NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|493460140|ref|WP_006415373|]
View 

MULTISPECIES: formate dehydrogenase subunit beta [Burkholderia]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FDH-beta super family cl36936
formate dehydrogenase, beta subunit, Fe-S containing; This model represents the beta subunit ...
 7-284 1.04e-156

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: 438.96  E-value: 1.04e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140    7 DIKRVSATTTPPPTAREPVTgSVAKLIDVSKCIGCKACQTACMEWNDLRDEIGT-NVGVYDNPADLTEHSWTVMRFSEYE 85
Cdd:TIGR01582   1 DIKRLSATKEPDPSVKTYPT-ELAKLIDVSSCIGCKACQAACQEWNDTTPPILSrKVGGYQNPPDLLPETFTLMRFKEGE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140   86 NPQGdLEWLIRKDGCMHCEDPGCLKACPSPGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSD 165
Cdd:TIGR01582  80 ESDG-LEWLIRKDGCMHCREPGCLKACPAPGAIIQYQNGIVDFDHSKCIGCGYCIVGCPFNIPRYDKVDNRPYKCTLCID 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  166 RVAVGQEPACVKTCPTGAIVFGTKEDMKQHAAERIEDLKERGFEHAGLYDPQGVGGTHVMYVLHHADKPSLYHGLPDNPS 245
Cdd:TIGR01582 159 RVSVGQEPACVKTCPTNAISFGFKEDMKERAEKRVADLKSRGYPNAGLYDPPGVGGTHVMYVLHHGDKPKDYQDLPEDPR 238

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 493460140  246 ISPMVRLWKGIAKPLAVAGLALTALAGFFHYVRVGPNEV 284
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 ...
 7-284 1.04e-156

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: 438.96  E-value: 1.04e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140    7 DIKRVSATTTPPPTAREPVTgSVAKLIDVSKCIGCKACQTACMEWNDLRDEIGT-NVGVYDNPADLTEHSWTVMRFSEYE 85
Cdd:TIGR01582   1 DIKRLSATKEPDPSVKTYPT-ELAKLIDVSSCIGCKACQAACQEWNDTTPPILSrKVGGYQNPPDLLPETFTLMRFKEGE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140   86 NPQGdLEWLIRKDGCMHCEDPGCLKACPSPGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSD 165
Cdd:TIGR01582  80 ESDG-LEWLIRKDGCMHCREPGCLKACPAPGAIIQYQNGIVDFDHSKCIGCGYCIVGCPFNIPRYDKVDNRPYKCTLCID 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  166 RVAVGQEPACVKTCPTGAIVFGTKEDMKQHAAERIEDLKERGFEHAGLYDPQGVGGTHVMYVLHHADKPSLYHGLPDNPS 245
Cdd:TIGR01582 159 RVSVGQEPACVKTCPTNAISFGFKEDMKERAEKRVADLKSRGYPNAGLYDPPGVGGTHVMYVLHHGDKPKDYQDLPEDPR 238

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 493460140  246 ISPMVRLWKGIAKPLAVAGLALTALAGFFHYVRVGPNEV 284
Cdd:TIGR01582 239 IDASVGLWKGVLKTIGSIAMGGTALGVFLHLILWGPNKV 277
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 30-238 5.90e-147

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: 411.01  E-value: 5.90e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  30 AKLIDVSKCIGCKACQTACMEWNDLRDEIGTNVGVYDNPADLTEHSWTVMRFSEYEnPQGDLEWLIRKDGCMHCEDPGCL 109
Cdd:cd10558    1 AKLIDVSKCIGCKACQVACKEWNDLRAEVGHNVGTYQNPADLSPETWTLMKFREVE-DNGKLEWLIRKDGCMHCADPGCL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 110 KACPSPGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSDRVAVGQEPACVKTCPTGAIVFGTK 189
Cdd:cd10558   80 KACPSPGAIVQYANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVGLEPACVKTCPTGALHFGTK 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 493460140 190 EDMKQHAAERIEDLKERGFEHAGLYDPQGVGGTHVMYVLHHADKPSLYH 238
Cdd:cd10558  160 EDMLALAEKRVAALKERGYTNAGLYDPKGVGGTHVMYVLHHADKPEGYP 208
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 30-227 2.02e-68

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 210.96  E-value: 2.02e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  30 AKLIDVSKCIGCKACQTACMEWNDLRDEIgtnvgvydnpadltehSWTVMRFSEyENPQGDLEWLIRKDGCMHCEDPGCL 109
Cdd:COG0437    7 GMVIDLTKCIGCRACVVACKEENNLPVGV----------------TWRRVRRYE-EGEFPNVEWLFVPVLCNHCDDPPCV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 110 KACPSpGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSDRVAVGQEPACVKTCPTGAIVFGTK 189
Cdd:COG0437   70 KVCPT-GATYKREDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVEACPTGALVFGDL 148

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 493460140 190 EDMKQHAAERIEDLKERGFehaglyDPQGVGGTHVMYV 227
Cdd:COG0437  149 DDPESEVSKRLAELPAYRL------LPELGTKPSVYYL 180
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
11-266 4.73e-48

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 163.30  E-value: 4.73e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  11 VSATTTPPPTAREPVTGSVAKLIDVSKCIGCKACQTACMEWNDLRDEIGTNvGVYDNPADLTEHSWTVMRF----SEYEN 86
Cdd:PRK10882  20 LPSVSHAAAENRPPIPGALGMLYDSTLCVGCQACVTKCQEINFPERNPQGE-QTWDNPDKLSPYTNNIIKVwksgTGVNK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  87 PQGDLEWLIRKDGCMHCEDPGCLKACPSPGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRI--SKKDHRAYKCTLCS 164
Cdd:PRK10882  99 DQEENGYAYIKKQCMHCVDPNCVSVCPVSALTKDPKTGIVHYDKDVCTGCRYCMVACPFNVPKYdyNNPFGAIHKCELCN 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 165 D----RVAVGQEPACVKTCPTGAIVFGTKEDMKQHAAERI------EDLKERGFEHAG-------------LYDPQGVGG 221
Cdd:PRK10882 179 QkgveRLDKGGLPGCVEVCPTGAVIFGTREELLAEAKRRLalkpgsEYHYPRQTLKSGdtylhtvpkyyphVYGEKEGGG 258

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493460140 222 THVMYvLHHADKPSLyhGLPDNPSISPMVR-------LWKGIAKPLAV-AGLA 266
Cdd:PRK10882 259 TQVLV-LSGVPFENL--GLPKLDDLSTGARsehiqhtLYKGMILPLAVlAGLT 308
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 91-187 2.95e-27

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: 101.94  E-value: 2.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140   91 LEWLIRKDGCMHCEDPGCLKACPSpGAIVQ-YNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSDRVAV 169
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPV-GAIYKdEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEA 79

                          90
                  ....*....|....*...
gi 493460140  170 GQEPACVKTCPTGAIVFG 187
Cdd:pfam13247  80 GLLPACVQTCPTGAMNFG 97
FDH3_beta NF038355
formate dehydrogenase FDH3 subunit beta; Members of this family are the beta subunit of the ...
 32-201 2.02e-20

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: 86.27  E-value: 2.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  32 LIDVSKCIGCKACQTACMEWNDLrdEIGTN----VGVYDNPADltEHSWTVmrfseyenpqgdlewlirkdGCMHCEDPG 107
Cdd:NF038355   6 LCDTERCIECNGCVVACKNAHEL--PWGINrrrvVTLNDGVPG--EKSISV--------------------ACMHCTDAP 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 108 CLKACPSpGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKD---HRAY--KCTLC-----------------SD 165
Cdd:NF038355  62 CAAVCPV-DCFYIRADGIVLHDKDKCIGCGYCLYACPFGAPQFPKDGafgARGKmdKCTFCaggpeetnseaerekygQN 140

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 493460140 166 RVAVGQEPACVKTCPTGAIVFGTKEDMKQHAAERIE 201
Cdd:NF038355 141 RIAEGKLPLCAEMCSTKALLAGDAEVVADIYRERVV 176
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 127-189 1.90e-06

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


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 47.93  E-value: 1.90e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493460140 127 DFH-EENCIGCGYCVTGCPFNvpRISKKDHRAY---KCTLCSdrvavgqepACVKTCPTGAIVFGTK 189
Cdd:NF038196 180 KFHvTDKCIGCGICAKVCPVN--NIEMEDGKPVwghNCTHCL---------ACIHRCPKEAIEYGKK 235
 
Name Accession Description Interval E-value
FDH-beta TIGR01582
formate dehydrogenase, beta subunit, Fe-S containing; This model represents the beta subunit ...
 7-284 1.04e-156

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: 438.96  E-value: 1.04e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140    7 DIKRVSATTTPPPTAREPVTgSVAKLIDVSKCIGCKACQTACMEWNDLRDEIGT-NVGVYDNPADLTEHSWTVMRFSEYE 85
Cdd:TIGR01582   1 DIKRLSATKEPDPSVKTYPT-ELAKLIDVSSCIGCKACQAACQEWNDTTPPILSrKVGGYQNPPDLLPETFTLMRFKEGE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140   86 NPQGdLEWLIRKDGCMHCEDPGCLKACPSPGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSD 165
Cdd:TIGR01582  80 ESDG-LEWLIRKDGCMHCREPGCLKACPAPGAIIQYQNGIVDFDHSKCIGCGYCIVGCPFNIPRYDKVDNRPYKCTLCID 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  166 RVAVGQEPACVKTCPTGAIVFGTKEDMKQHAAERIEDLKERGFEHAGLYDPQGVGGTHVMYVLHHADKPSLYHGLPDNPS 245
Cdd:TIGR01582 159 RVSVGQEPACVKTCPTNAISFGFKEDMKERAEKRVADLKSRGYPNAGLYDPPGVGGTHVMYVLHHGDKPKDYQDLPEDPR 238

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 493460140  246 ISPMVRLWKGIAKPLAVAGLALTALAGFFHYVRVGPNEV 284
Cdd:TIGR01582 239 IDASVGLWKGVLKTIGSIAMGGTALGVFLHLILWGPNKV 277
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 30-238 5.90e-147

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: 411.01  E-value: 5.90e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  30 AKLIDVSKCIGCKACQTACMEWNDLRDEIGTNVGVYDNPADLTEHSWTVMRFSEYEnPQGDLEWLIRKDGCMHCEDPGCL 109
Cdd:cd10558    1 AKLIDVSKCIGCKACQVACKEWNDLRAEVGHNVGTYQNPADLSPETWTLMKFREVE-DNGKLEWLIRKDGCMHCADPGCL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 110 KACPSPGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSDRVAVGQEPACVKTCPTGAIVFGTK 189
Cdd:cd10558   80 KACPSPGAIVQYANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVGLEPACVKTCPTGALHFGTK 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 493460140 190 EDMKQHAAERIEDLKERGFEHAGLYDPQGVGGTHVMYVLHHADKPSLYH 238
Cdd:cd10558  160 EDMLALAEKRVAALKERGYTNAGLYDPKGVGGTHVMYVLHHADKPEGYP 208
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 31-187 1.63e-86

beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family contains beta FeS subunits of several dehydrogenases in the DMSO reductase superfamily, including formate dehydrogenase N (FDH-N), tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N is a major component of nitrate respiration of Escherichia coli; it catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate to a cytochrome. W-FDH contains a tungsten instead of molybdenum at the catalytic center and seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate.


Pssm-ID: 319888 [Multi-domain]  Cd Length: 156  Bit Score: 255.79  E-value: 1.63e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  31 KLIDVSKCIGCKACQTACMEWNDLRDEIGTNVGVYDNPADLTEHSWTVMRFSEYENPQGDLEWLIRKDGCMHCEDPGCLK 110
Cdd:cd16366    1 FLVDTSRCTGCRACQVACKQWNGLPAEKTEFTGSYQNPPDLTAHTWTLVRFYEVEKPGGDLSWLFRKDQCMHCTDAGCLA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493460140 111 ACPSpGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSDRVAVGQEPACVKTCPTGAIVFG 187
Cdd:cd16366   81 ACPT-GAIIRTETGTVVVDPETCIGCGYCVNACPFDIPRFDEETGRVAKCTLCYDRISNGLQPACVKTCPTGALTFG 156
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 32-244 6.58e-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: 249.23  E-value: 6.58e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  32 LIDVSKCIGCKACQTACMEWNDLR-DEIGTNVGVYDNPADLTEHSWTVMRFSE------YENPQGDLEWLIRKDGCMHCE 104
Cdd:cd10560    3 FTDTSICIGCKACEVACKQWNQLPaDGYDFSGMSYDNTGDLSASTWRHVKFIErptedgPANEGGDLQWLFMSDVCKHCT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 105 DPGCLKACPSpGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSDRVAVGQEPACVKTCPTGAI 184
Cdd:cd10560   83 DAGCLEACPT-GAIFRTEFGTVYIQPDICNGCGYCVAACPFGVIDRNEETGRAHKCTLCYDRLKDGLEPACAKACPTGSI 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493460140 185 VFGTKEDMKQHAAERIEDLKERGFEHAGLY--DP-QGVGGTHVMYVLhhADKPSLYhGLPDNP 244
Cdd:cd10560  162 QFGPLEELRERARARVEQLHEQGVVEAYLYgaDPtEGYGGLNAFFLL--LDKPEVY-GLPADP 221
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 31-192 9.75e-79

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: 236.43  E-value: 9.75e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  31 KLIDVSKCIGCKACQTACMEWNDLRDEIGTNVGVYDNPADLTEHSWTVMRFSEYENPQGDLEWLIRKDGCMHCEDPGCLK 110
Cdd:cd10562    1 MLVDTSKCTACRGCQVACKQWNQLPAEKTPFTGSYQNPPDLTPNTWTLIRFYEHEEDNGGIRWLFRKRQCMHCTDAACVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 111 ACPSpGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSDRVAVGQEPACVKTCPTGAIVFGTKE 190
Cdd:cd10562   81 VCPT-GALYKTENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCFDRIENGMQPACVKTCPTGALTFGDRD 159


                 ..
gi 493460140 191 DM 192
Cdd:cd10562  160 EL 161
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 30-227 2.02e-68

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 210.96  E-value: 2.02e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  30 AKLIDVSKCIGCKACQTACMEWNDLRDEIgtnvgvydnpadltehSWTVMRFSEyENPQGDLEWLIRKDGCMHCEDPGCL 109
Cdd:COG0437    7 GMVIDLTKCIGCRACVVACKEENNLPVGV----------------TWRRVRRYE-EGEFPNVEWLFVPVLCNHCDDPPCV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 110 KACPSpGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSDRVAVGQEPACVKTCPTGAIVFGTK 189
Cdd:COG0437   70 KVCPT-GATYKREDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVEACPTGALVFGDL 148

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 493460140 190 EDMKQHAAERIEDLKERGFehaglyDPQGVGGTHVMYV 227
Cdd:COG0437  149 DDPESEVSKRLAELPAYRL------LPELGTKPSVYYL 180
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 30-226 4.13e-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: 4.13e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  30 AKLIDVSKCIGCKACQTACMEWNDLRDEIGTNVGVYDNPADLTEHSWTVMRFseYENPQGDLEWLIRKDGCMHCEDPGCL 109
Cdd:cd10561    1 GVLYDTTRCIGCRACEVACKEWNGLPAEDTAFGPGWDNPRDLSAKTYTVIKR--YEVETGGKGFVFVKRQCMHCLDPACV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 110 KACPSpGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRI--SKKDHRAYKCTLCSDRVAVGQEPACVKTCPTGAIVFG 187
Cdd:cd10561   79 SACPV-GALRKTPEGPVTYDEDKCIGCRYCMVACPFNIPKYewDSANPKIRKCTMCYDRLKEGKQPACVEACPTGALLFG 157

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 493460140 188 TKEDMKQHAAERIEDLKERGFEHagLYDPQGVGGTHVMY 226
Cdd:cd10561  158 KREELLAEAKRRIAANPGRYVDH--VYGEKEAGGTSVLY 194
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 32-230 1.42e-59

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: 188.80  E-value: 1.42e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  32 LIDVSKCIGCKACQTACMEWNDLRDEIGTNVGVYDNPADLTEHSWTVMRFSEYENPQGDLEWLIRKDGCMHCEDPGCLKA 111
Cdd:cd10559    3 LIDTTRCTACRGCQVACKQWNQLPAEQTKNTGSHQNPPDLSANTYKLVRFNEVRNENGKPDWLFFPDQCRHCVTPPCKDA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 112 CPS-PGAIVQ-YNNGIVDFHEENCIGCGYCVT-GCPFNVPRISKKDHRAYKCTLCSDRVAVGQEPACVKTCPTGAIVFGT 188
Cdd:cd10559   83 ADMvPGAVIQdEATGAVVFTEKTAELDFDDVLsACPYNIPRKNEATGRIVKCDMCIDRVSNGLQPACVKACPTGAMNFGD 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 493460140 189 KEDMKQHAAERIEDLKERgFEHAGLYDPQGVggtHVMYVLHH 230
Cdd:cd10559  163 RDEMLAMASKRLEELKKR-YPKANLYDPDDV---RVIWLLAE 200
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 32-187 1.23e-48

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: 158.71  E-value: 1.23e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  32 LIDVSKCIGCKACQTACMEWNDLRdeigtnvgvydnpadlTEHSWTVMRFSEyenpQGDLEWLIRKDGCMHCEDPGCLKA 111
Cdd:cd04410    2 VVDLDRCIGCGTCEVACKQEHGLR----------------PGPDWSRIKVIE----GGGLERAFLPVSCMHCEDPPCVKA 61

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493460140 112 CPSpGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSDRVAVGQEPACVKTCPTGAIVFG 187
Cdd:cd04410   62 CPT-GAIYKDEDGIVLIDEDKCIGCGSCVEACPYGAIVFDPEPGKAVKCDLCGDRLDEGLEPACVKACPTGALTFG 136
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
11-266 4.73e-48

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 163.30  E-value: 4.73e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  11 VSATTTPPPTAREPVTGSVAKLIDVSKCIGCKACQTACMEWNDLRDEIGTNvGVYDNPADLTEHSWTVMRF----SEYEN 86
Cdd:PRK10882  20 LPSVSHAAAENRPPIPGALGMLYDSTLCVGCQACVTKCQEINFPERNPQGE-QTWDNPDKLSPYTNNIIKVwksgTGVNK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  87 PQGDLEWLIRKDGCMHCEDPGCLKACPSPGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRI--SKKDHRAYKCTLCS 164
Cdd:PRK10882  99 DQEENGYAYIKKQCMHCVDPNCVSVCPVSALTKDPKTGIVHYDKDVCTGCRYCMVACPFNVPKYdyNNPFGAIHKCELCN 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 165 D----RVAVGQEPACVKTCPTGAIVFGTKEDMKQHAAERI------EDLKERGFEHAG-------------LYDPQGVGG 221
Cdd:PRK10882 179 QkgveRLDKGGLPGCVEVCPTGAVIFGTREELLAEAKRRLalkpgsEYHYPRQTLKSGdtylhtvpkyyphVYGEKEGGG 258

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493460140 222 THVMYvLHHADKPSLyhGLPDNPSISPMVR-------LWKGIAKPLAV-AGLA 266
Cdd:PRK10882 259 TQVLV-LSGVPFENL--GLPKLDDLSTGARsehiqhtLYKGMILPLAVlAGLT 308
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 32-187 9.72e-47

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: 153.87  E-value: 9.72e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  32 LIDVSKCIGCKACQTACMEWNDLRDEIgtnvgvydnpadltehSW-TVMRFSEYENPQGDLEWLIRkdGCMHCEDPGCLK 110
Cdd:cd16371    3 YFDQERCIGCKACEIACKDKNDLPPGV----------------NWrRVYEYEGGEFPEVFAYFLSM--SCNHCENPACVK 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493460140 111 ACPSpGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSDRVAVGQEPACVKTCPTGAIVFG 187
Cdd:cd16371   65 VCPT-GAITKREDGIVVVDQDKCIGCGYCVWACPYGAPQYNPETGKMDKCDMCVDRLDEGEKPACVAACPTRALDFG 140
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 32-187 9.29e-44

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


Pssm-ID: 319873 [Multi-domain]  Cd Length: 185  Bit Score: 147.68  E-value: 9.29e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  32 LIDVSKCIGCKACQTACMEWNDLRDEIgtnvgvydnpadltehSWT-VMRFSEYENPQGDLEWLIRkdGCMHCEDPGCLK 110
Cdd:cd10551    2 VIDLRKCIGCGACVVACKAENNVPPGV----------------FRNrVLEYEVGEYPNVKRTFLPV--LCNHCENPPCVK 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 111 ACPSpGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAY------------KCTLCSDRVAVGQEPACVKT 178
Cdd:cd10551   64 VCPT-GATYKREDGIVLVDYDKCIGCRYCMAACPYGARYFNPEEPHEFgevpvrpkgvveKCTFCYHRLDEGLLPACVEA 142


                 ....*....
gi 493460140 179 CPTGAIVFG 187
Cdd:cd10551  143 CPTGARIFG 151
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 32-191 6.17e-34

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


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 120.84  E-value: 6.17e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  32 LIDVSKCIGCKACQTACMEWNDLRDEIgtNVGVYDnpaDLTEHSWTvmrfseyenpqgdlewlirkdgCMHCEDPGCLKA 111
Cdd:cd16374    2 YVDPERCIGCRACEIACAREHSGKPRI--SVEVVE---DLASVPVR----------------------CRHCEDAPCMEV 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 112 CPSpGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSDRVAVGQEPACVKTCPTGAIVFGTKED 191
Cdd:cd16374   55 CPT-GAIYRDEDGAVLVDPDKCIGCGMCAMACPFGVPRFDPSLKVAVKCDLCIDRRREGKLPACVEACPTGALKFGDIEE 133
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 33-194 2.62e-33

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


Pssm-ID: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 120.19  E-value: 2.62e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  33 IDVSKCIGCKACQTACMEWNDLRDEIGTNVGvYDNPADLTEHSWTVmrfseyenpqgdlewlirkdgCMHCEDPGCLKAC 112
Cdd:cd16369    6 IDPSRCIGCRACVAACRECGTHRGKSMIHVD-YIDRGESTQTAPTV---------------------CMHCEDPTCAEVC 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 113 PSpGAIVQYNNGIV-DFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSDRVAVGQEPACVKTCPTGAIVFGTKED 191
Cdd:cd16369   64 PA-DAIKVTEDGVVqSALKPRCIGCSNCVNACPFGVPKYDEERNLMMKCDMCYDRTSVGKAPMCASVCPSGALFYGTREE 142


                 ...
gi 493460140 192 MKQ 194
Cdd:cd16369  143 IQA 145
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 32-187 2.98e-30

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: 111.19  E-value: 2.98e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  32 LIDVSKCIGCKACQTACMewndlrdeigtnvgvydnpadlTEHSWT---VMRFSEYENPQ--------GDLEWLIRkdgC 100
Cdd:cd10563    3 FIDEEKCLGCKLCEVACA----------------------VAHSKSkdlIKAKLEKERPRprirveesGGRSFPLQ---C 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 101 MHCEDPGCLKACPSpGAIVQY-NNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSDRvavgQEPACVKTC 179
Cdd:cd10563   58 RHCDEPPCVKACMS-GAMHKDpETGIVIHDEEKCVGCWMCVMVCPYGAIRPDKERKVALKCDLCPDR----ETPACVEAC 132


                 ....*...
gi 493460140 180 PTGAIVFG 187
Cdd:cd10563  133 PTGALVLE 140
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 34-188 5.15e-29

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: 108.22  E-value: 5.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  34 DVSKCIGCKACQTACMEWNdlrdeigtNVGVYDNPADLTEhswtvmrfSEYENPQGDLEWLIRKDGCMHCEDPGCLKACP 113
Cdd:cd10553    8 DSKRCIGCLACEVHCKVKN--------NLPVGPRLCRIFA--------VGPKMVGGKPRLKFVYMSCFHCENPWCVKACP 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493460140 114 SPGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSDRVAVGQEPACVKTCPTGAIVFGT 188
Cdd:cd10553   72 TGAMQKREKDGIVYVDQELCIGCKACIEACPWGIPQWNPATGKVVKCDYCMDRIDQGLKPACVTGCTTHALSFVR 146
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
32-186 4.20e-28

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 105.51  E-value: 4.20e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  32 LIDVSKCIGCKACQTACMEwndlrdeigtnvgVYDNPADLTEHSW-TVMRFSEYENPQGdlewlirkdgCMHCEDPGCLK 110
Cdd:COG1142    6 IADPEKCIGCRTCEAACAV-------------AHEGEEGEPFLPRiRVVRKAGVSAPVQ----------CRHCEDAPCAE 62

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493460140 111 ACPSpGAIVQyNNGIVDFHEENCIGCGYCVTGCPFNV--PRISKKDHRAYKCTLCSDRvavGQEPACVKTCPTGAIVF 186
Cdd:COG1142   63 VCPV-GAITR-DDGAVVVDEEKCIGCGLCVLACPFGAitMVGEKSRAVAVKCDLCGGR---EGGPACVEACPTGALRL 135
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 32-186 1.49e-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: 1.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  32 LIDVSKCIGCKACQTACMEWNDlrdeigtnvGVYdNPadltehSWTVMRFSEYENPQgdlewLIRKDGCMHCEDPGCLKA 111
Cdd:cd10550    2 VVDPEKCTGCRTCELACSLKHE---------GVF-NP------SLSRIRVVRFEPEG-----LDVPVVCRQCEDAPCVEA 60

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493460140 112 CPSpGAIVQ-YNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCsdrvavGQEPACVKTCPTGAIVF 186
Cdd:cd10550   61 CPV-GAISRdEETGAVVVDEDKCIGCGMCVEACPFGAIRVDPETGKAIKCDLC------GGDPACVKVCPTGALEF 129
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 91-187 2.95e-27

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: 101.94  E-value: 2.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140   91 LEWLIRKDGCMHCEDPGCLKACPSpGAIVQ-YNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSDRVAV 169
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPV-GAIYKdEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEA 79

                          90
                  ....*....|....*...
gi 493460140  170 GQEPACVKTCPTGAIVFG 187
Cdd:pfam13247  80 GLLPACVQTCPTGAMNFG 97
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 29-197 3.37e-27

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


Pssm-ID: 319890 [Multi-domain]  Cd Length: 200  Bit Score: 105.20  E-value: 3.37e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  29 VAKLIDVSKCIGCK-----ACQTACME-------------------------WNDLRDEIGTnvgvydnpadLTEHSWTV 78
Cdd:cd16368    1 LATLIDLTKCDGCPgesipACVRACREknqarfpepvskpiqpywprkriedWSDKRDVTDR----------LTPYNWLY 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  79 MRFSEYENPQGDLEWLI-RKdgCMHCEDPGCLKACPSpGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPR----ISKK 153
Cdd:cd16368   71 VQKLTVDTAGGEKEVFIpRR--CMHCDNPPCAKLCPF-GAARKTPEGAVYIDDDLCFGGAKCRDVCPWHIPQrqagVGIY 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493460140 154 DHRA---------YKCTLCSDRVAVGQEPACVKTCPTGAIVFGTKEDMKQHAA 197
Cdd:cd16368  148 LHLApeyagggvmYKCDLCKDLLAQGKPPACIEACPKGAQYFGPRKEMVALAR 200
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 32-204 1.89e-26

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: 102.79  E-value: 1.89e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  32 LIDVSKCIGCKACQTACMewndlrDE-IGTNVGVYDNPADLTEHSWtvMRFSEYEN---PQGDLEWLIRKdgCMHCEDPG 107
Cdd:cd10552    2 VIDVAKCNGCYNCFLACK------DEhVGNDWPGYAAPQPRHGHFW--MRILRRERgqyPKVDVAYLPVP--CNHCDNAP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 108 CLKACPSpGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSDRVAVG-QEPACVKTCPTGAIVF 186
Cdd:cd10552   72 CIKAAKD-GAVYKRDDGIVIIDPEKAKGQKQLVDACPYGAIYWNEELQVPQKCTFCAHLLDDGwKEPRCVQACPTGALRF 150

                        170       180
                 ....*....|....*....|.
gi 493460140 187 GTKED--MKQHAA-ERIEDLK 204
Cdd:cd10552  151 GKLEDeeMAAKAAeEGLEVLH 171
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 34-184 1.04e-25

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: 99.64  E-value: 1.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  34 DVSKCIGCKACQTACMEWNdlRDEIGTNVGvydnPADLTEHSwtvmRFseyenpqgdleWLIRKDG------CMHCEDPG 107
Cdd:cd10554    5 DPDKCIGCRTCEVACAAAH--SGKGIFEAG----TDGLPFLP----RL-----------RVVKTGEvtapvqCRQCEDAP 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 108 CLKACPSpGAIVQyNNGIVDFHEENCIGCGYCVTGCPF---NVPRISKKDHR--------AYKCTLCSDRvavGQEPACV 176
Cdd:cd10554   64 CANVCPV-GAISQ-EDGVVQVDEERCIGCKLCVLACPFgaiEMAPTTVPGVDwergpravAVKCDLCAGR---EGGPACV 138


                 ....*...
gi 493460140 177 KTCPTGAI 184
Cdd:cd10554  139 EACPTKAL 146
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
30-191 4.40e-24

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 98.02  E-value: 4.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  30 AKLIDVSKCIGCKACQTACmewndlrdeigtnvgVYDNPADLTEHSWTVMRFSEYENPQGDLEWLIRKDGCMHCEDPGCL 109
Cdd:PRK14993  45 AMLIDLRRCIGCQSCTVSC---------------TIENQTPQGAFRTTVNQYQVQREGSQEVTNVLLPRLCNHCDNPPCV 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 110 KACPSPgAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSDRVAVGQEPACVKTCPTGAIVFGTK 189
Cdd:PRK14993 110 PVCPVQ-ATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDI 188


                 ..
gi 493460140 190 ED 191
Cdd:PRK14993 189 KD 190
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 32-185 2.45e-22

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: 90.44  E-value: 2.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  32 LIDVSKCIGCKACQTACMEwndlrdeigtnvgVYDNPADLTEHswtVMRFSEYENPQGdlewlirkdgCMHCEDPGCLKA 111
Cdd:cd16367   15 VIDLDRCIRCDNCEKACAD-------------THDGHSRLDRN---GLRFGNLLVPTA----------CRHCVDPVCMIG 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493460140 112 CPsPGAIVQYNNGIVdFHEENCIGCGYCVTGCPFNVPRIskkdHRAYKCTLCSDrvavGQEPACVKTCPTGAIV 185
Cdd:cd16367   69 CP-TGAIHRDDGGEV-VISDACCGCGNCASACPYGAIQM----VRAVKCDLCAG----YAGPACVSACPTGAAI 132
FDH3_beta NF038355
formate dehydrogenase FDH3 subunit beta; Members of this family are the beta subunit of the ...
 32-201 2.02e-20

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: 86.27  E-value: 2.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  32 LIDVSKCIGCKACQTACMEWNDLrdEIGTN----VGVYDNPADltEHSWTVmrfseyenpqgdlewlirkdGCMHCEDPG 107
Cdd:NF038355   6 LCDTERCIECNGCVVACKNAHEL--PWGINrrrvVTLNDGVPG--EKSISV--------------------ACMHCTDAP 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 108 CLKACPSpGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKD---HRAY--KCTLC-----------------SD 165
Cdd:NF038355  62 CAAVCPV-DCFYIRADGIVLHDKDKCIGCGYCLYACPFGAPQFPKDGafgARGKmdKCTFCaggpeetnseaerekygQN 140

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 493460140 166 RVAVGQEPACVKTCPTGAIVFGTKEDMKQHAAERIE 201
Cdd:NF038355 141 RIAEGKLPLCAEMCSTKALLAGDAEVVADIYRERVV 176
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 34-199 2.13e-20

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 91.35  E-value: 2.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  34 DVSKCIGCKACQTACMewndlrdeIGTNVGVY-DNPADLTEHSwTVMRFSEYENPQGdlewlirkdgCMHCEDPGCLKAC 112
Cdd:PRK12769   8 NSQQCLGCHACEIACV--------MAHNDEQHvLSQHHFHPRI-TVIKHQQQRSAVT----------CHHCEDAPCARSC 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 113 PSpGAIVQYNNGiVDFHEENCIGCGYCVTGCPFNVPRI-------SKKDHRAYKCTLCSDRvavGQEPACVKTCPTGAIV 185
Cdd:PRK12769  69 PN-GAISHVDDS-IQVNQQKCIGCKSCVVACPFGTMQIvltpvaaGKVKATAHKCDLCAGR---ENGPACVENCPADALQ 143

                        170
                 ....*....|....
gi 493460140 186 FGTKEDMKQHAAER 199
Cdd:PRK12769 144 LVTEQALSGMAKSR 157
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 29-191 1.62e-19

beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene dehydrogenase (EBDH, EC 1.17.99.2), a member of the DMSO reductase family. EBDH oxidizes the hydrocarbon ethylbenzene to (S)-1-phenylethanol. It is a heterotrimer, with the alpha subunit containing the catalytic center with a molybdenum held by two molybdopterin-guanine dinucleotides, the beta subunit containing four iron-sulfur clusters (the electron transfer subunit) and the gamma subunit containing a methionine and a lysine as axial heme ligands. During catalysis, electrons produced by substrate oxidation are transferred to a heme in the gamma subunit and then presumably to a separate cytochrome involved in nitrate respiration.


Pssm-ID: 319877 [Multi-domain]  Cd Length: 316  Bit Score: 86.97  E-value: 1.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  29 VAKLIDVSKCIGCKACQTAC------------MEWNDLR-----------DEIG---TNVGV-----------------Y 65
Cdd:cd10555    5 LAMVMDLNKCIGCQTCTVACktlwtnrngreyMYWNNVEtqpgkgypknwEKKGggfKDKGElkpgiiptledygvpweY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  66 DNPADLTEHSWTVMRFSEYENP---------QGDLEW-------LIRKdgCMHCEDPGCLKACPSpGAI-VQYNNGIVDF 128
Cdd:cd10555   85 NHEEELFEGKGGRVRPSPKGDPtwgpnwdedQGAGEYpnsyyfyLPRI--CNHCTNPACLAACPR-KAIyKREEDGIVLV 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493460140 129 HEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSDRVAVGQEPACVKTCPTGAIVFGTKED 191
Cdd:cd10555  162 DQDRCRGYRYCVEACPYKKIYFNPVEQKSEKCIFCYPRIEKGVAPACARQCVGRIRFVGYLDD 224
Form-deh_trans pfam09163
Formate dehydrogenase N, transmembrane; Members of this family are predominantly found in the ...
 246-285 3.58e-19

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


Pssm-ID: 430440  Cd Length: 43  Bit Score: 78.82  E-value: 3.58e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 493460140  246 ISPMVRLWKGIAKPLAVAGLALTALAGFFHYVRVGPNEVT 285
Cdd:pfam09163   1 ISPSVELWKGVLKPLGAAGMGAAALAGFFHYITVGPNKVE 40
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 29-194 5.50e-19

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


Pssm-ID: 319887 [Multi-domain]  Cd Length: 201  Bit Score: 83.02  E-value: 5.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  29 VAKLIDVSKCIGCKACQTAC------------MEWNdlrdeigtNVGVYdnPADLTEHSWTVMRFSEYENpqgdLEWLIR 96
Cdd:cd16365    3 FAAVFNLNKCIGCQTCTVACknawtyrkgqeyMWWN--------NVETK--PGGGYPQDWEVKTIDNGGN----TRFFFY 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  97 -KDGCMHCEDPGCLKACPSPGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSDRVAVGQEPAC 175
Cdd:cd16365   69 lQRLCNHCTNPACLAACPRGAIYKREEDGIVLIDQKRCRGYRKCVEQCPYKKIYFNGLSRVSEKCIACYPRIEGGDPTRC 148

                        170
                 ....*....|....*....
gi 493460140 176 VKTCPTGAIVFGTKEDMKQ 194
Cdd:cd16365  149 MSACVGRIRLQGFLDDNPK 167
PRK09898 PRK09898
ferredoxin-like protein;
36-184 2.59e-18

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 81.42  E-value: 2.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  36 SKCIGCKACQTACMEWNDlrdeigTNVGVYDNPADLTEHSWTVMRFSEYENP-QGDLewLIRKDGCMHCEDPGCLKACPS 114
Cdd:PRK09898  66 ARCTGCHRCEISCTNFND------GSVGTFFSRIKIHRNYFFGDNGVGSGGGlYGDL--NYTADTCRQCKEPQCMNVCPI 137

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 115 PGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSdrvavgqepACVKTCPTGAI 184
Cdd:PRK09898 138 GAITWQQKEGCITVDHKRCIGCSACTTACPWMMATVNTESKKSSKCVLCG---------ECANACPTGAL 198
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 34-199 2.15e-16

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 79.30  E-value: 2.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  34 DVSKCIGCKACQTACM------EW----NDLRDEIgtNVGVYDNPADLTehswtvmrfseyenpqgdlewlirkdGCMHC 103
Cdd:PRK12809   8 EAAECIGCHACEIACAvahnqeNWplshSDFRPRI--HVVGKGQAANPV--------------------------ACHHC 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 104 EDPGCLKACPSPGAIVQYNNgiVDFHEENCIGCGYCVTGCPFNVprISKKDHRAYKCTLCSDRVAvGQEpACVKTCPTGA 183
Cdd:PRK12809  60 NNAPCVTACPVNALTFQSDS--VQLDEQKCIGCKRCAIACPFGV--VEMVDTIAQKCDLCNQRSS-GTQ-ACIEVCPTQA 133

                        170
                 ....*....|....*.
gi 493460140 184 IVFGTKEDMKQHAAER 199
Cdd:PRK12809 134 LRLMDDKGLQQIKVAR 149
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 100-179 5.09e-16

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


Pssm-ID: 319879 [Multi-domain]  Cd Length: 363  Bit Score: 77.40  E-value: 5.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 100 CMHCEDPGCLKACPSpGAIVQYN-NGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSDRVAVGQEPACVKT 178
Cdd:cd10557  179 CNHCLNPACVAACPS-GAIYKREeDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSEKCIFCYPRLEAGQPTVCSET 257


                 .
gi 493460140 179 C 179
Cdd:cd10557  258 C 258
PRK10330 PRK10330
electron transport protein HydN;
32-199 5.19e-15

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 71.84  E-value: 5.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  32 LIDVSKCIGCKACQTACMEWNDLRDEIgtnvgvydnpADLTEHSWtVMRFSEYENPQGDLEWLirkdgCMHCEDPGCLKA 111
Cdd:PRK10330   6 IADASKCIGCRTCEVACVVSHQENQDC----------ASLTPETF-LPRIHVIKGVNVSTATV-----CRQCEDAPCANV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 112 CPSpGAIVQyNNGIVDFHEENCIGCGYCVTGCPFNV------PRISKK---------DHRAYKCTLCSDRVAvgqEPACV 176
Cdd:PRK10330  70 CPN-GAISR-DKGFVHVMQERCIGCKTCVVACPYGAmevvvrPVIRNSgaglnvraeKAEANKCDLCNHRED---GPACM 144

                        170       180
                 ....*....|....*....|...
gi 493460140 177 KTCPTGAIVFGTKEDMKQHAAER 199
Cdd:PRK10330 145 AACPTHALICVDRNKLEQLSAEK 167
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 100-179 4.92e-14

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


Pssm-ID: 440755 [Multi-domain]  Cd Length: 485  Bit Score: 72.15  E-value: 4.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 100 CMHCEDPGCLKACPSpGAIvqYN---NGIVDFHEENCIGCGYCVTGCP-----FNvprisKKDHRAYKCTLCSDRVAVGQ 171
Cdd:COG1140  182 CEHCLNPACVASCPS-GAI--YKreeDGIVLVDQDKCRGWRMCVSGCPykkvyFN-----WKTGKAEKCIFCYPRIEAGQ 253


                 ....*...
gi 493460140 172 EPACVKTC 179
Cdd:COG1140  254 PTVCSETC 261
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 31-186 1.03e-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: 1.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  31 KLIDVSKCIGCKACQTACmewndlrdeigtnVGVYDNPADLTEhswTVMRFSEYENPQGDLEWLIrkdgCMHCEDPGCLK 110
Cdd:cd16370    4 RVKDMERCIGCYSCMLAC-------------SRRVHKSASLSK---SAIRVRTRGGLEGGFTVVV----CRACEDPPCAE 63

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493460140 111 ACPSpGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSdrvavgqepACVKTCPTGAIVF 186
Cdd:cd16370   64 ACPT-GALEPRKGGGVVLDKEKCIGCGNCVKACIVGAIFWDEETNKPIICIHCG---------YCARYCPHDVLAM 129
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 29-180 3.52e-12

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


Pssm-ID: 319878 [Multi-domain]  Cd Length: 287  Bit Score: 65.56  E-value: 3.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  29 VAKLIDVSKCIGCKACQTAC------------MEWNDLRDE------IGTNVGVYDNPADLT---EHSWTVMRFSE---- 83
Cdd:cd10556   12 FAMVFDTNKCIACQTCTMACkstwtsgkgqeyMWWNNVETKpyggypLGWDVRLLDEEGGQTwaeGGVYEGKTIFEaaaa 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  84 ---------------YEN-----------PQGDLE---------WLIRKdgCMHCEDPGCLKACPSPGAIVQYNNGIVDF 128
Cdd:cd10556   92 geqvlgyrpededwrYPNigedevngertPDTGSSlpphpiwffYLPRI--CNHCTYPACLAACPRKAIYKREEDGIVLI 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493460140 129 HEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSDRVAVGQEPACVKTCP 180
Cdd:cd10556  170 DQERCRGYRECVEACPYKKPMYNPTTRVSEKCIGCYPRIEEGDQTQCVSACI 221
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 33-184 5.57e-12

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


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 61.97  E-value: 5.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  33 IDVSKCIGCKACQTAC-MEWNDLRDeigtnvgvydnpadlTEHSwtVMRFSEYENPqgdlewlIRKDGCMHCEDpgCLKA 111
Cdd:cd16372    5 TDPEKCIGCLQCEEACsKTFFKEED---------------REKS--CIRITETEGG-------YAINVCNQCGE--CIDV 58

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493460140 112 CPSpGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSdrvavgqepACVKTCPTGAI 184
Cdd:cd16372   59 CPT-GAITRDANGVVMINKKLCVGCLMCVGFCPEGAMFKHEDYPEPFKCIACG---------ICVKACPTGAL 121
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
100-185 2.75e-08

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 54.65  E-value: 2.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 100 CMHCEDPGCLKACPSPGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVprISKKDHRAY----KCTLCsdrvavGQepaC 175
Cdd:COG4624   60 CCCRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCYPCVRACPVKA--IKVDDGKAEideeKCISC------GQ---C 128

                         90
                 ....*....|
gi 493460140 176 VKTCPTGAIV 185
Cdd:COG4624  129 VAVCPFGAIT 138
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
130-192 3.88e-08

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 49.73  E-value: 3.88e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493460140 130 EENCIGCGYCVTGCPFNVprISKKDHRAY----KCTLCsdrvavgqePACVKTCPTGAIVFGTKEDM 192
Cdd:COG2768   10 EEKCIGCGACVKVCPVGA--ISIEDGKAVidpeKCIGC---------GACIEVCPVGAIKIEWEEDE 65
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
125-193 7.49e-08

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 52.37  E-value: 7.49e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493460140 125 IVDFHEENCIGCGYCVTGCPFNVPrISKKDHRAYKCTLCSDrvavgqepaCVKTCPTGAIVFGTKEDMK 193
Cdd:COG0348  204 RVRYDRGDCIDCGLCVKVCPMGID-IRKGEINQSECINCGR---------CIDACPKDAIRFSSRGEKT 262
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 97-184 1.14e-07

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 49.70  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  97 KDGCMHCEDpgCLKACPSpGAIVQYNNGIV----DFHEENCIGCGYCVTGCPFNVPRISKKdhraYKCTLCSDRVAVGQE 172
Cdd:cd10549    5 PEKCIGCGI--CVKACPT-DAIELGPNGAIargpEIDEDKCVFCGACVEVCPTGAIELTPE----GKEYVPKEKEAEIDE 77

                         90
                 ....*....|....*...
gi 493460140 173 P------ACVKTCPTGAI 184
Cdd:cd10549   78 EkcigcgLCVKVCPVDAI 95
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 121-190 1.79e-07

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 47.42  E-value: 1.79e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493460140 121 YNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDH---RAYKCTLCSdrvavgqepACVKTCPTGAIVFGTKE 190
Cdd:COG1149    1 VKRKIPVIDEEKCIGCGLCVEVCPEGAIKLDDGGApvvDPDLCTGCG---------ACVGVCPTGAITLEERE 64
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 130-194 2.34e-07

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 47.40  E-value: 2.34e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 130 EENCIGCGYCVTGCPFNVPRISKKDHRAY-----KCTLCSdrvavgqepACVKTCPTGAIVFGTKEDMKQ 194
Cdd:COG1146    7 TDKCIGCGACVEVCPVDVLELDEEGKKALvinpeECIGCG---------ACELVCPVGAITVEDDEPEEQ 67
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 96-207 3.60e-07

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


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 50.38  E-value: 3.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  96 RKDGCMHCEDpgCLKACPSpGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSD---RVAVGQE 172
Cdd:COG2878  135 CEYGCIGCGD--CIKACPF-DAIVGAAKGMHTVDEDKCTGCGLCVEACPVDCIEMVPVSPTVVVSSWDKGkavRKVVGCI 211

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 493460140 173 PACVKTCPTGAIvfgtkeDMKQHAAERIEDLKERG 207
Cdd:COG2878  212 GLCCKKCCPAAA------ITVNNLAAIIDYKKCTC 240
NapF COG1145
Ferredoxin [Energy production and conversion];
130-190 4.48e-07

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 50.11  E-value: 4.48e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493460140 130 EENCIGCGYCVTGCPFNVPRISKK----DHRAYKCTLCsdrvavgqePACVKTCPTGAIVFGTKE 190
Cdd:COG1145  181 AEKCIGCGLCVKVCPTGAIRLKDGkpqiVVDPDKCIGC---------GACVKVCPVGAISLEPKE 236
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 33-147 6.74e-07

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 47.39  E-value: 6.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  33 IDVSKCIGCKACQTACmewndlrdeigtnvgvydnPADLTEhswtvMRFSEYENPQGDLEWLIRKDGCMHCEDpgCLKAC 112
Cdd:cd10549   37 IDEDKCVFCGACVEVC-------------------PTGAIE-----LTPEGKEYVPKEKEAEIDEEKCIGCGL--CVKVC 90

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 493460140 113 PSpGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNV 147
Cdd:cd10549   91 PV-DAITLEDELEIVIDKEKCIGCGICAEVCPVNA 124
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
94-146 7.96e-07

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 45.88  E-value: 7.96e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493460140  94 LIRKDGCMHCEDpgCLKACPSpGAIVQyNNGIVDFHEENCIGCGYCVTGCPFN 146
Cdd:COG2768    7 YVDEEKCIGCGA--CVKVCPV-GAISI-EDGKAVIDPEKCIGCGACIEVCPVG 55
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 130-190 8.48e-07

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 45.51  E-value: 8.48e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493460140 130 EENCIGCGYCVTGCPFNVPRISKKDHRAY------KCTLCSdrvavgqepACVKTCPTGAIVFGTKE 190
Cdd:COG1143    1 EDKCIGCGLCVRVCPVDAITIEDGEPGKVyvidpdKCIGCG---------LCVEVCPTGAISMTPFE 58
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 95-147 1.22e-06

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 45.43  E-value: 1.22e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493460140  95 IRKDGCMHCEDpgCLKACPSpGAIVqYNNGIVDFHEENCIGCGYCVTGCPFNV 147
Cdd:COG2221   12 IDEEKCIGCGL--CVAVCPT-GAIS-LDDGKLVIDEEKCIGCGACIRVCPTGA 60
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 127-189 1.90e-06

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


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 47.93  E-value: 1.90e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493460140 127 DFH-EENCIGCGYCVTGCPFNvpRISKKDHRAY---KCTLCSdrvavgqepACVKTCPTGAIVFGTK 189
Cdd:NF038196 180 KFHvTDKCIGCGICAKVCPVN--NIEMEDGKPVwghNCTHCL---------ACIHRCPKEAIEYGKK 235
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 128-184 2.09e-06

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 44.66  E-value: 2.09e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493460140 128 FHEENCIGCGYCVTGCPFNVprISKKDHRAY----KCTLCSdrvavgqepACVKTCPTGAI 184
Cdd:COG2221   12 IDEEKCIGCGLCVAVCPTGA--ISLDDGKLVideeKCIGCG---------ACIRVCPTGAI 61
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
99-185 2.21e-06

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 48.01  E-value: 2.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  99 GCMHCEDpgCLKACPSpGAIvQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKDHRAYkcTLCS--DRVAVGQEP--- 173
Cdd:PRK07118 140 GCLGLGS--CVAACPF-DAI-HIENGLPVVDEDKCTGCGACVKACPRNVIELIPKSARVF--VACNskDKGKAVKKVcev 213

                         90
                 ....*....|....*...
gi 493460140 174 ------ACVKTCPTGAIV 185
Cdd:PRK07118 214 gcigcgKCVKACPAGAIT 231
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 95-146 2.90e-06

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 44.33  E-value: 2.90e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493460140  95 IRKDGCMHCEDpgCLKACPsPGAIVQYNNGIVDFHEENCIGCGYCVTGCPFN 146
Cdd:COG1149    8 IDEEKCIGCGL--CVEVCP-EGAIKLDDGGAPVVDPDLCTGCGACVGVCPTG 56
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
95-146 3.32e-06

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 48.10  E-value: 3.32e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493460140  95 IRKDGCMHCEDpgCLKACPsPGAIvQYNNGIVDFHEENCIGCGYCVTGCPFN 146
Cdd:COG4624   88 RDKEKCKNCYP--CVRACP-VKAI-KVDDGKAEIDEEKCISCGQCVAVCPFG 135
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
130-186 3.33e-06

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 48.32  E-value: 3.33e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493460140 130 EENCIGCGYCVTGCPFNVPRIsKKDHRAY----KCTLCsdrvavGqepACVKTCPTGAIVF 186
Cdd:COG1148  495 PEKCTGCGRCVEVCPYGAISI-DEKGVAEvnpaLCKGC------G---TCAAACPSGAISL 545
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 92-186 3.71e-06

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 45.47  E-value: 3.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  92 EWLIRKDGCMHCEDpgCLKACP---------SPGAIVQYNNGIVDfhEENCIGCGYCVTGCPFNV--------PRISKKd 154
Cdd:cd10549   34 GPEIDEDKCVFCGA--CVEVCPtgaieltpeGKEYVPKEKEAEID--EEKCIGCGLCVKVCPVDAitledeleIVIDKE- 108

                         90       100       110
                 ....*....|....*....|....*....|..
gi 493460140 155 hrayKCTLCSdrvavgqepACVKTCPTGAIVF 186
Cdd:cd10549  109 ----KCIGCG---------ICAEVCPVNAIKL 127
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 128-185 6.80e-06

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 43.50  E-value: 6.80e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493460140 128 FHEENCIGCGYCVTGCPFNVprISKKDHRAY-----KCTLCSdrvavgqepACVKTCPTGAIV 185
Cdd:COG1144   27 VDEDKCIGCGLCWIVCPDGA--IRVDDGKYYgidydYCKGCG---------ICAEVCPVKAIE 78
Fer4_9 pfam13187
4Fe-4S dicluster domain;
132-184 7.56e-06

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 42.54  E-value: 7.56e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 493460140  132 NCIGCGYCVTGCPFNVPRISKK------DHRAYKCTLCSdrvavgqepACVKTCPTGAI 184
Cdd:pfam13187   1 KCTGCGACVAACPAGAIVPDLVgqtirgDIAGLACIGCG---------ACVDACPRGAI 50
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 130-185 9.56e-06

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 43.11  E-value: 9.56e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493460140 130 EENCIGCGYCVTGCPFNVPRISKKDHR--AYKCTLCSdrvavgqepACVKTCPTGAIV 185
Cdd:COG4231   21 EDKCTGCGACVKVCPADAIEEGDGKAVidPDLCIGCG---------SCVQVCPVDAIK 69
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 127-201 2.24e-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: 2.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 127 DFHEENCIGCGYCVTGCPFNVPRISKKDHRAY-------KCTLCSdrvavgqepACVKTCPTGAIVFGTKEDMKQHAAER 199
Cdd:cd10549    2 KYDPEKCIGCGICVKACPTDAIELGPNGAIARgpeidedKCVFCG---------ACVEVCPTGAIELTPEGKEYVPKEKE 72


                 ..
gi 493460140 200 IE 201
Cdd:cd10549   73 AE 74
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 93-144 3.39e-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: 40.70  E-value: 3.39e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 493460140   93 WLIRKDGCMHCEDpgCLKACPSPGAIVQ-----YNNGIVDFHEENCIGCGYCVTGCP 144
Cdd:pfam13237   2 VVIDPDKCIGCGR--CTAACPAGLTRVGaiverLEGEAVRIGVWKCIGCGACVEACP 56
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 133-183 5.37e-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: 40.20  E-value: 5.37e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  133 CIGCGYCVTGCPFNVPRISKK---------DHRAYKCTLCsdrvavgqePACVKTCPTGA 183
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVgekkgtktvVIDPERCVGC---------GACVAVCPTGA 51
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 100-147 1.07e-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: 39.43  E-value: 1.07e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 493460140  100 CMHCEDpgCLKACPS-----PGAIVQYNNGIVDFHEENCIGCGYCVTGCPFNV 147
Cdd:pfam12838   1 CIGCGA--CVAACPVgaitlDEVGEKKGTKTVVIDPERCVGCGACVAVCPTGA 51
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
 127-196 1.19e-04

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 41.94  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 127 DFHEENCIGCGYCVTGCPFN---VPRISKKDHRAY-----KCTLCSdrvavgqepACVKTCPTGAIVFGT--------KE 190
Cdd:PRK12387  34 EYNPQQCIGCAACVNACPSNaltVETDLATGELAWefnlgRCIFCG---------RCEEVCPTAAIKLSQefelavwkKE 104


                 ....*.
gi 493460140 191 DMKQHA 196
Cdd:PRK12387 105 DLLQQS 110
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 95-146 1.69e-04

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: 39.65  E-value: 1.69e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493460140  95 IRKDGCMHCEDpgCLKACPsPGAIVQYNNGIVDFHEENCIGCGYCVTGCPFN 146
Cdd:COG1144   27 VDEDKCIGCGL--CWIVCP-DGAIRVDDGKYYGIDYDYCKGCGICAEVCPVK 75
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 97-146 1.73e-04

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 38.96  E-value: 1.73e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493460140  97 KDGCMHCEDpgCLKACPSpGAIVQYNNG---IVDFHEENCIGCGYCVTGCPFN 146
Cdd:COG1143    1 EDKCIGCGL--CVRVCPV-DAITIEDGEpgkVYVIDPDKCIGCGLCVEVCPTG 50
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
99-168 1.75e-04

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 42.23  E-value: 1.75e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  99 GCMHCEDpgCLKACPSpGAIVQYNNGIVDFHEEnCIGCGYCVTGCPFNVPRISKKDHRAYKCTLCSDRVA 168
Cdd:PRK07118 214 GCIGCGK--CVKACPA-GAITMENNLAVIDQEK-CTSCGKCVEKCPTKAIRILNKPPKVKEPKKAAAEAA 279
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
130-203 2.18e-04

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 41.02  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140 130 EENCIGCGYCVTGCPFNVPRI-------SKKDHRAY-----KCTLCSdrvavgqepACVKTCPTGAIVFGTKEDMkqhAA 197
Cdd:PRK05888  57 EERCIACKLCAAICPADAITIeaaeredGRRRTTRYdinfgRCIFCG---------FCEEACPTDAIVETPDFEL---AT 124


                 ....*.
gi 493460140 198 ERIEDL 203
Cdd:PRK05888 125 ETREEL 130
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 133-193 2.19e-04

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 40.70  E-value: 2.19e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493460140 133 CIGCGYCVTGCPFNV---------------PRIskkDHRAYKCTLCSDrvavgqepACVKTCPTGAIVFGTKEDMK 193
Cdd:cd16373   16 CIRCGLCVEACPTGViqpagledgleggrtPYL---DPREGPCDLCCD--------ACVEVCPTGALRPLDLEEQK 80
NapF COG1145
Ferredoxin [Energy production and conversion];
93-147 2.73e-04

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 41.63  E-value: 2.73e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493460140  93 WLIRKDGCMHCEDpgCLKACPSpGAIVQYNNG-IVDFHEENCIGCGYCVTGCPFNV 147
Cdd:COG1145  177 AVIDAEKCIGCGL--CVKVCPT-GAIRLKDGKpQIVVDPDKCIGCGACVKVCPVGA 229
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 124-184 3.48e-04

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 39.82  E-value: 3.48e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493460140 124 GIVDFHEENCIGCGYCVTGCPFNV----PRISKKDHRAYKCTLCSDrvavgqepaCVKTCPTGAI 184
Cdd:PRK08348  35 GKILYDVDKCVGCRMCVTVCPAGVfvylPEIRKVALWTGRCVFCGQ---------CVDVCPTGAL 90
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
133-189 3.49e-04

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 41.46  E-value: 3.49e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493460140 133 CIGCGYCVTGCPFN----VPRISKKDHRayKCTLCSdrvavgqepACVKTCPTGAIVFGTK 189
Cdd:PRK07118 141 CLGLGSCVAACPFDaihiENGLPVVDED--KCTGCG---------ACVKACPRNVIELIPK 190
flavo_MJ0208 TIGR02700
archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of ...
 91-146 3.80e-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: 41.01  E-value: 3.80e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 493460140   91 LEWLIRKDGCMHCEDpgCLKACPSpGAIVQyNNGIVDFHEENCIGCGYCVTGCPFN 146
Cdd:TIGR02700 141 TPYMIDRKRCKGCGI--CVDACPR-SAIDM-VDGKAFIRLLKCVGCGKCKEACPYN 192
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 95-146 4.80e-04

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 38.10  E-value: 4.80e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493460140  95 IRKDGCMHCEDpgCLKACPSpGAIVQyNNGIVDFHEENCIGCGYCVTGCPFN 146
Cdd:COG4231   19 IDEDKCTGCGA--CVKVCPA-DAIEE-GDGKAVIDPDLCIGCGSCVQVCPVD 66
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
95-144 7.14e-04

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 41.00  E-value: 7.14e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 493460140  95 IRKDGCMHCEdpGCLKACPSpGAIVQYNNGIVDFHEENCIGCGYCVTGCP 144
Cdd:COG1148  493 VDPEKCTGCG--RCVEVCPY-GAISIDEKGVAEVNPALCKGCGTCAAACP 539
porD PRK09625
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
 49-146 1.54e-03

pyruvate flavodoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 236596 [Multi-domain]  Cd Length: 133  Bit Score: 38.19  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  49 MEWNDLrdEIGTNVGVYDNPADLTEHSWTVMR----FSEYENPQGDleWLIRK-----DGCMHCEDpgCLKACPSpGAIV 119
Cdd:PRK09625   5 KGWDEF--EMGAVLFPFEKNAQSEMEKHNEERhyteQSSFTTSVAH--WRVEKpvhnnEICINCFN--CWVYCPD-AAIL 77

                         90       100
                 ....*....|....*....|....*..
gi 493460140 120 QYNNGIVDFHEENCIGCGYCVTGCPFN 146
Cdd:PRK09625  78 SRDKKLKGVDYSHCKGCGVCVEVCPTN 104
napG PRK09476
quinol dehydrogenase periplasmic component; Provisional
 133-183 1.60e-03

quinol dehydrogenase periplasmic component; Provisional


Pssm-ID: 236534 [Multi-domain]  Cd Length: 254  Bit Score: 39.22  E-value: 1.60e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493460140 133 CIGCGYCVTGCPFNVPRISK-KDH----------RAYKCTLCSDrvavgqePACVKTCPTGA 183
Cdd:PRK09476  61 CIRCGLCVQACPYDTLKLATlASGlsagtpyfvaRDIPCEMCED-------IPCVKACPSGA 115
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
131-188 2.26e-03

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 37.71  E-value: 2.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493460140 131 ENCIGCGYCVTGCPFN---------VPRIS--KKDHR--AYKCTLCSDRvavgqepACVKTCPTGAIVFGT 188
Cdd:COG1142   10 EKCIGCRTCEAACAVAhegeegepfLPRIRvvRKAGVsaPVQCRHCEDA-------PCAEVCPVGAITRDD 73
PRK13795 PRK13795
hypothetical protein; Provisional
 94-144 3.15e-03

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 39.21  E-value: 3.15e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493460140  94 LIRKDGCMHCedpG-CLKACPSpGAI-VQYNNGIVDFHEENCIGCGYCVTGCP 144
Cdd:PRK13795 577 LRRAAECVGC---GvCVGACPT-GAIrIEEGKRKISVDEEKCIHCGKCTEVCP 625
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 96-185 3.18e-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: 37.62  E-value: 3.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140  96 RKDGCMHCEDpGCLKACPSpGAIV-------QYNNGIVDFHEENCI------GCGYCVTGCPFNVPRISKKDHRAY---- 158
Cdd:cd16373   51 REGPCDLCCD-ACVEVCPT-GALRpldleeqKVKMGVAVIDKDRCLawqggtDCGVCVEACPTEAIAIVLEDDVLRpvvd 128

                         90       100       110
                 ....*....|....*....|....*....|..
gi 493460140 159 --KCTLCsdrvavGqepACVKTCPT---GAIV 185
Cdd:cd16373  129 edKCVGC------G---LCEYVCPVeppKAIV 151
PRK13795 PRK13795
hypothetical protein; Provisional
 133-180 3.51e-03

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 38.82  E-value: 3.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493460140 133 CIGCGYCVTGCPFNVprISKKDHRAY------KCTLCSDrvavgqepaCVKTCP 180
Cdd:PRK13795 583 CVGCGVCVGACPTGA--IRIEEGKRKisvdeeKCIHCGK---------CTEVCP 625
IOR_alpha TIGR03336
indolepyruvate ferredoxin oxidoreductase, alpha subunit; Indolepyruvate ferredoxin ...
 10-145 4.77e-03

indolepyruvate ferredoxin oxidoreductase, alpha subunit; Indolepyruvate ferredoxin oxidoreductase (IOR) is an alpha 2/beta 2 tetramer related to ketoacid oxidoreductases for pyruvate (1.2.7.1, POR), 2-ketoglutarate (1.2.7.3, KOR), and 2-oxoisovalerate (1.2.7.7, VOR). These multi-subunit enzymes typically are found in anaerobes and are inactiviated by oxygen. IOR in Pyrococcus acts in fermentation of all three aromatic amino acids, following removal of the amino group by transamination. In Methanococcus maripaludis, by contrast, IOR acts in the opposite direction, in pathways of amino acid biosynthesis from phenylacetate, indoleacetate, and p-hydroxyphenylacetate. In M. maripaludis and many other species, iorA and iorB are found next to an apparent phenylacetate-CoA ligase.


Pssm-ID: 274526 [Multi-domain]  Cd Length: 595  Bit Score: 38.55  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493460140   10 RVSATT--TPPPTAREPVTGSVAKLIDVSKCigCKACQTacmewndlrdeigTNVGVYDnPADLTEHSWTVMRFSEYE-- 85
Cdd:TIGR03336 459 RITAMTghQPNPGTGVTGMGEATKEISIEEL--CRASGV-------------EFVEVVD-PLNVKETIEVFKAALAAEgv 522

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493460140   86 ------------NPQGDLEWLIRK---DGCMHCEDpgCLK--ACPspgAIVQYNNGIVDfhEENCIGCGYCVTGCPF 145
Cdd:TIGR03336 523 sviiakqpcvlsNKRAGKRAGPYKvdqDKCIGCKK--CIKelGCP---AIEPEDKEAVI--DPLCTGCGVCAQICPF 592
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
129-146 4.79e-03

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 38.25  E-value: 4.79e-03
                         10
                 ....*....|....*...
gi 493460140 129 HEENCIGCGYCVTGCPFN 146
Cdd:PRK13409  47 SEELCIGCGICVKKCPFD 64
ndhI CHL00014
NADH dehydrogenase subunit I
 124-181 5.74e-03

NADH dehydrogenase subunit I


Pssm-ID: 214334 [Multi-domain]  Cd Length: 167  Bit Score: 37.05  E-value: 5.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493460140 124 GIVDFHEENCIGCGYCVTGCPFNVP--------RISKKDHRAYK-----CTLCSDrvavgqepaCVKTCPT 181
Cdd:CHL00014  52 GRIHFEFDKCIACEVCVRVCPIDLPvvdwkletDIRKKRLLNYSidfgvCIFCGN---------CVEYCPT 113
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
86-154 6.27e-03

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 35.69  E-value: 6.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493460140  86 NPQGDleW-----LIRKDGCMHCEDpgCLKACPSPgAIVQYNNGIVDFHEENCIGCGYCVTGCPFNVPRISKKD 154
Cdd:PRK09623  36 NFTGD--WrtfmpVVDESKCVKCYI--CWKFCPEP-AIYIKEDGYVAIDYDYCKGCGICANECPTKAITMVKEE 104
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 129-146 9.43e-03

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 37.46  E-value: 9.43e-03
                         10
                 ....*....|....*...
gi 493460140 129 HEENCIGCGYCVTGCPFN 146
Cdd:COG1245   47 SEELCIGCGICVKKCPFD 64
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH