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Conserved domains on  [gi|835524450|ref|WP_047537960|]
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MULTISPECIES: 4Fe-4S dicluster domain-containing protein [Shewanella]

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 ...
 4-226 3.93e-109

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: 312.87  E-value: 3.93e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450    4 SKRRFLKGACALLAgASGSTLLATVNASNEAKaEPSVKYALIHDETKCIGCRACEVACRETNQVPEGVARLKIEQTGPYG 83
Cdd:TIGR03149   3 SRRNFLAGVGALIL-TTGTAGTSVVSLAKEDK-DKTKRYGMVHDETACIGCTACMDACREVNKVPEGVSRLEIIRSEPYG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450   84 EYPNQFYHFSRKSCQHCEDAPCVNVCPTGAAFIDKETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCRET 163
Cdd:TIGR03149  81 EFPDVEYRFFRKSCQHCDNAPCVAVCPTGASFKDEETGIVDVHKDLCVGCQYCIAACPYRVRFIHPVTKSADKCNFCRDT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 835524450  164 NLAQGKQPACVAACPTKALVFGNLKDPTSQVVQVLKANPTQRAKVDLGTRPKLFRIVAKSGEV 226
Cdd:TIGR03149 161 NLAEGKLPACVESCPTKALTFGDLNDPNSEVSQKLKQKPVYRTKVELGTKPKLYKIPFKKGEV 223
 
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 ...
 4-226 3.93e-109

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: 312.87  E-value: 3.93e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450    4 SKRRFLKGACALLAgASGSTLLATVNASNEAKaEPSVKYALIHDETKCIGCRACEVACRETNQVPEGVARLKIEQTGPYG 83
Cdd:TIGR03149   3 SRRNFLAGVGALIL-TTGTAGTSVVSLAKEDK-DKTKRYGMVHDETACIGCTACMDACREVNKVPEGVSRLEIIRSEPYG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450   84 EYPNQFYHFSRKSCQHCEDAPCVNVCPTGAAFIDKETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCRET 163
Cdd:TIGR03149  81 EFPDVEYRFFRKSCQHCDNAPCVAVCPTGASFKDEETGIVDVHKDLCVGCQYCIAACPYRVRFIHPVTKSADKCNFCRDT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 835524450  164 NLAQGKQPACVAACPTKALVFGNLKDPTSQVVQVLKANPTQRAKVDLGTRPKLFRIVAKSGEV 226
Cdd:TIGR03149 161 NLAEGKLPACVESCPTKALTFGDLNDPNSEVSQKLKQKPVYRTKVELGTKPKLYKIPFKKGEV 223
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 44-219 5.27e-77

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: 229.73  E-value: 5.27e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  44 LIHDETKCIGCRACEVACRETNQVPEGVARLKIEQTGPyGEYPNQFYHFSRKSCQHCEDAPCVNVCPTGAAFIDkETGIV 123
Cdd:cd10551    1 MVIDLRKCIGCGACVVACKAENNVPPGVFRNRVLEYEV-GEYPNVKRTFLPVLCNHCENPPCVKVCPTGATYKR-EDGIV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450 124 AVDAWKCVGCQYCIAACPYKIRFINPV------------THAADKCDFCRETnLAQGKQPACVAACPTKALVFGNLKDPT 191
Cdd:cd10551   79 LVDYDKCIGCRYCMAACPYGARYFNPEephefgevpvrpKGVVEKCTFCYHR-LDEGLLPACVEACPTGARIFGDLDDPN 157

                        170       180
                 ....*....|....*....|....*...
gi 835524450 192 SQVVQVLKANPTQRAKVDLGTRPKLFRI 219
Cdd:cd10551  158 SEVSKLLAERRAYVLKPELGTKPKVYYI 185
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 37-222 4.46e-75

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 224.83  E-value: 4.46e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  37 EPSVKYALIHDETKCIGCRACEVACRETNQVPEGVARLKIEQTgPYGEYPNQFYHFSRKSCQHCEDAPCVNVCPTGAAFI 116
Cdd:COG0437    1 LSMKRYGMVIDLTKCIGCRACVVACKEENNLPVGVTWRRVRRY-EEGEFPNVEWLFVPVLCNHCDDPPCVKVCPTGATYK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450 117 DkETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCREtNLAQGKQPACVAACPTKALVFGNLKDPTSQVVQ 196
Cdd:COG0437   80 R-EDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCAD-RLDEGLLPACVEACPTGALVFGDLDDPESEVSK 157

                        170       180
                 ....*....|....*....|....*.
gi 835524450 197 VLKANPTQRAKVDLGTRPKLFRIVAK 222
Cdd:COG0437  158 RLAELPAYRLLPELGTKPSVYYLPKR 183
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
1-217 6.89e-45

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 150.02  E-value: 6.89e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450   1 MENSKRRFLKGACALLAGASGSTLLATVNASNEAKAEPSVK--YALIHDETKCIGCRACEVACRETNQVPEGVARLKIEQ 78
Cdd:PRK14993   1 MDSSKRQFLQQLGVLTAGASLVPLAEAKFPFSPERHEGSPRhrYAMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  79 TGPYGEYPNQFYH-FSRKSCQHCEDAPCVNVCPTGAAFiDKETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKC 157
Cdd:PRK14993  81 YQVQREGSQEVTNvLLPRLCNHCDNPPCVPVCPVQATF-QREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKC 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 835524450 158 DFCREtNLAQGKQPACVAACPTKALVFGNLKDPTSQVVQVLKANPTQRA--KVDLGTRPKLF 217
Cdd:PRK14993 160 TFCVH-RLEAGLLPACVESCVGGARIIGDIKDPHSRIATMLHQHRDAIKvlKPENGTSPHVF 220
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 89-187 9.25e-27

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


Pssm-ID: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 98.86  E-value: 9.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450   89 FYHFSRKsCQHCEDAPCVNVCPTGAAFIDKETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCREtNLAQG 168
Cdd:pfam13247   3 WLFFPEQ-CRHCLNPPCKASCPVGAIYKDEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYD-RVEAG 80

                          90
                  ....*....|....*....
gi 835524450  169 KQPACVAACPTKALVFGNL 187
Cdd:pfam13247  81 LLPACVQTCPTGAMNFGDR 99
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 129-186 1.79e-03

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: 38.30  E-value: 1.79e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 835524450 129 KCVGCQYCIAACPYK-IRFIN--PVTHaaDKCDFCRetnlaqgkqpACVAACPTKALVFGN 186
Cdd:NF038196 186 KCIGCGICAKVCPVNnIEMEDgkPVWG--HNCTHCL----------ACIHRCPKEAIEYGK 234
 
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 ...
 4-226 3.93e-109

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: 312.87  E-value: 3.93e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450    4 SKRRFLKGACALLAgASGSTLLATVNASNEAKaEPSVKYALIHDETKCIGCRACEVACRETNQVPEGVARLKIEQTGPYG 83
Cdd:TIGR03149   3 SRRNFLAGVGALIL-TTGTAGTSVVSLAKEDK-DKTKRYGMVHDETACIGCTACMDACREVNKVPEGVSRLEIIRSEPYG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450   84 EYPNQFYHFSRKSCQHCEDAPCVNVCPTGAAFIDKETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCRET 163
Cdd:TIGR03149  81 EFPDVEYRFFRKSCQHCDNAPCVAVCPTGASFKDEETGIVDVHKDLCVGCQYCIAACPYRVRFIHPVTKSADKCNFCRDT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 835524450  164 NLAQGKQPACVAACPTKALVFGNLKDPTSQVVQVLKANPTQRAKVDLGTRPKLFRIVAKSGEV 226
Cdd:TIGR03149 161 NLAEGKLPACVESCPTKALTFGDLNDPNSEVSQKLKQKPVYRTKVELGTKPKLYKIPFKKGEV 223
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 44-219 5.27e-77

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: 229.73  E-value: 5.27e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  44 LIHDETKCIGCRACEVACRETNQVPEGVARLKIEQTGPyGEYPNQFYHFSRKSCQHCEDAPCVNVCPTGAAFIDkETGIV 123
Cdd:cd10551    1 MVIDLRKCIGCGACVVACKAENNVPPGVFRNRVLEYEV-GEYPNVKRTFLPVLCNHCENPPCVKVCPTGATYKR-EDGIV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450 124 AVDAWKCVGCQYCIAACPYKIRFINPV------------THAADKCDFCRETnLAQGKQPACVAACPTKALVFGNLKDPT 191
Cdd:cd10551   79 LVDYDKCIGCRYCMAACPYGARYFNPEephefgevpvrpKGVVEKCTFCYHR-LDEGLLPACVEACPTGARIFGDLDDPN 157

                        170       180
                 ....*....|....*....|....*...
gi 835524450 192 SQVVQVLKANPTQRAKVDLGTRPKLFRI 219
Cdd:cd10551  158 SEVSKLLAERRAYVLKPELGTKPKVYYI 185
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 37-222 4.46e-75

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 224.83  E-value: 4.46e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  37 EPSVKYALIHDETKCIGCRACEVACRETNQVPEGVARLKIEQTgPYGEYPNQFYHFSRKSCQHCEDAPCVNVCPTGAAFI 116
Cdd:COG0437    1 LSMKRYGMVIDLTKCIGCRACVVACKEENNLPVGVTWRRVRRY-EEGEFPNVEWLFVPVLCNHCDDPPCVKVCPTGATYK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450 117 DkETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCREtNLAQGKQPACVAACPTKALVFGNLKDPTSQVVQ 196
Cdd:COG0437   80 R-EDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCAD-RLDEGLLPACVEACPTGALVFGDLDDPESEVSK 157

                        170       180
                 ....*....|....*....|....*.
gi 835524450 197 VLKANPTQRAKVDLGTRPKLFRIVAK 222
Cdd:COG0437  158 RLAELPAYRLLPELGTKPSVYYLPKR 183
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 45-185 5.14e-52

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: 164.66  E-value: 5.14e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  45 IHDETKCIGCRACEVACRETNQVPEGVARLKIEQTGPyGEYPNQF-YHFSrKSCQHCEDAPCVNVCPTGAAFIDkETGIV 123
Cdd:cd16371    3 YFDQERCIGCKACEIACKDKNDLPPGVNWRRVYEYEG-GEFPEVFaYFLS-MSCNHCENPACVKVCPTGAITKR-EDGIV 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 835524450 124 AVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCREtNLAQGKQPACVAACPTKALVFG 185
Cdd:cd16371   80 VVDQDKCIGCGYCVWACPYGAPQYNPETGKMDKCDMCVD-RLDEGEKPACVAACPTRALDFG 140
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 44-185 6.53e-45

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: 146.77  E-value: 6.53e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  44 LIHDETKCIGCRACEVACRETNQVPEGVARLKIeqtgPYGEYPNQFYHFSRKSCQHCEDAPCVNVCPTGAAFIDkETGIV 123
Cdd:cd04410    1 LVVDLDRCIGCGTCEVACKQEHGLRPGPDWSRI----KVIEGGGLERAFLPVSCMHCEDPPCVKACPTGAIYKD-EDGIV 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 835524450 124 AVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCREtNLAQGKQPACVAACPTKALVFG 185
Cdd:cd04410   76 LIDEDKCIGCGSCVEACPYGAIVFDPEPGKAVKCDLCGD-RLDEGLEPACVKACPTGALTFG 136
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
1-217 6.89e-45

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 150.02  E-value: 6.89e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450   1 MENSKRRFLKGACALLAGASGSTLLATVNASNEAKAEPSVK--YALIHDETKCIGCRACEVACRETNQVPEGVARLKIEQ 78
Cdd:PRK14993   1 MDSSKRQFLQQLGVLTAGASLVPLAEAKFPFSPERHEGSPRhrYAMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  79 TGPYGEYPNQFYH-FSRKSCQHCEDAPCVNVCPTGAAFiDKETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKC 157
Cdd:PRK14993  81 YQVQREGSQEVTNvLLPRLCNHCDNPPCVPVCPVQATF-QREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKC 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 835524450 158 DFCREtNLAQGKQPACVAACPTKALVFGNLKDPTSQVVQVLKANPTQRA--KVDLGTRPKLF 217
Cdd:PRK14993 160 TFCVH-RLEAGLLPACVESCVGGARIIGDIKDPHSRIATMLHQHRDAIKvlKPENGTSPHVF 220
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 43-185 1.14e-43

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: 145.43  E-value: 1.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  43 ALIHDETKCIGCRACEVACRETNQVPEGVARLKIEQTGPYG--------------EYPNQFYHFSRKSCQHCEDAPCVNV 108
Cdd:cd10561    1 GVLYDTTRCIGCRACEVACKEWNGLPAEDTAFGPGWDNPRDlsaktytvikryevETGGKGFVFVKRQCMHCLDPACVSA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450 109 CPTGAafIDK-ETGIVAVDAWKCVGCQYCIAACPYKI-RF----INPVTHaadKCDFCRETnLAQGKQPACVAACPTKAL 182
Cdd:cd10561   81 CPVGA--LRKtPEGPVTYDEDKCIGCRYCMVACPFNIpKYewdsANPKIR---KCTMCYDR-LKEGKQPACVEACPTGAL 154


                 ...
gi 835524450 183 VFG 185
Cdd:cd10561  155 LFG 157
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 41-185 1.85e-41

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: 138.27  E-value: 1.85e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  41 KYALIHDETKCIGCRACEVACRETNQVPEGVARLKIEQTGP--YGEYPNQFYHFsrKSCQHCEDAPCVNVCPTGAAFIDK 118
Cdd:cd10553    2 KYYLYHDSKRCIGCLACEVHCKVKNNLPVGPRLCRIFAVGPkmVGGKPRLKFVY--MSCFHCENPWCVKACPTGAMQKRE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 835524450 119 ETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCREtNLAQGKQPACVAACPTKALVFG 185
Cdd:cd10553   80 KDGIVYVDQELCIGCKACIEACPWGIPQWNPATGKVVKCDYCMD-RIDQGLKPACVTGCTTHALSFV 145
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 46-186 6.54e-41

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: 137.05  E-value: 6.54e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  46 HDETKCIGCRACEVACRETNQVPEgvarLKIEQTGPYGEYPN---------QFYH-----------FSRKSCQHCEDAPC 105
Cdd:cd10562    3 VDTSKCTACRGCQVACKQWNQLPA----EKTPFTGSYQNPPDltpntwtliRFYEheednggirwlFRKRQCMHCTDAAC 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450 106 VNVCPTGAAFIDkETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCREtNLAQGKQPACVAACPTKALVFG 185
Cdd:cd10562   79 VKVCPTGALYKT-ENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCFD-RIENGMQPACVKTCPTGALTFG 156


                 .
gi 835524450 186 N 186
Cdd:cd10562  157 D 157
DMSO_dmsB TIGR02951
DMSO reductase, iron-sulfur subunit; This family consists of the iron-sulfur subunit, or chain ...
 41-187 9.90e-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: 136.79  E-value: 9.90e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450   41 KYALIHDETKCIGCRACEVACRETNQVPEGVA-RLKIEQTG----PYGEYPNQ---FYHFSrKSCQHCEDAPCVNVCPTG 112
Cdd:TIGR02951   1 QYGFYVDQTRCSGCKTCQIACKDKNDLEVGVLfRRVYEYEGggwtEEGEGFHPdvfAYYIS-ISCNHCADPACVKNCPTG 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 835524450  113 AAFIDKETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCRETnLAQGKQPACVAACPTKALVFGNL 187
Cdd:TIGR02951  80 AMYKREEDGLVLVDQDKCIGCRYCVWACPYGAPQYDPQQGVMGKCDGCYDR-VEKGLRPACVDACPMRALDFGPI 153
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 43-200 2.38e-40

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: 137.13  E-value: 2.38e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  43 ALIHDETKCIGCRACEVACRETNQVPEGVARLKIEQTGPYGEYPNQF---------------YHFSRKSCQHCEDAPCVN 107
Cdd:cd10558    1 AKLIDVSKCIGCKACQVACKEWNDLRAEVGHNVGTYQNPADLSPETWtlmkfrevedngkleWLIRKDGCMHCADPGCLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450 108 VCPTGAAFIDKETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCrETNLAQGKQPACVAACPTKALVFGNL 187
Cdd:cd10558   81 ACPSPGAIVQYANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLC-SDRVSVGLEPACVKTCPTGALHFGTK 159

                        170
                 ....*....|....*.
gi 835524450 188 KDPTS---QVVQVLKA 200
Cdd:cd10558  160 EDMLAlaeKRVAALKE 175
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
4-189 2.95e-40

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 140.57  E-value: 2.95e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450   4 SKRRFLKGACAllAGASGSTLLATVNASNEAKAEPSVKYALIHDETKCIGCRACEVACRETNQ---VPEG---------- 70
Cdd:PRK10882   2 NRRNFLKAASA--GALLAGALPSVSHAAAENRPPIPGALGMLYDSTLCVGCQACVTKCQEINFperNPQGeqtwdnpdkl 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  71 ------VARLKIEQTGPYGEYPNQFYHFSRKSCQHCEDAPCVNVCPTGAAFIDKETGIVAVDAWKCVGCQYCIAACPY-- 142
Cdd:PRK10882  80 spytnnIIKVWKSGTGVNKDQEENGYAYIKKQCMHCVDPNCVSVCPVSALTKDPKTGIVHYDKDVCTGCRYCMVACPFnv 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 835524450 143 -KIRFINPvTHAADKCDFCRETNL---AQGKQPACVAACPTKALVFGNLKD 189
Cdd:PRK10882 160 pKYDYNNP-FGAIHKCELCNQKGVerlDKGGLPGCVEVCPTGAVIFGTREE 209
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 47-185 7.24e-40

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: 134.45  E-value: 7.24e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  47 DETKCIGCRACEVACRETNQVPEGvarlKIEQTGPYGEYPN---------QFY-----------HFSRKSCQHCEDAPCV 106
Cdd:cd16366    4 DTSRCTGCRACQVACKQWNGLPAE----KTEFTGSYQNPPDltahtwtlvRFYevekpggdlswLFRKDQCMHCTDAGCL 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 835524450 107 NVCPTGAAFIDkETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCREtNLAQGKQPACVAACPTKALVFG 185
Cdd:cd16366   80 AACPTGAIIRT-ETGTVVVDPETCIGCGYCVNACPFDIPRFDEETGRVAKCTLCYD-RISNGLQPACVKTCPTGALTFG 156
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 47-185 1.21e-37

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: 128.14  E-value: 1.21e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  47 DETKCIGCRACEVACRE-----------TNQVPEGVARLKIEQTGPYgEYPNQfyhfsrksCQHCEDAPCVNVCPTGAAF 115
Cdd:cd10563    5 DEEKCLGCKLCEVACAVahskskdlikaKLEKERPRPRIRVEESGGR-SFPLQ--------CRHCDEPPCVKACMSGAMH 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450 116 IDKETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCRETnlaqgKQPACVAACPTKALVFG 185
Cdd:cd10563   76 KDPETGIVIHDEEKCVGCWMCVMVCPYGAIRPDKERKVALKCDLCPDR-----ETPACVEACPTGALVLE 140
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 44-184 1.37e-37

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: 127.69  E-value: 1.37e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  44 LIHDETKCIGCRACEVACRETNqvpEGV-----ARLKIEQTGPYGEY-PNQfyhfsrksCQHCEDAPCVNVCPTGAAFID 117
Cdd:cd10550    1 LVVDPEKCTGCRTCELACSLKH---EGVfnpslSRIRVVRFEPEGLDvPVV--------CRQCEDAPCVEACPVGAISRD 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 835524450 118 KETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCretnlaqGKQPACVAACPTKALVF 184
Cdd:cd10550   70 EETGAVVVDEDKCIGCGMCVEACPFGAIRVDPETGKAIKCDLC-------GGDPACVKVCPTGALEF 129
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 50-189 2.30e-37

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: 127.39  E-value: 2.30e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  50 KCIGCRACEVACRETNqvpEGVARLKIEQTGPYGEYPNQfyhfsrksCQHCEDAPCVNVCPTGAAFIDkETGIVAVDAWK 129
Cdd:cd16374    7 RCIGCRACEIACAREH---SGKPRISVEVVEDLASVPVR--------CRHCEDAPCMEVCPTGAIYRD-EDGAVLVDPDK 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450 130 CVGCQYCIAACPYKIRFINPVTHAADKCDFCREtNLAQGKQPACVAACPTKALVFGNLKD 189
Cdd:cd16374   75 CIGCGMCAMACPFGVPRFDPSLKVAVKCDLCID-RRREGKLPACVEACPTGALKFGDIEE 133
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 47-189 7.92e-37

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: 128.66  E-value: 7.92e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  47 DETKCIGCRACEVACRETNQVPEGVARLK--------------------IEQTGPYGEYPNQF---YHFSRKSCQHCEDA 103
Cdd:cd10560    5 DTSICIGCKACEVACKQWNQLPADGYDFSgmsydntgdlsastwrhvkfIERPTEDGPANEGGdlqWLFMSDVCKHCTDA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450 104 PCVNVCPTGAaFIDKETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCREtNLAQGKQPACVAACPTKALV 183
Cdd:cd10560   85 GCLEACPTGA-IFRTEFGTVYIQPDICNGCGYCVAACPFGVIDRNEETGRAHKCTLCYD-RLKDGLEPACAKACPTGSIQ 162


                 ....*.
gi 835524450 184 FGNLKD 189
Cdd:cd10560  163 FGPLEE 168
FDH-beta TIGR01582
formate dehydrogenase, beta subunit, Fe-S containing; This model represents the beta subunit ...
 26-200 3.93e-32

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: 118.09  E-value: 3.93e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450   26 ATVNASNEAKAEPsVKYALIHDETKCIGCRACEVACRETNQVPEGVARLKIE--QTGP-------------YGEYPNQFY 90
Cdd:TIGR01582   7 ATKEPDPSVKTYP-TELAKLIDVSSCIGCKACQAACQEWNDTTPPILSRKVGgyQNPPdllpetftlmrfkEGEESDGLE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450   91 HFSRK-SCQHCEDAPCVNVCPTGAAFIDKETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCREtNLAQGK 169
Cdd:TIGR01582  86 WLIRKdGCMHCREPGCLKACPAPGAIIQYQNGIVDFDHSKCIGCGYCIVGCPFNIPRYDKVDNRPYKCTLCID-RVSVGQ 164

                         170       180       190
                  ....*....|....*....|....*....|....
gi 835524450  170 QPACVAACPTKALVFG---NLKDPTSQVVQVLKA 200
Cdd:TIGR01582 165 EPACVKTCPTNAISFGfkeDMKERAEKRVADLKS 198
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 83-219 5.24e-31

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: 115.86  E-value: 5.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  83 GEYPNQFYHFSRKSCQHCEDAPCVNVCPTGAAFIDKETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFC-- 160
Cdd:cd10555  119 GEYPNSYYFYLPRICNHCTNPACLAACPRKAIYKREEDGIVLVDQDRCRGYRYCVEACPYKKIYFNPVEQKSEKCIFCyp 198

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 835524450 161 RetnLAQGKQPACVAACPTKALVFGNLKDPTSQVVQVLKanptqRAKVDL------GTRPKLFRI 219
Cdd:cd10555  199 R---IEKGVAPACARQCVGRIRFVGYLDDEESPVYKLVK-----KWKVALplhpeyGTEPNVFYV 255
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
41-184 1.84e-30

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 109.75  E-value: 1.84e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  41 KYALIHDETKCIGCRACEVACRETNQVPEG---VARLKIEQTGPYgEYPNQfyhfsrksCQHCEDAPCVNVCPTGAafID 117
Cdd:COG1142    2 NKFIIADPEKCIGCRTCEAACAVAHEGEEGepfLPRIRVVRKAGV-SAPVQ--------CRHCEDAPCAEVCPVGA--IT 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 835524450 118 KETGIVAVDAWKCVGCQYCIAACPYKIRFIN--PVTHAADKCDFCREtnlaQGKQPACVAACPTKALVF 184
Cdd:COG1142   71 RDDGAVVVDEEKCIGCGLCVLACPFGAITMVgeKSRAVAVKCDLCGG----REGGPACVEACPTGALRL 135
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 47-182 1.60e-29

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: 107.35  E-value: 1.60e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  47 DETKCIGCRACEVAC----RETNQVPEG------VARLKIEQTGPyGEYPNQfyhfsrksCQHCEDAPCVNVCPTGAafI 116
Cdd:cd10554    5 DPDKCIGCRTCEVACaaahSGKGIFEAGtdglpfLPRLRVVKTGE-VTAPVQ--------CRQCEDAPCANVCPVGA--I 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 835524450 117 DKETGIVAVDAWKCVGCQYCIAACPY-----------KIRFINPVTHAADKCDFCRETNlaqgKQPACVAACPTKAL 182
Cdd:cd10554   74 SQEDGVVQVDEERCIGCKLCVLACPFgaiemapttvpGVDWERGPRAVAVKCDLCAGRE----GGPACVEACPTKAL 146
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 44-217 9.67e-28

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: 103.94  E-value: 9.67e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  44 LIHDETKCIGCRACEVACRETN-----------QVPEGVARLKIEQTgPYGEYPNQFYHFSRKSCQHCEDAPCVNVCPTG 112
Cdd:cd10552    1 LVIDVAKCNGCYNCFLACKDEHvgndwpgyaapQPRHGHFWMRILRR-ERGQYPKVDVAYLPVPCNHCDNAPCIKAAKDG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450 113 AafIDK-ETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCRETnLAQG-KQPACVAACPTKALVFGNLKDP 190
Cdd:cd10552   80 A--VYKrDDGIVIIDPEKAKGQKQLVDACPYGAIYWNEELQVPQKCTFCAHL-LDDGwKEPRCVQACPTGALRFGKLEDE 156

                        170       180
                 ....*....|....*....|....*..
gi 835524450 191 TSQvvQVLKANPTQRAKVDLGTRPKLF 217
Cdd:cd10552  157 EMA--AKAAEEGLEVLHPELGTKPRVY 181
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 89-187 9.25e-27

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


Pssm-ID: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 98.86  E-value: 9.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450   89 FYHFSRKsCQHCEDAPCVNVCPTGAAFIDKETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCREtNLAQG 168
Cdd:pfam13247   3 WLFFPEQ-CRHCLNPPCKASCPVGAIYKDEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYD-RVEAG 80

                          90
                  ....*....|....*....
gi 835524450  169 KQPACVAACPTKALVFGNL 187
Cdd:pfam13247  81 LLPACVQTCPTGAMNFGDR 99
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 41-199 9.77e-27

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: 101.89  E-value: 9.77e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  41 KYALIHDETKCIGCRACEVACRETNQVPEGV--ARLKIEQTGPYGEYPN-------------QFYHFSRKSCQHCEDAPC 105
Cdd:cd16365    2 QFAAVFNLNKCIGCQTCTVACKNAWTYRKGQeyMWWNNVETKPGGGYPQdwevktidnggntRFFFYLQRLCNHCTNPAC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450 106 VNVCPTGAAFIDKETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCRETnlAQGKQP-ACVAACPTKALVF 184
Cdd:cd16365   82 LAACPRGAIYKREEDGIVLIDQKRCRGYRKCVEQCPYKKIYFNGLSRVSEKCIACYPR--IEGGDPtRCMSACVGRIRLQ 159

                        170
                 ....*....|....*.
gi 835524450 185 GNLKD-PTSQVVQVLK 199
Cdd:cd16365  160 GFLDDnPKSPVTKLIR 175
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 44-182 1.38e-24

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 101.36  E-value: 1.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  44 LIHDETKCIGCRACEVACRETNQvpEGVARLKIEQTGPYGEYPNQFYHFSRKSCQHCEDAPCVNVCPTGAafIDKETGIV 123
Cdd:PRK12769   5 IMANSQQCLGCHACEIACVMAHN--DEQHVLSQHHFHPRITVIKHQQQRSAVTCHHCEDAPCARSCPNGA--ISHVDDSI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 835524450 124 AVDAWKCVGCQYCIAACPYKIRFI-------NPVTHAADKCDFCretnLAQGKQPACVAACPTKAL 182
Cdd:PRK12769  81 QVNQQKCIGCKSCVVACPFGTMQIvltpvaaGKVKATAHKCDLC----AGRENGPACVENCPADAL 142
PRK10330 PRK10330
electron transport protein HydN;
44-183 4.80e-24

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 94.19  E-value: 4.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  44 LIHDETKCIGCRACEVACRETNQVPEGVARLKIEQTGPYGEYPNQFYHFSRKSCQHCEDAPCVNVCPTGAafIDKETGIV 123
Cdd:PRK10330   5 IIADASKCIGCRTCEVACVVSHQENQDCASLTPETFLPRIHVIKGVNVSTATVCRQCEDAPCANVCPNGA--ISRDKGFV 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 835524450 124 AVDAWKCVGCQYCIAACPYKIR--FINPVTH-------------AADKCDFC--RETNlaqgkqPACVAACPTKALV 183
Cdd:PRK10330  83 HVMQERCIGCKTCVVACPYGAMevVVRPVIRnsgaglnvraekaEANKCDLCnhREDG------PACMAACPTHALI 153
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 47-185 1.26e-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: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 92.84  E-value: 1.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  47 DETKCIGCRACEVACRE--------TNQVpEGVARLKIEQTGPYgeypnqfyhfsrkSCQHCEDAPCVNVCPTGAAFIDK 118
Cdd:cd16369    7 DPSRCIGCRACVAACREcgthrgksMIHV-DYIDRGESTQTAPT-------------VCMHCEDPTCAEVCPADAIKVTE 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 835524450 119 ETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCRETNlAQGKQPACVAACPTKALVFG 185
Cdd:cd16369   73 DGVVQSALKPRCIGCSNCVNACPFGVPKYDEERNLMMKCDMCYDRT-SVGKAPMCASVCPSGALFYG 138
PRK09898 PRK09898
ferredoxin-like protein;
4-182 2.86e-23

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 92.98  E-value: 2.86e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450   4 SKRRFL----KGACALLAGASGSTLLATVN---ASNEAKAEPSVKYALIHDETKCIGCRACEVACRETN--QVPEGVARL 74
Cdd:PRK09898  14 TRLEFLrisgKGLAGLTIAPALLSLLGCKQediDSGTVGLINTPKGVLVTQRARCTGCHRCEISCTNFNdgSVGTFFSRI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  75 KIEQTGPYGE----YPNQFY---HFSRKSCQHCEDAPCVNVCPTGAAFIDKETGIVAVDAWKCVGCQYCIAACPYKIRFI 147
Cdd:PRK09898  94 KIHRNYFFGDngvgSGGGLYgdlNYTADTCRQCKEPQCMNVCPIGAITWQQKEGCITVDHKRCIGCSACTTACPWMMATV 173

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 835524450 148 NPVTHAADKCDFCREtnlaqgkqpaCVAACPTKAL 182
Cdd:PRK09898 174 NTESKKSSKCVLCGE----------CANACPTGAL 198
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 43-189 2.90e-23

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: 92.88  E-value: 2.90e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  43 ALIHDETKCIGCRACEVACRETNQVPEGVArlkiEQTGPYGEYPN---------------------QFYHFSRKsCQHCE 101
Cdd:cd10559    1 SFLIDTTRCTACRGCQVACKQWNQLPAEQT----KNTGSHQNPPDlsantyklvrfnevrnengkpDWLFFPDQ-CRHCV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450 102 DAPCVNVCP--TGAAFIDKETG-IVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFC--RETNlaqGKQPACVAA 176
Cdd:cd10559   76 TPPCKDAADmvPGAVIQDEATGaVVFTEKTAELDFDDVLSACPYNIPRKNEATGRIVKCDMCidRVSN---GLQPACVKA 152

                        170
                 ....*....|...
gi 835524450 177 CPTKALVFGNLKD 189
Cdd:cd10559  153 CPTGAMNFGDRDE 165
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 42-185 1.10e-22

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


Pssm-ID: 319890 [Multi-domain]  Cd Length: 200  Bit Score: 91.33  E-value: 1.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  42 YALIHDETKCIGCR-----ACEVACRETNQ--VPEGVA------------------RLKIEQTGPYG-----------EY 85
Cdd:cd16368    1 LATLIDLTKCDGCPgesipACVRACREKNQarFPEPVSkpiqpywprkriedwsdkRDVTDRLTPYNwlyvqkltvdtAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  86 PNQFYHFSRKsCQHCEDAPCVNVCPTGAAFIDKEtGIVAVDAWKCVGCQYCIAACPYKI----RFINPVTHAAD------ 155
Cdd:cd16368   81 GEKEVFIPRR-CMHCDNPPCAKLCPFGAARKTPE-GAVYIDDDLCFGGAKCRDVCPWHIpqrqAGVGIYLHLAPeyaggg 158

                        170       180       190
                 ....*....|....*....|....*....|...
gi 835524450 156 ---KCDFCRETnLAQGKQPACVAACPTKALVFG 185
Cdd:cd16368  159 vmyKCDLCKDL-LAQGKPPACIEACPKGAQYFG 190
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 44-182 2.25e-21

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 92.01  E-value: 2.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  44 LIHDETKCIGCRACEVACRETNQVPEGVarlkiEQTGPYGEYPNQFYH---FSRKSCQHCEDAPCVNVCPTGAAFIDKET 120
Cdd:PRK12809   5 IAAEAAECIGCHACEIACAVAHNQENWP-----LSHSDFRPRIHVVGKgqaANPVACHHCNNAPCVTACPVNALTFQSDS 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 835524450 121 giVAVDAWKCVGCQYCIAACPYKIrfINPVTHAADKCDFCretNLAQGKQPACVAACPTKAL 182
Cdd:PRK12809  80 --VQLDEQKCIGCKRCAIACPFGV--VEMVDTIAQKCDLC---NQRSSGTQACIEVCPTQAL 134
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 36-219 4.36e-21

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: 88.67  E-value: 4.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  36 AEPSVKYALIHDETKCIGCRACEVACRET------------NQV--------PEG-----VARLKIEQTGPYG------- 83
Cdd:cd10556    6 SRPDKQFAMVFDTNKCIACQTCTMACKSTwtsgkgqeymwwNNVetkpyggyPLGwdvrlLDEEGGQTWAEGGvyegkti 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  84 --------------------EYPN----------------------QFYHFSRKSCQHCEDAPCVNVCPTGAAFIDKETG 121
Cdd:cd10556   86 feaaaageqvlgyrpededwRYPNigedevngertpdtgsslpphpIWFFYLPRICNHCTYPACLAACPRKAIYKREEDG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450 122 IVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCReTNLAQGKQPACVAACPTKALVFGNLKDPTSQVVQVLKAN 201
Cdd:cd10556  166 IVLIDQERCRGYRECVEACPYKKPMYNPTTRVSEKCIGCY-PRIEEGDQTQCVSACIGKIRLQGFINTPPDARWADDRDN 244

                        250       260
                 ....*....|....*....|....*...
gi 835524450 202 PT----QRAKVDL------GTRPKLFRI 219
Cdd:cd10556  245 PIdflvHIKKVALplypqfGTEPNVYYI 272
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 41-183 7.93e-21

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: 84.67  E-value: 7.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  41 KYALIHDETKCIGCRACEVACRETNQvpeGVARLKIEqTGPYGEYpnqfyHFSrKSCQHCEDAPCVNVCPTGAAFIDkET 120
Cdd:cd16367   11 TNLLVIDLDRCIRCDNCEKACADTHD---GHSRLDRN-GLRFGNL-----LVP-TACRHCVDPVCMIGCPTGAIHRD-DG 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 835524450 121 GIVAVDAWkCVGCQYCIAACPYKIRFInpvtHAADKCDFCRETNlaqgkQPACVAACPTKALV 183
Cdd:cd16367   80 GEVVISDA-CCGCGNCASACPYGAIQM----VRAVKCDLCAGYA-----GPACVSACPTGAAI 132
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 82-177 2.15e-18

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: 82.41  E-value: 2.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  82 YGEYPNQFYHFSRKSCQHCEDAPCVNVCPTGAAFIDKETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFC- 160
Cdd:cd10557  164 YLEFENTFMFYLPRICNHCLNPACVAACPSGAIYKREEDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSEKCIFCy 243

                         90
                 ....*....|....*...
gi 835524450 161 -RetnLAQGKQPACVAAC 177
Cdd:cd10557  244 pR---LEAGQPTVCSETC 258
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 44-182 4.45e-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: 4.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  44 LIHDETKCIGCRACEVACRET-NQVPEG-VARLKIEQTGpygeypnqfYHFSRKSCQHCedAPCVNVCPTGAAFIDKEtG 121
Cdd:cd16372    3 LVTDPEKCIGCLQCEEACSKTfFKEEDReKSCIRITETE---------GGYAINVCNQC--GECIDVCPTGAITRDAN-G 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 835524450 122 IVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCretnlaqgkqPACVAACPTKAL 182
Cdd:cd16372   71 VVMINKKLCVGCLMCVGFCPEGAMFKHEDYPEPFKCIAC----------GICVKACPTGAL 121
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 50-184 7.81e-11

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


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 57.67  E-value: 7.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  50 KCIGCRACEVACRETNQVPEGVARLKIeQTGPYGEYPNQFyhfSRKSCQHCEDAPCVNVCPTGaAFIDKETGIVAVDAWK 129
Cdd:cd16370   10 RCIGCYSCMLACSRRVHKSASLSKSAI-RVRTRGGLEGGF---TVVVCRACEDPPCAEACPTG-ALEPRKGGGVVLDKEK 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 835524450 130 CVGCQYCIAACPYKIRFINPVTHAADKCDFCretnlaqgkqPACVAACPTKALVF 184
Cdd:cd16370   85 CIGCGNCVKACIVGAIFWDEETNKPIICIHC----------GYCARYCPHDVLAM 129
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
44-197 4.40e-09

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 55.80  E-value: 4.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  44 LIHDETKCIGCRACEVACRETNQVPEGVARLKIEQTGPYGEYPNQFYHFSRKSCQHCEDAPCVNVC------PTGAAFID 117
Cdd:COG4624    1 LLLLLRACCCCCIEEGDELLLLEEAERVLRIIILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVaisciqVRGIIIID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450 118 KETGIVAVDAWKCVGCQYCIAACPYK-IRFINPVTH-AADKCDFCretnlaqGKqpaCVAACPTKAL--------VFGNL 187
Cdd:COG4624   81 KRGPSIIRDKEKCKNCYPCVRACPVKaIKVDDGKAEiDEEKCISC-------GQ---CVAVCPFGAIteksdiekVKKAL 150

                        170
                 ....*....|
gi 835524450 188 KDPTSQVVQV 197
Cdd:COG4624  151 KDPEKVVAQV 160
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 47-141 2.18e-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: 2.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  47 DETKCIGCRACEVACretnqvPEGVarLKIEQTGPYGEYPNQFYHFSRKSCQHCEDapCVNVCPTGAAFIDKETGIVaVD 126
Cdd:cd10549   38 DEDKCVFCGACVEVC------PTGA--IELTPEGKEYVPKEKEAEIDEEKCIGCGL--CVKVCPVDAITLEDELEIV-ID 106

                         90
                 ....*....|....*
gi 835524450 127 AWKCVGCQYCIAACP 141
Cdd:cd10549  107 KEKCIGCGICAEVCP 121
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 44-184 2.80e-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: 50.86  E-value: 2.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  44 LIHDETKCIGCRACEVACretnqvPEGVarLKIEQTGPYGEYPNqfyhFSRKSCQHCEDapCVNVCPTGA-------AFI 116
Cdd:cd10549    1 LKYDPEKCIGCGICVKAC------PTDA--IELGPNGAIARGPE----IDEDKCVFCGA--CVEVCPTGAieltpegKEY 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 835524450 117 DKETGIVAVDAWKCVGCQYCIAACPY---KIRFINPVTHAADKCDFCRetnlaqgkqpACVAACPTKALVF 184
Cdd:cd10549   67 VPKEKEAEIDEEKCIGCGLCVKVCPVdaiTLEDELEIVIDKEKCIGCG----------ICAEVCPVNAIKL 127
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
105-191 6.19e-08

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 51.60  E-value: 6.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450 105 CVNVCPTGA---AFIDKETGIVAVDAWKCVGCQYCIAACPYKIrFINPVTHAADKCDFCRetnlaqgkqpACVAACPTKA 181
Cdd:COG0348  184 CRYLCPYGAfqgLLSDLSTLRVRYDRGDCIDCGLCVKVCPMGI-DIRKGEINQSECINCG----------RCIDACPKDA 252

                         90
                 ....*....|
gi 835524450 182 LVFGNLKDPT 191
Cdd:COG0348  253 IRFSSRGEKT 262
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
97-151 1.24e-07

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 47.42  E-value: 1.24e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 835524450  97 CQHCEDapCVNVCPTGAafIDKETGIVAVDAWKCVGCQYCIAACPYKIRFINPVT 151
Cdd:COG2768   13 CIGCGA--CVKVCPVGA--ISIEDGKAVIDPEKCIGCGACIEVCPVGAIKIEWEE 63
PRK13795 PRK13795
hypothetical protein; Provisional
 105-149 1.73e-07

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 51.15  E-value: 1.73e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 835524450 105 CVNVCPTGAAFIDKETGIVAVDAWKCVGCQYCIAACPYkIRFINP 149
Cdd:PRK13795 589 CVGACPTGAIRIEEGKRKISVDEEKCIHCGKCTEVCPV-VKYKDK 632
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
121-200 6.74e-07

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 49.47  E-value: 6.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450 121 GIVA-VDAWKCVGCQYCIAACPYKIRFINPVTHA---ADKCDFCretnlaqGkqpACVAACPTKALVFGNLKDPtsQVVQ 196
Cdd:COG1148  488 PSVAeVDPEKCTGCGRCVEVCPYGAISIDEKGVAevnPALCKGC-------G---TCAAACPSGAISLKGFTDD--QILA 555


                 ....
gi 835524450 197 VLKA 200
Cdd:COG1148  556 QIDA 559
napG PRK09476
quinol dehydrogenase periplasmic component; Provisional
 1-141 9.13e-07

quinol dehydrogenase periplasmic component; Provisional


Pssm-ID: 236534 [Multi-domain]  Cd Length: 254  Bit Score: 48.08  E-value: 9.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450   1 MENSKRRFLKGACALLAGASGSTLLATVnASNEAKAEPSV---KYALIHDE--TKCIGCRACEVACR-ETnqvpegvarL 74
Cdd:PRK09476   7 PQNGRRRFLRDVVRTAGGLAAVGVALGL-QQQQARASGVAlrpPGALNENDflSACIRCGLCVQACPyDT---------L 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 835524450  75 KIEQTGPYGEYPNQFYHFSRKSCQHCEDAPCVNVCPTGA-----AFIDK-ETGI-VAVD-----AWKCVGCQYCIAACP 141
Cdd:PRK09476  77 KLATLASGLSAGTPYFVARDIPCEMCEDIPCVKACPSGAldrelVDIDDaRMGLaVLVDqenclNFQGLRCDVCYRVCP 155
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 50-179 2.60e-06

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 45.71  E-value: 2.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  50 KCIGCRACEVACretnqvPEGVARLKIEQTG-PYGEYPnqFYHFSRKSCQHCEDApCVNVCPTGA--------------- 113
Cdd:cd16373   15 LCIRCGLCVEAC------PTGVIQPAGLEDGlEGGRTP--YLDPREGPCDLCCDA-CVEVCPTGAlrpldleeqkvkmgv 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 835524450 114 AFIDKETGIVAVDAwkcVGCQYCIAACPYKIRFINPVTHA------ADKCDFCretnlaqGkqpACVAACPT 179
Cdd:cd16373   86 AVIDKDRCLAWQGG---TDCGVCVEACPTEAIAIVLEDDVlrpvvdEDKCVGC-------G---LCEYVCPV 144
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 81-141 3.04e-06

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 43.50  E-value: 3.04e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 835524450  81 PYGEYPNQFYHFSRKSCQHCEDapCVNVCPTGAafIDKETGIVAVDAWKCVGCQYCIAACP 141
Cdd:COG2221    1 PYGIIGTWPPKIDEEKCIGCGL--CVAVCPTGA--ISLDDGKLVIDEEKCIGCGACIRVCP 57
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 97-144 1.09e-05

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 41.74  E-value: 1.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 835524450   97 CQHCEDapCVNVCPTGAAFID-----KETGIVAVDAWKCVGCQYCIAACPYKI 144
Cdd:pfam12838   1 CIGCGA--CVAACPVGAITLDevgekKGTKTVVIDPERCVGCGACVAVCPTGA 51
NapF COG1145
Ferredoxin [Energy production and conversion];
94-182 2.36e-05

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 43.94  E-value: 2.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  94 RKSCQHCEDAPCVNVCPTGAAFIDKETGIVAVDAWKCVGCQYCIAACPYK-IRFIN---PVTHAADKCDFCRetnlaqgk 169
Cdd:COG1145  148 GAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVCPTGaIRLKDgkpQIVVDPDKCIGCG-------- 219

                         90
                 ....*....|...
gi 835524450 170 qpACVAACPTKAL 182
Cdd:COG1145  220 --ACVKVCPVGAI 230
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
105-141 2.47e-05

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 44.47  E-value: 2.47e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 835524450 105 CVNVCPTGAAFIDkETGIVAVDAWKCVGCQYCIAACP 141
Cdd:COG1148  504 CVEVCPYGAISID-EKGVAEVNPALCKGCGTCAAACP 539
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 51-182 6.10e-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: 41.46  E-value: 6.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  51 CIGCRACEVACretnqvPEGVarLKIEQTGpygeYPnqFYHFSRKSCQHCEDapCVNVCPTGAaFIDKETGIVAVDA--- 127
Cdd:cd10564   15 CTRCGDCVEAC------PEGI--IVRGDGG----FP--ELDFSRGECTFCGA--CAEACPEGA-LDPAREAPWPLRAeig 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 835524450 128 -----WKCVGCQYCIAACPYK-IRFINPVTHAA------DKCDFCretnlaqGkqpACVAACPTKAL 182
Cdd:cd10564   78 dsclaLQGVECRSCQDACPTQaIRFRPRLGGIAlpeldaDACTGC-------G---ACVSVCPVGAI 134
PRK14028 PRK14028
pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional
 47-113 1.61e-04

pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional


Pssm-ID: 172522 [Multi-domain]  Cd Length: 312  Bit Score: 41.91  E-value: 1.61e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 835524450  47 DETKCIGCRACEVACREtnqvpEGVARLKIEQTGPYG-EYPNQFYHFSRKSCQHCedAPCVNVCPTGA 113
Cdd:PRK14028 245 DHSKCIMCRKCWLYCPD-----DAIIEAWREAEGPRGrKFRMKMIDFDYQYCKGC--GVCAEVCPTGA 305
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 122-184 1.82e-04

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 38.56  E-value: 1.82e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 835524450 122 IVAVDAWKCVGCQYCIAACPYK-IRFIN--PVTHAADKCDFCRetnlaqgkqpACVAACPTKALVF 184
Cdd:COG1149    5 IPVIDEEKCIGCGLCVEVCPEGaIKLDDggAPVVDPDLCTGCG----------ACVGVCPTGAITL 60
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 105-143 2.31e-04

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 38.19  E-value: 2.31e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 835524450 105 CVNVCPTGAAFI--DKETGIVAVDAWKCVGCQYCIAACPYK 143
Cdd:COG1143   10 CVRVCPVDAITIedGEPGKVYVIDPDKCIGCGLCVEVCPTG 50
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 97-143 2.49e-04

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 38.49  E-value: 2.49e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 835524450  97 CQHCEDapCVNVCPTGAafIDKETGIVAVDAWKCVGCQYCIAACPYK 143
Cdd:COG4231   24 CTGCGA--CVKVCPADA--IEEGDGKAVIDPDLCIGCGSCVQVCPVD 66
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 105-141 2.51e-04

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: 41.13  E-value: 2.51e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 835524450 105 CVNVCPTGAAFIDkETGIVAVDAWKCVGCQYCIAACP 141
Cdd:COG2878  145 CIKACPFDAIVGA-AKGMHTVDEDKCTGCGLCVEACP 180
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 94-141 3.82e-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: 37.62  E-value: 3.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 835524450   94 RKSCQHCedAPCVNVCPT-----GAAFIDKETGIVAVDAWKCVGCQYCIAACP 141
Cdd:pfam13237   6 PDKCIGC--GRCTAACPAgltrvGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
105-144 4.54e-04

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 40.30  E-value: 4.54e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 835524450 105 CVNVCPTGAAFIdkETGIVAVDAWKCVGCQYCIAACPYKI 144
Cdd:PRK07118 147 CVAACPFDAIHI--ENGLPVVDEDKCTGCGACVKACPRNV 184
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 105-143 6.73e-04

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 37.01  E-value: 6.73e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 835524450 105 CVNVCPTGAAFIDKETGIVaVDAWKCVGCQYCIAACPYK 143
Cdd:COG1149   19 CVEVCPEGAIKLDDGGAPV-VDPDLCTGCGACVGVCPTG 56
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 43-113 7.48e-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: 38.33  E-value: 7.48e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 835524450  43 ALIHDETKCIGCRACEVACretnqvPEGVARLkIEQTGPygeypnqfyhfSRKsCQHCEDAP-CVNVCPTGA 113
Cdd:cd10550   74 AVVVDEDKCIGCGMCVEAC------PFGAIRV-DPETGK-----------AIK-CDLCGGDPaCVKVCPTGA 126
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 129-193 8.82e-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: 36.65  E-value: 8.82e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 835524450 129 KCVGCQYCIAACPYKIRFINPVTHA------ADKCDFCRetnlaqgkqpACVAACPTKALVFGNLKDPTSQ 193
Cdd:COG1143    3 KCIGCGLCVRVCPVDAITIEDGEPGkvyvidPDKCIGCG----------LCVEVCPTGAISMTPFELAVED 63
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 96-141 9.14e-04

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 39.86  E-value: 9.14e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 835524450  96 SCQHC-EDAPCVNVCPTGAAFIDKETGIVAVDAWKCVGCQYCIAACP 141
Cdd:PRK12771 508 SCGNCfECDNCYGACPQDAIIKLGPGRRYHFDYDKCTGCHICADVCP 554
PRK13795 PRK13795
hypothetical protein; Provisional
 118-178 1.01e-03

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 39.59  E-value: 1.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 835524450 118 KETGIVAVDAWKCVGCQYCIAACPYK-IRFINP---VTHAADKCDFCREtnlaqgkqpaCVAACP 178
Cdd:PRK13795 571 KDAARLLRRAAECVGCGVCVGACPTGaIRIEEGkrkISVDEEKCIHCGK----------CTEVCP 625
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 97-141 1.05e-03

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 36.61  E-value: 1.05e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 835524450  97 CQHCEDapCVNVCPTGAAFIDKETG-IVAVDAWKCVGCQYCIAACP 141
Cdd:COG1146   10 CIGCGA--CVEVCPVDVLELDEEGKkALVINPEECIGCGACELVCP 53
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 123-186 1.23e-03

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 39.62  E-value: 1.23e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 835524450 123 VAVDAWKCVGCQYCIAAC---------PYKIRFINPVTHAADKCDFCRETNLAQGKQPACVAACPTKALVFGN 186
Cdd:PRK12809   5 IAAEAAECIGCHACEIACavahnqenwPLSHSDFRPRIHVVGKGQAANPVACHHCNNAPCVTACPVNALTFQS 77
Fer4_9 pfam13187
4Fe-4S dicluster domain;
129-182 1.43e-03

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 35.61  E-value: 1.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 835524450  129 KCVGCQYCIAACP------YKIRFINPVTHAADKCDFCRetnlaqgkqpACVAACPTKAL 182
Cdd:pfam13187   1 KCTGCGACVAACPagaivpDLVGQTIRGDIAGLACIGCG----------ACVDACPRGAI 50
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 129-186 1.79e-03

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: 38.30  E-value: 1.79e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 835524450 129 KCVGCQYCIAACPYK-IRFIN--PVTHaaDKCDFCRetnlaqgkqpACVAACPTKALVFGN 186
Cdd:NF038196 186 KCIGCGICAKVCPVNnIEMEDgkPVWG--HNCTHCL----------ACIHRCPKEAIEYGK 234
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
125-184 2.23e-03

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 35.86  E-value: 2.23e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 835524450 125 VDAWKCVGCQYCIAACPYK-IRFINPVTHA-ADKCDFCretnlaqgkqPACVAACPTKALVF 184
Cdd:COG2768    8 VDEEKCIGCGACVKVCPVGaISIEDGKAVIdPEKCIGC----------GACIEVCPVGAIKI 59
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 121-184 2.37e-03

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 35.46  E-value: 2.37e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 835524450 121 GIVAVDAWKCVGCQYCIAACPYKI-----RFINPVTHAADKCDFCRetnlaqgkqpACVAACPTKALVF 184
Cdd:COG1146    1 MMPVIDTDKCIGCGACVEVCPVDVleldeEGKKALVINPEECIGCG----------ACELVCPVGAITV 59
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
105-148 3.32e-03

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 38.25  E-value: 3.32e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 835524450 105 CVNVCP---TG--AAFIDKETGIVAVDAWKCVGCQYCIAACPYK-IRFIN 148
Cdd:PRK13409  21 CIKYCPvvrTGeeTIEIDEDDGKPVISEELCIGCGICVKKCPFDaISIVN 70
PRK06273 PRK06273
ferredoxin; Provisional
 96-141 4.92e-03

ferredoxin; Provisional


Pssm-ID: 235764 [Multi-domain]  Cd Length: 165  Bit Score: 36.61  E-value: 4.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 835524450  96 SCQHCEDapCVNVCPTGA-AFIDKE----------TGIVAVDAWKCVGCQYCIAACP 141
Cdd:PRK06273  50 LCIGCGG--CANVCPTKAiEMIPVEpvkitegyvkTKIPKIDYEKCVYCLYCHDFCP 104
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 51-113 4.99e-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: 34.04  E-value: 4.99e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 835524450   51 CIGCRACEVACretnqvPEGVARLKIEQTGPYGEYpnqfYHFSRKSCQHCEDapCVNVCPTGA 113
Cdd:pfam12838   1 CIGCGACVAAC------PVGAITLDEVGEKKGTKT----VVIDPERCVGCGA--CVAVCPTGA 51
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 130-181 5.40e-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: 34.04  E-value: 5.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 835524450  130 CVGCQYCIAACPYKIRFINPVTHA---------ADKCDFCRetnlaqgkqpACVAACPTKA 181
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKkgtktvvidPERCVGCG----------ACVAVCPTGA 51
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
117-182 5.90e-03

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 35.31  E-value: 5.90e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 835524450 117 DKETGIVAVDAWKCVGCQYCIAACPYKIRFINPVTHAADKCDFCRETNLaqgkqpaCVAACPTKAL 182
Cdd:PRK09623  40 DWRTFMPVVDESKCVKCYICWKFCPEPAIYIKEDGYVAIDYDYCKGCGI-------CANECPTKAI 98
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 125-183 7.32e-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: 7.32e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 835524450 125 VDAWKCVGCQYCIAACPY---KIRFINPVTHAADKCDFCRetnlaqgkqpACVAACPTKALV 183
Cdd:COG1144   27 VDEDKCIGCGLCWIVCPDgaiRVDDGKYYGIDYDYCKGCG----------ICAEVCPVKAIE 78
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 47-119 7.68e-03

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 33.91  E-value: 7.68e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 835524450  47 DETKCIGCRACEVACretnqvPEGVarLKIEQTGPYGEYPNQfyhfsrKSCQHCEdaPCVNVCPTGAAFIDKE 119
Cdd:COG1146    6 DTDKCIGCGACVEVC------PVDV--LELDEEGKKALVINP------EECIGCG--ACELVCPVGAITVEDD 62
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 97-143 8.49e-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: 34.26  E-value: 8.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 835524450  97 CQHCedAPCVNVCPTGAAFIDKETGIVaVDAWKCVGCQYCIAACPYK 143
Cdd:COG1144   32 CIGC--GLCWIVCPDGAIRVDDGKYYG-IDYDYCKGCGICAEVCPVK 75
 
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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