [Glaesserella parasuis]

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 ...
 8-286 8.01e-179

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: 494.81  E-value: 8.01e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091    8 DIIKSSAISflTPPPQARSHQVEVAKLIDVTTCIGCKACQVGCSEWNDIRSTPDAACTGVYDNPADLNPKAWTVMRFNEV 87
Cdd:TIGR01582   1 DIKRLSATK--EPDPSVKTYPTELAKLIDVSSCIGCKACQAACQEWNDTTPPILSRKVGGYQNPPDLLPETFTLMRFKEG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091   88 EENDRLEWLIRKDGCMHCSEPGCLKACPSPGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVD 167
Cdd:TIGR01582  79 EESDGLEWLIRKDGCMHCREPGCLKACPAPGAIIQYQNGIVDFDHSKCIGCGYCIVGCPFNIPRYDKVDNRPYKCTLCID 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  168 RVTVGQEPACVKTCPTGAIRFGSKEEMKEYASKRIADLKSRGYENAGLYDPEGVGGTHVMYVLHHADKPELYSGLPKDPQ 247
Cdd:TIGR01582 159 RVSVGQEPACVKTCPTNAISFGFKEDMKERAEKRVADLKSRGYPNAGLYDPPGVGGTHVMYVLHHGDKPKDYQDLPEDPR 238

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 498485091  248 IDLSVTLWKDVLKPVAAVAMGGLVLSEIAHYIAIGPNTE 286
Cdd:TIGR01582 239 IDASVGLWKGVLKTIGSIAMGGTALGVFLHLILWGPNKV 277
 
Name Accession Description Interval E-value
FDH-beta TIGR01582
formate dehydrogenase, beta subunit, Fe-S containing; This model represents the beta subunit ...
 8-286 8.01e-179

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: 494.81  E-value: 8.01e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091    8 DIIKSSAISflTPPPQARSHQVEVAKLIDVTTCIGCKACQVGCSEWNDIRSTPDAACTGVYDNPADLNPKAWTVMRFNEV 87
Cdd:TIGR01582   1 DIKRLSATK--EPDPSVKTYPTELAKLIDVSSCIGCKACQAACQEWNDTTPPILSRKVGGYQNPPDLLPETFTLMRFKEG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091   88 EENDRLEWLIRKDGCMHCSEPGCLKACPSPGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVD 167
Cdd:TIGR01582  79 EESDGLEWLIRKDGCMHCREPGCLKACPAPGAIIQYQNGIVDFDHSKCIGCGYCIVGCPFNIPRYDKVDNRPYKCTLCID 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  168 RVTVGQEPACVKTCPTGAIRFGSKEEMKEYASKRIADLKSRGYENAGLYDPEGVGGTHVMYVLHHADKPELYSGLPKDPQ 247
Cdd:TIGR01582 159 RVSVGQEPACVKTCPTNAISFGFKEDMKERAEKRVADLKSRGYPNAGLYDPPGVGGTHVMYVLHHGDKPKDYQDLPEDPR 238

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 498485091  248 IDLSVTLWKDVLKPVAAVAMGGLVLSEIAHYIAIGPNTE 286
Cdd:TIGR01582 239 IDASVGLWKGVLKTIGSIAMGGTALGVFLHLILWGPNKV 277
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 32-240 3.63e-144

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: 404.08  E-value: 3.63e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  32 AKLIDVTTCIGCKACQVGCSEWNDIRsTPDAACTGVYDNPADLNPKAWTVMRFNEVEENDRLEWLIRKDGCMHCSEPGCL 111
Cdd:cd10558    1 AKLIDVSKCIGCKACQVACKEWNDLR-AEVGHNVGTYQNPADLSPETWTLMKFREVEDNGKLEWLIRKDGCMHCADPGCL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 112 KACPSPGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVDRVTVGQEPACVKTCPTGAIRFGSK 191
Cdd:cd10558   80 KACPSPGAIVQYANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVGLEPACVKTCPTGALHFGTK 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 498485091 192 EEMKEYASKRIADLKSRGYENAGLYDPEGVGGTHVMYVLHHADKPELYS 240
Cdd:cd10558  160 EDMLALAEKRVAALKERGYTNAGLYDPKGVGGTHVMYVLHHADKPEGYP 208
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 32-229 6.67e-70

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 214.81  E-value: 6.67e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  32 AKLIDVTTCIGCKACQVGCSEWNDIrstpdaactgvydnPADLNpkaWTVMRFNEVEENDRLEWLIRKDGCMHCSEPGCL 111
Cdd:COG0437    7 GMVIDLTKCIGCRACVVACKEENNL--------------PVGVT---WRRVRRYEEGEFPNVEWLFVPVLCNHCDDPPCV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 112 KACPSpGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVDRVTVGQEPACVKTCPTGAIRFGSK 191
Cdd:COG0437   70 KVCPT-GATYKREDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVEACPTGALVFGDL 148

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 498485091 192 EEMKEYASKRIADLKSRGyenaglYDPEGVGGTHVMYV 229
Cdd:COG0437  149 DDPESEVSKRLAELPAYR------LLPELGTKPSVYYL 180
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
20-239 1.57e-43

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 151.75  E-value: 1.57e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  20 PPPQArshqveVAKLIDVTTCIGCKACQVGCSEWNDIRSTPDAActGVYDNPADLNPKAWTVM---RFNEVEENDRLE-- 94
Cdd:PRK10882  33 PIPGA------LGMLYDSTLCVGCQACVTKCQEINFPERNPQGE--QTWDNPDKLSPYTNNIIkvwKSGTGVNKDQEEng 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  95 WLIRKDGCMHCSEPGCLKACPSpGAIIQYA-NGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDH--RVYKCTLC----VD 167
Cdd:PRK10882 105 YAYIKKQCMHCVDPNCVSVCPV-SALTKDPkTGIVHYDKDVCTGCRYCMVACPFNVPKYDYNNPfgAIHKCELCnqkgVE 183

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498485091 168 RVTVGQEPACVKTCPTGAIRFGSKEEMKEYASKRIAdlKSRGYENAGLYDPEGVGGTHVMYVLHHadKPELY 239
Cdd:PRK10882 184 RLDKGGLPGCVEVCPTGAVIFGTREELLAEAKRRLA--LKPGSEYHYPRQTLKSGDTYLHTVPKY--YPHVY 251
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 93-189 2.46e-30

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


Pssm-ID: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 110.03  E-value: 2.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091   93 LEWLIRKDGCMHCSEPGCLKACPSpGAIIQ-YANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVDRVTV 171
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPV-GAIYKdEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEA 79

                          90
                  ....*....|....*...
gi 498485091  172 GQEPACVKTCPTGAIRFG 189
Cdd:pfam13247  80 GLLPACVQTCPTGAMNFG 97
FDH3_beta NF038355
formate dehydrogenase FDH3 subunit beta; Members of this family are the beta subunit of the ...
 34-210 3.64e-19

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: 83.19  E-value: 3.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  34 LIDVTTCIGCKACQVGCSEWNDIrstpdaactgvydnPADLNPKawTVMRFNEVEENDRLEWLirkdGCMHCSEPGCLKA 113
Cdd:NF038355   6 LCDTERCIECNGCVVACKNAHEL--------------PWGINRR--RVVTLNDGVPGEKSISV----ACMHCTDAPCAAV 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 114 CPSpGAIIQYANGIVDFQSDKCIGCGYCIAGCPF---NIPRMNPEDHR--VYKCTLC-----------------VDRVTV 171
Cdd:NF038355  66 CPV-DCFYIRADGIVLHDKDKCIGCGYCLYACPFgapQFPKDGAFGARgkMDKCTFCaggpeetnseaerekygQNRIAE 144

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 498485091 172 GQEPACVKTCPTGAIRFGSKEEMKEYASKRIAdlkSRGY 210
Cdd:NF038355 145 GKLPLCAEMCSTKALLAGDAEVVADIYRERVV---ARGA 180
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 132-196 1.97e-07

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: 51.01  E-value: 1.97e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498485091 132 SDKCIGCGYCIAGCPFNIPRMnpEDHRVY---KCTLCVdrvtvgqepACVKTCPTGAIRFGSKEEMKE 196
Cdd:NF038196 184 TDKCIGCGICAKVCPVNNIEM--EDGKPVwghNCTHCL---------ACIHRCPKEAIEYGKKTKKKG 240
 
Name Accession Description Interval E-value
FDH-beta TIGR01582
formate dehydrogenase, beta subunit, Fe-S containing; This model represents the beta subunit ...
 8-286 8.01e-179

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: 494.81  E-value: 8.01e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091    8 DIIKSSAISflTPPPQARSHQVEVAKLIDVTTCIGCKACQVGCSEWNDIRSTPDAACTGVYDNPADLNPKAWTVMRFNEV 87
Cdd:TIGR01582   1 DIKRLSATK--EPDPSVKTYPTELAKLIDVSSCIGCKACQAACQEWNDTTPPILSRKVGGYQNPPDLLPETFTLMRFKEG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091   88 EENDRLEWLIRKDGCMHCSEPGCLKACPSPGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVD 167
Cdd:TIGR01582  79 EESDGLEWLIRKDGCMHCREPGCLKACPAPGAIIQYQNGIVDFDHSKCIGCGYCIVGCPFNIPRYDKVDNRPYKCTLCID 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  168 RVTVGQEPACVKTCPTGAIRFGSKEEMKEYASKRIADLKSRGYENAGLYDPEGVGGTHVMYVLHHADKPELYSGLPKDPQ 247
Cdd:TIGR01582 159 RVSVGQEPACVKTCPTNAISFGFKEDMKERAEKRVADLKSRGYPNAGLYDPPGVGGTHVMYVLHHGDKPKDYQDLPEDPR 238

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 498485091  248 IDLSVTLWKDVLKPVAAVAMGGLVLSEIAHYIAIGPNTE 286
Cdd:TIGR01582 239 IDASVGLWKGVLKTIGSIAMGGTALGVFLHLILWGPNKV 277
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 32-240 3.63e-144

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: 404.08  E-value: 3.63e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  32 AKLIDVTTCIGCKACQVGCSEWNDIRsTPDAACTGVYDNPADLNPKAWTVMRFNEVEENDRLEWLIRKDGCMHCSEPGCL 111
Cdd:cd10558    1 AKLIDVSKCIGCKACQVACKEWNDLR-AEVGHNVGTYQNPADLSPETWTLMKFREVEDNGKLEWLIRKDGCMHCADPGCL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 112 KACPSPGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVDRVTVGQEPACVKTCPTGAIRFGSK 191
Cdd:cd10558   80 KACPSPGAIVQYANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVGLEPACVKTCPTGALHFGTK 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 498485091 192 EEMKEYASKRIADLKSRGYENAGLYDPEGVGGTHVMYVLHHADKPELYS 240
Cdd:cd10558  160 EDMLALAEKRVAALKERGYTNAGLYDPKGVGGTHVMYVLHHADKPEGYP 208
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 34-247 7.15e-83

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: 249.61  E-value: 7.15e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  34 LIDVTTCIGCKACQVGCSEWNDIRSTPDAACTGVYDNPADLNPKAWTVMRF-------NEVEENDRLEWLIRKDGCMHCS 106
Cdd:cd10560    3 FTDTSICIGCKACEVACKQWNQLPADGYDFSGMSYDNTGDLSASTWRHVKFierptedGPANEGGDLQWLFMSDVCKHCT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 107 EPGCLKACPSpGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVDRVTVGQEPACVKTCPTGAI 186
Cdd:cd10560   83 DAGCLEACPT-GAIFRTEFGTVYIQPDICNGCGYCVAACPFGVIDRNEETGRAHKCTLCYDRLKDGLEPACAKACPTGSI 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498485091 187 RFGSKEEMKEYASKRIADLKSRGYENAGLY--DP-EGVGGTHVMYVLhhADKPELYsGLPKDPQ 247
Cdd:cd10560  162 QFGPLEELRERARARVEQLHEQGVVEAYLYgaDPtEGYGGLNAFFLL--LDKPEVY-GLPADPL 222
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 33-189 5.87e-82

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: 244.62  E-value: 5.87e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  33 KLIDVTTCIGCKACQVGCSEWNDIRSTPdAACTGVYDNPADLNPKAWTVMRFNEVEEND-RLEWLIRKDGCMHCSEPGCL 111
Cdd:cd16366    1 FLVDTSRCTGCRACQVACKQWNGLPAEK-TEFTGSYQNPPDLTAHTWTLVRFYEVEKPGgDLSWLFRKDQCMHCTDAGCL 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498485091 112 KACPSpGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVDRVTVGQEPACVKTCPTGAIRFG 189
Cdd:cd16366   80 AACPT-GAIIRTETGTVVVDPETCIGCGYCVNACPFDIPRFDEETGRVAKCTLCYDRISNGLQPACVKTCPTGALTFG 156
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 33-194 3.27e-74

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: 224.87  E-value: 3.27e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  33 KLIDVTTCIGCKACQVGCSEWNDIRSTPDAAcTGVYDNPADLNPKAWTVMRFNEVEE-NDRLEWLIRKDGCMHCSEPGCL 111
Cdd:cd10562    1 MLVDTSKCTACRGCQVACKQWNQLPAEKTPF-TGSYQNPPDLTPNTWTLIRFYEHEEdNGGIRWLFRKRQCMHCTDAACV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 112 KACPSpGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVDRVTVGQEPACVKTCPTGAIRFGSK 191
Cdd:cd10562   80 KVCPT-GALYKTENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCFDRIENGMQPACVKTCPTGALTFGDR 158


                 ...
gi 498485091 192 EEM 194
Cdd:cd10562  159 DEL 161
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 32-229 6.67e-70

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 214.81  E-value: 6.67e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  32 AKLIDVTTCIGCKACQVGCSEWNDIrstpdaactgvydnPADLNpkaWTVMRFNEVEENDRLEWLIRKDGCMHCSEPGCL 111
Cdd:COG0437    7 GMVIDLTKCIGCRACVVACKEENNL--------------PVGVT---WRRVRRYEEGEFPNVEWLFVPVLCNHCDDPPCV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 112 KACPSpGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVDRVTVGQEPACVKTCPTGAIRFGSK 191
Cdd:COG0437   70 KVCPT-GATYKREDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVEACPTGALVFGDL 148

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 498485091 192 EEMKEYASKRIADLKSRGyenaglYDPEGVGGTHVMYV 229
Cdd:COG0437  149 DDPESEVSKRLAELPAYR------LLPELGTKPSVYYL 180
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 32-228 5.36e-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: 210.53  E-value: 5.36e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  32 AKLIDVTTCIGCKACQVGCSEWNDIrSTPDAACTGVYDNPADLNPKAWTVMRFNEVEeNDRLEWLIRKDGCMHCSEPGCL 111
Cdd:cd10561    1 GVLYDTTRCIGCRACEVACKEWNGL-PAEDTAFGPGWDNPRDLSAKTYTVIKRYEVE-TGGKGFVFVKRQCMHCLDPACV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 112 KACPSpGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRM-----NPedhRVYKCTLCVDRVTVGQEPACVKTCPTGAI 186
Cdd:cd10561   79 SACPV-GALRKTPEGPVTYDEDKCIGCRYCMVACPFNIPKYewdsaNP---KIRKCTMCYDRLKEGKQPACVEACPTGAL 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 498485091 187 RFGSKEEMKEYASKRIADLKSRGYENagLYDPEGVGGTHVMY 228
Cdd:cd10561  155 LFGKREELLAEAKRRIAANPGRYVDH--VYGEKEAGGTSVLY 194
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 34-232 7.57e-63

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: 197.66  E-value: 7.57e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  34 LIDVTTCIGCKACQVGCSEWNDIRSTPDAAcTGVYDNPADLNPKAWTVMRFNEVE-ENDRLEWLIRKDGCMHCSEPGCLK 112
Cdd:cd10559    3 LIDTTRCTACRGCQVACKQWNQLPAEQTKN-TGSHQNPPDLSANTYKLVRFNEVRnENGKPDWLFFPDQCRHCVTPPCKD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 113 ACPS-PGAIIQ-YANGIVDF-QSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVDRVTVGQEPACVKTCPTGAIRFG 189
Cdd:cd10559   82 AADMvPGAVIQdEATGAVVFtEKTAELDFDDVLSACPYNIPRKNEATGRIVKCDMCIDRVSNGLQPACVKACPTGAMNFG 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 498485091 190 SKEEMKEYASKRIADLKSRgYENAGLYDPEGVggtHVMYVLHH 232
Cdd:cd10559  162 DRDEMLAMASKRLEELKKR-YPKANLYDPDDV---RVIWLLAE 200
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 34-189 3.41e-49

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


Pssm-ID: 319870 [Multi-domain]  Cd Length: 136  Bit Score: 160.25  E-value: 3.41e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  34 LIDVTTCIGCKACQVGCSEWNDIRSTPDAACTgvydnpadlnpkawtvmrfnEVEENDRLEWLIRKDGCMHCSEPGCLKA 113
Cdd:cd04410    2 VVDLDRCIGCGTCEVACKQEHGLRPGPDWSRI--------------------KVIEGGGLERAFLPVSCMHCEDPPCVKA 61

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498485091 114 CPSpGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVDRVTVGQEPACVKTCPTGAIRFG 189
Cdd:cd04410   62 CPT-GAIYKDEDGIVLIDEDKCIGCGSCVEACPYGAIVFDPEPGKAVKCDLCGDRLDEGLEPACVKACPTGALTFG 136
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 34-189 1.36e-46

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: 153.49  E-value: 1.36e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  34 LIDVTTCIGCKACQVGCSEWNDIRSTPdaactgvydnpadlnpkawtvmRFNEVEENDRLEWLIRKD-----GCMHCSEP 108
Cdd:cd16371    3 YFDQERCIGCKACEIACKDKNDLPPGV----------------------NWRRVYEYEGGEFPEVFAyflsmSCNHCENP 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 109 GCLKACPSpGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVDRVTVGQEPACVKTCPTGAIRF 188
Cdd:cd16371   61 ACVKVCPT-GAITKREDGIVVVDQDKCIGCGYCVWACPYGAPQYNPETGKMDKCDMCVDRLDEGEKPACVAACPTRALDF 139


                 .
gi 498485091 189 G 189
Cdd:cd16371  140 G 140
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
20-239 1.57e-43

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 151.75  E-value: 1.57e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  20 PPPQArshqveVAKLIDVTTCIGCKACQVGCSEWNDIRSTPDAActGVYDNPADLNPKAWTVM---RFNEVEENDRLE-- 94
Cdd:PRK10882  33 PIPGA------LGMLYDSTLCVGCQACVTKCQEINFPERNPQGE--QTWDNPDKLSPYTNNIIkvwKSGTGVNKDQEEng 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  95 WLIRKDGCMHCSEPGCLKACPSpGAIIQYA-NGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDH--RVYKCTLC----VD 167
Cdd:PRK10882 105 YAYIKKQCMHCVDPNCVSVCPV-SALTKDPkTGIVHYDKDVCTGCRYCMVACPFNVPKYDYNNPfgAIHKCELCnqkgVE 183

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498485091 168 RVTVGQEPACVKTCPTGAIRFGSKEEMKEYASKRIAdlKSRGYENAGLYDPEGVGGTHVMYVLHHadKPELY 239
Cdd:PRK10882 184 RLDKGGLPGCVEVCPTGAVIFGTREELLAEAKRRLA--LKPGSEYHYPRQTLKSGDTYLHTVPKY--YPHVY 251
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 34-208 1.01e-41

polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial polysulfide reductase (PsrABC), an integral membrane-bound enzyme responsible for quinone-coupled reduction of polysulfides, a process important in extreme environments such as deep-sea vents and hot springs. Polysulfide reductase contains three subunits: a catalytic subunit PsrA, an electron transfer PsrB subunit and the hydrophobic transmembrane PsrC subunit. PsrB belongs to the DMSO reductase superfamily that contains [4Fe-4S] clusters which transfer the electrons from the A subunit to the hydrophobic integral membrane C subunit via the B subunit. In Shewanella oneidensis, which has highly diverse anaerobic respiratory pathways, PsrABC is responsible for H2S generation as well as its regulation via respiration of sulfur species. PsrB transfers electrons from PsrC (serving as quinol oxidase) to the catalytic subunit PsrA for reduction of corresponding electron acceptors. It has been shown that T. thermophilus polysulfide reductase could be a key energy-conserving enzyme of the respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane.


Pssm-ID: 319873 [Multi-domain]  Cd Length: 185  Bit Score: 142.67  E-value: 1.01e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  34 LIDVTTCIGCKACQVGCSEWNDIRstpdaacTGVYdnpadlnpkaWTVMRFNEVEE--NDRLEWLIRkdGCMHCSEPGCL 111
Cdd:cd10551    2 VIDLRKCIGCGACVVACKAENNVP-------PGVF----------RNRVLEYEVGEypNVKRTFLPV--LCNHCENPPCV 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 112 KACPSpGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPED------------HRVYKCTLCVDRVTVGQEPACVK 179
Cdd:cd10551   63 KVCPT-GATYKREDGIVLVDYDKCIGCRYCMAACPYGARYFNPEEphefgevpvrpkGVVEKCTFCYHRLDEGLLPACVE 141

                        170       180
                 ....*....|....*....|....*....
gi 498485091 180 TCPTGAIRFGSKEEMKEYASKRIADLKSR 208
Cdd:cd10551  142 ACPTGARIFGDLDDPNSEVSKLLAERRAY 170
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 36-190 5.66e-33

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


Pssm-ID: 319875 [Multi-domain]  Cd Length: 146  Bit Score: 118.62  E-value: 5.66e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  36 DVTTCIGCKACQVGCSEWNDIRSTPdAACTGVYDNPADLNPKAWTVMRFNEveendrlewlirkdgCMHCSEPGCLKACP 115
Cdd:cd10553    8 DSKRCIGCLACEVHCKVKNNLPVGP-RLCRIFAVGPKMVGGKPRLKFVYMS---------------CFHCENPWCVKACP 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498485091 116 SpGAIIQY-ANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVDRVTVGQEPACVKTCPTGAIRFGS 190
Cdd:cd10553   72 T-GAMQKReKDGIVYVDQELCIGCKACIEACPWGIPQWNPATGKVVKCDYCMDRIDQGLKPACVTGCTTHALSFVR 146
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 34-193 2.81e-32

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


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 116.61  E-value: 2.81e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  34 LIDVTTCIGCKACQVGCSEWNDIRStpdaactgvydnpadlnpkawtvmRFNEVEENDRLEWLIRkdgCMHCSEPGCLKA 113
Cdd:cd16374    2 YVDPERCIGCRACEIACAREHSGKP------------------------RISVEVVEDLASVPVR---CRHCEDAPCMEV 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 114 CPSpGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVDRVTVGQEPACVKTCPTGAIRFGSKEE 193
Cdd:cd16374   55 CPT-GAIYRDEDGAVLVDPDKCIGCGMCAMACPFGVPRFDPSLKVAVKCDLCIDRRREGKLPACVEACPTGALKFGDIEE 133
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 35-196 4.99e-32

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


Pssm-ID: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 117.10  E-value: 4.99e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  35 IDVTTCIGCKACQVGCSEWNDIRSTPdaactgvydnpadlnpkawtvmrFNEVEENDRLEW-----LIrkdgCMHCSEPG 109
Cdd:cd16369    6 IDPSRCIGCRACVAACRECGTHRGKS-----------------------MIHVDYIDRGEStqtapTV----CMHCEDPT 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 110 CLKACPSpGAIIQYANGIV-DFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVDRVTVGQEPACVKTCPTGAIRF 188
Cdd:cd16369   59 CAEVCPA-DAIKVTEDGVVqSALKPRCIGCSNCVNACPFGVPKYDEERNLMMKCDMCYDRTSVGKAPMCASVCPSGALFY 137


                 ....*...
gi 498485091 189 GSKEEMKE 196
Cdd:cd16369  138 GTREEIQA 145
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 93-189 2.46e-30

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


Pssm-ID: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 110.03  E-value: 2.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091   93 LEWLIRKDGCMHCSEPGCLKACPSpGAIIQ-YANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVDRVTV 171
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPV-GAIYKdEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEA 79

                          90
                  ....*....|....*...
gi 498485091  172 GQEPACVKTCPTGAIRFG 189
Cdd:pfam13247  80 GLLPACVQTCPTGAMNFG 97
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 31-198 1.37e-28

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


Pssm-ID: 319890 [Multi-domain]  Cd Length: 200  Bit Score: 109.05  E-value: 1.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  31 VAKLIDVTTCIGCK-----ACQVGCSEWNDIRsTPDAAC---------------TGVYDNPADLNPKAWTVMRFNEVEEN 90
Cdd:cd16368    1 LATLIDLTKCDGCPgesipACVRACREKNQAR-FPEPVSkpiqpywprkriedwSDKRDVTDRLTPYNWLYVQKLTVDTA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  91 DRLEWLIRKDGCMHCSEPGCLKACPSpGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPR----------MNPE---DH 157
Cdd:cd16368   80 GGEKEVFIPRRCMHCDNPPCAKLCPF-GAARKTPEGAVYIDDDLCFGGAKCRDVCPWHIPQrqagvgiylhLAPEyagGG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 498485091 158 RVYKCTLCVDRVTVGQEPACVKTCPTGAIRFGSKEEMKEYA 198
Cdd:cd16368  159 VMYKCDLCKDLLAQGKPPACIEACPKGAQYFGPRKEMVALA 199
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 34-188 1.41e-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: 1.41e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  34 LIDVTTCIGCKACQVGCSEWNDirstpdaactGVYdnpadlNPK--AWTVMRFNEVEendrlewLIRKDGCMHCSEPGCL 111
Cdd:cd10550    2 VVDPEKCTGCRTCELACSLKHE----------GVF------NPSlsRIRVVRFEPEG-------LDVPVVCRQCEDAPCV 58

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498485091 112 KACPSpGAIIQ-YANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCvdrvtvGQEPACVKTCPTGAIRF 188
Cdd:cd10550   59 EACPV-GAISRdEETGAVVVDEDKCIGCGMCVEACPFGAIRVDPETGKAIKCDLC------GGDPACVKVCPTGALEF 129
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 34-189 4.28e-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: 103.10  E-value: 4.28e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  34 LIDVTTCIGCKACQVGCSEWNDirSTPDAactgVYDNPADLNPKAwtvmrFNEVEENDRLEWLIRkdgCMHCSEPGCLKA 113
Cdd:cd10563    3 FIDEEKCLGCKLCEVACAVAHS--KSKDL----IKAKLEKERPRP-----RIRVEESGGRSFPLQ---CRHCDEPPCVKA 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498485091 114 CPSpGAIIQY-ANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVDRvtvgQEPACVKTCPTGAIRFG 189
Cdd:cd10563   69 CMS-GAMHKDpETGIVIHDEEKCVGCWMCVMVCPYGAIRPDKERKVALKCDLCPDR----ETPACVEACPTGALVLE 140
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
32-185 1.86e-22

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 93.79  E-value: 1.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  32 AKLIDVTTCIGCKACQVGCSEWNdirSTPDAAC-TGVydNPADLNPKAwtvmrfNEVEENDRLEWLirkdgCMHCSEPGC 110
Cdd:PRK14993  45 AMLIDLRRCIGCQSCTVSCTIEN---QTPQGAFrTTV--NQYQVQREG------SQEVTNVLLPRL-----CNHCDNPPC 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498485091 111 LKACPSPgAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVDRVTVGQEPACVKTCPTGA 185
Cdd:PRK14993 109 VPVCPVQ-ATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGA 182
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
34-188 4.16e-22

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 89.72  E-value: 4.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  34 LIDVTTCIGCKACQVGCSEwndirstpdaactgVYDNPADLNPKAW-TVMRFNEVEENDRlewlirkdgCMHCSEPGCLK 112
Cdd:COG1142    6 IADPEKCIGCRTCEAACAV--------------AHEGEEGEPFLPRiRVVRKAGVSAPVQ---------CRHCEDAPCAE 62

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498485091 113 ACPSpGAIIQyANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHR--VYKCTLCVDRvtvGQEPACVKTCPTGAIRF 188
Cdd:COG1142   63 VCPV-GAITR-DDGAVVVDEEKCIGCGLCVLACPFGAITMVGEKSRavAVKCDLCGGR---EGGPACVEACPTGALRL 135
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 30-188 5.34e-22

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: 91.49  E-value: 5.34e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  30 EVAKLIDVTTCIGCKACQVGC-SEWNDIRSTPDAACTGVYDNPADLNPKAWtvmrfnEVEENDRLEWL----IRKDGCMH 104
Cdd:cd16365    2 QFAAVFNLNKCIGCQTCTVACkNAWTYRKGQEYMWWNNVETKPGGGYPQDW------EVKTIDNGGNTrfffYLQRLCNH 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 105 CSEPGCLKACPSPGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVDRVTVGQEPACVKTCPtG 184
Cdd:cd16365   76 CTNPACLAACPRGAIYKREEDGIVLIDQKRCRGYRKCVEQCPYKKIYFNGLSRVSEKCIACYPRIEGGDPTRCMSACV-G 154


                 ....
gi 498485091 185 AIRF 188
Cdd:cd16365  155 RIRL 158
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 40-188 1.08e-21

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: 88.86  E-value: 1.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  40 CIGCKACQVGCSEWNDirstpDAACTGVYDNPADLNPkawtvmrfneveendRLeWLIRKDG------CMHCSEPGCLKA 113
Cdd:cd10554    9 CIGCRTCEVACAAAHS-----GKGIFEAGTDGLPFLP---------------RL-RVVKTGEvtapvqCRQCEDAPCANV 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 114 CPSpGAIIQyANGIVDFQSDKCIGCGYCIAGCPF----------NIPRMNPEDHRV-YKCTLCVDRvtvGQEPACVKTCP 182
Cdd:cd10554   68 CPV-GAISQ-EDGVVQVDEERCIGCKLCVLACPFgaiemapttvPGVDWERGPRAVaVKCDLCAGR---EGGPACVEACP 142


                 ....*.
gi 498485091 183 TGAIRF 188
Cdd:cd10554  143 TKALTL 148
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 34-206 2.74e-19

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: 83.53  E-value: 2.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  34 LIDVTTCIGCKACQVGC-SEWNDIRSTPdaactgvYDNPADLNPKAWtvMRFNEVE--ENDRLEWLIRKDGCMHCSEPGC 110
Cdd:cd10552    2 VIDVAKCNGCYNCFLACkDEHVGNDWPG-------YAAPQPRHGHFW--MRILRRErgQYPKVDVAYLPVPCNHCDNAPC 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 111 LKACPSpGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVDRVTVG-QEPACVKTCPTGAIRFG 189
Cdd:cd10552   73 IKAAKD-GAVYKRDDGIVIIDPEKAKGQKQLVDACPYGAIYWNEELQVPQKCTFCAHLLDDGwKEPRCVQACPTGALRFG 151

                        170
                 ....*....|....*..
gi 498485091 190 SKEEMKEYASKRIADLK 206
Cdd:cd10552  152 KLEDEEMAAKAAEEGLE 168
FDH3_beta NF038355
formate dehydrogenase FDH3 subunit beta; Members of this family are the beta subunit of the ...
 34-210 3.64e-19

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: 83.19  E-value: 3.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  34 LIDVTTCIGCKACQVGCSEWNDIrstpdaactgvydnPADLNPKawTVMRFNEVEENDRLEWLirkdGCMHCSEPGCLKA 113
Cdd:NF038355   6 LCDTERCIECNGCVVACKNAHEL--------------PWGINRR--RVVTLNDGVPGEKSISV----ACMHCTDAPCAAV 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 114 CPSpGAIIQYANGIVDFQSDKCIGCGYCIAGCPF---NIPRMNPEDHR--VYKCTLC-----------------VDRVTV 171
Cdd:NF038355  66 CPV-DCFYIRADGIVLHDKDKCIGCGYCLYACPFgapQFPKDGAFGARgkMDKCTFCaggpeetnseaerekygQNRIAE 144

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 498485091 172 GQEPACVKTCPTGAIRFGSKEEMKEYASKRIAdlkSRGY 210
Cdd:NF038355 145 GKLPLCAEMCSTKALLAGDAEVVADIYRERVV---ARGA 180
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 102-188 1.47e-18

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: 84.28  E-value: 1.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 102 CMHCSEPGCLKACPSpGAIIQYA-NGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVDRVTVGQEPACVKT 180
Cdd:cd10555  133 CNHCTNPACLAACPR-KAIYKREeDGIVLVDQDRCRGYRYCVEACPYKKIYFNPVEQKSEKCIFCYPRIEKGVAPACARQ 211


                 ....*...
gi 498485091 181 CPtGAIRF 188
Cdd:cd10555  212 CV-GRIRF 218
PRK09898 PRK09898
ferredoxin-like protein;
40-187 3.57e-18

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 81.04  E-value: 3.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  40 CIGCKACQVGCSEWNDIRSTPDAACTGVYDNpadlnpkawtvmrFNEVEENDRLE------WLIRKDGCMHCSEPGCLKA 113
Cdd:PRK09898  68 CTGCHRCEISCTNFNDGSVGTFFSRIKIHRN-------------YFFGDNGVGSGgglygdLNYTADTCRQCKEPQCMNV 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498485091 114 CPSPGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCvdrvtvgqePACVKTCPTGAIR 187
Cdd:PRK09898 135 CPIGAITWQQKEGCITVDHKRCIGCSACTTACPWMMATVNTESKKSSKCVLC---------GECANACPTGALK 199
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 34-193 3.71e-17

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


Pssm-ID: 319889 [Multi-domain]  Cd Length: 138  Bit Score: 76.58  E-value: 3.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  34 LIDVTTCIGCKACqvgcsEWndirstpdaACTGVYDNPADLNPKAWTVMRFNEVeendrlewlirkDGCMHCSEPGCLKA 113
Cdd:cd16367   15 VIDLDRCIRCDNC-----EK---------ACADTHDGHSRLDRNGLRFGNLLVP------------TACRHCVDPVCMIG 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 114 CPsPGAIIQYANGIVdFQSDKCIGCGYCIAGCPFNIPRMnpedHRVYKCTLCVDrvtvGQEPACVKTCPTGAIRFGSKEE 193
Cdd:cd16367   69 CP-TGAIHRDDGGEV-VISDACCGCGNCASACPYGAIQM----VRAVKCDLCAG----YAGPACVSACPTGAAIRVNPEE 138
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 36-247 1.71e-16

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 79.68  E-value: 1.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  36 DVTTCIGCKACQVGCSEWNDIRSTPDAActgvydnpADLNPKAWTVMRFNEVEENdrlewlirkdGCMHCSEPGCLKACP 115
Cdd:PRK12809   8 EAAECIGCHACEIACAVAHNQENWPLSH--------SDFRPRIHVVGKGQAANPV----------ACHHCNNAPCVTACP 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 116 SPGAIiqYANGIVDFQSDKCIGCGYCIAGCPFNIPRMnpEDHRVYKCTLCVDRVTvGQEpACVKTCPTGAIRFGSKE--- 192
Cdd:PRK12809  70 VNALT--FQSDSVQLDEQKCIGCKRCAIACPFGVVEM--VDTIAQKCDLCNQRSS-GTQ-ACIEVCPTQALRLMDDKglq 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498485091 193 ------EMKEYASKRIADlkSRGYENAGLYD-PEGVGGTHVMYVLHHADKPELYSGLpkDPQ 247
Cdd:PRK12809 144 qikvarQRKTAAGKASSD--AQPSRSAALLPvNSRKGADKISASERKTHFGEIYCGL--DPQ 201
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 102-188 2.24e-16

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


Pssm-ID: 319879 [Multi-domain]  Cd Length: 363  Bit Score: 78.56  E-value: 2.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 102 CMHCSEPGCLKACPSpGAIIQYA-NGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVDRVTVGQEPACVKT 180
Cdd:cd10557  179 CNHCLNPACVAACPS-GAIYKREeDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSEKCIFCYPRLEAGQPTVCSET 257


                 ....*...
gi 498485091 181 CpTGAIRF 188
Cdd:cd10557  258 C-VGRIRY 264
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 40-201 4.91e-16

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 78.25  E-value: 4.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  40 CIGCKACQVGCS-EWNDIRSTpdaactgvyDNPADLNPKawtVMRFNEVEENDRLEwlirkdgCMHCSEPGCLKACPSpG 118
Cdd:PRK12769  12 CLGCHACEIACVmAHNDEQHV---------LSQHHFHPR---ITVIKHQQQRSAVT-------CHHCEDAPCARSCPN-G 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 119 AIIQYANGIVDFQsDKCIGCGYCIAGCPFNIPRM-----NPEDHRV--YKCTLCVDRvtvGQEPACVKTCPTGAIRFGSK 191
Cdd:PRK12769  72 AISHVDDSIQVNQ-QKCIGCKSCVVACPFGTMQIvltpvAAGKVKAtaHKCDLCAGR---ENGPACVENCPADALQLVTE 147

                        170
                 ....*....|
gi 498485091 192 EEMKEYASKR 201
Cdd:PRK12769 148 QALSGMAKSR 157
Form-deh_trans pfam09163
Formate dehydrogenase N, transmembrane; Members of this family are predominantly found in the ...
 248-289 2.68e-14

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: 65.72  E-value: 2.68e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 498485091  248 IDLSVTLWKDVLKPVAAVAMGGLVLSEIAHYIAIGPNTEDLD 289
Cdd:pfam09163   1 ISPSVELWKGVLKPLGAAGMGAAALAGFFHYITVGPNKVEEE 42
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 102-188 2.96e-14

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


Pssm-ID: 440755 [Multi-domain]  Cd Length: 485  Bit Score: 72.92  E-value: 2.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 102 CMHCSEPGCLKACPSpGAIIQYA-NGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVDRVTVGQEPACVKT 180
Cdd:COG1140  182 CEHCLNPACVASCPS-GAIYKREeDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGKAEKCIFCYPRIEAGQPTVCSET 260


                 ....*...
gi 498485091 181 CpTGAIRF 188
Cdd:COG1140  261 C-VGRIRY 267
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 102-188 1.01e-13

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


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 66.91  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 102 CMHCSEPGCLKACPSpGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCvdrvtvgqePACVKTC 181
Cdd:cd16370   53 CRACEDPPCAEACPT-GALEPRKGGGVVLDKEKCIGCGNCVKACIVGAIFWDEETNKPIICIHC---------GYCARYC 122


                 ....*..
gi 498485091 182 PTGAIRF 188
Cdd:cd16370  123 PHDVLAM 129
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 102-187 4.05e-13

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


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 65.05  E-value: 4.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 102 CMHCSEpgCLKACPSpGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCvdrvtvgqePACVKTC 181
Cdd:cd16372   49 CNQCGE--CIDVCPT-GAITRDANGVVMINKKLCVGCLMCVGFCPEGAMFKHEDYPEPFKCIAC---------GICVKAC 116


                 ....*.
gi 498485091 182 PTGAIR 187
Cdd:cd16372  117 PTGALE 122
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 102-187 7.29e-13

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: 67.48  E-value: 7.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 102 CMHCSEPGCLKACPSPGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTLCVDRVTVGQEPACVKTC 181
Cdd:cd10556  141 CNHCTYPACLAACPRKAIYKREEDGIVLIDQERCRGYRECVEACPYKKPMYNPTTRVSEKCIGCYPRIEEGDQTQCVSAC 220


                 ....*.
gi 498485091 182 PtGAIR 187
Cdd:cd10556  221 I-GKIR 225
PRK10330 PRK10330
electron transport protein HydN;
34-186 6.97e-10

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 57.21  E-value: 6.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  34 LIDVTTCIGCKACQVGC----SEWNDIRSTpdaactgvydNPADLNPKAWTVMRFNeveendrlewLIRKDGCMHCSEPG 109
Cdd:PRK10330   6 IADASKCIGCRTCEVACvvshQENQDCASL----------TPETFLPRIHVIKGVN----------VSTATVCRQCEDAP 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 110 CLKACPSpGAIIQyANGIVDFQSDKCIGCGYCIAGCPF-------------NIPRMN--PEDHRVYKCTLCVDRVTvgqE 174
Cdd:PRK10330  66 CANVCPN-GAISR-DKGFVHVMQERCIGCKTCVVACPYgamevvvrpvirnSGAGLNvrAEKAEANKCDLCNHRED---G 140

                        170
                 ....*....|..
gi 498485091 175 PACVKTCPTGAI 186
Cdd:PRK10330 141 PACMAACPTHAL 152
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 98-187 8.81e-09

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


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 55.00  E-value: 8.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  98 RKDGCMHCSEpgCLKACPSpGAIIQYANGI--VDfqSDKCIGCGYCIAGCPFNIPRMNPEDHRVYKCTL---CVDRVTVG 172
Cdd:COG2878  135 CEYGCIGCGD--CIKACPF-DAIVGAAKGMhtVD--EDKCTGCGLCVEACPVDCIEMVPVSPTVVVSSWdkgKAVRKVVG 209

                         90
                 ....*....|....*
gi 498485091 173 QEPACVKTCPTGAIR 187
Cdd:COG2878  210 CIGLCCKKCCPAAAI 224
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 123-193 1.00e-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: 48.19  E-value: 1.00e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498485091 123 YANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRV---YKCTLCVdrvtvgqepACVKTCPTGAIRFGSKEE 193
Cdd:COG1149    1 VKRKIPVIDEEKCIGCGLCVEVCPEGAIKLDDGGAPVvdpDLCTGCG---------ACVGVCPTGAITLEEREA 65
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
133-197 1.91e-07

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 47.80  E-value: 1.91e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498485091 133 DKCIGCGYCIAGCPFNIPRMNPEDHRV--YKCTLCvdrvtvgqePACVKTCPTGAIRFGSK------EEMKEY 197
Cdd:COG2768   11 EKCIGCGACVKVCPVGAISIEDGKAVIdpEKCIGC---------GACIEVCPVGAIKIEWEedeefqEKMAEY 74
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 132-196 1.97e-07

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: 51.01  E-value: 1.97e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498485091 132 SDKCIGCGYCIAGCPFNIPRMnpEDHRVY---KCTLCVdrvtvgqepACVKTCPTGAIRFGSKEEMKE 196
Cdd:NF038196 184 TDKCIGCGICAKVCPVNNIEM--EDGKPVwghNCTHCL---------ACIHRCPKEAIEYGKKTKKKG 240
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
127-195 2.17e-07

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 51.22  E-value: 2.17e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 127 IVDFQSDKCIGCGYCIAGCPFNI-PRMNPEDHrvYKCTLCVDrvtvgqepaCVKTCPTGAIRFGSKEEMK 195
Cdd:COG0348  204 RVRYDRGDCIDCGLCVKVCPMGIdIRKGEINQ--SECINCGR---------CIDACPKDAIRFSSRGEKT 262
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 129-202 2.32e-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: 48.93  E-value: 2.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 129 DFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVY-------KCTLCvdrvtvgqePACVKTCPTGAIRFGSKEEMKEYASKR 201
Cdd:cd10549    2 KYDPEKCIGCGICVKACPTDAIELGPNGAIARgpeidedKCVFC---------GACVEVCPTGAIELTPEGKEYVPKEKE 72


                 .
gi 498485091 202 I 202
Cdd:cd10549   73 A 73
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
97-186 2.50e-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: 2.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  97 IRKDGCMHCSEPGCLKACP----SPGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVY--KCTLCvdrvt 170
Cdd:COG4624   51 CPRCCLCCCCCCRCCVAISciqvRGIIIIDKRGPSIIRDKEKCKNCYPCVRACPVKAIKVDDGKAEIDeeKCISC----- 125

                         90
                 ....*....|....*.
gi 498485091 171 vGQepaCVKTCPTGAI 186
Cdd:COG4624  126 -GQ---CVAVCPFGAI 137
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 133-196 5.43e-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: 5.43e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498485091 133 DKCIGCGYCIAGCPFNIPRMNPEDHRVY-----KCTLCvdrvtvgqePACVKTCPTGAIRFGSKEEMKE 196
Cdd:COG1146    8 DKCIGCGACVEVCPVDVLELDEEGKKALvinpeECIGC---------GACELVCPVGAITVEDDEPEEQ 67
NapF COG1145
Ferredoxin [Energy production and conversion];
76-192 5.79e-07

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 49.72  E-value: 5.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  76 PKAWTVMRFNEVEENDRLEWLIRKDGCMHCSEPGCLKACPSPGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPE 155
Cdd:COG1145  125 VVAAGEVLLVIAAALAEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVCPTGAIRLKDG 204

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 498485091 156 DHRVY----KCTLCvdrvtvgqePACVKTCPTGAIRFGSKE 192
Cdd:COG1145  205 KPQIVvdpdKCIGC---------GACVKVCPVGAISLEPKE 236
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
96-156 1.40e-06

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 45.11  E-value: 1.40e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498485091  96 LIRKDGCMHCSEpgCLKACPSpGAIIQyANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPED 156
Cdd:COG2768    7 YVDEEKCIGCGA--CVKVCPV-GAISI-EDGKAVIDPEKCIGCGACIEVCPVGAIKIEWEE 63
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 133-192 2.24e-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: 44.35  E-value: 2.24e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498485091 133 DKCIGCGYCIAGCPFNIPRMNPEDHRVY------KCTLCVdrvtvgqepACVKTCPTGAIRFGSKE 192
Cdd:COG1143    2 DKCIGCGLCVRVCPVDAITIEDGEPGKVyvidpdKCIGCG---------LCVEVCPTGAISMTPFE 58
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
101-187 2.75e-06

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 48.01  E-value: 2.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 101 GCMHCSEpgCLKACPSpGAIIqYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYkcTLCVDRVTVGQEPA---- 176
Cdd:PRK07118 140 GCLGLGS--CVAACPF-DAIH-IENGLPVVDEDKCTGCGACVKACPRNVIELIPKSARVF--VACNSKDKGKAVKKvcev 213

                         90
                 ....*....|....*...
gi 498485091 177 -------CVKTCPTGAIR 187
Cdd:PRK07118 214 gcigcgkCVKACPAGAIT 231
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 117-195 3.75e-06

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: 46.09  E-value: 3.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 117 PGAIiqyanGIVDFQSdKCIGCGYCIAGCPFNI---------------PRMNPedhRVYKCTLCVDrvtvgqepACVKTC 181
Cdd:cd16373    4 PGAL-----DEEEFLA-LCIRCGLCVEACPTGViqpagledgleggrtPYLDP---REGPCDLCCD--------ACVEVC 66

                         90
                 ....*....|....
gi 498485091 182 PTGAIRFGSKEEMK 195
Cdd:cd16373   67 PTGALRPLDLEEQK 80
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 97-148 4.86e-06

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 43.50  E-value: 4.86e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 498485091  97 IRKDGCMHCSEpgCLKACPSpGAIiQYANGIVDFQSDKCIGCGYCIAGCPFN 148
Cdd:COG2221   12 IDEEKCIGCGL--CVAVCPT-GAI-SLDDGKLVIDEEKCIGCGACIRVCPTG 59
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
133-188 5.72e-06

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 47.55  E-value: 5.72e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 133 DKCIGCGYCIAGCPFNIPRMNpEDHRVY----KCTLCvdrvtvGqepACVKTCPTGAIRF 188
Cdd:COG1148  496 EKCTGCGRCVEVCPYGAISID-EKGVAEvnpaLCKGC------G---TCAAACPSGAISL 545
FeFe_hydrog_B1 TIGR04105
[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups.
 110-147 1.06e-05

[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups.


Pssm-ID: 274983 [Multi-domain]  Cd Length: 462  Bit Score: 46.82  E-value: 1.06e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 498485091  110 CLKACPsPGAIIQYANGIVDFQSDKCIGCGYCIAGCPF 147
Cdd:TIGR04105 166 CEKACP-VGAISSDEDGRAVIDYDKCISCGACMVACPF 202
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 117-187 1.30e-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: 1.30e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498485091 117 PGAIIQYANGIVDfqSDKCIGCGYCIAGCPFNIPRMnpEDHRVY----KCTLCvdrvtvgqePACVKTCPTGAIR 187
Cdd:COG2221    1 PYGIIGTWPPKID--EEKCIGCGLCVAVCPTGAISL--DDGKLVideeKCIGC---------GACIRVCPTGAIK 62
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 133-187 1.54e-05

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 42.34  E-value: 1.54e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 498485091 133 DKCIGCGYCIAGCPFNIPRMNPEDHRV--YKCTLCVdrvtvgqepACVKTCPTGAIR 187
Cdd:COG4231   22 DKCTGCGACVKVCPADAIEEGDGKAVIdpDLCIGCG---------SCVQVCPVDAIK 69
Fer4_9 pfam13187
4Fe-4S dicluster domain;
134-186 1.54e-05

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 41.77  E-value: 1.54e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 498485091  134 KCIGCGYCIAGCPF------NIPRMNPEDHRVYKCTLCVdrvtvgqepACVKTCPTGAI 186
Cdd:pfam13187   1 KCTGCGACVAACPAgaivpdLVGQTIRGDIAGLACIGCG---------ACVDACPRGAI 50
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 99-188 2.09e-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: 2.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  99 KDGCMHCSEpgCLKACPSpGAIIQYANGIV----DFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVYK------------- 161
Cdd:cd10549    5 PEKCIGCGI--CVKACPT-DAIELGPNGAIargpEIDEDKCVFCGACVEVCPTGAIELTPEGKEYVPkekeaeideekci 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 498485091 162 -CTLCVD-------RVTVGQEP-----------ACVKTCPTGAIRF 188
Cdd:cd10549   82 gCGLCVKvcpvdaiTLEDELEIvidkekcigcgICAEVCPVNAIKL 127
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 97-148 2.33e-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: 2.33e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 498485091  97 IRKDGCMHCSEpgCLKACPSpGAIIQYANGIVDFQSDKCIGCGYCIAGCPFN 148
Cdd:cd10549   75 IDEEKCIGCGL--CVKVCPV-DAITLEDELEIVIDKEKCIGCGICAEVCPVN 123
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 97-148 2.37e-05

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 41.64  E-value: 2.37e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 498485091  97 IRKDGCMHCSEpgCLKACPsPGAIIQYANGIVDFQSDKCIGCGYCIAGCPFN 148
Cdd:COG1149    8 IDEEKCIGCGL--CVEVCP-EGAIKLDDGGAPVVDPDLCTGCGACVGVCPTG 56
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 95-146 3.05e-05

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


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 41.08  E-value: 3.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 498485091   95 WLIRKDGCMHCsePGCLKACPSPGAI-----IQYANGIVDFQSDKCIGCGYCIAGCP 146
Cdd:pfam13237   2 VVIDPDKCIGC--GRCTAACPAGLTRvgaivERLEGEAVRIGVWKCIGCGACVEACP 56
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 132-200 4.29e-05

NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes "I" subunits from the closely related F420H2 dehydrogenase and formate hydrogenlyase complexes. [Energy metabolism, Electron transport]


Pssm-ID: 273902 [Multi-domain]  Cd Length: 122  Bit Score: 42.40  E-value: 4.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  132 SDKCIGCGYCIAGCPFNIPRMNP---EDHRVY---------KCTLCvdrvtvgqePACVKTCPTGAIRFGSKEEMKEYAS 199
Cdd:TIGR01971  42 EEKCIGCTLCAAVCPADAIRVVPaegEDGKRRlkfyeinfgRCIFC---------GLCEEACPTDAIVLTPEFELATYTR 112


                  .
gi 498485091  200 K 200
Cdd:TIGR01971 113 S 113
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 126-187 8.22e-05

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 41.36  E-value: 8.22e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498485091 126 GIVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHRVY----KCTLCvdrvtvGQepaCVKTCPTGAIR 187
Cdd:PRK08348  35 GKILYDVDKCVGCRMCVTVCPAGVFVYLPEIRKVAlwtgRCVFC------GQ---CVDVCPTGALQ 91
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 135-185 9.26e-05

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 39.43  E-value: 9.26e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  135 CIGCGYCIAGCPFNIPRMNPE---------DHRVYKCTLCvdrvtvgqePACVKTCPTGA 185
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVgekkgtktvVIDPERCVGC---------GACVAVCPTGA 51
NapF COG1145
Ferredoxin [Energy production and conversion];
31-158 1.24e-04

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 42.79  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  31 VAKLIDVTTCIGCKACQVGCSEWNDIRSTPDAACTGVYDNPADLNPKAWTVMRFNEVEENDRLEWLIRKDGCMHCSEpgC 110
Cdd:COG1145  113 LIISAVKLVAGLVVAAGEVLLVIAAALAEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGL--C 190

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 498485091 111 LKACPSpGAIIQYANG-IVDFQSDKCIGCGYCIAGCPFNIPRMNPEDHR 158
Cdd:COG1145  191 VKVCPT-GAIRLKDGKpQIVVDPDKCIGCGACVKVCPVGAISLEPKEIE 238
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 96-155 1.70e-04

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


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 41.32  E-value: 1.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091   96 LIRKDGCMHCSEpgCLKACPSpGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPE 155
Cdd:TIGR01944 109 LIDEDNCIGCTK--CIQACPV-DAIVGAAKAMHTVIADECTGCDLCVEPCPTDCIEMIPV 165
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
134-219 2.15e-04

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 41.02  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 134 KCIGCGYCIAGCPFNIPRMNPEDH-------RVY-----KCTLCvdrvtvGqepACVKTCPTGAIRFGskeEMKEYASKR 201
Cdd:PRK05888  59 RCIACKLCAAICPADAITIEAAERedgrrrtTRYdinfgRCIFC------G---FCEEACPTDAIVET---PDFELATET 126

                         90
                 ....*....|....*...
gi 498485091 202 IADLksrgyenagLYDPE 219
Cdd:PRK05888 127 REEL---------IYDKE 135
flavo_MJ0208 TIGR02700
archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of ...
 93-148 4.83e-04

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


Pssm-ID: 131747 [Multi-domain]  Cd Length: 234  Bit Score: 40.63  E-value: 4.83e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 498485091   93 LEWLIRKDGCMHCSEpgCLKACPSpGAIIQyANGIVDFQSDKCIGCGYCIAGCPFN 148
Cdd:TIGR02700 141 TPYMIDRKRCKGCGI--CVDACPR-SAIDM-VDGKAFIRLLKCVGCGKCKEACPYN 192
PRK13795 PRK13795
hypothetical protein; Provisional
 96-146 5.69e-04

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 41.52  E-value: 5.69e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 498485091  96 LIRKDGCMHCSEpgCLKACPSpGAI-IQYANGIVDFQSDKCIGCGYCIAGCP 146
Cdd:PRK13795 577 LRRAAECVGCGV--CVGACPT-GAIrIEEGKRKISVDEEKCIHCGKCTEVCP 625
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
35-152 5.76e-04

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 40.69  E-value: 5.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  35 IDVTTCIGCKACQVGCSEwNDIRSTPDAACTGVYDNPADlnpKAWTVMRFNEVeendrlewlirkdGCMHCSEpgCLKAC 114
Cdd:PRK07118 165 VDEDKCTGCGACVKACPR-NVIELIPKSARVFVACNSKD---KGKAVKKVCEV-------------GCIGCGK--CVKAC 225

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 498485091 115 PSpGAIIQyANGIVDFQSDKCIGCGYCIAGCPFNIPRM 152
Cdd:PRK07118 226 PA-GAITM-ENNLAVIDQEKCTSCGKCVEKCPTKAIRI 261
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 102-149 6.19e-04

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 37.12  E-value: 6.19e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 498485091  102 CMHCSEpgCLKACPS-----PGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNI 149
Cdd:pfam12838   1 CIGCGA--CVAACPVgaitlDEVGEKKGTKTVVIDPERCVGCGACVAVCPTGA 51
Fer COG1141
Ferredoxin [Energy production and conversion];
133-187 8.10e-04

Ferredoxin [Energy production and conversion];


Pssm-ID: 440756 [Multi-domain]  Cd Length: 63  Bit Score: 37.17  E-value: 8.10e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 498485091 133 DKCIGCGYCIAGCPfNIPRMNPEDhrvyKCTLCVDRVTVGQEPAC---VKTCPTGAIR 187
Cdd:COG1141    8 DTCIGCGLCVALAP-EVFELDDDG----KAVVLDEEVPEELEEDVreaADACPVGAIT 60
napG PRK09476
quinol dehydrogenase periplasmic component; Provisional
 129-185 8.84e-04

quinol dehydrogenase periplasmic component; Provisional


Pssm-ID: 236534 [Multi-domain]  Cd Length: 254  Bit Score: 39.99  E-value: 8.84e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498485091 129 DFQSdKCIGCGYCIAGCPFNIPRM-NPEDH----------RVYKCTLCVDrvtvgqePACVKTCPTGA 185
Cdd:PRK09476  56 DFLS-ACIRCGLCVQACPYDTLKLaTLASGlsagtpyfvaRDIPCEMCED-------IPCVKACPSGA 115
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 97-156 1.43e-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: 36.95  E-value: 1.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  97 IRKDGCMHCSEpgCLKACPsPGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPED 156
Cdd:COG1144   27 VDEDKCIGCGL--CWIVCP-DGAIRVDDGKYYGIDYDYCKGCGICAEVCPVKAIEMVPEE 83
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 130-193 1.89e-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: 36.57  E-value: 1.89e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498485091 130 FQSDKCIGCGYCIAGCPFNIPRMNPEDHRV---YKCTLCvdrvtvgqePACVKTCPTGAIRFGSKEE 193
Cdd:COG1144   27 VDEDKCIGCGLCWIVCPDGAIRVDDGKYYGidyDYCKGC---------GICAEVCPVKAIEMVPEEK 84
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 133-201 1.98e-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: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 133 DKCIGCGYCIAGCPFNI--------PR-----------------MNPEDHRV-YKCTLCvdRvtvgqepACVKTCPTGaI 186
Cdd:COG0247   78 DACVGCGFCRAMCPSYKatgdekdsPRgrinllrevlegelpldLSEEVYEVlDLCLTC--K-------ACETACPSG-V 147

                         90
                 ....*....|....*.
gi 498485091 187 RFGS-KEEMKEYASKR 201
Cdd:COG0247  148 DIADlIAEARAQLVER 163
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
97-153 2.08e-03

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 39.46  E-value: 2.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 498485091  97 IRKDGCMHCSEpgCLKACPSpGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMN 153
Cdd:COG1148  493 VDPEKCTGCGR--CVEVCPY-GAISIDEKGVAEVNPALCKGCGTCAAACPSGAISLK 546
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 133-182 2.10e-03

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


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 35.69  E-value: 2.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 498485091  133 DKCIGCGYCIAGCPFN---------IPRMNPEDHRVYKCTLCVdrvtvgqepACVKTCP 182
Cdd:pfam13237   7 DKCIGCGRCTAACPAGltrvgaiveRLEGEAVRIGVWKCIGCG---------ACVEACP 56
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
96-156 2.39e-03

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 36.85  E-value: 2.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498485091  96 LIRKDGCMHCSEpgCLKACPSPgAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPED 156
Cdd:PRK09623  47 VVDESKCVKCYI--CWKFCPEP-AIYIKEDGYVAIDYDYCKGCGICANECPTKAITMVKEE 104
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 102-156 3.11e-03

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 39.09  E-value: 3.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 498485091 102 CMHCSE-PGCLKACPSpGAIIQYANGI-VDFQSDKCIGCGYCIAGCPFNIPRMNPED 156
Cdd:PRK12771 509 CGNCFEcDNCYGACPQ-DAIIKLGPGRrYHFDYDKCTGCHICADVCPCGAIEMGPGE 564
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
 133-209 4.15e-03

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 37.32  E-value: 4.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091 133 DKCIGCGYCIAGCPFNIPRMNPEDHRVYK--------CTLCvdrvtvGQepaCVKTCPTGAIRFGSKEEMkeyASKRIAD 204
Cdd:PRK12387  38 QQCIGCAACVNACPSNALTVETDLATGELawefnlgrCIFC------GR---CEEVCPTAAIKLSQEFEL---AVWKKED 105


                 ....*
gi 498485091 205 LKSRG 209
Cdd:PRK12387 106 LLQQS 110
PorD_KorD TIGR02179
2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate family; A number ...
 97-156 4.60e-03

2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate family; A number of anaerobic and microaerophilic species lack pyruvate dehydrogenase and have instead a four subunit, oxygen-sensitive pyruvate oxidoreductase, with either ferredoxins or flavodoxins used as the acceptor. Several related four-subunit enzymes may exist in the same species. This model describes a subfamily of delta subunits, representing mostly pyruvate, 2-ketoisovalerate, and 2-oxoglutarate specific enzymes. The delta subunit is the smallest and resembles ferredoxins.


Pssm-ID: 131234 [Multi-domain]  Cd Length: 78  Bit Score: 35.39  E-value: 4.60e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091   97 IRKDGCMHCSEpgCLKACPSpGAIIQYANGIVDFQSDKCIGCGYCIAGCPFNIPRMNPED 156
Cdd:TIGR02179  22 VDKEKCIKCKN--CWLYCPE-GAIQEDEGGFVGIDYDYCKGCGICANVCPVKAIEMVREE 78
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 99-148 4.64e-03

Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; Epoxyqueuosine reductase QueG (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441208 [Multi-domain]  Cd Length: 345  Bit Score: 38.26  E-value: 4.64e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498485091  99 KDGCMHCSEpgCLKACPSpGAIIqyANGIVDFQsdKCI------------------------GCGYCIAGCPFN 148
Cdd:COG1600  183 EDHCGSCTR--CLDACPT-GAIV--APYVLDAR--RCIsyltielkgpipeelrpkmgnriyGCDDCQDVCPWN 249
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
125-188 5.08e-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: 5.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498485091 125 NGIVDFQSDKCIGCGYCIAGCPFN---------IPRM----NPEDHRVYKCTLCVDRvtvgqepACVKTCPTGAIRF 188
Cdd:COG1142    2 NKFIIADPEKCIGCRTCEAACAVAhegeegepfLPRIrvvrKAGVSAPVQCRHCEDA-------PCAEVCPVGAITR 71
Fer4_21 pfam14697
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 97-146 6.04e-03

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: 434137 [Multi-domain]  Cd Length: 59  Bit Score: 34.56  E-value: 6.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 498485091   97 IRKDGCMHCSEpgCLKACPSPG--AIIQYANGIVDFQSDKCIGCGYCIAGCP 146
Cdd:pfam14697   3 IDEDTCIGCGK--CYIACPDTShqAIVGDGKRHHTVIEDECTGCNLCVSVCP 52
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 110-146 7.37e-03

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 36.46  E-value: 7.37e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 498485091 110 CLKACPSPGAIIQ--YANGIVDFQSDKCIGCGYCIAGCP 146
Cdd:cd16373  105 CVEACPTEAIAIVleDDVLRPVVDEDKCVGCGLCEYVCP 143
Fer4_13 pfam13370
4Fe-4S single cluster domain of Ferredoxin I; Fer4_13 is a ferredoxin I from sulfate-reducing ...
 133-187 8.60e-03

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


Pssm-ID: 433153 [Multi-domain]  Cd Length: 58  Bit Score: 34.20  E-value: 8.60e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498485091  133 DKCIGCGYCIAGCPfNIPRMNPEDHRVYkctlcVDRVTVGQ-EPACVK----TCPTGAIR 187
Cdd:pfam13370   4 DTCIDCGTCRELAP-EVFKYDDDGGASF-----VHDQPVNEeEEDLAEealdSCPVEAIG 57
 
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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