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Conserved domains on  [gi|516456416|ref|WP_017845256|]
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MULTISPECIES: cytochrome c oxidase accessory protein CcoG [Pseudomonas]

Protein Classification

cytochrome c oxidase accessory protein CcoG( domain architecture ID 11494955)

cytochrome c oxidase accessory protein CcoG is a RdxA/RdxB/FixG family protein similar to Sinorhizobium meliloti nitrogen fixation protein FixG and Rhodobacter sphaeroides RdxB and is required for the formation of a high-affinity cbb3-type cytochrome oxidase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ccoG_rdxA_fixG TIGR02745
cytochrome c oxidase accessory protein FixG; Member of this ferredoxin-like protein family are ...
 39-467 0e+00

cytochrome c oxidase accessory protein FixG; Member of this ferredoxin-like protein family are found exclusively in species with an operon encoding the cbb3 type of cytochrome c oxidase (cco-cbb3), and near the cco-cbb3 operon in about half the cases. The cco-cbb3 is found in a variety of proteobacteria and almost nowhere else, and is associated with oxygen use under microaerobic conditions. Some (but not all) of these proteobacteria are also nitrogen-fixing, hence the gene symbol fixG. FixG was shown essential for functional cco-cbb3 expression in Bradyrhizobium japonicum.


:

Pssm-ID: 274278 [Multi-domain]  Cd Length: 434  Bit Score: 660.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416   39 FRNLRMLGGAGLFLLYFGTVWLNWGGHQAVWWDLPERKFFIFGATFWPQDFILLSGILIVAAFGLFFITVYAGRIWCGYT 118
Cdd:TIGR02745   1 FRKLRYVIGAVLLLIFLITPWIRWNGNQAVLLDFAHRQFHFFGITFWPQEFYLLAGLLIIAALGLFFITTLAGRVWCGYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416  119 CPQSVWTWIFMWCEKVTEGDRNQRIKLDKAPMGANKFLRKFSKHTLWLLIGFVTGMTFVGYFSPIRELVFDFFTGQADGW 198
Cdd:TIGR02745  81 CPQTVWTDLFDWIERKIEGDRNKRMKLDKAPWTFDKVWKKTLKHLLWLVISLVTGGTFIFYFVPAPDLFAYLFTGPADHP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416  199 SYFWVGFFTLATYGNAGWLREQVCIYMCPYARFQSVMFDKDTLIVSYDPRRGEVRGPRKKGADYKAQG-LGDCIDCTMCV 277
Cdd:TIGR02745 161 AYFWVLFFTAATYIFDGWMREQFCIYMCPYARIQSVMFDKDTLIVVYDEKRGEPRGPRKGKKDPKAPGpLGDCIDCNLCV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416  278 QVCPTGIDIRDGLQIECIGCAACIDACDNIMDKMDYPRGLISYTTEHNLSGQKT-HKLRPRLIGYALVLLAMMSLLATAF 356
Cdd:TIGR02745 241 QVCPTGIDIRDGLQLECINCGLCIDACDDVMEKMGKPKGLISYTSEAALEGRKKvRLLRPRTIGYAAVLAIVIGLLAIAL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416  357 FMRPLVGFDVSKDR-VLYRENAEGRIENVYSLKIMNKDQRDHTYVLDAAGLPDLKLQGRRE-IKVAAGDIVSMPVELSSA 434
Cdd:TIGR02745 321 STREPMDLNVLRDRnLLYVRNSDGVVENTYTLKILNKTEQPHEYYLSVLGLPGIKIEGPGApIHVKAGEKVKLPVFLRTP 400

                         410       420       430
                  ....*....|....*....|....*....|....
gi 516456416  435 PEQLPSSTNEVKFILKDADDA-SVHIEAKSRFIG 467
Cdd:TIGR02745 401 PDALKSGITSIEIRAYAEDDSeGIRVERESVFVG 434
 
Name Accession Description Interval E-value
ccoG_rdxA_fixG TIGR02745
cytochrome c oxidase accessory protein FixG; Member of this ferredoxin-like protein family are ...
 39-467 0e+00

cytochrome c oxidase accessory protein FixG; Member of this ferredoxin-like protein family are found exclusively in species with an operon encoding the cbb3 type of cytochrome c oxidase (cco-cbb3), and near the cco-cbb3 operon in about half the cases. The cco-cbb3 is found in a variety of proteobacteria and almost nowhere else, and is associated with oxygen use under microaerobic conditions. Some (but not all) of these proteobacteria are also nitrogen-fixing, hence the gene symbol fixG. FixG was shown essential for functional cco-cbb3 expression in Bradyrhizobium japonicum.


Pssm-ID: 274278 [Multi-domain]  Cd Length: 434  Bit Score: 660.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416   39 FRNLRMLGGAGLFLLYFGTVWLNWGGHQAVWWDLPERKFFIFGATFWPQDFILLSGILIVAAFGLFFITVYAGRIWCGYT 118
Cdd:TIGR02745   1 FRKLRYVIGAVLLLIFLITPWIRWNGNQAVLLDFAHRQFHFFGITFWPQEFYLLAGLLIIAALGLFFITTLAGRVWCGYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416  119 CPQSVWTWIFMWCEKVTEGDRNQRIKLDKAPMGANKFLRKFSKHTLWLLIGFVTGMTFVGYFSPIRELVFDFFTGQADGW 198
Cdd:TIGR02745  81 CPQTVWTDLFDWIERKIEGDRNKRMKLDKAPWTFDKVWKKTLKHLLWLVISLVTGGTFIFYFVPAPDLFAYLFTGPADHP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416  199 SYFWVGFFTLATYGNAGWLREQVCIYMCPYARFQSVMFDKDTLIVSYDPRRGEVRGPRKKGADYKAQG-LGDCIDCTMCV 277
Cdd:TIGR02745 161 AYFWVLFFTAATYIFDGWMREQFCIYMCPYARIQSVMFDKDTLIVVYDEKRGEPRGPRKGKKDPKAPGpLGDCIDCNLCV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416  278 QVCPTGIDIRDGLQIECIGCAACIDACDNIMDKMDYPRGLISYTTEHNLSGQKT-HKLRPRLIGYALVLLAMMSLLATAF 356
Cdd:TIGR02745 241 QVCPTGIDIRDGLQLECINCGLCIDACDDVMEKMGKPKGLISYTSEAALEGRKKvRLLRPRTIGYAAVLAIVIGLLAIAL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416  357 FMRPLVGFDVSKDR-VLYRENAEGRIENVYSLKIMNKDQRDHTYVLDAAGLPDLKLQGRRE-IKVAAGDIVSMPVELSSA 434
Cdd:TIGR02745 321 STREPMDLNVLRDRnLLYVRNSDGVVENTYTLKILNKTEQPHEYYLSVLGLPGIKIEGPGApIHVKAGEKVKLPVFLRTP 400

                         410       420       430
                  ....*....|....*....|....*....|....
gi 516456416  435 PEQLPSSTNEVKFILKDADDA-SVHIEAKSRFIG 467
Cdd:TIGR02745 401 PDALKSGITSIEIRAYAEDDSeGIRVERESVFVG 434
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
31-325 1.55e-90

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 276.17  E-value: 1.55e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416  31 YTRAFTGLFRNLRMLGGAGLFLLYFGTVWLNWGGHQAVWWDLPERKFFIFGaTFWpqDFILLSGILIVAAFGLFFITVYA 110
Cdd:COG0348    3 YPRLVKGRFRRLRRLVQLLFLLLFLLGPWLRWLGDPAVLLDLAERRFYLFG-LFW--DFYLLALLLIGAALALFLLTLLF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416 111 GRIWCGYTCPQSVWTWIFMWCEKVTeGDRNQRIkldkaPMGANKFLR--KFSKHTLWLLIGFVTGMTFVGYFSPIRELVF 188
Cdd:COG0348   80 GRVWCGWVCPQGVLTELFSWLERKL-GDRRLKL-----PWSLSKILRwlKYIILALWLLLALLTGLTFFGYFSPIGTLLR 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416 189 DFFTGQADGWsyfWVGFFTLATYGNAGWLREQVCIYMCPYARFQSVMFDKDTLIVSYDPrrgevrgprkkgadykaqglG 268
Cdd:COG0348  154 LLLFGVLGLW---LLLILLAAFLLLALFLRRQWCRYLCPYGAFQGLLSDLSTLRVRYDR--------------------G 210

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 516456416 269 DCIDCTMCVQVCPTGIDIRDGL--QIECIGCAACIDACDNIMdkmdyprglISYTTEHN 325
Cdd:COG0348  211 DCIDCGLCVKVCPMGIDIRKGEinQSECINCGRCIDACPKDA---------IRFSSRGE 260
Fer4_18 pfam13746
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 217-323 1.11e-61

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: 404610 [Multi-domain]  Cd Length: 114  Bit Score: 196.47  E-value: 1.11e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416  217 LREQVCIYMCPYARFQSVMFDKDTLIVSYDPRRGE-VRGPRKKGADYK------AQGLGDCIDCTMCVQVCPTGIDIRDG 289
Cdd:pfam13746   1 ARENFCIYACPYGRFQSVMYDEDTLTVVYDAVRGEgIYGRKPPKAGLKtkelrqQKGVGDCIDCESCVQVCPTGIDIRKG 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 516456416  290 LQIECIGCAACIDACDNIMDKMDYPRGLISYTTE 323
Cdd:pfam13746  81 LQLECINCGLCIDACNTIMGKLGKPRGLIRYSSE 114
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 269-305 6.75e-08

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: 51.24  E-value: 6.75e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 516456416 269 DCIDCTMCVQVCPTG-IDIRDGLQIE-----CIGCAACIDACD 305
Cdd:cd10549   79 KCIGCGLCVKVCPVDaITLEDELEIVidkekCIGCGICAEVCP 121
napH PRK09477
quinol dehydrogenase membrane component; Provisional
 79-305 4.45e-07

quinol dehydrogenase membrane component; Provisional


Pssm-ID: 236535 [Multi-domain]  Cd Length: 271  Bit Score: 51.05  E-value: 4.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416  79 IFGATFWPqDFILLSGILIVAAFGLFFitvyAGRIWCGYTCPQSVWT----WIfmwcekvtegdrnqRIKLdkapmGANK 154
Cdd:PRK09477  58 SLAAGHLP-ATVALIGALIITVFYALA----GGRAFCSWVCPVNLVTdlanWL--------------RRKL-----GLNQ 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416 155 FLrKFSKHT------LWLLIGFVTGMTFVGYFSPI----RELVFDFFTGqadGWSYFWVGFFTLATYGNaGWlreqvCIY 224
Cdd:PRK09477 114 SA-TLPRNLrywllvLVLVGSALTGTLAWEWINPVsmlhRGLVFGFGSG---WWLILAIFLFDLFVVEH-GW-----CGH 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416 225 MCPYARFQSVMFDKDTLIVsydprrgevrgprkkgadyKAQGLGDCIDCTMCVQVCP-------------TGIDIRDGlq 291
Cdd:PRK09477 184 LCPLGAFYGLIGKKSLIRV-------------------KAHDRQKCTRCMDCFHVCPepqvlrpplkgkqSPSQVTSG-- 242

                        250
                 ....*....|....
gi 516456416 292 iECIGCAACIDACD 305
Cdd:PRK09477 243 -DCITCGRCIDVCS 255
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 269-304 1.09e-04

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


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 43.69  E-value: 1.09e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 516456416 269 DCIDCTMCVQVCPTG-IDIRDGLQI---ECIGCAACIDAC 304
Cdd:NF038196 186 KCIGCGICAKVCPVNnIEMEDGKPVwghNCTHCLACIHRC 225
 
Name Accession Description Interval E-value
ccoG_rdxA_fixG TIGR02745
cytochrome c oxidase accessory protein FixG; Member of this ferredoxin-like protein family are ...
 39-467 0e+00

cytochrome c oxidase accessory protein FixG; Member of this ferredoxin-like protein family are found exclusively in species with an operon encoding the cbb3 type of cytochrome c oxidase (cco-cbb3), and near the cco-cbb3 operon in about half the cases. The cco-cbb3 is found in a variety of proteobacteria and almost nowhere else, and is associated with oxygen use under microaerobic conditions. Some (but not all) of these proteobacteria are also nitrogen-fixing, hence the gene symbol fixG. FixG was shown essential for functional cco-cbb3 expression in Bradyrhizobium japonicum.


Pssm-ID: 274278 [Multi-domain]  Cd Length: 434  Bit Score: 660.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416   39 FRNLRMLGGAGLFLLYFGTVWLNWGGHQAVWWDLPERKFFIFGATFWPQDFILLSGILIVAAFGLFFITVYAGRIWCGYT 118
Cdd:TIGR02745   1 FRKLRYVIGAVLLLIFLITPWIRWNGNQAVLLDFAHRQFHFFGITFWPQEFYLLAGLLIIAALGLFFITTLAGRVWCGYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416  119 CPQSVWTWIFMWCEKVTEGDRNQRIKLDKAPMGANKFLRKFSKHTLWLLIGFVTGMTFVGYFSPIRELVFDFFTGQADGW 198
Cdd:TIGR02745  81 CPQTVWTDLFDWIERKIEGDRNKRMKLDKAPWTFDKVWKKTLKHLLWLVISLVTGGTFIFYFVPAPDLFAYLFTGPADHP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416  199 SYFWVGFFTLATYGNAGWLREQVCIYMCPYARFQSVMFDKDTLIVSYDPRRGEVRGPRKKGADYKAQG-LGDCIDCTMCV 277
Cdd:TIGR02745 161 AYFWVLFFTAATYIFDGWMREQFCIYMCPYARIQSVMFDKDTLIVVYDEKRGEPRGPRKGKKDPKAPGpLGDCIDCNLCV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416  278 QVCPTGIDIRDGLQIECIGCAACIDACDNIMDKMDYPRGLISYTTEHNLSGQKT-HKLRPRLIGYALVLLAMMSLLATAF 356
Cdd:TIGR02745 241 QVCPTGIDIRDGLQLECINCGLCIDACDDVMEKMGKPKGLISYTSEAALEGRKKvRLLRPRTIGYAAVLAIVIGLLAIAL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416  357 FMRPLVGFDVSKDR-VLYRENAEGRIENVYSLKIMNKDQRDHTYVLDAAGLPDLKLQGRRE-IKVAAGDIVSMPVELSSA 434
Cdd:TIGR02745 321 STREPMDLNVLRDRnLLYVRNSDGVVENTYTLKILNKTEQPHEYYLSVLGLPGIKIEGPGApIHVKAGEKVKLPVFLRTP 400

                         410       420       430
                  ....*....|....*....|....*....|....
gi 516456416  435 PEQLPSSTNEVKFILKDADDA-SVHIEAKSRFIG 467
Cdd:TIGR02745 401 PDALKSGITSIEIRAYAEDDSeGIRVERESVFVG 434
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
31-325 1.55e-90

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 276.17  E-value: 1.55e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416  31 YTRAFTGLFRNLRMLGGAGLFLLYFGTVWLNWGGHQAVWWDLPERKFFIFGaTFWpqDFILLSGILIVAAFGLFFITVYA 110
Cdd:COG0348    3 YPRLVKGRFRRLRRLVQLLFLLLFLLGPWLRWLGDPAVLLDLAERRFYLFG-LFW--DFYLLALLLIGAALALFLLTLLF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416 111 GRIWCGYTCPQSVWTWIFMWCEKVTeGDRNQRIkldkaPMGANKFLR--KFSKHTLWLLIGFVTGMTFVGYFSPIRELVF 188
Cdd:COG0348   80 GRVWCGWVCPQGVLTELFSWLERKL-GDRRLKL-----PWSLSKILRwlKYIILALWLLLALLTGLTFFGYFSPIGTLLR 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416 189 DFFTGQADGWsyfWVGFFTLATYGNAGWLREQVCIYMCPYARFQSVMFDKDTLIVSYDPrrgevrgprkkgadykaqglG 268
Cdd:COG0348  154 LLLFGVLGLW---LLLILLAAFLLLALFLRRQWCRYLCPYGAFQGLLSDLSTLRVRYDR--------------------G 210

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 516456416 269 DCIDCTMCVQVCPTGIDIRDGL--QIECIGCAACIDACDNIMdkmdyprglISYTTEHN 325
Cdd:COG0348  211 DCIDCGLCVKVCPMGIDIRKGEinQSECINCGRCIDACPKDA---------IRFSSRGE 260
Fer4_18 pfam13746
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 217-323 1.11e-61

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: 404610 [Multi-domain]  Cd Length: 114  Bit Score: 196.47  E-value: 1.11e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416  217 LREQVCIYMCPYARFQSVMFDKDTLIVSYDPRRGE-VRGPRKKGADYK------AQGLGDCIDCTMCVQVCPTGIDIRDG 289
Cdd:pfam13746   1 ARENFCIYACPYGRFQSVMYDEDTLTVVYDAVRGEgIYGRKPPKAGLKtkelrqQKGVGDCIDCESCVQVCPTGIDIRKG 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 516456416  290 LQIECIGCAACIDACDNIMDKMDYPRGLISYTTE 323
Cdd:pfam13746  81 LQLECINCGLCIDACNTIMGKLGKPRGLIRYSSE 114
FixG_C pfam11614
IG-like fold at C-terminal of FixG, putative oxidoreductase; This domain is part of a ...
 354-467 8.94e-36

IG-like fold at C-terminal of FixG, putative oxidoreductase; This domain is part of a transmembrane protein, FixG, itself part of the FixGHIS operon closely associated with the FixNOPQ operon that is the symbiotically essential cbb3-type haem-copper oxidase complex. FixG expression is induced by oxygen-deprivation. This C-terminal domain adopts an E-set Ig-like fold.


Pssm-ID: 431960 [Multi-domain]  Cd Length: 116  Bit Score: 128.49  E-value: 8.94e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416  354 TAFFMRPLVGFDVSKDR-VLYRENAEGRIENVYSLKIMNKDQRDHTYVLDAAGLPDLKL-QGRREIKVAAGDIVSMPVEL 431
Cdd:pfam11614   1 YALATREPLELDVLRDRgPLFVELSDGSIENVYTLKIINKTEEPRRYTLSVEGLPGLKLeGGPQEIEVAPGEVRTLPVFV 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 516456416  432 SSAPEQLPSSTNEVKFILKDADDASVHIEAKSRFIG 467
Cdd:pfam11614  81 TVPPEAAKSGSTPITFTVTADDDGGETVTEKSRFLG 116
napH_ TIGR02163
ferredoxin-type protein, NapH/MauN family; Most members of this family are the NapH protein, ...
 38-282 4.78e-10

ferredoxin-type protein, NapH/MauN family; Most members of this family are the NapH protein, found next to NapG,in operons that encode the periplasmic nitrate reductase. Some species with this reductase lack NapC but accomplish electron transfer to NapAB in some other manner, likely to involve NapH, NapG, and/or some other protein. A few members of this protein are designated MauN and are found in methylamine utilization operons in species that appear to lack a periplasmic nitrate reductase.


Pssm-ID: 274004 [Multi-domain]  Cd Length: 255  Bit Score: 60.06  E-value: 4.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416   38 LFRNLRMLGGAGLFLL-YFGTVWLNWGGHQA--VWWDLPERKFFIFG---ATFWPQDFILLSGILIVAAFGLFFitvyAG 111
Cdd:TIGR02163   3 ILRRLVQLSILGLFLLgPYAGVWILKGNLSSsrLLGTIPLSDPLITLqilLAGHSPPTNALIGALIIVAFYALF----GG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416  112 RIWCGYTCPQSVWTWIFMWCekvtegdrNQRIKLDKapmgankfLRKFSKHT-LWLLIG-----FVTGMTFVGYFSPI-- 183
Cdd:TIGR02163  79 RAFCSWVCPVNLVTDFAAWL--------RRKLGINK--------IIKLPRNLrYWVLVLflllsFLSGLLIWEWFNPVgi 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416  184 --RELVFdfftGQADGWSYFWVGFFTLATYGNAGWlreqvCIYMCPYARFQSVMFDKDTLIVSYDPRRG----------- 250
Cdd:TIGR02163 143 lhRGIIF----GMGAGIWLILLVFLFDLLFSERGW-----CGHLCPLGAFYGLIGRKSLIKIAASDREKctncmdcfnvc 213

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 516456416  251 ---EV-RGPRKKGADYKAQGlGDCIDCTMCVQVCPT 282
Cdd:TIGR02163 214 pepQVlRMPLKKGGSTLVLS-GDCTLCGRCIDVCHE 248
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
269-304 2.44e-08

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 50.88  E-value: 2.44e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 516456416 269 DCIDCTMCVQVCPTG-IDIRDG-LQI---ECIGCAACIDAC 304
Cdd:COG2768   12 KCIGCGACVKVCPVGaISIEDGkAVIdpeKCIGCGACIEVC 52
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 270-304 3.23e-08

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 50.43  E-value: 3.23e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 516456416 270 CIDCTMCVQVCPTG-IDIRDG-LQIE---CIGCAACIDAC 304
Cdd:COG2221   17 CIGCGLCVAVCPTGaISLDDGkLVIDeekCIGCGACIRVC 56
Fer4_9 pfam13187
4Fe-4S dicluster domain;
269-304 3.63e-08

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 49.47  E-value: 3.63e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 516456416  269 DCIDCTMCVQVCPTGIDIRDGLQIE---------CIGCAACIDAC 304
Cdd:pfam13187   1 KCTGCGACVAACPAGAIVPDLVGQTirgdiaglaCIGCGACVDAC 45
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 269-305 6.75e-08

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: 51.24  E-value: 6.75e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 516456416 269 DCIDCTMCVQVCPTG-IDIRDGLQIE-----CIGCAACIDACD 305
Cdd:cd10549   79 KCIGCGLCVKVCPVDaITLEDELEIVidkekCIGCGICAEVCP 121
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 270-304 1.28e-07

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 48.89  E-value: 1.28e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 516456416 270 CIDCTMCVQVCPTG-IDIRDGL----QIECIGCAACIDAC 304
Cdd:COG4231   24 CTGCGACVKVCPADaIEEGDGKavidPDLCIGCGSCVQVC 63
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 270-304 1.41e-07

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 48.20  E-value: 1.41e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 516456416 270 CIDCTMCVQVCPTG-IDIRDGLQIE--------CIGCAACIDAC 304
Cdd:COG1143    4 CIGCGLCVRVCPVDaITIEDGEPGKvyvidpdkCIGCGLCVEVC 47
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 270-304 1.46e-07

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 48.55  E-value: 1.46e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 516456416 270 CIDCTMCVQVCPTG-IDIRDG----LQI---ECIGCAACIDAC 304
Cdd:COG1146   10 CIGCGACVEVCPVDvLELDEEgkkaLVInpeECIGCGACELVC 52
NapF COG1145
Ferredoxin [Energy production and conversion];
270-304 2.75e-07

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 51.65  E-value: 2.75e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 516456416 270 CIDCTMCVQVCPTG-IDIRDG---LQI---ECIGCAACIDAC 304
Cdd:COG1145  184 CIGCGLCVKVCPTGaIRLKDGkpqIVVdpdKCIGCGACVKVC 225
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 270-304 3.02e-07

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 47.42  E-value: 3.02e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 516456416 270 CIDCTMCVQVCPTG-IDIRDGLQIE-----CIGCAACIDAC 304
Cdd:COG1149   13 CIGCGLCVEVCPEGaIKLDDGGAPVvdpdlCTGCGACVGVC 53
napH PRK09477
quinol dehydrogenase membrane component; Provisional
 79-305 4.45e-07

quinol dehydrogenase membrane component; Provisional


Pssm-ID: 236535 [Multi-domain]  Cd Length: 271  Bit Score: 51.05  E-value: 4.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416  79 IFGATFWPqDFILLSGILIVAAFGLFFitvyAGRIWCGYTCPQSVWT----WIfmwcekvtegdrnqRIKLdkapmGANK 154
Cdd:PRK09477  58 SLAAGHLP-ATVALIGALIITVFYALA----GGRAFCSWVCPVNLVTdlanWL--------------RRKL-----GLNQ 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416 155 FLrKFSKHT------LWLLIGFVTGMTFVGYFSPI----RELVFDFFTGqadGWSYFWVGFFTLATYGNaGWlreqvCIY 224
Cdd:PRK09477 114 SA-TLPRNLrywllvLVLVGSALTGTLAWEWINPVsmlhRGLVFGFGSG---WWLILAIFLFDLFVVEH-GW-----CGH 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416 225 MCPYARFQSVMFDKDTLIVsydprrgevrgprkkgadyKAQGLGDCIDCTMCVQVCP-------------TGIDIRDGlq 291
Cdd:PRK09477 184 LCPLGAFYGLIGKKSLIRV-------------------KAHDRQKCTRCMDCFHVCPepqvlrpplkgkqSPSQVTSG-- 242

                        250
                 ....*....|....
gi 516456416 292 iECIGCAACIDACD 305
Cdd:PRK09477 243 -DCITCGRCIDVCS 255
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 270-319 4.99e-07

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


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 50.76  E-value: 4.99e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 516456416 270 CIDCTMCVQVCPTG-IDI-RDGLQI----ECIGCAACIDACdnimdkmdyPRGLIS 319
Cdd:COG2878  139 CIGCGDCIKACPFDaIVGaAKGMHTvdedKCTGCGLCVEAC---------PVDCIE 185
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 270-333 1.98e-06

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 47.01  E-value: 1.98e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516456416 270 CIDCTMCVQVCPTG-IDIRDGLQIE---------CIGCAACIDACdnimdkmdyPRGLISYTTEHNLSGQKTHK 333
Cdd:cd10549    8 CIGCGICVKACPTDaIELGPNGAIArgpeidedkCVFCGACVEVC---------PTGAIELTPEGKEYVPKEKE 72
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 267-304 4.96e-06

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 45.85  E-value: 4.96e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 516456416 267 LGDCIDCTMCVQVCPTG-IDIRDGLQI-------------ECIGCAACIDAC 304
Cdd:cd10549   39 EDKCVFCGACVEVCPTGaIELTPEGKEyvpkekeaeideeKCIGCGLCVKVC 90
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 270-304 7.27e-06

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


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 44.27  E-value: 7.27e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 516456416 270 CIDCTMCVQVCPTG-IDIRDGLQIE-----CIGCAACIDAC 304
Cdd:COG1144   32 CIGCGLCWIVCPDGaIRVDDGKYYGidydyCKGCGICAEVC 72
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 270-304 9.30e-06

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: 42.90  E-value: 9.30e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 516456416  270 CIDCTMCVQVCPT------------GIDIRDGLQIECIGCAACIDAC 304
Cdd:pfam12838   1 CIGCGACVAACPVgaitldevgekkGTKTVVIDPERCVGCGACVAVC 47
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 270-304 1.02e-05

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


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 43.01  E-value: 1.02e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 516456416  270 CIDCTMCVQVCPTGIDIRDGLQI------------ECIGCAACIDAC 304
Cdd:pfam13237   9 CIGCGRCTAACPAGLTRVGAIVErlegeavrigvwKCIGCGACVEAC 55
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
270-304 1.62e-05

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 46.94  E-value: 1.62e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 516456416 270 CIDCTMCVQVCPTG-IDIRDGL----QIECIGCAACIDAC 304
Cdd:COG4624   93 CKNCYPCVRACPVKaIKVDDGKaeidEEKCISCGQCVAVC 132
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
270-323 2.10e-05

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 44.26  E-value: 2.10e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516456416 270 CIDCTMCVQVCPTG-IDIRD----GLQIECIGCA------ACIDACdnimdkmdyPRGLISYTTE 323
Cdd:COG1142   83 CIGCGLCVLACPFGaITMVGeksrAVAVKCDLCGgreggpACVEAC---------PTGALRLVDV 138
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 264-304 2.22e-05

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: 44.16  E-value: 2.22e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 516456416 264 AQGLGDCIDCTMCVQVCPTGI-----------DIRDGlqiECIGCAACIDAC 304
Cdd:cd10564    9 ALFLDLCTRCGDCVEACPEGIivrgdggfpelDFSRG---ECTFCGACAEAC 57
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 276-304 3.19e-05

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: 43.89  E-value: 3.19e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 516456416 276 CVQVCPTGIDIR---DGL----QIECIGCAACIDAC 304
Cdd:cd10553   66 CVKACPTGAMQKrekDGIvyvdQELCIGCKACIEAC 101
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 269-304 4.58e-05

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


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 43.63  E-value: 4.58e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 516456416  269 DCIDCTMCVQVCPTgiDIRDG--------LQIECIGCAACIDAC 304
Cdd:TIGR01944 114 NCIGCTKCIQACPV--DAIVGaakamhtvIADECTGCDLCVEPC 155
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 276-304 5.60e-05

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: 43.67  E-value: 5.60e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 516456416 276 CVQVCPTG-IDIR-DGL-QIE---CIGCAACIDAC 304
Cdd:cd10551   61 CVKVCPTGaTYKReDGIvLVDydkCIGCRYCMAAC 95
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
221-304 5.92e-05

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 44.92  E-value: 5.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416 221 VCIYMCPyarfQSVMfdkdTLIvsydPRRGEVRGP---RKKGADYKAQGLGDCIDCTMCVQVCPTG-IDIRDGL----QI 292
Cdd:PRK07118 175 ACVKACP----RNVI----ELI----PKSARVFVAcnsKDKGKAVKKVCEVGCIGCGKCVKACPAGaITMENNLavidQE 242

                         90
                 ....*....|..
gi 516456416 293 ECIGCAACIDAC 304
Cdd:PRK07118 243 KCTSCGKCVEKC 254
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 269-304 1.09e-04

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


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 43.69  E-value: 1.09e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 516456416 269 DCIDCTMCVQVCPTG-IDIRDGLQI---ECIGCAACIDAC 304
Cdd:NF038196 186 KCIGCGICAKVCPVNnIEMEDGKPVwghNCTHCLACIHRC 225
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 270-304 1.34e-04

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


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 41.79  E-value: 1.34e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 516456416 270 CIDCT--MCVQVCPTG---IDIRDGLQI----ECIGCAACIDAC 304
Cdd:cd10550   49 CRQCEdaPCVEACPVGaisRDEETGAVVvdedKCIGCGMCVEAC 92
Fer4_21 pfam14697
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 269-304 1.85e-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: 434137 [Multi-domain]  Cd Length: 59  Bit Score: 39.19  E-value: 1.85e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 516456416  269 DCIDCTMCVQVCP-TGID--IRDGLQI------ECIGCAACIDAC 304
Cdd:pfam14697   7 TCIGCGKCYIACPdTSHQaiVGDGKRHhtviedECTGCNLCVSVC 51
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 222-284 2.10e-04

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 39.05  E-value: 2.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516456416  222 CIYMCPYarfQSVMFDKDTlivsydprrgevrgpRKKGADYKAQGLGDCIDCTMCVQVCPTGI 284
Cdd:pfam12838   7 CVAACPV---GAITLDEVG---------------EKKGTKTVVIDPERCVGCGACVAVCPTGA 51
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
276-323 2.94e-04

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 40.80  E-value: 2.94e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 516456416 276 CVQVCPTG-IDIRDGL-QIE---CIGCAACIDACdnimdkmdyPRGLISYTTE 323
Cdd:COG1142   60 CAEVCPVGaITRDDGAvVVDeekCIGCGLCVLAC---------PFGAITMVGE 103
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 269-304 3.34e-04

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


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 40.40  E-value: 3.34e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 516456416 269 DCIDCTMCVQVCPTGIDIRDGLQIE---CIGCAACIDAC 304
Cdd:cd16372   78 LCVGCLMCVGFCPEGAMFKHEDYPEpfkCIACGICVKAC 116
PRK08764 PRK08764
Rnf electron transport complex subunit RnfB;
243-304 4.87e-04

Rnf electron transport complex subunit RnfB;


Pssm-ID: 181550 [Multi-domain]  Cd Length: 135  Bit Score: 40.29  E-value: 4.87e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516456416 243 VSYDPRRGEVRGPRkkgADYKAQGlgDCIDCTMCVQVCPTGIDIRDGLQIE------CIGCAACIDAC 304
Cdd:PRK08764  65 RPYDRSRGTHKLPQ---VAWIVEA--DCIGCTKCIQACPVDAIVGGAKHMHtviaplCTGCELCVPAC 127
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 269-293 6.80e-04

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 38.15  E-value: 6.80e-04
                         10        20
                 ....*....|....*....|....*.
gi 516456416 269 DCIDCTMCVQVCPTG-IDIRDGLQIE 293
Cdd:COG1146   41 ECIGCGACELVCPVGaITVEDDEPEE 66
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
258-318 7.46e-04

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 41.46  E-value: 7.46e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516456416 258 KGADYKAQGLGDCidctmcVQVCPTG-IDIRDGLQI----ECIGCAACIDACdnimdkmdyPRGLI 318
Cdd:PRK07118 135 KGCSYGCLGLGSC------VAACPFDaIHIENGLPVvdedKCTGCGACVKAC---------PRNVI 185
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 270-304 8.72e-04

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 39.05  E-value: 8.72e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 516456416 270 CIDCTMCVQVCPTGI--DIRDGLQI-----ECIGCAACIDAC 304
Cdd:PRK08348  44 CVGCRMCVTVCPAGVfvYLPEIRKValwtgRCVFCGQCVDVC 85
PRK13795 PRK13795
hypothetical protein; Provisional
 270-304 1.01e-03

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 41.52  E-value: 1.01e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 516456416 270 CIDCTMCVQVCPTG-IDIRDGLQI------ECIGCAACIDAC 304
Cdd:PRK13795 583 CVGCGVCVGACPTGaIRIEEGKRKisvdeeKCIHCGKCTEVC 624
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 276-304 1.06e-03

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 39.93  E-value: 1.06e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 516456416 276 CVQVCPTG-IDIR-DGL-QIE---CIGCAACIDAC 304
Cdd:COG0437   68 CVKVCPTGaTYKReDGIvLVDydkCIGCRYCVAAC 102
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 271-304 1.26e-03

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 39.16  E-value: 1.26e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 516456416 271 IDCTMCVQVCPTG---IDIRDGLQI------ECIGCAACIDAC 304
Cdd:cd16373  100 TDCGVCVEACPTEaiaIVLEDDVLRpvvdedKCVGCGLCEYVC 142
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 276-304 1.37e-03

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: 39.17  E-value: 1.37e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 516456416 276 CVQVCPTG-IDIRDG-LQIE---CIGCAACIDAC 304
Cdd:cd10554   64 CANVCPVGaISQEDGvVQVDeerCIGCKLCVLAC 97
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
266-304 1.46e-03

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 39.48  E-value: 1.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 516456416 266 GLGDCIDCTMCVQVCP------TGIDIRDG------LQIE---CIGCAACIDAC 304
Cdd:PRK05888  56 GEERCIACKLCAAICPadaitiEAAEREDGrrrttrYDINfgrCIFCGFCEEAC 109
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 270-304 2.62e-03

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: 38.14  E-value: 2.62e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 516456416 270 CIDCT--MCVQVCPTG--IDIRDGLQI----ECIGCAACIDAC 304
Cdd:cd04410   50 CMHCEdpPCVKACPTGaiYKDEDGIVLidedKCIGCGSCVEAC 92
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 276-304 3.42e-03

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 39.73  E-value: 3.42e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 516456416 276 CVQVCPTG--IDIRDGLQI---ECIGCAACIDAC 304
Cdd:PRK12769  64 CARSCPNGaiSHVDDSIQVnqqKCIGCKSCVVAC 97
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 276-304 3.88e-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: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 37.64  E-value: 3.88e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 516456416 276 CVQVCPTG---IDIRDGLQIE---CIGCAACIDAC 304
Cdd:cd16374   51 CMEVCPTGaiyRDEDGAVLVDpdkCIGCGMCAMAC 85
ndhI CHL00014
NADH dehydrogenase subunit I
 270-334 4.08e-03

NADH dehydrogenase subunit I


Pssm-ID: 214334 [Multi-domain]  Cd Length: 167  Bit Score: 38.20  E-value: 4.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416 270 CIDCTMCVQVCPTGIDIRD-GLQIE---------------CIGCAACIDACdnimdkmdyPRGLISYTTEHNLSGQKTHK 333
Cdd:CHL00014  61 CIACEVCVRVCPIDLPVVDwKLETDirkkrllnysidfgvCIFCGNCVEYC---------PTNCLSMTEEYELSTYDRHE 131


                 .
gi 516456416 334 L 334
Cdd:CHL00014 132 L 132
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 267-283 4.96e-03

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 35.49  E-value: 4.96e-03
                         10
                 ....*....|....*..
gi 516456416 267 LGDCIDCTMCVQVCPTG 283
Cdd:COG1143   34 PDKCIGCGLCVEVCPTG 50
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 222-306 5.21e-03

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: 37.24  E-value: 5.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416 222 CIYMCPYARFQsvmFDKDTLIVSYDPRRgevrgprkkgadykaqglgdCIDCTMCVQVCPTGIDIRDGLQ---IECIGCA 298
Cdd:cd10563   65 CVKACMSGAMH---KDPETGIVIHDEEK--------------------CVGCWMCVMVCPYGAIRPDKERkvaLKCDLCP 121

                         90
                 ....*....|...
gi 516456416 299 -----ACIDACDN 306
Cdd:cd10563  122 dretpACVEACPT 134
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 270-304 6.37e-03

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


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 36.87  E-value: 6.37e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 516456416 270 CIDCTMCVQVCPTG---IDIRDGLQIECIGCA---------ACIDAC 304
Cdd:cd16374   75 CIGCGMCAMACPFGvprFDPSLKVAVKCDLCIdrrregklpACVEAC 121
psaC CHL00065
photosystem I subunit VII
 270-304 6.39e-03

photosystem I subunit VII


Pssm-ID: 177005 [Multi-domain]  Cd Length: 81  Bit Score: 35.51  E-value: 6.39e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 516456416 270 CIDCTMCVQVCPTGI------DIRDGLQI-------ECIGCAACIDAC 304
Cdd:CHL00065  11 CIGCTQCVRACPTDVlemipwDGCKAKQIasaprteDCVGCKRCESAC 58
PLN00071 PLN00071
photosystem I subunit VII; Provisional
 268-304 6.58e-03

photosystem I subunit VII; Provisional


Pssm-ID: 177700 [Multi-domain]  Cd Length: 81  Bit Score: 35.69  E-value: 6.58e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 516456416 268 GDCIDCTMCVQVCPTGI------DIRDGLQI-------ECIGCAACIDAC 304
Cdd:PLN00071   9 DTCIGCTQCVRACPTDVlemipwDGCKAKQIasaprteDCVGCKRCESAC 58
ACS_1 cd01916
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
 248-315 6.81e-03

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: 38.93  E-value: 6.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456416 248 RRGEVRGPRKKGADYK--AQGLGDCIDCTMCVQVCPTGIDIRDG--------------LQIECIGCAACIDACD------ 305
Cdd:cd01916  343 AVKPKRKGEKKLPTDEefQELAAKCTDCGWCTRACPNSLRIKEAmeaakegdfsgladLFDQCVGCGRCEQECPkeipii 422

                         90
                 ....*....|
gi 516456416 306 NIMDKMDYPR 315
Cdd:cd01916  423 NMIEKAARER 432
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
270-304 7.89e-03

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 38.69  E-value: 7.89e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 516456416 270 CIDCTMCVQVCPTG-IDIRDGLQIE-----CIGCAACIDAC 304
Cdd:COG1148  498 CTGCGRCVEVCPYGaISIDEKGVAEvnpalCKGCGTCAAAC 538
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 270-307 7.94e-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: 319889 [Multi-domain]  Cd Length: 138  Bit Score: 36.90  E-value: 7.94e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 516456416 270 CIDCT--MCVQVCPTGIDIRDG---LQIE--CIGCAACIDAC--DNI 307
Cdd:cd16367   57 CRHCVdpVCMIGCPTGAIHRDDggeVVISdaCCGCGNCASACpyGAI 103
Fer4_5 pfam12801
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 96-121 8.67e-03

4Fe-4S binding 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.


Pssm-ID: 432796 [Multi-domain]  Cd Length: 48  Bit Score: 34.46  E-value: 8.67e-03
                          10        20
                  ....*....|....*....|....*.
gi 516456416   96 LIVAAFGLFFITVYAGRIWCGYTCPQ 121
Cdd:pfam12801   5 GLILFLAVLVLTLLFGRVFCGWLCPF 30
PRK09898 PRK09898
ferredoxin-like protein;
270-304 9.08e-03

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 37.51  E-value: 9.08e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 516456416 270 CIDCTMCVQVCPTG---IDIRDGLQIECIGCAACIDAC 304
Cdd:PRK09898 156 CIGCSACTTACPWMmatVNTESKKSSKCVLCGECANAC 193
 
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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