NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|839824826|gb|KMI97293|]
View 

formate dehydrogenase-O iron-sulfur subunit [Klebsiella pneumoniae]

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 ...
7-283 9.72e-165

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


The actual alignment was detected with superfamily member TIGR01582:

Pssm-ID: 273705 [Multi-domain]  Cd Length: 283  Bit Score: 458.99  E-value: 9.72e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826    7 DIIRRSATNGftPAPQARDHQQEVAKLIDVTTCIGCKACQVACSEWNDIRDEVG-HNVGVYDNPADLTAKSWTVMRFSEV 85
Cdd:TIGR01582   1 DIKRLSATKE--PDPSVKTYPTELAKLIDVSSCIGCKACQAACQEWNDTTPPILsRKVGGYQNPPDLLPETFTLMRFKEG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826   86 EQNDKLEWLIRKDGCMHCADPGCLKACPSEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVD 165
Cdd:TIGR01582  79 EESDGLEWLIRKDGCMHCREPGCLKACPAPGAIIQYQNGIVDFDHSKCIGCGYCIVGCPFNIPRYDKVDNRPYKCTLCID 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  166 RVTVGQEPACVKTCPTGAIHFGSKEDMKTLAGERVAELKTRGYDNAGLYDPAGVGGTHVMYVLHHADKPNLYHGLPENPE 245
Cdd:TIGR01582 159 RVSVGQEPACVKTCPTNAISFGFKEDMKERAEKRVADLKSRGYPNAGLYDPPGVGGTHVMYVLHHGDKPKDYQDLPEDPR 238
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 839824826  246 ISQTVKFWKGIWKPLAAVGFAATFAASIFHYVGVGPNR 283
Cdd:TIGR01582 239 IDASVGLWKGVLKTIGSIAMGGTALGVFLHLILWGPNK 276
 
Name Accession Description Interval E-value
FDH-beta TIGR01582
formate dehydrogenase, beta subunit, Fe-S containing; This model represents the beta subunit ...
7-283 9.72e-165

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


Pssm-ID: 273705 [Multi-domain]  Cd Length: 283  Bit Score: 458.99  E-value: 9.72e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826    7 DIIRRSATNGftPAPQARDHQQEVAKLIDVTTCIGCKACQVACSEWNDIRDEVG-HNVGVYDNPADLTAKSWTVMRFSEV 85
Cdd:TIGR01582   1 DIKRLSATKE--PDPSVKTYPTELAKLIDVSSCIGCKACQAACQEWNDTTPPILsRKVGGYQNPPDLLPETFTLMRFKEG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826   86 EQNDKLEWLIRKDGCMHCADPGCLKACPSEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVD 165
Cdd:TIGR01582  79 EESDGLEWLIRKDGCMHCREPGCLKACPAPGAIIQYQNGIVDFDHSKCIGCGYCIVGCPFNIPRYDKVDNRPYKCTLCID 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  166 RVTVGQEPACVKTCPTGAIHFGSKEDMKTLAGERVAELKTRGYDNAGLYDPAGVGGTHVMYVLHHADKPNLYHGLPENPE 245
Cdd:TIGR01582 159 RVSVGQEPACVKTCPTNAISFGFKEDMKERAEKRVADLKSRGYPNAGLYDPPGVGGTHVMYVLHHGDKPKDYQDLPEDPR 238
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 839824826  246 ISQTVKFWKGIWKPLAAVGFAATFAASIFHYVGVGPNR 283
Cdd:TIGR01582 239 IDASVGLWKGVLKTIGSIAMGGTALGVFLHLILWGPNK 276
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
31-238 6.98e-153

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: 426.03  E-value: 6.98e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  31 AKLIDVTTCIGCKACQVACSEWNDIRDEVGHNVGVYDNPADLTAKSWTVMRFSEVEQNDKLEWLIRKDGCMHCADPGCLK 110
Cdd:cd10558    1 AKLIDVSKCIGCKACQVACKEWNDLRAEVGHNVGTYQNPADLSPETWTLMKFREVEDNGKLEWLIRKDGCMHCADPGCLK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 111 ACPSEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVDRVTVGQEPACVKTCPTGAIHFGSKE 190
Cdd:cd10558   81 ACPSPGAIVQYANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVGLEPACVKTCPTGALHFGTKE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 839824826 191 DMKTLAGERVAELKTRGYDNAGLYDPAGVGGTHVMYVLHHADKPNLYH 238
Cdd:cd10558  161 DMLALAEKRVAALKERGYTNAGLYDPKGVGGTHVMYVLHHADKPEGYP 208
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
25-227 2.23e-71

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 218.28  E-value: 2.23e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  25 DHQQEVAKLIDVTTCIGCKACQVACSEWNDIRDEVghnvgvydnpadltakSWTVMRFSEVEQNDKLEWLIRKDGCMHCA 104
Cdd:COG0437    1 LSMKRYGMVIDLTKCIGCRACVVACKEENNLPVGV----------------TWRRVRRYEEGEFPNVEWLFVPVLCNHCD 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 105 DPGCLKACPSeGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVDRVTVGQEPACVKTCPTGAI 184
Cdd:COG0437   65 DPPCVKVCPT-GATYKREDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVEACPTGAL 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 839824826 185 HFGSKEDMKTLAGERVAELKTRgydnaGLYDPAGvGGTHVMYV 227
Cdd:COG0437  144 VFGDLDDPESEVSKRLAELPAY-----RLLPELG-TKPSVYYL 180
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
13-270 1.36e-44

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 154.06  E-value: 1.36e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  13 ATNGFTPAPQARDHQQE------VAKLIDVTTCIGCKACQVACSEWNDIRDEVGHNvGVYDNPADLTAKSWTVM---RFS 83
Cdd:PRK10882  15 LLAGALPSVSHAAAENRppipgaLGMLYDSTLCVGCQACVTKCQEINFPERNPQGE-QTWDNPDKLSPYTNNIIkvwKSG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  84 EVEQNDKLE--WLIRKDGCMHCADPGCLKACPSEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPED--NRVYK 159
Cdd:PRK10882  94 TGVNKDQEEngYAYIKKQCMHCVDPNCVSVCPVSALTKDPKTGIVHYDKDVCTGCRYCMVACPFNVPKYDYNNpfGAIHK 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 160 CTLC----VDRVTVGQEPACVKTCPTGAIHFGSKEDMKTLAGERVAE-------------------LKTRGYDNAGLYDP 216
Cdd:PRK10882 174 CELCnqkgVERLDKGGLPGCVEVCPTGAVIFGTREELLAEAKRRLALkpgseyhyprqtlksgdtyLHTVPKYYPHVYGE 253
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 839824826 217 AGVGGTHVMYvLHHADKPNLyhGLPENPEISQTVK-------FWKGIWKPLAAVGFAATFA 270
Cdd:PRK10882 254 KEGGGTQVLV-LSGVPFENL--GLPKLDDLSTGARsehiqhtLYKGMILPLAVLAGLTVLV 311
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
91-187 1.66e-29

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


Pssm-ID: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 107.72  E-value: 1.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826   91 LEWLIRKDGCMHCADPGCLKACPSeGAIIQ-YANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVDRVTV 169
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPV-GAIYKdEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEA 79
                          90
                  ....*....|....*...
gi 839824826  170 GQEPACVKTCPTGAIHFG 187
Cdd:pfam13247  80 GLLPACVQTCPTGAMNFG 97
FDH3_beta NF038355
formate dehydrogenase FDH3 subunit beta; Members of this family are the beta subunit of the ...
33-208 4.90e-21

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


Pssm-ID: 439648 [Multi-domain]  Cd Length: 180  Bit Score: 88.20  E-value: 4.90e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  33 LIDVTTCIGCKACQVACSEWNDIrdevghnvgvydnpadltakSWTVMRFSEVEQNDKLEWLIRKD-GCMHCADPGCLKA 111
Cdd:NF038355   6 LCDTERCIECNGCVVACKNAHEL--------------------PWGINRRRVVTLNDGVPGEKSISvACMHCTDAPCAAV 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 112 CPSEgAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLnPEDN------RVYKCTLC-----------------VDRVT 168
Cdd:NF038355  66 CPVD-CFYIRADGIVLHDKDKCIGCGYCLYACPFGAPQF-PKDGafgargKMDKCTFCaggpeetnseaerekygQNRIA 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 839824826 169 VGQEPACVKTCPTGAIHFGSKEDMKTLAGERVAelkTRGY 208
Cdd:NF038355 144 EGKLPLCAEMCSTKALLAGDAEVVADIYRERVV---ARGA 180
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
130-189 2.12e-05

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


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 44.85  E-value: 2.12e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 839824826 130 SEQCIGCGYCIAGCPFDVPRLnpEDNRVY---KCTLCVdrvtvgqepACVKTCPTGAIHFGSK 189
Cdd:NF038196 184 TDKCIGCGICAKVCPVNNIEM--EDGKPVwghNCTHCL---------ACIHRCPKEAIEYGKK 235
 
Name Accession Description Interval E-value
FDH-beta TIGR01582
formate dehydrogenase, beta subunit, Fe-S containing; This model represents the beta subunit ...
7-283 9.72e-165

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


Pssm-ID: 273705 [Multi-domain]  Cd Length: 283  Bit Score: 458.99  E-value: 9.72e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826    7 DIIRRSATNGftPAPQARDHQQEVAKLIDVTTCIGCKACQVACSEWNDIRDEVG-HNVGVYDNPADLTAKSWTVMRFSEV 85
Cdd:TIGR01582   1 DIKRLSATKE--PDPSVKTYPTELAKLIDVSSCIGCKACQAACQEWNDTTPPILsRKVGGYQNPPDLLPETFTLMRFKEG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826   86 EQNDKLEWLIRKDGCMHCADPGCLKACPSEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVD 165
Cdd:TIGR01582  79 EESDGLEWLIRKDGCMHCREPGCLKACPAPGAIIQYQNGIVDFDHSKCIGCGYCIVGCPFNIPRYDKVDNRPYKCTLCID 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  166 RVTVGQEPACVKTCPTGAIHFGSKEDMKTLAGERVAELKTRGYDNAGLYDPAGVGGTHVMYVLHHADKPNLYHGLPENPE 245
Cdd:TIGR01582 159 RVSVGQEPACVKTCPTNAISFGFKEDMKERAEKRVADLKSRGYPNAGLYDPPGVGGTHVMYVLHHGDKPKDYQDLPEDPR 238
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 839824826  246 ISQTVKFWKGIWKPLAAVGFAATFAASIFHYVGVGPNR 283
Cdd:TIGR01582 239 IDASVGLWKGVLKTIGSIAMGGTALGVFLHLILWGPNK 276
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
31-238 6.98e-153

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: 426.03  E-value: 6.98e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  31 AKLIDVTTCIGCKACQVACSEWNDIRDEVGHNVGVYDNPADLTAKSWTVMRFSEVEQNDKLEWLIRKDGCMHCADPGCLK 110
Cdd:cd10558    1 AKLIDVSKCIGCKACQVACKEWNDLRAEVGHNVGTYQNPADLSPETWTLMKFREVEDNGKLEWLIRKDGCMHCADPGCLK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 111 ACPSEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVDRVTVGQEPACVKTCPTGAIHFGSKE 190
Cdd:cd10558   81 ACPSPGAIVQYANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVGLEPACVKTCPTGALHFGTKE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 839824826 191 DMKTLAGERVAELKTRGYDNAGLYDPAGVGGTHVMYVLHHADKPNLYH 238
Cdd:cd10558  161 DMLALAEKRVAALKERGYTNAGLYDPKGVGGTHVMYVLHHADKPEGYP 208
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
32-187 8.85e-87

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: 256.56  E-value: 8.85e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  32 KLIDVTTCIGCKACQVACSEWNDIRDEVGHNVGVYDNPADLTAKSWTVMRFSEVEQND-KLEWLIRKDGCMHCADPGCLK 110
Cdd:cd16366    1 FLVDTSRCTGCRACQVACKQWNGLPAEKTEFTGSYQNPPDLTAHTWTLVRFYEVEKPGgDLSWLFRKDQCMHCTDAGCLA 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 839824826 111 ACPSeGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVDRVTVGQEPACVKTCPTGAIHFG 187
Cdd:cd16366   81 ACPT-GAIIRTETGTVVVDPETCIGCGYCVNACPFDIPRFDEETGRVAKCTLCYDRISNGLQPACVKTCPTGALTFG 156
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
33-248 1.81e-81

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: 245.37  E-value: 1.81e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  33 LIDVTTCIGCKACQVACSEWNDIRDEVGHNVG-VYDNPADLTAKSWTVMRFSEVEQNDK-------LEWLIRKDGCMHCA 104
Cdd:cd10560    3 FTDTSICIGCKACEVACKQWNQLPADGYDFSGmSYDNTGDLSASTWRHVKFIERPTEDGpaneggdLQWLFMSDVCKHCT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 105 DPGCLKACPSeGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVDRVTVGQEPACVKTCPTGAI 184
Cdd:cd10560   83 DAGCLEACPT-GAIFRTEFGTVYIQPDICNGCGYCVAACPFGVIDRNEETGRAHKCTLCYDRLKDGLEPACAKACPTGSI 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 839824826 185 HFGSKEDMKTLAGERVAELKTRGYDNAGLY--DP-AGVGGTHVMYVLhhADKPNLYhGLPENPEISQ 248
Cdd:cd10560  162 QFGPLEELRERARARVEQLHEQGVVEAYLYgaDPtEGYGGLNAFFLL--LDKPEVY-GLPADPLLPT 225
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
32-192 2.89e-75

uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes the beta-subunit of formate dehydrogenases that are as yet uncharacterized. Members of the DMSO reductase family include formate dehydrogenase N and O (FDH-N, FDH-O) and tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N, a major component of nitrate respiration of Escherichia coli, is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. It forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.


Pssm-ID: 319884 [Multi-domain]  Cd Length: 161  Bit Score: 227.57  E-value: 2.89e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  32 KLIDVTTCIGCKACQVACSEWNDIRDEVGHNVGVYDNPADLTAKSWTVMRFSEVE-QNDKLEWLIRKDGCMHCADPGCLK 110
Cdd:cd10562    1 MLVDTSKCTACRGCQVACKQWNQLPAEKTPFTGSYQNPPDLTPNTWTLIRFYEHEeDNGGIRWLFRKRQCMHCTDAACVK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 111 ACPsEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVDRVTVGQEPACVKTCPTGAIHFGSKE 190
Cdd:cd10562   81 VCP-TGALYKTENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCFDRIENGMQPACVKTCPTGALTFGDRD 159

                 ..
gi 839824826 191 DM 192
Cdd:cd10562  160 EL 161
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
25-227 2.23e-71

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 218.28  E-value: 2.23e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  25 DHQQEVAKLIDVTTCIGCKACQVACSEWNDIRDEVghnvgvydnpadltakSWTVMRFSEVEQNDKLEWLIRKDGCMHCA 104
Cdd:COG0437    1 LSMKRYGMVIDLTKCIGCRACVVACKEENNLPVGV----------------TWRRVRRYEEGEFPNVEWLFVPVLCNHCD 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 105 DPGCLKACPSeGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVDRVTVGQEPACVKTCPTGAI 184
Cdd:COG0437   65 DPPCVKVCPT-GATYKREDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVEACPTGAL 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 839824826 185 HFGSKEDMKTLAGERVAELKTRgydnaGLYDPAGvGGTHVMYV 227
Cdd:COG0437  144 VFGDLDDPESEVSKRLAELPAY-----RLLPELG-TKPSVYYL 180
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
31-226 6.88e-66

the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 (Hyd-2), an enzyme that catalyzes the reversible oxidation of H2 to protons and electrons. Hyd-2 is membrane-associated and forms an unusual heterotetrameric [NiFe]-hydrogenase in that it lacks the typical cytochrome b membrane anchor subunit that transfers electrons to the quinone pool. The electron transfer subunit of Hyd-2 (HybA) which is predicted to contain four iron-sulfur clusters, is essential for electron transfer from Hyd-2 to menaquinone/demethylmenaquinone (MQ/DMQ) to couple hydrogen oxidation to fumarate reduction.


Pssm-ID: 319883 [Multi-domain]  Cd Length: 196  Bit Score: 204.75  E-value: 6.88e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  31 AKLIDVTTCIGCKACQVACSEWNDIRDEVGHNVGVYDNPADLTAKSWTVMRFSEVEqNDKLEWLIRKDGCMHCADPGCLK 110
Cdd:cd10561    1 GVLYDTTRCIGCRACEVACKEWNGLPAEDTAFGPGWDNPRDLSAKTYTVIKRYEVE-TGGKGFVFVKRQCMHCLDPACVS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 111 ACPSeGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPR-----LNPednRVYKCTLCVDRVTVGQEPACVKTCPTGAIH 185
Cdd:cd10561   80 ACPV-GALRKTPEGPVTYDEDKCIGCRYCMVACPFNIPKyewdsANP---KIRKCTMCYDRLKEGKQPACVEACPTGALL 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 839824826 186 FGSKEDMKTLAGERVAELKTRGYDNA-GLYDpagVGGTHVMY 226
Cdd:cd10561  156 FGKREELLAEAKRRIAANPGRYVDHVyGEKE---AGGTSVLY 194
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
33-230 7.13e-63

tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit of Tungsten-containing formate dehydrogenase (W-FDH), a member of the DMSO reductase family. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.


Pssm-ID: 319881 [Multi-domain]  Cd Length: 200  Bit Score: 197.27  E-value: 7.13e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  33 LIDVTTCIGCKACQVACSEWNDIRDEVGHNVGVYDNPADLTAKSWTVMRFSEVE-QNDKLEWLIRKDGCMHCADPGCLKA 111
Cdd:cd10559    3 LIDTTRCTACRGCQVACKQWNQLPAEQTKNTGSHQNPPDLSANTYKLVRFNEVRnENGKPDWLFFPDQCRHCVTPPCKDA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 112 CPS-EGAIIQ-YANGIVDFQSEQCIGC-GYCIAGCPFDVPRLNPEDNRVYKCTLCVDRVTVGQEPACVKTCPTGAIHFGS 188
Cdd:cd10559   83 ADMvPGAVIQdEATGAVVFTEKTAELDfDDVLSACPYNIPRKNEATGRIVKCDMCIDRVSNGLQPACVKACPTGAMNFGD 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 839824826 189 KEDMKTLAGERVAELKTRgYDNAGLYDPAGVggtHVMYVLHH 230
Cdd:cd10559  163 RDEMLAMASKRLEELKKR-YPKANLYDPDDV---RVIWLLAE 200
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
33-187 5.46e-50

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


Pssm-ID: 319870 [Multi-domain]  Cd Length: 136  Bit Score: 162.17  E-value: 5.46e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  33 LIDVTTCIGCKACQVACSEWNDIRdevghnvgvydnpadlTAKSWTVMRFSEVEqndKLEWLIRKDGCMHCADPGCLKAC 112
Cdd:cd04410    2 VVDLDRCIGCGTCEVACKQEHGLR----------------PGPDWSRIKVIEGG---GLERAFLPVSCMHCEDPPCVKAC 62
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 839824826 113 PSeGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVDRVTVGQEPACVKTCPTGAIHFG 187
Cdd:cd04410   63 PT-GAIYKDEDGIVLIDEDKCIGCGSCVEACPYGAIVFDPEPGKAVKCDLCGDRLDEGLEPACVKACPTGALTFG 136
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
33-187 4.91e-49

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


Pssm-ID: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 159.65  E-value: 4.91e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  33 LIDVTTCIGCKACQVACSEWNDIRDEVghnvgvydnpadltakswtvmRFSEVEQNDKLEWLIRKD-----GCMHCADPG 107
Cdd:cd16371    3 YFDQERCIGCKACEIACKDKNDLPPGV---------------------NWRRVYEYEGGEFPEVFAyflsmSCNHCENPA 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 108 CLKACPsEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVDRVTVGQEPACVKTCPTGAIHFG 187
Cdd:cd16371   62 CVKVCP-TGAITKREDGIVVVDQDKCIGCGYCVWACPYGAPQYNPETGKMDKCDMCVDRLDEGEKPACVAACPTRALDFG 140
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
33-206 3.60e-46

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: 153.84  E-value: 3.60e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  33 LIDVTTCIGCKACQVACSEWNDIRDEVGHNvgvydnpadltaksWTVMRFSEVEQNDKLEWLIRkdGCMHCADPGCLKAC 112
Cdd:cd10551    2 VIDLRKCIGCGACVVACKAENNVPPGVFRN--------------RVLEYEVGEYPNVKRTFLPV--LCNHCENPPCVKVC 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 113 PSeGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVY------------KCTLCVDRVTVGQEPACVKTCP 180
Cdd:cd10551   66 PT-GATYKREDGIVLVDYDKCIGCRYCMAACPYGARYFNPEEPHEFgevpvrpkgvveKCTFCYHRLDEGLLPACVEACP 144
                        170       180
                 ....*....|....*....|....*.
gi 839824826 181 TGAIHFGSKEDMKTLAGERVAELKTR 206
Cdd:cd10551  145 TGARIFGDLDDPNSEVSKLLAERRAY 170
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
13-270 1.36e-44

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 154.06  E-value: 1.36e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  13 ATNGFTPAPQARDHQQE------VAKLIDVTTCIGCKACQVACSEWNDIRDEVGHNvGVYDNPADLTAKSWTVM---RFS 83
Cdd:PRK10882  15 LLAGALPSVSHAAAENRppipgaLGMLYDSTLCVGCQACVTKCQEINFPERNPQGE-QTWDNPDKLSPYTNNIIkvwKSG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  84 EVEQNDKLE--WLIRKDGCMHCADPGCLKACPSEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPED--NRVYK 159
Cdd:PRK10882  94 TGVNKDQEEngYAYIKKQCMHCVDPNCVSVCPVSALTKDPKTGIVHYDKDVCTGCRYCMVACPFNVPKYDYNNpfGAIHK 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 160 CTLC----VDRVTVGQEPACVKTCPTGAIHFGSKEDMKTLAGERVAE-------------------LKTRGYDNAGLYDP 216
Cdd:PRK10882 174 CELCnqkgVERLDKGGLPGCVEVCPTGAVIFGTREELLAEAKRRLALkpgseyhyprqtlksgdtyLHTVPKYYPHVYGE 253
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 839824826 217 AGVGGTHVMYvLHHADKPNLyhGLPENPEISQTVK-------FWKGIWKPLAAVGFAATFA 270
Cdd:PRK10882 254 KEGGGTQVLV-LSGVPFENL--GLPKLDDLSTGARsehiqhtLYKGMILPLAVLAGLTVLV 311
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
33-191 7.38e-35

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


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 123.15  E-value: 7.38e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  33 LIDVTTCIGCKACQVACSEWNDirdevGHNvgvydnpadltakswtvmRFSEVEQNDKLEWLIRkdgCMHCADPGCLKAC 112
Cdd:cd16374    2 YVDPERCIGCRACEIACAREHS-----GKP------------------RISVEVVEDLASVPVR---CRHCEDAPCMEVC 55
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 839824826 113 PSeGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVDRVTVGQEPACVKTCPTGAIHFGSKED 191
Cdd:cd16374   56 PT-GAIYRDEDGAVLVDPDKCIGCGMCAMACPFGVPRFDPSLKVAVKCDLCIDRRREGKLPACVEACPTGALKFGDIEE 133
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
34-192 2.71e-34

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


Pssm-ID: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 122.88  E-value: 2.71e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  34 IDVTTCIGCKACQVACSEWNDIRDEVGHNVGvYDNPADLTAKSWTVmrfseveqndklewlirkdgCMHCADPGCLKACP 113
Cdd:cd16369    6 IDPSRCIGCRACVAACRECGTHRGKSMIHVD-YIDRGESTQTAPTV--------------------CMHCEDPTCAEVCP 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 114 SEgAIIQYANGIV-DFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVDRVTVGQEPACVKTCPTGAIHFGSKEDM 192
Cdd:cd16369   65 AD-AIKVTEDGVVqSALKPRCIGCSNCVNACPFGVPKYDEERNLMMKCDMCYDRTSVGKAPMCASVCPSGALFYGTREEI 143
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
35-188 1.21e-32

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


Pssm-ID: 319875 [Multi-domain]  Cd Length: 146  Bit Score: 117.46  E-value: 1.21e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  35 DVTTCIGCKACQVACSEWNdirdevghNVGVYDNPADLTAKSwtvmrFSEVEQNDKLEWLIRKdgCMHCADPGCLKACPS 114
Cdd:cd10553    8 DSKRCIGCLACEVHCKVKN--------NLPVGPRLCRIFAVG-----PKMVGGKPRLKFVYMS--CFHCENPWCVKACPT 72
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 839824826 115 eGAIIQY-ANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVDRVTVGQEPACVKTCPTGAIHFGS 188
Cdd:cd10553   73 -GAMQKReKDGIVYVDQELCIGCKACIEACPWGIPQWNPATGKVVKCDYCMDRIDQGLKPACVTGCTTHALSFVR 146
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
33-187 1.49e-29

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


Pssm-ID: 319885 [Multi-domain]  Cd Length: 140  Bit Score: 109.27  E-value: 1.49e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  33 LIDVTTCIGCKACQVACSewndirdeVGHNVgvYDNPADLTAKSWTVMRFSEVEQNDKLEWLIRkdgCMHCADPGCLKAC 112
Cdd:cd10563    3 FIDEEKCLGCKLCEVACA--------VAHSK--SKDLIKAKLEKERPRPRIRVEESGGRSFPLQ---CRHCDEPPCVKAC 69
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 839824826 113 PSeGAIIQY-ANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVDRvtvgQEPACVKTCPTGAIHFG 187
Cdd:cd10563   70 MS-GAMHKDpETGIVIHDEEKCVGCWMCVMVCPYGAIRPDKERKVALKCDLCPDR----ETPACVEACPTGALVLE 140
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
91-187 1.66e-29

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


Pssm-ID: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 107.72  E-value: 1.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826   91 LEWLIRKDGCMHCADPGCLKACPSeGAIIQ-YANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVDRVTV 169
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPV-GAIYKdEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEA 79
                          90
                  ....*....|....*...
gi 839824826  170 GQEPACVKTCPTGAIHFG 187
Cdd:pfam13247  80 GLLPACVQTCPTGAMNFG 97
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
33-186 9.34e-29

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


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 106.89  E-value: 9.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  33 LIDVTTCIGCKACQVACSEwndirdevgHNVGVYdNPAdltaKS-WTVMRFSEVEqndklewLIRKDGCMHCADPGCLKA 111
Cdd:cd10550    2 VVDPEKCTGCRTCELACSL---------KHEGVF-NPS----LSrIRVVRFEPEG-------LDVPVVCRQCEDAPCVEA 60
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 839824826 112 CPsEGAIIQ-YANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCvdrvtvGQEPACVKTCPTGAIHF 186
Cdd:cd10550   61 CP-VGAISRdEETGAVVVDEDKCIGCGMCVEACPFGAIRVDPETGKAIKCDLC------GGDPACVKVCPTGALEF 129
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
30-196 1.68e-28

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


Pssm-ID: 319890 [Multi-domain]  Cd Length: 200  Bit Score: 108.28  E-value: 1.68e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  30 VAKLIDVTTCIGCK-----ACQVACSEWNDIR--DEVGHNVGVY-------------DNPADLTAKSWTVMRFSEVEQND 89
Cdd:cd16368    1 LATLIDLTKCDGCPgesipACVRACREKNQARfpEPVSKPIQPYwprkriedwsdkrDVTDRLTPYNWLYVQKLTVDTAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  90 KLEWLIRKDGCMHCADPGCLKACPSeGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPR----------LNPE---DNR 156
Cdd:cd16368   81 GEKEVFIPRRCMHCDNPPCAKLCPF-GAARKTPEGAVYIDDDLCFGGAKCRDVCPWHIPQrqagvgiylhLAPEyagGGV 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 839824826 157 VYKCTLCVDRVTVGQEPACVKTCPTGAIHFGSKEDMKTLA 196
Cdd:cd16368  160 MYKCDLCKDLLAQGKPPACIEACPKGAQYFGPRKEMVALA 199
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
13-204 9.95e-27

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 104.96  E-value: 9.95e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  13 ATNGFTPAPQARDHQQEVAKLIDVTTCIGCKACQVACSEWNDI-RDEVGHNVGVYDnpadltakswTVMRFSEVEQNDKL 91
Cdd:PRK14993  27 AKFPFSPERHEGSPRHRYAMLIDLRRCIGCQSCTVSCTIENQTpQGAFRTTVNQYQ----------VQREGSQEVTNVLL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  92 EWLirkdgCMHCADPGCLKACPSEgAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVDRVTVGQ 171
Cdd:PRK14993  97 PRL-----CNHCDNPPCVPVCPVQ-ATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGL 170
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 839824826 172 EPACVKTCPTGAIHFGSKED----MKTLAGERVAELK 204
Cdd:PRK14993 171 LPACVESCVGGARIIGDIKDphsrIATMLHQHRDAIK 207
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
33-203 2.63e-24

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: 97.01  E-value: 2.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  33 LIDVTTCIGCKACQVACsewndiRDE-VGHNVGVYDNPADLTAKSWtvMRFSEVEQND--KLEWLIRKDGCMHCADPGCL 109
Cdd:cd10552    2 VIDVAKCNGCYNCFLAC------KDEhVGNDWPGYAAPQPRHGHFW--MRILRRERGQypKVDVAYLPVPCNHCDNAPCI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 110 KACPSeGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVDRVTVG-QEPACVKTCPTGAIHFGS 188
Cdd:cd10552   74 KAAKD-GAVYKRDDGIVIIDPEKAKGQKQLVDACPYGAIYWNEELQVPQKCTFCAHLLDDGwKEPRCVQACPTGALRFGK 152
                        170
                 ....*....|....*..
gi 839824826 189 KED--MKTLAGERVAEL 203
Cdd:cd10552  153 LEDeeMAAKAAEEGLEV 169
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
33-186 5.32e-23

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 92.03  E-value: 5.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  33 LIDVTTCIGCKACQVACSewndirdeVGHNVGVYDNPadltaKSW-TVMRFSEVeqndklewlIRKDGCMHCADPGCLKA 111
Cdd:COG1142    6 IADPEKCIGCRTCEAACA--------VAHEGEEGEPF-----LPRiRVVRKAGV---------SAPVQCRHCEDAPCAEV 63
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 839824826 112 CPsEGAIIQyANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNR--VYKCTLCVDRvtvGQEPACVKTCPTGAIHF 186
Cdd:COG1142   64 CP-VGAITR-DDGAVVVDEEKCIGCGLCVLACPFGAITMVGEKSRavAVKCDLCGGR---EGGPACVEACPTGALRL 135
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
39-186 1.57e-22

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


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 91.17  E-value: 1.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  39 CIGCKACQVACSEWNdirdEVGHNVGVYDNPADLTAKSWtvmrfseveqndklewLIRKDG------CMHCADPGCLKAC 112
Cdd:cd10554    9 CIGCRTCEVACAAAH----SGKGIFEAGTDGLPFLPRLR----------------VVKTGEvtapvqCRQCEDAPCANVC 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 113 PSeGAIIQyANGIVDFQSEQCIGCGYCIAGCPF-----------DVPRLNPEDNRVYKCTLCVDRvtvGQEPACVKTCPT 181
Cdd:cd10554   69 PV-GAISQ-EDGVVQVDEERCIGCKLCVLACPFgaiemapttvpGVDWERGPRAVAVKCDLCAGR---EGGPACVEACPT 143

                 ....*
gi 839824826 182 GAIHF 186
Cdd:cd10554  144 KALTL 148
FDH3_beta NF038355
formate dehydrogenase FDH3 subunit beta; Members of this family are the beta subunit of the ...
33-208 4.90e-21

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


Pssm-ID: 439648 [Multi-domain]  Cd Length: 180  Bit Score: 88.20  E-value: 4.90e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  33 LIDVTTCIGCKACQVACSEWNDIrdevghnvgvydnpadltakSWTVMRFSEVEQNDKLEWLIRKD-GCMHCADPGCLKA 111
Cdd:NF038355   6 LCDTERCIECNGCVVACKNAHEL--------------------PWGINRRRVVTLNDGVPGEKSISvACMHCTDAPCAAV 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 112 CPSEgAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLnPEDN------RVYKCTLC-----------------VDRVT 168
Cdd:NF038355  66 CPVD-CFYIRADGIVLHDKDKCIGCGYCLYACPFGAPQF-PKDGafgargKMDKCTFCaggpeetnseaerekygQNRIA 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 839824826 169 VGQEPACVKTCPTGAIHFGSKEDMKTLAGERVAelkTRGY 208
Cdd:NF038355 144 EGKLPLCAEMCSTKALLAGDAEVVADIYRERVV---ARGA 180
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
28-194 2.75e-20

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


Pssm-ID: 319887 [Multi-domain]  Cd Length: 201  Bit Score: 86.48  E-value: 2.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  28 QEVAKLIDVTTCIGCKACQVACSEWNDIRDEVGH----NVGVYdnPADLTAKSWtvmrfsEVEQNDKLEWL----IRKDG 99
Cdd:cd16365    1 KQFAAVFNLNKCIGCQTCTVACKNAWTYRKGQEYmwwnNVETK--PGGGYPQDW------EVKTIDNGGNTrfffYLQRL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 100 CMHCADPGCLKACPSEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVDRVTVGQEPACVKTC 179
Cdd:cd16365   73 CNHCTNPACLAACPRGAIYKREEDGIVLIDQKRCRGYRKCVEQCPYKKIYFNGLSRVSEKCIACYPRIEGGDPTRCMSAC 152
                        170
                 ....*....|....*
gi 839824826 180 PTGAIHFGSKEDMKT 194
Cdd:cd16365  153 VGRIRLQGFLDDNPK 167
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
39-199 4.59e-20

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 90.19  E-value: 4.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  39 CIGCKACQVACSewndirdeVGHNVGVY-DNPADLTAKswtVMRFSEVEQNDKLEwlirkdgCMHCADPGCLKACPSeGA 117
Cdd:PRK12769  12 CLGCHACEIACV--------MAHNDEQHvLSQHHFHPR---ITVIKHQQQRSAVT-------CHHCEDAPCARSCPN-GA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 118 IIQYANGIVDFQsEQCIGCGYCIAGCPFDVPR--LNPEDN-----RVYKCTLCVDRvtvGQEPACVKTCPTGAIHFGSKE 190
Cdd:PRK12769  73 ISHVDDSIQVNQ-QKCIGCKSCVVACPFGTMQivLTPVAAgkvkaTAHKCDLCAGR---ENGPACVENCPADALQLVTEQ 148

                 ....*....
gi 839824826 191 DMKTLAGER 199
Cdd:PRK12769 149 ALSGMAKSR 157
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
100-191 4.83e-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: 85.43  E-value: 4.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 100 CMHCADPGCLKACPSeGAIIQYA-NGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVDRVTVGQEPACVKT 178
Cdd:cd10555  133 CNHCTNPACLAACPR-KAIYKREeDGIVLVDQDRCRGYRYCVEACPYKKIYFNPVEQKSEKCIFCYPRIEKGVAPACARQ 211
                         90
                 ....*....|...
gi 839824826 179 CPTGAIHFGSKED 191
Cdd:cd10555  212 CVGRIRFVGYLDD 224
PRK09898 PRK09898
ferredoxin-like protein;
39-194 2.25e-18

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 81.42  E-value: 2.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  39 CIGCKACQVACSEWND-------IRDEVGHNVGVYDNpadltakswtvmrfsEVEQNDKL--EWLIRKDGCMHCADPGCL 109
Cdd:PRK09898  68 CTGCHRCEISCTNFNDgsvgtffSRIKIHRNYFFGDN---------------GVGSGGGLygDLNYTADTCRQCKEPQCM 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 110 KACPSEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCvdrvtvgqePACVKTCPTGAIHFGSK 189
Cdd:PRK09898 133 NVCPIGAITWQQKEGCITVDHKRCIGCSACTTACPWMMATVNTESKKSSKCVLC---------GECANACPTGALKIIEW 203

                 ....*
gi 839824826 190 EDMKT 194
Cdd:PRK09898 204 KDITV 208
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
33-185 7.73e-18

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: 78.12  E-value: 7.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  33 LIDVTTCIGCKACQVACSEWNDIRDEVGHNVGVYDNpadltakswtvmrfseveqndkleWLIrKDGCMHCADPGCLKAC 112
Cdd:cd16367   15 VIDLDRCIRCDNCEKACADTHDGHSRLDRNGLRFGN------------------------LLV-PTACRHCVDPVCMIGC 69
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 839824826 113 PsEGAIIQYANGIVdFQSEQCIGCGYCIAGCPFDVPRLnpedNRVYKCTLCVDrvtvGQEPACVKTCPTGAIH 185
Cdd:cd16367   70 P-TGAIHRDDGGEV-VISDACCGCGNCASACPYGAIQM----VRAVKCDLCAG----YAGPACVSACPTGAAI 132
Form-deh_trans pfam09163
Formate dehydrogenase N, transmembrane; Members of this family are predominantly found in the ...
246-284 3.51e-16

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: 70.73  E-value: 3.51e-16
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 839824826  246 ISQTVKFWKGIWKPLAAVGFAATFAASIFHYVGVGPNRA 284
Cdd:pfam09163   1 ISPSVELWKGVLKPLGAAGMGAAALAGFFHYITVGPNKV 39
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
35-199 6.68e-16

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 77.76  E-value: 6.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  35 DVTTCIGCKACQVACS------EW----NDIRDEVgHNVGvYDNPADLTAkswtvmrfseveqndklewlirkdgCMHCA 104
Cdd:PRK12809   8 EAAECIGCHACEIACAvahnqeNWplshSDFRPRI-HVVG-KGQAANPVA-------------------------CHHCN 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 105 DPGCLKACPSEGAIiqYANGIVDFQSEQCIGCGYCIAGCPFDVPRLnpEDNRVYKCTLCVDRVTvGQEpACVKTCPTGAI 184
Cdd:PRK12809  61 NAPCVTACPVNALT--FQSDSVQLDEQKCIGCKRCAIACPFGVVEM--VDTIAQKCDLCNQRSS-GTQ-ACIEVCPTQAL 134
                        170
                 ....*....|....*
gi 839824826 185 HFGSKEDMKTLAGER 199
Cdd:PRK12809 135 RLMDDKGLQQIKVAR 149
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
100-179 7.24e-16

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


Pssm-ID: 319879 [Multi-domain]  Cd Length: 363  Bit Score: 77.02  E-value: 7.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 100 CMHCADPGCLKACPSeGAIIQYA-NGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVDRVTVGQEPACVKT 178
Cdd:cd10557  179 CNHCLNPACVAACPS-GAIYKREeDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSEKCIFCYPRLEAGQPTVCSET 257

                 .
gi 839824826 179 C 179
Cdd:cd10557  258 C 258
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
100-179 2.50e-13

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


Pssm-ID: 440755 [Multi-domain]  Cd Length: 485  Bit Score: 69.84  E-value: 2.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 100 CMHCADPGCLKACPSeGAIIQYA-NGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVDRVTVGQEPACVKT 178
Cdd:COG1140  182 CEHCLNPACVASCPS-GAIYKREeDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGKAEKCIFCYPRIEAGQPTVCSET 260

                 .
gi 839824826 179 C 179
Cdd:COG1140  261 C 261
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
100-184 5.00e-13

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


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 64.99  E-value: 5.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 100 CMHCADPGCLKACPsEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCvdrvtvgqePACVKTC 179
Cdd:cd16370   53 CRACEDPPCAEACP-TGALEPRKGGGVVLDKEKCIGCGNCVKACIVGAIFWDEETNKPIICIHC---------GYCARYC 122

                 ....*
gi 839824826 180 PTGAI 184
Cdd:cd16370  123 PHDVL 127
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
19-180 3.71e-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: 3.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  19 PAPQARDHQQeVAKLIDVTTCIGCKACQVACSE------------WNDIRDE------VGHNVGVYDNPADLT---AKSW 77
Cdd:cd10556    2 PYEESRPDKQ-FAMVFDTNKCIACQTCTMACKStwtsgkgqeymwWNNVETKpyggypLGWDVRLLDEEGGQTwaeGGVY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  78 TVMRFSEVE---------QNDKLEW---LIRKDG--------------------------CMHCADPGCLKACPSEGAII 119
Cdd:cd10556   81 EGKTIFEAAaageqvlgyRPEDEDWrypNIGEDEvngertpdtgsslpphpiwffylpriCNHCTYPACLAACPRKAIYK 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 839824826 120 QYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCVDRVTVGQEPACVKTCP 180
Cdd:cd10556  161 REEDGIVLIDQERCRGYRECVEACPYKKPMYNPTTRVSEKCIGCYPRIEEGDQTQCVSACI 221
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
34-184 1.01e-11

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


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 61.20  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  34 IDVTTCIGCKACQVACSE-WNDIRDevghnvgvydnpadlTAKSwtVMRFSEVEQNDKLewlirkDGCMHCADpgCLKAC 112
Cdd:cd16372    5 TDPEKCIGCLQCEEACSKtFFKEED---------------REKS--CIRITETEGGYAI------NVCNQCGE--CIDVC 59
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 839824826 113 PsEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTLCvdrvtvgqePACVKTCPTGAI 184
Cdd:cd16372   60 P-TGAITRDANGVVMINKKLCVGCLMCVGFCPEGAMFKHEDYPEPFKCIAC---------GICVKACPTGAL 121
PRK10330 PRK10330
electron transport protein HydN;
33-199 2.13e-11

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 61.44  E-value: 2.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  33 LIDVTTCIGCKACQVACSewndirdeVGHNVGvyDNPADLTAKSWtVMRFSEVEQNDKLEWLIrkdgCMHCADPGCLKAC 112
Cdd:PRK10330   6 IADASKCIGCRTCEVACV--------VSHQEN--QDCASLTPETF-LPRIHVIKGVNVSTATV----CRQCEDAPCANVC 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 113 PSeGAIIQyANGIVDFQSEQCIGCGYCIAGCPFDVPRL---------------NPEDNRVYKCTLCVDRVTvgqEPACVK 177
Cdd:PRK10330  71 PN-GAISR-DKGFVHVMQERCIGCKTCVVACPYGAMEVvvrpvirnsgaglnvRAEKAEANKCDLCNHRED---GPACMA 145
                        170       180
                 ....*....|....*....|..
gi 839824826 178 TCPTGAIHFGSKEDMKTLAGER 199
Cdd:PRK10330 146 ACPTHALICVDRNKLEQLSAEK 167
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
96-185 3.19e-08

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: 53.46  E-value: 3.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  96 RKDGCMHCADpgCLKACPSeGAIIQYANGI--VDfqSEQCIGCGYCIAGCPFDVPRLNPEDNRVYKCTL---CVDRVTVG 170
Cdd:COG2878  135 CEYGCIGCGD--CIKACPF-DAIVGAAKGMhtVD--EDKCTGCGLCVEACPVDCIEMVPVSPTVVVSSWdkgKAVRKVVG 209
                         90
                 ....*....|....*
gi 839824826 171 QEPACVKTCPTGAIH 185
Cdd:COG2878  210 CIGLCCKKCCPAAAI 224
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
131-202 1.39e-07

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 48.19  E-value: 1.39e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 839824826 131 EQCIGCGYCIAGCPFDVPRLnpEDNRVY----KCTLCvdrvtvgqePACVKTCPTGAIHFGSKEDMKTLagERVAE 202
Cdd:COG2768   11 EKCIGCGACVKVCPVGAISI--EDGKAVidpeKCIGC---------GACIEVCPVGAIKIEWEEDEEFQ--EKMAE 73
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
121-190 2.77e-07

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 47.03  E-value: 2.77e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 839824826 121 YANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRV---YKCTLCVdrvtvgqepACVKTCPTGAIHFGSKE 190
Cdd:COG1149    1 VKRKIPVIDEEKCIGCGLCVEVCPEGAIKLDDGGAPVvdpDLCTGCG---------ACVGVCPTGAITLEERE 64
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
95-185 3.44e-07

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 51.18  E-value: 3.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  95 IRKDGCMHCADPGCLKACPSEG----AIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNpeDNRVY----KCTLCvdr 166
Cdd:COG4624   51 CPRCCLCCCCCCRCCVAISCIQvrgiIIIDKRGPSIIRDKEKCKNCYPCVRACPVKAIKVD--DGKAEideeKCISC--- 125
                         90
                 ....*....|....*....
gi 839824826 167 vtvGQepaCVKTCPTGAIH 185
Cdd:COG4624  126 ---GQ---CVAVCPFGAIT 138
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
131-193 5.47e-07

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 46.24  E-value: 5.47e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 839824826 131 EQCIGCGYCIAGCPFDVPRLNPEDNRVY-----KCTLCvdrvtvgqePACVKTCPTGAIHFGSKEDMK 193
Cdd:COG1146    8 DKCIGCGACVEVCPVDVLELDEEGKKALvinpeECIGC---------GACELVCPVGAITVEDDEPEE 66
NapF COG1145
Ferredoxin [Energy production and conversion];
89-190 8.60e-07

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 49.34  E-value: 8.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  89 DKLEWLIRKDGCMHCADPGCLKACPSEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVY----KCTLCv 164
Cdd:COG1145  140 AEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVCPTGAIRLKDGKPQIVvdpdKCIGC- 218
                         90       100
                 ....*....|....*....|....*.
gi 839824826 165 drvtvgqePACVKTCPTGAIHFGSKE 190
Cdd:COG1145  219 --------GACVKVCPVGAISLEPKE 236
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
127-187 8.85e-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: 8.85e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 839824826 127 DFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVY-------KCTLCvdrvtvGqepACVKTCPTGAIHFG 187
Cdd:cd10549    2 KYDPEKCIGCGICVKACPTDAIELGPNGAIARgpeidedKCVFC------G---ACVEVCPTGAIELT 60
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
99-185 4.51e-06

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 47.24  E-value: 4.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  99 GCMHCADpgCLKACPSEGAIIQyaNGIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYkcTLCVDRVTVGQEPA---- 174
Cdd:PRK07118 140 GCLGLGS--CVAACPFDAIHIE--NGLPVVDEDKCTGCGACVKACPRNVIELIPKSARVF--VACNSKDKGKAVKKvcev 213
                         90
                 ....*....|....*...
gi 839824826 175 -------CVKTCPTGAIH 185
Cdd:PRK07118 214 gcigcgkCVKACPAGAIT 231
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
97-185 4.82e-06

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 45.08  E-value: 4.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  97 KDGCMHCADpgCLKACPSeGAIIQYANGIV----DFQSEQCIGCGYCIAGCPFDVPRLNPEdnrvYKCTLCVDRVTVGQE 172
Cdd:cd10549    5 PEKCIGCGI--CVKACPT-DAIELGPNGAIargpEIDEDKCVFCGACVEVCPTGAIELTPE----GKEYVPKEKEAEIDE 77
                         90
                 ....*....|....*....
gi 839824826 173 P------ACVKTCPTGAIH 185
Cdd:cd10549   78 EkcigcgLCVKVCPVDAIT 96
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
94-154 4.83e-06

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 43.57  E-value: 4.83e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 839824826  94 LIRKDGCMHCADpgCLKACPsEGAIIQyANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPED 154
Cdd:COG2768    7 YVDEEKCIGCGA--CVKVCP-VGAISI-EDGKAVIDPEKCIGCGACIEVCPVGAIKIEWEE 63
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
131-190 6.52e-06

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 43.20  E-value: 6.52e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 839824826 131 EQCIGCGYCIAGCPFDVPRLNPEDNRVY------KCTLCVdrvtvgqepACVKTCPTGAIHFGSKE 190
Cdd:COG1143    2 DKCIGCGLCVRVCPVDAITIEDGEPGKVyvidpdKCIGCG---------LCVEVCPTGAISMTPFE 58
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
125-193 8.74e-06

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 46.21  E-value: 8.74e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 839824826 125 IVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRvYKCTLCVDrvtvgqepaCVKTCPTGAIHFGSKEDMK 193
Cdd:COG0348  204 RVRYDRGDCIDCGLCVKVCPMGIDIRKGEINQ-SECINCGR---------CIDACPKDAIRFSSRGEKT 262
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
93-144 1.57e-05

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


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 41.85  E-value: 1.57e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 839824826   93 WLIRKDGCMHCADpgCLKACPSEGAI-----IQYANGIVDFQSEQCIGCGYCIAGCP 144
Cdd:pfam13237   2 VVIDPDKCIGCGR--CTAACPAGLTRvgaivERLEGEAVRIGVWKCIGCGACVEACP 56
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
130-189 2.12e-05

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


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 44.85  E-value: 2.12e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 839824826 130 SEQCIGCGYCIAGCPFDVPRLnpEDNRVY---KCTLCVdrvtvgqepACVKTCPTGAIHFGSK 189
Cdd:NF038196 184 TDKCIGCGICAKVCPVNNIEM--EDGKPVwghNCTHCL---------ACIHRCPKEAIEYGKK 235
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
95-147 2.38e-05

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 41.58  E-value: 2.38e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 839824826  95 IRKDGCMHCADpgCLKACPsEGAIiQYANGIVDFQSEQCIGCGYCIAGCPFDV 147
Cdd:COG2221   12 IDEEKCIGCGL--CVAVCP-TGAI-SLDDGKLVIDEEKCIGCGACIRVCPTGA 60
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
131-186 2.49e-05

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 45.62  E-value: 2.49e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 131 EQCIGCGYCIAGCPFDVPRLNpEDNRVY----KCTLCvdrvtvGqepACVKTCPTGAIHF 186
Cdd:COG1148  496 EKCTGCGRCVEVCPYGAISID-EKGVAEvnpaLCKGC------G---TCAAACPSGAISL 545
Fer4_9 pfam13187
4Fe-4S dicluster domain;
132-184 2.87e-05

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 41.00  E-value: 2.87e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 839824826  132 QCIGCGYCIAGCPFDV------PRLNPEDNRVYKCTLCVdrvtvgqepACVKTCPTGAI 184
Cdd:pfam13187   1 KCTGCGACVAACPAGAivpdlvGQTIRGDIAGLACIGCG---------ACVDACPRGAI 50
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
34-147 3.57e-05

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 42.77  E-value: 3.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  34 IDVTTCIGCKACQVACSewndirdevghnVGVYdnpadltakswTVMRFSEVEQNDKLEWLIRKDGCMHCADpgCLKACP 113
Cdd:cd10549   37 IDEDKCVFCGACVEVCP------------TGAI-----------ELTPEGKEYVPKEKEAEIDEEKCIGCGL--CVKVCP 91
                         90       100       110
                 ....*....|....*....|....*....|....
gi 839824826 114 sEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDV 147
Cdd:cd10549   92 -VDAITLEDELEIVIDKEKCIGCGICAEVCPVNA 124
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
133-194 4.09e-05

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: 43.01  E-value: 4.09e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 839824826 133 CIGCGYCIAGCPFDV---------------PRLNPEDNrvyKCTLCVDrvtvgqepACVKTCPTGAIHFGSKEDMKT 194
Cdd:cd16373   16 CIRCGLCVEACPTGViqpagledgleggrtPYLDPREG---PCDLCCD--------ACVEVCPTGALRPLDLEEQKV 81
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
95-146 5.51e-05

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 40.48  E-value: 5.51e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 839824826  95 IRKDGCMHCADpgCLKACPsEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFD 146
Cdd:COG1149    8 IDEEKCIGCGL--CVEVCP-EGAIKLDDGGAPVVDPDLCTGCGACVGVCPTG 56
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
117-185 6.89e-05

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 40.42  E-value: 6.89e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 839824826 117 AIIQYANGIVDfqSEQCIGCGYCIAGCPFDVprLNPEDNRVY----KCTLCvdrvtvgqePACVKTCPTGAIH 185
Cdd:COG2221    3 GIIGTWPPKID--EEKCIGCGLCVAVCPTGA--ISLDDGKLVideeKCIGC---------GACIRVCPTGAIK 62
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
124-204 9.55e-05

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 41.36  E-value: 9.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826 124 GIVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVY----KCTLCvdrvtvGQepaCVKTCPTGAIHFGSK---------- 189
Cdd:PRK08348  35 GKILYDVDKCVGCRMCVTVCPAGVFVYLPEIRKVAlwtgRCVFC------GQ---CVDVCPTGALQMSDDfllasydrfd 105
                         90
                 ....*....|....*
gi 839824826 190 EDMKTLAGERVAELK 204
Cdd:PRK08348 106 EKFIPLKPEKVEEIK 120
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
131-184 1.28e-04

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 39.64  E-value: 1.28e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 839824826 131 EQCIGCGYCIAGCPFDVprLNPEDNRVY----KCTLCVdrvtvgqepACVKTCPTGAI 184
Cdd:COG4231   22 DKCTGCGACVKVCPADA--IEEGDGKAVidpdLCIGCG---------SCVQVCPVDAI 68
napG PRK09476
quinol dehydrogenase periplasmic component; Provisional
127-183 1.49e-04

quinol dehydrogenase periplasmic component; Provisional


Pssm-ID: 236534 [Multi-domain]  Cd Length: 254  Bit Score: 42.30  E-value: 1.49e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 839824826 127 DFQSeQCIGCGYCIAGCPFDVPRL-NPEDN----------RVYKCTLCVDrvtvgqePACVKTCPTGA 183
Cdd:PRK09476  56 DFLS-ACIRCGLCVQACPYDTLKLaTLASGlsagtpyfvaRDIPCEMCED-------IPCVKACPSGA 115
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
84-145 1.89e-04

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 42.71  E-value: 1.89e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 839824826  84 EVEQNDKLEWLIRKDGCMHCADPG-------CLKACPSEgaIIQYANGIVDFQSEQCIGCGYCIAGCPF 145
Cdd:COG4624   68 ISCIQVRGIIIIDKRGPSIIRDKEkckncypCVRACPVK--AIKVDDGKAEIDEEKCISCGQCVAVCPF 134
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
98-186 2.15e-04

NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 40.69  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  98 DGCMHCADpgCLKACPsEGAIIQYANGI--VDFQSEQCIGCGYCIAGCP---FDVPRLNPED------------NRVYkC 160
Cdd:cd10564   13 DLCTRCGD--CVEACP-EGIIVRGDGGFpeLDFSRGECTFCGACAEACPegaLDPAREAPWPlraeigdsclalQGVE-C 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 839824826 161 TLCVD-----------RVTVGQEP-----------ACVKTCPTGAIHF 186
Cdd:cd10564   89 RSCQDacptqairfrpRLGGIALPeldadactgcgACVSVCPVGAITL 136
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
133-183 3.30e-04

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 37.89  E-value: 3.30e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  133 CIGCGYCIAGCPFDVPRLNPEDN---------RVYKCTLCvdrvtvgqePACVKTCPTGA 183
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEkkgtktvviDPERCVGC---------GACVAVCPTGA 51
flavo_MJ0208 TIGR02700
archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of ...
90-146 4.15e-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: 4.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 839824826   90 KLEWLIRKDGCMHCADpgCLKACPSEGaiIQYANGIVDFQSEQCIGCGYCIAGCPFD 146
Cdd:TIGR02700 140 ITPYMIDRKRCKGCGI--CVDACPRSA--IDMVDGKAFIRLLKCVGCGKCKEACPYN 192
Fer COG1141
Ferredoxin [Energy production and conversion];
131-185 4.86e-04

Ferredoxin [Energy production and conversion];


Pssm-ID: 440756 [Multi-domain]  Cd Length: 63  Bit Score: 37.55  E-value: 4.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 839824826 131 EQCIGCGYCIAGCPfDVPRLNPEDnrvyKCTLCVDRVTVGQEPAC---VKTCPTGAIH 185
Cdd:COG1141    8 DTCIGCGLCVALAP-EVFELDDDG----KAVVLDEEVPEELEEDVreaADACPVGAIT 60
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
100-147 7.41e-04

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 36.74  E-value: 7.41e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 839824826  100 CMHCADpgCLKACPS-----EGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDV 147
Cdd:pfam12838   1 CIGCGA--CVAACPVgaitlDEVGEKKGTKTVVIDPERCVGCGACVAVCPTGA 51
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
94-153 8.10e-04

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


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 39.40  E-value: 8.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826   94 LIRKDGCMHCADpgCLKACPSEgAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLNPE 153
Cdd:TIGR01944 109 LIDEDNCIGCTK--CIQACPVD-AIVGAAKAMHTVIADECTGCDLCVEPCPTDCIEMIPV 165
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
95-151 8.16e-04

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 40.61  E-value: 8.16e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 839824826  95 IRKDGCMHCAdpGCLKACPSeGAIIQYANGIVDFQSEQCIGCGYCIAGCPFDVPRLN 151
Cdd:COG1148  493 VDPEKCTGCG--RCVEVCPY-GAISIDEKGVAEVNPALCKGCGTCAAACPSGAISLK 546
PRK13795 PRK13795
hypothetical protein; Provisional
94-144 1.24e-03

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 40.36  E-value: 1.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 839824826  94 LIRKDGCMHCadpG-CLKACPsEGAI-IQYANGIVDFQSEQCIGCGYCIAGCP 144
Cdd:PRK13795 577 LRRAAECVGC---GvCVGACP-TGAIrIEEGKRKISVDEEKCIHCGKCTEVCP 625
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
95-146 1.55e-03

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 36.56  E-value: 1.55e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 839824826  95 IRKDGCMHCADpgCLKACPSEgaIIQYANGIVDFQSEQCIGCGYCIAGCPFD 146
Cdd:COG4231   19 IDEDKCTGCGA--CVKVCPAD--AIEEGDGKAVIDPDLCIGCGSCVQVCPVD 66
Fer4_13 pfam13370
4Fe-4S single cluster domain of Ferredoxin I; Fer4_13 is a ferredoxin I from sulfate-reducing ...
131-185 1.60e-03

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


Pssm-ID: 433153 [Multi-domain]  Cd Length: 58  Bit Score: 36.13  E-value: 1.60e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824826  131 EQCIGCGYCIAGCPfDVPRLNPEDNRVYkctlcVDRVTVGQ-EPACVK----TCPTGAIH 185
Cdd:pfam13370   4 DTCIDCGTCRELAP-EVFKYDDDGGASF-----VHDQPVNEeEEDLAEealdSCPVEAIG 57
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
95-146 1.91e-03

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


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 36.57  E-value: 1.91e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 839824826  95 IRKDGCMHCADpgCLKACPsEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFD 146
Cdd:COG1144   27 VDEDKCIGCGL--CWIVCP-DGAIRVDDGKYYGIDYDYCKGCGICAEVCPVK 75
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
128-184 3.83e-03

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


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 35.80  E-value: 3.83e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 839824826 128 FQSEQCIGCGYCIAGCPFDVprLNPEDNRVY-----KCTLCvdrvtvgqePACVKTCPTGAI 184
Cdd:COG1144   27 VDEDKCIGCGLCWIVCPDGA--IRVDDGKYYgidydYCKGC---------GICAEVCPVKAI 77
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
123-186 4.42e-03

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 36.94  E-value: 4.42e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 839824826 123 NGIVDFQSEQCIGCGYCIAGCPF---------DVPRL----NPEDNRVYKCTLCVDRvtvgqepACVKTCPTGAIHF 186
Cdd:COG1142    2 NKFIIADPEKCIGCRTCEAACAVahegeegepFLPRIrvvrKAGVSAPVQCRHCEDA-------PCAEVCPVGAITR 71
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
108-146 6.77e-03

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 37.87  E-value: 6.77e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 839824826 108 CLKACP-----SEGAIIQYANGIVDFQSEQCIGCGYCIAGCPFD 146
Cdd:PRK13409  21 CIKYCPvvrtgEETIEIDEDDGKPVISEELCIGCGICVKKCPFD 64
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
97-159 7.77e-03

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 34.34  E-value: 7.77e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 839824826  97 KDGCMHCADpgCLKACPSeGAIIQYANG---IVDFQSEQCIGCGYCIAGCPFDVPRLNPEDNRVYK 159
Cdd:COG1143    1 EDKCIGCGL--CVRVCPV-DAITIEDGEpgkVYVIDPDKCIGCGLCVEVCPTGAISMTPFELAVED 63
 
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