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Conserved domains on  [gi|743524057|ref|WP_039041283|]
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MULTISPECIES: 4Fe-4S dicluster domain-containing protein [Aeromonas]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyt_nit_nrfC super family cl37225
cytochrome c nitrite reductase, Fe-S protein; Members of this protein family are the Fe-S ...
 2-226 6.73e-127

cytochrome c nitrite reductase, Fe-S protein; Members of this protein family are the Fe-S protein, NrfC, of a cytochrome c nitrite reductase system for which the pentaheme cytochrome c protein, NrfB (family TIGR03146) is an unambiguous marker. Members of this protein family show similarity to other ferredoxin-like proteins, including a subunit of a polysulfide reductase. [Energy metabolism, Electron transport]


The actual alignment was detected with superfamily member TIGR03149:

Pssm-ID: 274451 [Multi-domain]  Cd Length: 225  Bit Score: 357.56  E-value: 6.73e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057    2 SCSRRHFMAGMsaGALIMMTGPTRSLATPLAHSQTIDGVRFGMLHDETACIGCTACMDACREVNQVPEGVSRLEIIRSGP 81
Cdd:TIGR03149   1 SCSRRNFLAGV--GALILTTGTAGTSVVSLAKEDKDKTKRYGMVHDETACIGCTACMDACREVNKVPEGVSRLEIIRSEP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057   82 IGTFPDAEYHFFRKSCQHCDNAPCVHVCPTGASHIRKEDGIVDVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCR 161
Cdd:TIGR03149  79 YGEFPDVEYRFFRKSCQHCDNAPCVAVCPTGASFKDEETGIVDVHKDLCVGCQYCIAACPYRVRFIHPVTKSADKCNFCR 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743524057  162 KTNLAAGKEPACVESCPTKALVFGNLDDPDSPIAKRLVKETTYRYKQALGTSPKMYRVP--KGEIKS 226
Cdd:TIGR03149 159 DTNLAEGKLPACVESCPTKALTFGDLNDPNSEVSQKLKQKPVYRTKVELGTKPKLYKIPfkKGEVRR 225
 
Name Accession Description Interval E-value
cyt_nit_nrfC TIGR03149
cytochrome c nitrite reductase, Fe-S protein; Members of this protein family are the Fe-S ...
 2-226 6.73e-127

cytochrome c nitrite reductase, Fe-S protein; Members of this protein family are the Fe-S protein, NrfC, of a cytochrome c nitrite reductase system for which the pentaheme cytochrome c protein, NrfB (family TIGR03146) is an unambiguous marker. Members of this protein family show similarity to other ferredoxin-like proteins, including a subunit of a polysulfide reductase. [Energy metabolism, Electron transport]


Pssm-ID: 274451 [Multi-domain]  Cd Length: 225  Bit Score: 357.56  E-value: 6.73e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057    2 SCSRRHFMAGMsaGALIMMTGPTRSLATPLAHSQTIDGVRFGMLHDETACIGCTACMDACREVNQVPEGVSRLEIIRSGP 81
Cdd:TIGR03149   1 SCSRRNFLAGV--GALILTTGTAGTSVVSLAKEDKDKTKRYGMVHDETACIGCTACMDACREVNKVPEGVSRLEIIRSEP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057   82 IGTFPDAEYHFFRKSCQHCDNAPCVHVCPTGASHIRKEDGIVDVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCR 161
Cdd:TIGR03149  79 YGEFPDVEYRFFRKSCQHCDNAPCVAVCPTGASFKDEETGIVDVHKDLCVGCQYCIAACPYRVRFIHPVTKSADKCNFCR 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743524057  162 KTNLAAGKEPACVESCPTKALVFGNLDDPDSPIAKRLVKETTYRYKQALGTSPKMYRVP--KGEIKS 226
Cdd:TIGR03149 159 DTNLAEGKLPACVESCPTKALTFGDLNDPNSEVSQKLKQKPVYRTKVELGTKPKLYKIPfkKGEVRR 225
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 44-217 4.13e-81

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: 240.13  E-value: 4.13e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  44 MLHDETACIGCTACMDACREVNQVPEGVSRLEIIRSGPiGTFPDAEYHFFRKSCQHCDNAPCVHVCPTGASHIRkEDGIV 123
Cdd:cd10551    1 MVIDLRKCIGCGACVVACKAENNVPPGVFRNRVLEYEV-GEYPNVKRTFLPVLCNHCENPPCVKVCPTGATYKR-EDGIV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057 124 DVNPDLCVGCMYCLAACPYQVRFINPV------------TKVADKCDFCRKTnLAAGKEPACVESCPTKALVFGNLDDPD 191
Cdd:cd10551   79 LVDYDKCIGCRYCMAACPYGARYFNPEephefgevpvrpKGVVEKCTFCYHR-LDEGLLPACVEACPTGARIFGDLDDPN 157

                        170       180
                 ....*....|....*....|....*.
gi 743524057 192 SPIAKRLVKETTYRYKQALGTSPKMY 217
Cdd:cd10551  158 SEVSKLLAERRAYVLKPELGTKPKVY 183
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 38-221 2.83e-75

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 225.21  E-value: 2.83e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  38 DGVRFGMLHDETACIGCTACMDACREVNQVPEGVSRLEIIRSgPIGTFPDAEYHFFRKSCQHCDNAPCVHVCPTGASHIR 117
Cdd:COG0437    2 SMKRYGMVIDLTKCIGCRACVVACKEENNLPVGVTWRRVRRY-EEGEFPNVEWLFVPVLCNHCDDPPCVKVCPTGATYKR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057 118 kEDGIVDVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCrKTNLAAGKEPACVESCPTKALVFGNLDDPDSPIAKR 197
Cdd:COG0437   81 -EDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFC-ADRLDEGLLPACVEACPTGALVFGDLDDPESEVSKR 158

                        170       180
                 ....*....|....*....|....
gi 743524057 198 LVKETTYRYKQALGTSPKMYRVPK 221
Cdd:COG0437  159 LAELPAYRLLPELGTKPSVYYLPK 182
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
4-223 7.57e-46

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 154.83  E-value: 7.57e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057   4 SRRHFMAGMSAGALIMMTGPTRSLAtPLAHSQTIDGVrFGMLHDETACIGCTACMDACREVNQvPEGVSRLE-------- 75
Cdd:PRK10882   2 NRRNFLKAASAGALLAGALPSVSHA-AAENRPPIPGA-LGMLYDSTLCVGCQACVTKCQEINF-PERNPQGEqtwdnpdk 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  76 -------II---RSGPIGTFPDAE--YHFFRKSCQHCDNAPCVHVCPTGASHIRKEDGIVDVNPDLCVGCMYCLAACPYQ 143
Cdd:PRK10882  79 lspytnnIIkvwKSGTGVNKDQEEngYAYIKKQCMHCVDPNCVSVCPVSALTKDPKTGIVHYDKDVCTGCRYCMVACPFN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057 144 V---RFINPVTKVAdKCDFCRKTNL---AAGKEPACVESCPTKALVFGNLDDPDSPIAKRLVKE--TTYRYKQALGTSPK 215
Cdd:PRK10882 159 VpkyDYNNPFGAIH-KCELCNQKGVerlDKGGLPGCVEVCPTGAVIFGTREELLAEAKRRLALKpgSEYHYPRQTLKSGD 237


                 ....*...
gi 743524057 216 MYRVPKGE 223
Cdd:PRK10882 238 TYLHTVPK 245
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 89-187 2.94e-28

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: 102.71  E-value: 2.94e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057   89 EYHFFRKSCQHCDNAPCVHVCPTGASHIRKEDGIVDVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCRkTNLAAG 168
Cdd:pfam13247   2 DWLFFPEQCRHCLNPPCKASCPVGAIYKDEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCY-DRVEAG 80

                          90
                  ....*....|....*....
gi 743524057  169 KEPACVESCPTKALVFGNL 187
Cdd:pfam13247  81 LLPACVQTCPTGAMNFGDR 99
 
Name Accession Description Interval E-value
cyt_nit_nrfC TIGR03149
cytochrome c nitrite reductase, Fe-S protein; Members of this protein family are the Fe-S ...
 2-226 6.73e-127

cytochrome c nitrite reductase, Fe-S protein; Members of this protein family are the Fe-S protein, NrfC, of a cytochrome c nitrite reductase system for which the pentaheme cytochrome c protein, NrfB (family TIGR03146) is an unambiguous marker. Members of this protein family show similarity to other ferredoxin-like proteins, including a subunit of a polysulfide reductase. [Energy metabolism, Electron transport]


Pssm-ID: 274451 [Multi-domain]  Cd Length: 225  Bit Score: 357.56  E-value: 6.73e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057    2 SCSRRHFMAGMsaGALIMMTGPTRSLATPLAHSQTIDGVRFGMLHDETACIGCTACMDACREVNQVPEGVSRLEIIRSGP 81
Cdd:TIGR03149   1 SCSRRNFLAGV--GALILTTGTAGTSVVSLAKEDKDKTKRYGMVHDETACIGCTACMDACREVNKVPEGVSRLEIIRSEP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057   82 IGTFPDAEYHFFRKSCQHCDNAPCVHVCPTGASHIRKEDGIVDVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCR 161
Cdd:TIGR03149  79 YGEFPDVEYRFFRKSCQHCDNAPCVAVCPTGASFKDEETGIVDVHKDLCVGCQYCIAACPYRVRFIHPVTKSADKCNFCR 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743524057  162 KTNLAAGKEPACVESCPTKALVFGNLDDPDSPIAKRLVKETTYRYKQALGTSPKMYRVP--KGEIKS 226
Cdd:TIGR03149 159 DTNLAEGKLPACVESCPTKALTFGDLNDPNSEVSQKLKQKPVYRTKVELGTKPKLYKIPfkKGEVRR 225
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 44-217 4.13e-81

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: 240.13  E-value: 4.13e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  44 MLHDETACIGCTACMDACREVNQVPEGVSRLEIIRSGPiGTFPDAEYHFFRKSCQHCDNAPCVHVCPTGASHIRkEDGIV 123
Cdd:cd10551    1 MVIDLRKCIGCGACVVACKAENNVPPGVFRNRVLEYEV-GEYPNVKRTFLPVLCNHCENPPCVKVCPTGATYKR-EDGIV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057 124 DVNPDLCVGCMYCLAACPYQVRFINPV------------TKVADKCDFCRKTnLAAGKEPACVESCPTKALVFGNLDDPD 191
Cdd:cd10551   79 LVDYDKCIGCRYCMAACPYGARYFNPEephefgevpvrpKGVVEKCTFCYHR-LDEGLLPACVEACPTGARIFGDLDDPN 157

                        170       180
                 ....*....|....*....|....*.
gi 743524057 192 SPIAKRLVKETTYRYKQALGTSPKMY 217
Cdd:cd10551  158 SEVSKLLAERRAYVLKPELGTKPKVY 183
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 38-221 2.83e-75

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 225.21  E-value: 2.83e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  38 DGVRFGMLHDETACIGCTACMDACREVNQVPEGVSRLEIIRSgPIGTFPDAEYHFFRKSCQHCDNAPCVHVCPTGASHIR 117
Cdd:COG0437    2 SMKRYGMVIDLTKCIGCRACVVACKEENNLPVGVTWRRVRRY-EEGEFPNVEWLFVPVLCNHCDDPPCVKVCPTGATYKR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057 118 kEDGIVDVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCrKTNLAAGKEPACVESCPTKALVFGNLDDPDSPIAKR 197
Cdd:COG0437   81 -EDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFC-ADRLDEGLLPACVEACPTGALVFGDLDDPESEVSKR 158

                        170       180
                 ....*....|....*....|....
gi 743524057 198 LVKETTYRYKQALGTSPKMYRVPK 221
Cdd:COG0437  159 LAELPAYRLLPELGTKPSVYYLPK 182
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 43-185 1.10e-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: 158.88  E-value: 1.10e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  43 GMLHDETACIGCTACMDACREVNQVPEGVSRLEIiRSGPIGTFPDAEYHFFRKSCQHCDNAPCVHVCPTGASHIRkEDGI 122
Cdd:cd16371    1 GFYFDQERCIGCKACEIACKDKNDLPPGVNWRRV-YEYEGGEFPEVFAYFLSMSCNHCENPACVKVCPTGAITKR-EDGI 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743524057 123 VDVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCRKtNLAAGKEPACVESCPTKALVFG 185
Cdd:cd16371   79 VVVDQDKCIGCGYCVWACPYGAPQYNPETGKMDKCDMCVD-RLDEGEKPACVAACPTRALDFG 140
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
4-223 7.57e-46

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 154.83  E-value: 7.57e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057   4 SRRHFMAGMSAGALIMMTGPTRSLAtPLAHSQTIDGVrFGMLHDETACIGCTACMDACREVNQvPEGVSRLE-------- 75
Cdd:PRK10882   2 NRRNFLKAASAGALLAGALPSVSHA-AAENRPPIPGA-LGMLYDSTLCVGCQACVTKCQEINF-PERNPQGEqtwdnpdk 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  76 -------II---RSGPIGTFPDAE--YHFFRKSCQHCDNAPCVHVCPTGASHIRKEDGIVDVNPDLCVGCMYCLAACPYQ 143
Cdd:PRK10882  79 lspytnnIIkvwKSGTGVNKDQEEngYAYIKKQCMHCVDPNCVSVCPVSALTKDPKTGIVHYDKDVCTGCRYCMVACPFN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057 144 V---RFINPVTKVAdKCDFCRKTNL---AAGKEPACVESCPTKALVFGNLDDPDSPIAKRLVKE--TTYRYKQALGTSPK 215
Cdd:PRK10882 159 VpkyDYNNPFGAIH-KCELCNQKGVerlDKGGLPGCVEVCPTGAVIFGTREELLAEAKRRLALKpgSEYHYPRQTLKSGD 237


                 ....*...
gi 743524057 216 MYRVPKGE 223
Cdd:PRK10882 238 TYLHTVPK 245
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 44-185 7.68e-43

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: 141.37  E-value: 7.68e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  44 MLHDETACIGCTACMDACREVNQVPEGVSRLEIirsgPIGTFPDAEYHFFRKSCQHCDNAPCVHVCPTGAsHIRKEDGIV 123
Cdd:cd04410    1 LVVDLDRCIGCGTCEVACKQEHGLRPGPDWSRI----KVIEGGGLERAFLPVSCMHCEDPPCVKACPTGA-IYKDEDGIV 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743524057 124 DVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCrKTNLAAGKEPACVESCPTKALVFG 185
Cdd:cd04410   76 LIDEDKCIGCGSCVEACPYGAIVFDPEPGKAVKCDLC-GDRLDEGLEPACVKACPTGALTFG 136
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 43-185 5.25e-42

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: 141.20  E-value: 5.25e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  43 GMLHDETACIGCTACMDACREVNQVPEGVSRLEIIRSGPIGT--------------FPDAEYHFFRKSCQHCDNAPCVHV 108
Cdd:cd10561    1 GVLYDTTRCIGCRACEVACKEWNGLPAEDTAFGPGWDNPRDLsaktytvikryeveTGGKGFVFVKRQCMHCLDPACVSA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057 109 CPTGAshIRK-EDGIVDVNPDLCVGCMYCLAACPYQV-RF----INPVTKvadKCDFCRkTNLAAGKEPACVESCPTKAL 182
Cdd:cd10561   81 CPVGA--LRKtPEGPVTYDEDKCIGCRYCMVACPFNIpKYewdsANPKIR---KCTMCY-DRLKEGKQPACVEACPTGAL 154


                 ...
gi 743524057 183 VFG 185
Cdd:cd10561  155 LFG 157
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
1-198 9.18e-42

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 141.94  E-value: 9.18e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057   1 MSCSRRHFM---AGMSAGALIMMTGPTRSLATPLAHSQTIDGvRFGMLHDETACIGCTACMDACREVNQVPEG-----VS 72
Cdd:PRK14993   1 MDSSKRQFLqqlGVLTAGASLVPLAEAKFPFSPERHEGSPRH-RYAMLIDLRRCIGCQSCTVSCTIENQTPQGafrttVN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  73 RLEIIRSGPIGTfpdaEYHFFRKSCQHCDNAPCVHVCPTGASHIRKeDGIVDVNPDLCVGCMYCLAACPYQVRFINPVTK 152
Cdd:PRK14993  80 QYQVQREGSQEV----TNVLLPRLCNHCDNPPCVPVCPVQATFQRE-DGIVVVDNKRCVGCAYCVQACPYDARFINHETQ 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 743524057 153 VADKCDFCRKtNLAAGKEPACVESCPTKALVFGNLDDPDSPIAKRL 198
Cdd:PRK14993 155 TADKCTFCVH-RLEAGLLPACVESCVGGARIIGDIKDPHSRIATML 199
DMSO_dmsB TIGR02951
DMSO reductase, iron-sulfur subunit; This family consists of the iron-sulfur subunit, or chain ...
 41-189 4.45e-41

DMSO reductase, iron-sulfur subunit; This family consists of the iron-sulfur subunit, or chain B, of an enzyme called the anaerobic dimethyl sulfoxide reductase. Chains A and B are catalytic, while chain C is a membrane anchor.


Pssm-ID: 131996 [Multi-domain]  Cd Length: 161  Bit Score: 137.56  E-value: 4.45e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057   41 RFGMLHDETACIGCTACMDACREVNQVPEGVSRLEI--------IRSGPiGTFPDAEYHFFRKSCQHCDNAPCVHVCPTG 112
Cdd:TIGR02951   1 QYGFYVDQTRCSGCKTCQIACKDKNDLEVGVLFRRVyeyegggwTEEGE-GFHPDVFAYYISISCNHCADPACVKNCPTG 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743524057  113 ASHIRKEDGIVDVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCRkTNLAAGKEPACVESCPTKALVFGNLDD 189
Cdd:TIGR02951  80 AMYKREEDGLVLVDQDKCIGCRYCVWACPYGAPQYDPQQGVMGKCDGCY-DRVEKGLRPACVDACPMRALDFGPIDE 155
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 43-189 3.68e-38

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: 132.12  E-value: 3.68e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  43 GMLHDETACIGCTACMDACREVNQVPEG----------------------VSRLEIIR-SGPIGTFPDAEYHFFRKSCQH 99
Cdd:cd10560    1 GFFTDTSICIGCKACEVACKQWNQLPADgydfsgmsydntgdlsastwrhVKFIERPTeDGPANEGGDLQWLFMSDVCKH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057 100 CDNAPCVHVCPTGAShIRKEDGIVDVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCRKtNLAAGKEPACVESCPT 179
Cdd:cd10560   81 CTDAGCLEACPTGAI-FRTEFGTVYIQPDICNGCGYCVAACPFGVIDRNEETGRAHKCTLCYD-RLKDGLEPACAKACPT 158

                        170
                 ....*....|
gi 743524057 180 KALVFGNLDD 189
Cdd:cd10560  159 GSIQFGPLEE 168
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 44-189 3.52e-37

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: 127.42  E-value: 3.52e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  44 MLHDETACIGCTACMDACREVNQVPEGVSRLEIIRSGPIGTFPDA----------------EYHFFRKSCQHCDNAPCVH 107
Cdd:cd10562    1 MLVDTSKCTACRGCQVACKQWNQLPAEKTPFTGSYQNPPDLTPNTwtlirfyeheednggiRWLFRKRQCMHCTDAACVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057 108 VCPTGASHiRKEDGIVDVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCRkTNLAAGKEPACVESCPTKALVFGNL 187
Cdd:cd10562   81 VCPTGALY-KTENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCF-DRIENGMQPACVKTCPTGALTFGDR 158


                 ..
gi 743524057 188 DD 189
Cdd:cd10562  159 DE 160
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 45-189 3.73e-37

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: 129.04  E-value: 3.73e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  45 LHDETACIGCTACMDACREVNQVPEGVSRLEIIRSGPIGTFPDA---------------EYHFFRKSCQHCDNAPCVHVC 109
Cdd:cd10558    3 LIDVSKCIGCKACQVACKEWNDLRAEVGHNVGTYQNPADLSPETwtlmkfrevedngklEWLIRKDGCMHCADPGCLKAC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057 110 PTGASHIRKEDGIVDVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCrKTNLAAGKEPACVESCPTKALVFGNLDD 189
Cdd:cd10558   83 PSPGAIVQYANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLC-SDRVSVGLEPACVKTCPTGALHFGTKED 161
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 46-185 3.85e-37

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: 127.09  E-value: 3.85e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  46 HDETACIGCTACMDACREVNQVPEGVSRLEIIRSGP--IGTFPDAEYHFfrKSCQHCDNAPCVHVCPTGASHIRKEDGIV 123
Cdd:cd10553    7 HDSKRCIGCLACEVHCKVKNNLPVGPRLCRIFAVGPkmVGGKPRLKFVY--MSCFHCENPWCVKACPTGAMQKREKDGIV 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743524057 124 DVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCRKtNLAAGKEPACVESCPTKALVFG 185
Cdd:cd10553   85 YVDQELCIGCKACIEACPWGIPQWNPATGKVVKCDYCMD-RIDQGLKPACVTGCTTHALSFV 145
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 83-220 3.32e-35

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: 126.65  E-value: 3.32e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  83 GTFPDAEYHFFRKSCQHCDNAPCVHVCPTGASHIRKEDGIVDVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFC-- 160
Cdd:cd10555  119 GEYPNSYYFYLPRICNHCTNPACLAACPRKAIYKREEDGIVLVDQDRCRGYRYCVEACPYKKIYFNPVEQKSEKCIFCyp 198

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743524057 161 RktnLAAGKEPACVESCPTKALVFGNLDDPDSPIAKrLVKEttyrYKQAL------GTSPKMYRVP 220
Cdd:cd10555  199 R---IEKGVAPACARQCVGRIRFVGYLDDEESPVYK-LVKK----WKVALplhpeyGTEPNVFYVP 256
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 51-189 1.27e-34

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


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 120.07  E-value: 1.27e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  51 CIGCTACMDACREVNqvpEGVSRLEIIRSGPIGTFPdaeyhffrKSCQHCDNAPCVHVCPTGASHiRKEDGIVDVNPDLC 130
Cdd:cd16374    8 CIGCRACEIACAREH---SGKPRISVEVVEDLASVP--------VRCRHCEDAPCMEVCPTGAIY-RDEDGAVLVDPDKC 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 743524057 131 VGCMYCLAACPYQVRFINPVTKVADKCDFCRKtNLAAGKEPACVESCPTKALVFGNLDD 189
Cdd:cd16374   76 IGCGMCAMACPFGVPRFDPSLKVAVKCDLCID-RRREGKLPACVEACPTGALKFGDIEE 133
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 44-185 4.06e-34

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: 119.43  E-value: 4.06e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  44 MLHDETACIGCTACMDACREVNQVPEGVSRLEIIRSGP----IGTF------------PDAEYHFFRKSCQHCDNAPCVH 107
Cdd:cd16366    1 FLVDTSRCTGCRACQVACKQWNGLPAEKTEFTGSYQNPpdltAHTWtlvrfyevekpgGDLSWLFRKDQCMHCTDAGCLA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743524057 108 VCPTGAShIRKEDGIVDVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCRkTNLAAGKEPACVESCPTKALVFG 185
Cdd:cd16366   81 ACPTGAI-IRTETGTVVVDPETCIGCGYCVNACPFDIPRFDEETGRVAKCTLCY-DRISNGLQPACVKTCPTGALTFG 156
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 44-184 1.65e-32

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


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 114.60  E-value: 1.65e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  44 MLHDETACIGCTACMDACREVNqvpEGV-----SRLEIIRSGPIGT-FPDAeyhffrksCQHCDNAPCVHVCPTGASHIR 117
Cdd:cd10550    1 LVVDPEKCTGCRTCELACSLKH---EGVfnpslSRIRVVRFEPEGLdVPVV--------CRQCEDAPCVEACPVGAISRD 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743524057 118 KEDGIVDVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCrktnlaaGKEPACVESCPTKALVF 184
Cdd:cd10550   70 EETGAVVVDEDKCIGCGMCVEACPFGAIRVDPETGKAIKCDLC-------GGDPACVKVCPTGALEF 129
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 44-217 9.08e-32

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: 114.35  E-value: 9.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  44 MLHDETACIGCTACMDACRE-----------VNQVPEGVSRLEIIRSgPIGTFPDAEYHFFRKSCQHCDNAPCVHVCPTG 112
Cdd:cd10552    1 LVIDVAKCNGCYNCFLACKDehvgndwpgyaAPQPRHGHFWMRILRR-ERGQYPKVDVAYLPVPCNHCDNAPCIKAAKDG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057 113 ASHiRKEDGIVDVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCRKTNLAAGKEPACVESCPTKALVFGNLDDPDS 192
Cdd:cd10552   80 AVY-KRDDGIVIIDPEKAKGQKQLVDACPYGAIYWNEELQVPQKCTFCAHLLDDGWKEPRCVQACPTGALRFGKLEDEEM 158

                        170       180
                 ....*....|....*....|....*
gi 743524057 193 piAKRLVKETTYRYKQALGTSPKMY 217
Cdd:cd10552  159 --AAKAAEEGLEVLHPELGTKPRVY 181
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 47-185 9.15e-31

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: 110.42  E-value: 9.15e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  47 DETACIGCTACMDACRE-----------VNQVPEGVSRLEIIRSGPigtfpdaeyHFFRKSCQHCDNAPCVHVCPTGASH 115
Cdd:cd10563    5 DEEKCLGCKLCEVACAVahskskdlikaKLEKERPRPRIRVEESGG---------RSFPLQCRHCDEPPCVKACMSGAMH 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057 116 IRKEDGIVDVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCRKTnlaagKEPACVESCPTKALVFG 185
Cdd:cd10563   76 KDPETGIVIHDEEKCVGCWMCVMVCPYGAIRPDKERKVALKCDLCPDR-----ETPACVEACPTGALVLE 140
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
47-184 2.55e-29

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 106.67  E-value: 2.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  47 DETACIGCTACMDACREVNQVPEG---VSRLEIIRSGPIgTFPDaeyhffrkSCQHCDNAPCVHVCPTGAshIRKEDGIV 123
Cdd:COG1142    8 DPEKCIGCRTCEAACAVAHEGEEGepfLPRIRVVRKAGV-SAPV--------QCRHCEDAPCAEVCPVGA--ITRDDGAV 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743524057 124 DVNPDLCVGCMYCLAACPYQVRFIN--PVTKVADKCDFCRKTNlaagKEPACVESCPTKALVF 184
Cdd:COG1142   77 VVDEEKCIGCGLCVLACPFGAITMVgeKSRAVAVKCDLCGGRE----GGPACVEACPTGALRL 135
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 51-182 1.33e-28

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: 105.03  E-value: 1.33e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  51 CIGCTACMDAC----REVNQVPEG------VSRLEIIRSGPIgTFPDAeyhffrksCQHCDNAPCVHVCPTGAshIRKED 120
Cdd:cd10554    9 CIGCRTCEVACaaahSGKGIFEAGtdglpfLPRLRVVKTGEV-TAPVQ--------CRQCEDAPCANVCPVGA--ISQED 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743524057 121 GIVDVNPDLCVGCMYCLAACPY-----------QVRFINPVTKVADKCDFCRKTNlaagKEPACVESCPTKAL 182
Cdd:cd10554   78 GVVQVDEERCIGCKLCVLACPFgaiemapttvpGVDWERGPRAVAVKCDLCAGRE----GGPACVEACPTKAL 146
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 89-187 2.94e-28

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: 102.71  E-value: 2.94e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057   89 EYHFFRKSCQHCDNAPCVHVCPTGASHIRKEDGIVDVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCRkTNLAAG 168
Cdd:pfam13247   2 DWLFFPEQCRHCLNPPCKASCPVGAIYKDEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCY-DRVEAG 80

                          90
                  ....*....|....*....
gi 743524057  169 KEPACVESCPTKALVFGNL 187
Cdd:pfam13247  81 LLPACVQTCPTGAMNFGDR 99
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 41-220 3.77e-28

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: 105.36  E-value: 3.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  41 RFGMLHDETACIGCTACMDACREVNQVPEGVS--RLEIIRSGPIGTFP-DAE------------YHFFRKSCQHCDNAPC 105
Cdd:cd16365    2 QFAAVFNLNKCIGCQTCTVACKNAWTYRKGQEymWWNNVETKPGGGYPqDWEvktidnggntrfFFYLQRLCNHCTNPAC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057 106 VHVCPTGASHIRKEDGIVDVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCRKtNLAAGKEPACVESCPTKALVFG 185
Cdd:cd16365   82 LAACPRGAIYKREEDGIVLIDQKRCRGYRKCVEQCPYKKIYFNGLSRVSEKCIACYP-RIEGGDPTRCMSACVGRIRLQG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 743524057 186 NLDD-PDSPIAKrLVKEttyrYKQAL------GTSPKMYRVP 220
Cdd:cd16365  161 FLDDnPKSPVTK-LIRH----WKVALplhpeyGTEPNIYYVP 197
FDH-beta TIGR01582
formate dehydrogenase, beta subunit, Fe-S containing; This model represents the beta subunit ...
 45-189 6.22e-27

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: 104.22  E-value: 6.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057   45 LHDETACIGCTACMDACREVNQVPEGVSRLEI-IRSGPIGTFPDA---------------EYHFFRKSCQHCDNAPCVHV 108
Cdd:TIGR01582  25 LIDVSSCIGCKACQAACQEWNDTTPPILSRKVgGYQNPPDLLPETftlmrfkegeesdglEWLIRKDGCMHCREPGCLKA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  109 CPTGASHIRKEDGIVDVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCrKTNLAAGKEPACVESCPTKALVFGNLD 188
Cdd:TIGR01582 105 CPAPGAIIQYQNGIVDFDHSKCIGCGYCIVGCPFNIPRYDKVDNRPYKCTLC-IDRVSVGQEPACVKTCPTNAISFGFKE 183


                  .
gi 743524057  189 D 189
Cdd:TIGR01582 184 D 184
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 47-185 4.42e-23

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: 92.10  E-value: 4.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  47 DETACIGCT-----ACMDACREVNQ--VPEGVS------------------RLEIIRSGP----------IGTFPDAEYH 91
Cdd:cd16368    6 DLTKCDGCPgesipACVRACREKNQarFPEPVSkpiqpywprkriedwsdkRDVTDRLTPynwlyvqkltVDTAGGEKEV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  92 FFRKSCQHCDNAPCVHVCPTGASHIRKEdGIVDVNPDLCVGCMYCLAACPYQV----RFINPVTKVAD---------KCD 158
Cdd:cd16368   86 FIPRRCMHCDNPPCAKLCPFGAARKTPE-GAVYIDDDLCFGGAKCRDVCPWHIpqrqAGVGIYLHLAPeyagggvmyKCD 164

                        170       180
                 ....*....|....*....|....*..
gi 743524057 159 FCrKTNLAAGKEPACVESCPTKALVFG 185
Cdd:cd16368  165 LC-KDLLAQGKPPACIEACPKGAQYFG 190
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 44-183 2.05e-20

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: 83.51  E-value: 2.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  44 MLHDETACIGCTACMDACREVNQvpeGVSRLeiIRSGPigtfPDAEYHFfRKSCQHCDNAPCVHVCPTGASHiRKEDGIV 123
Cdd:cd16367   14 LVIDLDRCIRCDNCEKACADTHD---GHSRL--DRNGL----RFGNLLV-PTACRHCVDPVCMIGCPTGAIH-RDDGGEV 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057 124 DVNpDLCVGCMYCLAACPYQVrfINPVtkVADKCDFCRKTNlaagkEPACVESCPTKALV 183
Cdd:cd16367   83 VIS-DACCGCGNCASACPYGA--IQMV--RAVKCDLCAGYA-----GPACVSACPTGAAI 132
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 97-193 2.14e-20

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: 86.74  E-value: 2.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  97 CQHCDNAPCVHVCPTGASHIRKEDGIVDVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCRKtNLAAGKEPACVES 176
Cdd:cd10556  141 CNHCTYPACLAACPRKAIYKREEDGIVLIDQERCRGYRECVEACPYKKPMYNPTTRVSEKCIGCYP-RIEEGDQTQCVSA 219

                         90
                 ....*....|....*..
gi 743524057 177 CPTKALVFGNLDDPDSP 193
Cdd:cd10556  220 CIGKIRLQGFINTPPDA 236
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 43-219 5.48e-20

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: 84.02  E-value: 5.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  43 GMLHDETACIGCTACMDACREVNQVPEGVSRleiiRSGPIGTFPDAEYH--------------------FFRKSCQHCDN 102
Cdd:cd10559    1 SFLIDTTRCTACRGCQVACKQWNQLPAEQTK----NTGSHQNPPDLSANtyklvrfnevrnengkpdwlFFPDQCRHCVT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057 103 APCVHVCPTGASHIRKED--GIVDVNP---DLCVGCMycLAACPYQVRFINPVTKVADKCDFC--RKTNlaaGKEPACVE 175
Cdd:cd10559   77 PPCKDAADMVPGAVIQDEatGAVVFTEktaELDFDDV--LSACPYNIPRKNEATGRIVKCDMCidRVSN---GLQPACVK 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 743524057 176 SCPTKALVFGNLDDPDSpIAKRLVKETTYRYKQALGTSPKMYRV 219
Cdd:cd10559  152 ACPTGAMNFGDRDEMLA-MASKRLEELKKRYPKANLYDPDDVRV 194
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 97-177 8.00e-20

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: 86.26  E-value: 8.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  97 CQHCDNAPCVHVCPTGASHIRKEDGIVDVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFC--RktnLAAGKEPACV 174
Cdd:cd10557  179 CNHCLNPACVAACPSGAIYKREEDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSEKCIFCypR---LEAGQPTVCS 255


                 ...
gi 743524057 175 ESC 177
Cdd:cd10557  256 ETC 258
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 51-182 8.61e-20

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 87.11  E-value: 8.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  51 CIGCTACMDACrevnqvpegvsrleiIRSGPIGTFPDAEYHFFRK-------------SCQHCDNAPCVHVCPTGAShIR 117
Cdd:PRK12769  12 CLGCHACEIAC---------------VMAHNDEQHVLSQHHFHPRitvikhqqqrsavTCHHCEDAPCARSCPNGAI-SH 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743524057 118 KEDGiVDVNPDLCVGCMYCLAACPYQVRFI-------NPVTKVADKCDFCrktnlaAGKE--PACVESCPTKAL 182
Cdd:PRK12769  76 VDDS-IQVNQQKCIGCKSCVVACPFGTMQIvltpvaaGKVKATAHKCDLC------AGREngPACVENCPADAL 142
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 47-182 1.31e-18

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 83.92  E-value: 1.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  47 DETACIGCTACMDACREV-NQVPEGVSRLEIIrsgpigtfpdAEYHFFRK-------SCQHCDNAPCVHVCPTGASHIRK 118
Cdd:PRK12809   8 EAAECIGCHACEIACAVAhNQENWPLSHSDFR----------PRIHVVGKgqaanpvACHHCNNAPCVTACPVNALTFQS 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743524057 119 EDgiVDVNPDLCVGCMYCLAACPYQVrfINPVTKVADKCDFCrktNLAAGKEPACVESCPTKAL 182
Cdd:PRK12809  78 DS--VQLDEQKCIGCKRCAIACPFGV--VEMVDTIAQKCDLC---NQRSSGTQACIEVCPTQAL 134
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 51-185 2.50e-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: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 78.97  E-value: 2.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  51 CIGCTACMDACREVNQvPEGVSRL---EIIRSGPIGTFPDAeyhffrksCQHCDNAPCVHVCPTGASHIrKEDGIV-DVN 126
Cdd:cd16369   11 CIGCRACVAACRECGT-HRGKSMIhvdYIDRGESTQTAPTV--------CMHCEDPTCAEVCPADAIKV-TEDGVVqSAL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 743524057 127 PDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCRKTNlAAGKEPACVESCPTKALVFG 185
Cdd:cd16369   81 KPRCIGCSNCVNACPFGVPKYDEERNLMMKCDMCYDRT-SVGKAPMCASVCPSGALFYG 138
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 97-177 2.30e-17

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


Pssm-ID: 440755 [Multi-domain]  Cd Length: 485  Bit Score: 79.85  E-value: 2.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  97 CQHCDNAPCVHVCPTGASHIRKEDGIVDVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFC--RktnLAAGKEPACV 174
Cdd:COG1140  182 CEHCLNPACVASCPSGAIYKREEDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGKAEKCIFCypR---IEAGQPTVCS 258


                 ...
gi 743524057 175 ESC 177
Cdd:COG1140  259 ETC 261
PRK10330 PRK10330
electron transport protein HydN;
47-183 3.94e-16

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 73.39  E-value: 3.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  47 DETACIGCTACMDACREVNQVPEGVS---------RLEIIRSGPIGTfpdaeyhffRKSCQHCDNAPCVHVCPTGAshIR 117
Cdd:PRK10330   8 DASKCIGCRTCEVACVVSHQENQDCAsltpetflpRIHVIKGVNVST---------ATVCRQCEDAPCANVCPNGA--IS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057 118 KEDGIVDVNPDLCVGCMYCLAACPYQVR--FINPVTK-------------VADKCDFCRktNLAAGkePACVESCPTKAL 182
Cdd:PRK10330  77 RDKGFVHVMQERCIGCKTCVVACPYGAMevVVRPVIRnsgaglnvraekaEANKCDLCN--HREDG--PACMAACPTHAL 152


                 .
gi 743524057 183 V 183
Cdd:PRK10330 153 I 153
PRK09898 PRK09898
ferredoxin-like protein;
51-182 6.21e-15

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 70.64  E-value: 6.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  51 CIGCTACMDACREVN--QVPEGVSRLEIIRSGPIGT----FPDAEY---HFFRKSCQHCDNAPCVHVCPTGASHIRKEDG 121
Cdd:PRK09898  68 CTGCHRCEISCTNFNdgSVGTFFSRIKIHRNYFFGDngvgSGGGLYgdlNYTADTCRQCKEPQCMNVCPIGAITWQQKEG 147

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743524057 122 IVDVNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCrktnlaagkePACVESCPTKAL 182
Cdd:PRK09898 148 CITVDHKRCIGCSACTTACPWMMATVNTESKKSSKCVLC----------GECANACPTGAL 198
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 51-184 5.68e-14

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


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 66.14  E-value: 5.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  51 CIGCTACMDACREVNQVPEGVSRLEIirsgPIGTFPDAEYHFFRKSCQHCDNAPCVHVCPTGASHIRKEDGIVdVNPDLC 130
Cdd:cd16370   11 CIGCYSCMLACSRRVHKSASLSKSAI----RVRTRGGLEGGFTVVVCRACEDPPCAEACPTGALEPRKGGGVV-LDKEKC 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 743524057 131 VGCMYCLAACPYQVRFINPVTKVADKCDFCrktnlaagkePACVESCPTKALVF 184
Cdd:cd16370   86 IGCGNCVKACIVGAIFWDEETNKPIICIHC----------GYCARYCPHDVLAM 129
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 47-182 3.54e-13

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


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 63.89  E-value: 3.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  47 DETACIGCTACMDACREV-NQVPEG-VSRLEIIrsgpigtfpDAEYHFFRKSCQHCDNapCVHVCPTGASHiRKEDGIVD 124
Cdd:cd16372    6 DPEKCIGCLQCEEACSKTfFKEEDReKSCIRIT---------ETEGGYAINVCNQCGE--CIDVCPTGAIT-RDANGVVM 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 743524057 125 VNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCrktnlaagkePACVESCPTKAL 182
Cdd:cd16372   74 INKKLCVGCLMCVGFCPEGAMFKHEDYPEPFKCIAC----------GICVKACPTGAL 121
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 46-184 4.67e-10

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: 55.48  E-value: 4.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  46 HDETACIGCTACMDACrevnqvPEGVsrLEIIRSGPIGTFPDaeyhFFRKSCQHCDNapCVHVCPTGASHIRKEDGIVD- 124
Cdd:cd10549    3 YDPEKCIGCGICVKAC------PTDA--IELGPNGAIARGPE----IDEDKCVFCGA--CVEVCPTGAIELTPEGKEYVp 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743524057 125 ------VNPDLCVGCMYCLAACPYQ---VRFINPVTKVADKCDFCRktnlaagkepACVESCPTKALVF 184
Cdd:cd10549   69 kekeaeIDEEKCIGCGLCVKVCPVDaitLEDELEIVIDKEKCIGCG----------ICAEVCPVNAIKL 127
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
51-141 8.88e-09

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 54.65  E-value: 8.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  51 CIGCTACMDACREVNQVPEGVSRLEIIRSGPIGTFpdaeyHFFRKSCQHCDnaPCVHVCPTGAshIRKEDGIVDVNPDLC 130
Cdd:COG4624   52 PRCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSI-----IRDKEKCKNCY--PCVRACPVKA--IKVDDGKAEIDEEKC 122

                         90
                 ....*....|.
gi 743524057 131 VGCMYCLAACP 141
Cdd:COG4624  123 ISCGQCVAVCP 133
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
97-151 4.03e-08

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 48.96  E-value: 4.03e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 743524057  97 CQHCDNapCVHVCPTGAshIRKEDGIVDVNPDLCVGCMYCLAACPYQVRFINPVT 151
Cdd:COG2768   13 CIGCGA--CVKVCPVGA--ISIEDGKAVIDPEKCIGCGACIEVCPVGAIKIEWEE 63
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 50-179 6.86e-08

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: 50.33  E-value: 6.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  50 ACIGCTACMDACrevnqvPEGVSRLEIIRSGPIGTF-PDAEYHffRKSCQHCDNApCVHVCPTGA-SHIRKED-----GI 122
Cdd:cd16373   15 LCIRCGLCVEAC------PTGVIQPAGLEDGLEGGRtPYLDPR--EGPCDLCCDA-CVEVCPTGAlRPLDLEEqkvkmGV 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743524057 123 VDVNPDLCV------GCMYCLAACPYQVRFINPVTKV------ADKCDFCrktnlaaGkepACVESCPT 179
Cdd:cd16373   86 AVIDKDRCLawqggtDCGVCVEACPTEAIAIVLEDDVlrpvvdEDKCVGC-------G---LCEYVCPV 144
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 97-141 5.20e-07

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 45.81  E-value: 5.20e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 743524057  97 CQHCDNapCVHVCPTGAshIRKEDGIVDVNPDLCVGCMYCLAACP 141
Cdd:COG2221   17 CIGCGL--CVAVCPTGA--ISLDDGKLVIDEEKCIGCGACIRVCP 57
NapF COG1145
Ferredoxin [Energy production and conversion];
97-144 1.17e-06

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 47.80  E-value: 1.17e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 743524057  97 CQHCDNapCVHVCPTGASHIRKEDGIVDVNPDLCVGCMYCLAACPYQV 144
Cdd:COG1145  184 CIGCGL--CVKVCPTGAIRLKDGKPQIVVDPDKCIGCGACVKVCPVGA 229
PRK13795 PRK13795
hypothetical protein; Provisional
 85-149 1.36e-06

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 48.45  E-value: 1.36e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743524057  85 FPDAEYHFFRKS-CQHCDnaPCVHVCPTGAshIRKEDG--IVDVNPDLCVGCMYCLAACPYqVRFINP 149
Cdd:PRK13795 570 FKDAARLLRRAAeCVGCG--VCVGACPTGA--IRIEEGkrKISVDEEKCIHCGKCTEVCPV-VKYKDK 632
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
105-144 4.04e-06

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 46.46  E-value: 4.04e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 743524057 105 CVHVCPTGASHIrkEDGIVDVNPDLCVGCMYCLAACPYQV 144
Cdd:PRK07118 147 CVAACPFDAIHI--ENGLPVVDEDKCTGCGACVKACPRNV 184
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
125-189 5.76e-06

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 46.39  E-value: 5.76e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743524057 125 VNPDLCVGCMYCLAACPYQVRFINPVTKV---ADKCDFCrktnlaaGkepACVESCPTKALVFGNLDD 189
Cdd:COG1148  493 VDPEKCTGCGRCVEVCPYGAISIDEKGVAevnPALCKGC-------G---TCAAACPSGAISLKGFTD 550
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
91-141 6.73e-06

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 46.39  E-value: 6.73e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 743524057  91 HFFRKSCQHCdnAPCVHVCPTGASHIrKEDGIVDVNPDLCVGCMYCLAACP 141
Cdd:COG1148  492 EVDPEKCTGC--GRCVEVCPYGAISI-DEKGVAEVNPALCKGCGTCAAACP 539
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
44-195 1.25e-05

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 45.40  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  44 MLHDETACIGCTACMDACREVNQVPEGVSRLEIIR-------SGPIGTFPDAEYHFFRKSCQHCDNAPCVHVCPTGAShI 116
Cdd:COG4624    1 LLLLLRACCCCCIEEGDELLLLEEAERVLRIIILEallpehvDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIII-I 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057 117 RKEDGIVDVNPDLCVGCMYCLAACPYQ-VRFINPVTKVA-DKCDFCrktnlaaGKepaCVESCPTKAL--------VFGN 186
Cdd:COG4624   80 DKRGPSIIRDKEKCKNCYPCVRACPVKaIKVDDGKAEIDeEKCISC-------GQ---CVAVCPFGAIteksdiekVKKA 149


                 ....*....
gi 743524057 187 LDDPDSPIA 195
Cdd:COG4624  150 LKDPEKVVA 158
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 105-141 1.68e-05

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: 44.60  E-value: 1.68e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 743524057 105 CVHVCPTGASHIrKEDGIVDVNPDLCVGCMYCLAACP 141
Cdd:COG2878  145 CIKACPFDAIVG-AAKGMHTVDEDKCTGCGLCVEACP 180
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 105-143 1.75e-05

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 41.57  E-value: 1.75e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 743524057 105 CVHVCPTGAshIRKEDGIVDVNPDLCVGCMYCLAACPYQ 143
Cdd:COG4231   30 CVKVCPADA--IEEGDGKAVIDPDLCIGCGSCVQVCPVD 66
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 97-141 1.91e-05

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: 41.96  E-value: 1.91e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 743524057  97 CQHCDNapCVHVCPTGAshIRKEDG-IVDVNPDLCVGCMYCLAACP 141
Cdd:COG1144   32 CIGCGL--CWIVCPDGA--IRVDDGkYYGIDYDYCKGCGICAEVCP 73
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 97-143 2.97e-05

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 40.87  E-value: 2.97e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 743524057  97 CQHCDNapCVHVCPTGASHIRKEDGIVdVNPDLCVGCMYCLAACPYQ 143
Cdd:COG1149   13 CIGCGL--CVEVCPEGAIKLDDGGAPV-VDPDLCTGCGACVGVCPTG 56
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
105-186 4.45e-05

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 43.13  E-value: 4.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057 105 CVHVCPTGA--SHIRKEDGI-VDVNPDLCVGCMYCLAACPYQVrFINPVTKVADKCDFCRktnlaagkepACVESCPTKA 181
Cdd:COG0348  184 CRYLCPYGAfqGLLSDLSTLrVRYDRGDCIDCGLCVKVCPMGI-DIRKGEINQSECINCG----------RCIDACPKDA 252


                 ....*
gi 743524057 182 LVFGN 186
Cdd:COG0348  253 IRFSS 257
ACS_1 cd01916
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
 77-172 4.64e-05

Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.


Pssm-ID: 238897 [Multi-domain]  Cd Length: 731  Bit Score: 43.94  E-value: 4.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  77 IRSGPIGTFPDAEYHFFRKSCQHCDNapCVHVCPtgaSHIRKEDGIV-----DVNP-----DLCVGCMYCLAACPYQVRF 146
Cdd:cd01916  347 KRKGEKKLPTDEEFQELAAKCTDCGW--CTRACP---NSLRIKEAMEaakegDFSGladlfDQCVGCGRCEQECPKEIPI 421

                         90       100
                 ....*....|....*....|....*.
gi 743524057 147 INPVTKVADKCDFCRKTNLAAGKEPA 172
Cdd:cd01916  422 INMIEKAARERIKEEKGKMRAGRGPI 447
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 122-184 6.51e-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: 39.71  E-value: 6.51e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743524057 122 IVDVNPDLCVGCMYCLAACPYQV-RFINPVTKV--ADKCDFCRktnlaagkepACVESCPTKALVF 184
Cdd:COG1149    5 IPVIDEEKCIGCGLCVEVCPEGAiKLDDGGAPVvdPDLCTGCG----------ACVGVCPTGAITL 60
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 127-190 6.73e-05

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: 39.73  E-value: 6.73e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057 127 PDLCVGCMYCLAACPYQVRFINPVTKV------ADKCDFCRktnlaagkepACVESCPTKALVFGNLDDP 190
Cdd:COG1143    1 EDKCIGCGLCVRVCPVDAITIEDGEPGkvyvidPDKCIGCG----------LCVEVCPTGAISMTPFELA 60
NapF COG1145
Ferredoxin [Energy production and conversion];
44-182 9.78e-05

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 42.40  E-value: 9.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  44 MLHDETACIGCTACMDACREVNQVPEGVSRLEIIRSGPIGTFPDAEYHFFRKSCQHCDNAPCVHVCPTGASHIRKEDGIV 123
Cdd:COG1145   98 LVLLLALAVAGAAKRLIISAVKLVAGLVVAAGEVLLVIAAALAEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKA 177

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743524057 124 DVNPDLCVGCMYCLAACPYQV-RFINPVTKV---ADKCDFCRktnlaagkepACVESCPTKAL 182
Cdd:COG1145  178 VIDAEKCIGCGLCVKVCPTGAiRLKDGKPQIvvdPDKCIGCG----------ACVKVCPVGAI 230
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 97-143 1.04e-04

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 39.34  E-value: 1.04e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 743524057  97 CQHCDNapCVHVCPTGASHIRKEDG--IVDVNPDLCVGCMYCLAACPYQ 143
Cdd:COG1143    4 CIGCGL--CVRVCPVDAITIEDGEPgkVYVIDPDKCIGCGLCVEVCPTG 50
NuoG COG1034
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ...
 45-113 1.89e-04

NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440657 [Multi-domain]  Cd Length: 453  Bit Score: 41.75  E-value: 1.89e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743524057  45 LHDETACIGCTACMDACREVNQVPEgvsrLEIIRSGP---IGTFPDAEYhffrkSCQHCDNapCVHVCPTGA 113
Cdd:COG1034  140 LLDMNRCILCTRCVRFCDEIAGDPE----LGVIGRGEhseIGTYLGKPL-----DSEFSGN--CIDVCPVGA 200
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 105-143 2.11e-04

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 38.54  E-value: 2.11e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 743524057 105 CVHVCPTGASHIRKEDG-IVDVNPDLCVGCMYCLAACPYQ 143
Cdd:COG1146   16 CVEVCPVDVLELDEEGKkALVINPEECIGCGACELVCPVG 55
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 121-184 3.94e-04

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 37.77  E-value: 3.94e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743524057 121 GIVDVNPDLCVGCMYCLAACPYQVRFINPVTKVA-----DKCDFCRktnlaagkepACVESCPTKALVF 184
Cdd:COG1146    1 MMPVIDTDKCIGCGACVEVCPVDVLELDEEGKKAlvinpEECIGCG----------ACELVCPVGAITV 59
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 94-141 4.13e-04

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: 37.23  E-value: 4.13e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 743524057   94 RKSCQHCdnAPCVHVCPTGASH-----IRKEDGIVDVNPDLCVGCMYCLAACP 141
Cdd:pfam13237   6 PDKCIGC--GRCTAACPAGLTRvgaivERLEGEAVRIGVWKCIGCGACVEACP 56
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 97-144 6.16e-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: 6.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 743524057   97 CQHCDNapCVHVCPTGA-----SHIRKEDGIVDVNPDLCVGCMYCLAACPYQV 144
Cdd:pfam12838   1 CIGCGA--CVAACPVGAitldeVGEKKGTKTVVIDPERCVGCGACVAVCPTGA 51
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
118-191 6.34e-04

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 37.40  E-value: 6.34e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743524057 118 KEDGIVDVNPDLCVGCMYCLAACPYQVrfINPVTKVA----DKCDFCrktnlaagkePACVESCPTKALVFGNLDDPD 191
Cdd:COG2768    1 HSLGKPYVDEEKCIGCGACVKVCPVGA--ISIEDGKAvidpEKCIGC----------GACIEVCPVGAIKIEWEEDEE 66
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 124-199 1.05e-03

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: 37.76  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057 124 DVNPDLCVGCMYCLAACPYQVRFINPVTKVA-------DKCDFCRKtnlaagkepaCVESCPTKALVFGNLDDPDSPIAK 196
Cdd:cd10549    2 KYDPEKCIGCGICVKACPTDAIELGPNGAIArgpeideDKCVFCGA----------CVEVCPTGAIELTPEGKEYVPKEK 71


                 ...
gi 743524057 197 RLV 199
Cdd:cd10549   72 EAE 74
FixX COG2440
Ferredoxin-like protein FixX [Energy production and conversion];
99-144 1.14e-03

Ferredoxin-like protein FixX [Energy production and conversion];


Pssm-ID: 441981 [Multi-domain]  Cd Length: 87  Bit Score: 36.72  E-value: 1.14e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 743524057  99 HCDNAPCVHVCPTGASHIrKEDGIVDVNPDLCVGCMYCLAACPYQV 144
Cdd:COG2440   26 RCLAKPCTRYCPAGVYEI-VGDGRLQINYENCLECGTCRIKCPTQN 70
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 50-182 1.26e-03

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


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 37.99  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  50 ACIGCTACMDACrevnqvPEGvsrleIIRSGpIGTFPdaEYHFFRKSCQHCDNapCVHVCPTGASHIRKEDGI---VDVN 126
Cdd:cd10564   14 LCTRCGDCVEAC------PEG-----IIVRG-DGGFP--ELDFSRGECTFCGA--CAEACPEGALDPAREAPWplrAEIG 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743524057 127 pDLC-----VGCMYCLAACPYQ-VRFINPVTKVA------DKCDFCrktnlaaGkepACVESCPTKAL 182
Cdd:cd10564   78 -DSClalqgVECRSCQDACPTQaIRFRPRLGGIAlpeldaDACTGC-------G---ACVSVCPVGAI 134
Fer4_6 pfam12837
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 122-144 2.03e-03

4Fe-4S binding domain; This 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.


Pssm-ID: 432822 [Multi-domain]  Cd Length: 24  Bit Score: 34.51  E-value: 2.03e-03
                          10        20
                  ....*....|....*....|...
gi 743524057  122 IVDVNPDLCVGCMYCLAACPYQV 144
Cdd:pfam12837   1 VVEVDPDKCIGCGRCVVVCPYGA 23
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 130-181 2.26e-03

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 35.19  E-value: 2.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743524057  130 CVGCMYCLAACPYQVRFINPVTKV---------ADKCDFCRktnlaagkepACVESCPTKA 181
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKkgtktvvidPERCVGCG----------ACVAVCPTGA 51
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 51-113 3.10e-03

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 34.81  E-value: 3.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743524057   51 CIGCTACMDACrevnqvPEGVsrLEIIRSGPIGTFPDAEYHFFRksCQHCDNapCVHVCPTGA 113
Cdd:pfam12838   1 CIGCGACVAAC------PVGA--ITLDEVGEKKGTKTVVIDPER--CVGCGA--CVAVCPTGA 51
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 125-182 3.17e-03

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 35.03  E-value: 3.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057 125 VNPDLCVGCMYCLAACPYQV-RFINPVTKV-ADKCDFCRktnlaagkepACVESCPTKAL 182
Cdd:COG2221   12 IDEEKCIGCGLCVAVCPTGAiSLDDGKLVIdEEKCIGCG----------ACIRVCPTGAI 61
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
47-141 3.17e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 37.61  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057  47 DETACIGCTACMDACrevnqvPEGVsrLEIIRSgpigtfpDAEYHFfrkSC----------QHCDNA-----PCVHVCPT 111
Cdd:PRK07118 166 DEDKCTGCGACVKAC------PRNV--IELIPK-------SARVFV---ACnskdkgkavkKVCEVGcigcgKCVKACPA 227

                         90       100       110
                 ....*....|....*....|....*....|
gi 743524057 112 GAshIRKEDGIVDVNPDLCVGCMYCLAACP 141
Cdd:PRK07118 228 GA--ITMENNLAVIDQEKCTSCGKCVEKCP 255
napG PRK09476
quinol dehydrogenase periplasmic component; Provisional
 1-113 3.50e-03

quinol dehydrogenase periplasmic component; Provisional


Pssm-ID: 236534 [Multi-domain]  Cd Length: 254  Bit Score: 37.68  E-value: 3.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743524057   1 MSCSRRHFMA-------GMSAGALIMMTGPTRSLATPLAhsqtidgVRF-GMLHDE---TACIGCTACMDACrevnqvPE 69
Cdd:PRK09476   7 PQNGRRRFLRdvvrtagGLAAVGVALGLQQQQARASGVA-------LRPpGALNENdflSACIRCGLCVQAC------PY 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 743524057  70 GVSRLEIIRSG-PIGTfPdaeyhFF---RKSCQHCDNAPCVHVCPTGA 113
Cdd:PRK09476  74 DTLKLATLASGlSAGT-P-----YFvarDIPCEMCEDIPCVKACPSGA 115
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 97-141 4.82e-03

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 37.55  E-value: 4.82e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 743524057  97 CQHCDNapCVHVCPTGASHIRKEDGIVDVNPDLCVGCMYCLAACP 141
Cdd:PRK12771 512 CFECDN--CYGACPQDAIIKLGPGRRYHFDYDKCTGCHICADVCP 554
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 121-182 5.26e-03

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 35.58  E-value: 5.26e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743524057 121 GIVDVNPDLCVGCMYCLAACPYQV-RFINPVTKVA---DKCDFCRKtnlaagkepaCVESCPTKAL 182
Cdd:PRK08348  35 GKILYDVDKCVGCRMCVTVCPAGVfVYLPEIRKVAlwtGRCVFCGQ----------CVDVCPTGAL 90
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 125-183 6.01e-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: 34.64  E-value: 6.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743524057 125 VNPDLCVGCMYCLAACPYQVRFINPVTKVA---DKCDFCRktnlaagkepACVESCPTKALV 183
Cdd:COG1144   27 VDEDKCIGCGLCWIVCPDGAIRVDDGKYYGidyDYCKGCG----------ICAEVCPVKAIE 78
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 97-143 6.22e-03

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 37.07  E-value: 6.22e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 743524057  97 CQ--HCdNAPCVHVCP---TG--ASHIRKEDGIVDVNPDLCVGCMYCLAACPYQ 143
Cdd:COG1245   12 CQpkKC-NYECIKYCPvnrTGkeAIEIDEDDGKPVISEELCIGCGICVKKCPFD 64
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 47-113 6.42e-03

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 34.32  E-value: 6.42e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743524057  47 DETACIGCTACMDACrevnqvPEGVsrleiirsgpIGTFPDAEYHFFRKSCQHCDNapCVHVCPTGA 113
Cdd:COG1149    9 DEEKCIGCGLCVEVC------PEGA----------IKLDDGGAPVVDPDLCTGCGA--CVGVCPTGA 57
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
125-182 6.49e-03

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 35.31  E-value: 6.49e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 743524057 125 VNPDLCVGCMYCLAACPYQVRFINPVTKVADKCDFCRKTNLaagkepaCVESCPTKAL 182
Cdd:PRK09623  48 VDESKCVKCYICWKFCPEPAIYIKEDGYVAIDYDYCKGCGI-------CANECPTKAI 98
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 125-186 6.72e-03

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


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 35.71  E-value: 6.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743524057 125 VNPDLCVGCMYCLAACPYQVRFINPVTKVADK------------CDFCRktnlaAGKEPACVESCPTKALVFGN 186
Cdd:cd16370    6 KDMERCIGCYSCMLACSRRVHKSASLSKSAIRvrtrggleggftVVVCR-----ACEDPPCAEACPTGALEPRK 74
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
105-141 8.78e-03

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 34.92  E-value: 8.78e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 743524057 105 CVHVCPTGASHIrKEDGIVDVNPDLCVGCMYCLAACP 141
Cdd:PRK09623  59 CWKFCPEPAIYI-KEDGYVAIDYDYCKGCGICANECP 94
Fer4_9 pfam13187
4Fe-4S dicluster domain;
130-182 9.39e-03

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 33.30  E-value: 9.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 743524057  130 CVGCMYCLAACPYQV------RFINPVTKVADKCDFCRktnlaagkepACVESCPTKAL 182
Cdd:pfam13187   2 CTGCGACVAACPAGAivpdlvGQTIRGDIAGLACIGCG----------ACVDACPRGAI 50
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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