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Conserved domains on  [gi|495957535|ref|WP_008682114|]
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MULTISPECIES: 4Fe-4S dicluster domain-containing protein [unclassified Desulfovibrio]

Protein Classification

4Fe-4S dicluster domain-containing protein( domain architecture ID 11586809)

4Fe-4S dicluster domain-containing protein similar to Escherichia coli formate hydrogenlyase subunit 2 (HycB), a probable electron transfer protein for hydrogenase 3

Gene Ontology:  GO:0051539|GO:0009061|GO:0046872|GO:0019645
SCOP:  3000020

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 4-165 2.66e-50

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: 159.73  E-value: 2.66e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535   4 HIQVVPDKCRACRRCEVACIAAHHGMSFKEAMKHRDVLVARVQVVKAEGFKTTVRCHQCDPAPCCNVCPTGALQQeEDGR 83
Cdd:cd10554    1 FVIADPDKCIGCRTCEVACAAAHSGKGIFEAGTDGLPFLPRLRVVKTGEVTAPVQCRQCEDAPCANVCPVGAISQ-EDGV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  84 ITMRVQFCVACKMCIAACPYGTISLDTIGMPDLSGsdaetlaQRARREVAVRCDMCRawreeNGKKITACMEACPVRALS 163
Cdd:cd10554   80 VQVDEERCIGCKLCVLACPFGAIEMAPTTVPGVDW-------ERGPRAVAVKCDLCA-----GREGGPACVEACPTKALT 147


                 ..
gi 495957535 164 MV 165
Cdd:cd10554  148 LV 149
 
Name Accession Description Interval E-value
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 4-165 2.66e-50

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: 159.73  E-value: 2.66e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535   4 HIQVVPDKCRACRRCEVACIAAHHGMSFKEAMKHRDVLVARVQVVKAEGFKTTVRCHQCDPAPCCNVCPTGALQQeEDGR 83
Cdd:cd10554    1 FVIADPDKCIGCRTCEVACAAAHSGKGIFEAGTDGLPFLPRLRVVKTGEVTAPVQCRQCEDAPCANVCPVGAISQ-EDGV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  84 ITMRVQFCVACKMCIAACPYGTISLDTIGMPDLSGsdaetlaQRARREVAVRCDMCRawreeNGKKITACMEACPVRALS 163
Cdd:cd10554   80 VQVDEERCIGCKLCVLACPFGAIEMAPTTVPGVDW-------ERGPRAVAVKCDLCA-----GREGGPACVEACPTKALT 147


                 ..
gi 495957535 164 MV 165
Cdd:cd10554  148 LV 149
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
1-167 9.58e-32

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 112.06  E-value: 9.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535   1 MLEHIQVVPDKCRACRRCEVACIAAHHGMSfkeamkhRDVLVARVQVVKAEGFKTTVRCHQCDPAPCCNVCPTGALQQeE 80
Cdd:COG1142    1 MNKFIIADPEKCIGCRTCEAACAVAHEGEE-------GEPFLPRIRVVRKAGVSAPVQCRHCEDAPCAEVCPVGAITR-D 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  81 DGRITMRVQFCVACKMCIAACPYGTISLDTigmpdlsgsdaetlaqRARREVAVRCDMCrawreENGKKITACMEACPVR 160
Cdd:COG1142   73 DGAVVVDEEKCIGCGLCVLACPFGAITMVG----------------EKSRAVAVKCDLC-----GGREGGPACVEACPTG 131


                 ....*..
gi 495957535 161 ALSMVEP 167
Cdd:COG1142  132 ALRLVDV 138
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 11-169 5.83e-27

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 107.14  E-value: 5.83e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  11 KCRACRRCEVACIAAHHGMSFKEAMKHrdvLVARVQVVKAEGFKTTVRCHQCDPAPCCNVCPTGALQQEEDGrITMRVQF 90
Cdd:PRK12769  11 QCLGCHACEIACVMAHNDEQHVLSQHH---FHPRITVIKHQQQRSAVTCHHCEDAPCARSCPNGAISHVDDS-IQVNQQK 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495957535  91 CVACKMCIAACPYGTISLDTigmpdlsgsdaETLAQRARREVAVRCDMCRAwrEENGKkitACMEACPVRALSMVEPDG 169
Cdd:PRK12769  87 CIGCKSCVVACPFGTMQIVL-----------TPVAAGKVKATAHKCDLCAG--RENGP---ACVENCPADALQLVTEQA 149
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 59-166 3.29e-08

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: 49.55  E-value: 3.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535   59 CHQCDPAPCCNVCPTGAL-QQEEDGRITMRVQFCVACKMCIAACPYGTISLDtigmpDLSGsdaetlaqrarreVAVRCD 137
Cdd:pfam13247  10 CRHCLNPPCKASCPVGAIyKDEETGAVLLDEKTCRGWRECVSACPYNIPRYN-----DETG-------------KAEKCD 71

                          90       100
                  ....*....|....*....|....*....
gi 495957535  138 MCRAwREENGKKiTACMEACPVRALSMVE 166
Cdd:pfam13247  72 MCYD-RVEAGLL-PACVQTCPTGAMNFGD 98
 
Name Accession Description Interval E-value
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 4-165 2.66e-50

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: 159.73  E-value: 2.66e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535   4 HIQVVPDKCRACRRCEVACIAAHHGMSFKEAMKHRDVLVARVQVVKAEGFKTTVRCHQCDPAPCCNVCPTGALQQeEDGR 83
Cdd:cd10554    1 FVIADPDKCIGCRTCEVACAAAHSGKGIFEAGTDGLPFLPRLRVVKTGEVTAPVQCRQCEDAPCANVCPVGAISQ-EDGV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  84 ITMRVQFCVACKMCIAACPYGTISLDTIGMPDLSGsdaetlaQRARREVAVRCDMCRawreeNGKKITACMEACPVRALS 163
Cdd:cd10554   80 VQVDEERCIGCKLCVLACPFGAIEMAPTTVPGVDW-------ERGPRAVAVKCDLCA-----GREGGPACVEACPTKALT 147


                 ..
gi 495957535 164 MV 165
Cdd:cd10554  148 LV 149
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
1-167 9.58e-32

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 112.06  E-value: 9.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535   1 MLEHIQVVPDKCRACRRCEVACIAAHHGMSfkeamkhRDVLVARVQVVKAEGFKTTVRCHQCDPAPCCNVCPTGALQQeE 80
Cdd:COG1142    1 MNKFIIADPEKCIGCRTCEAACAVAHEGEE-------GEPFLPRIRVVRKAGVSAPVQCRHCEDAPCAEVCPVGAITR-D 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  81 DGRITMRVQFCVACKMCIAACPYGTISLDTigmpdlsgsdaetlaqRARREVAVRCDMCrawreENGKKITACMEACPVR 160
Cdd:COG1142   73 DGAVVVDEEKCIGCGLCVLACPFGAITMVG----------------EKSRAVAVKCDLC-----GGREGGPACVEACPTG 131


                 ....*..
gi 495957535 161 ALSMVEP 167
Cdd:COG1142  132 ALRLVDV 138
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 5-168 2.84e-27

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


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 100.43  E-value: 2.84e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535   5 IQVVPDKCRACRRCEVACIAAHHGMSFkeamkhrdvlvARVQVVKaEGFKTTVRCHQCDPAPCCNVCPTGALQQEEDGRI 84
Cdd:cd16374    1 VYVDPERCIGCRACEIACAREHSGKPR-----------ISVEVVE-DLASVPVRCRHCEDAPCMEVCPTGAIYRDEDGAV 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  85 TMRVQFCVACKMCIAACPYGTISLDtigmpdlsgsdaetlaqrARREVAVRCDMCrAWREENGkKITACMEACPVRALSM 164
Cdd:cd16374   69 LVDPDKCIGCGMCAMACPFGVPRFD------------------PSLKVAVKCDLC-IDRRREG-KLPACVEACPTGALKF 128


                 ....
gi 495957535 165 VEPD 168
Cdd:cd16374  129 GDIE 132
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 11-169 5.83e-27

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 107.14  E-value: 5.83e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  11 KCRACRRCEVACIAAHHGMSFKEAMKHrdvLVARVQVVKAEGFKTTVRCHQCDPAPCCNVCPTGALQQEEDGrITMRVQF 90
Cdd:PRK12769  11 QCLGCHACEIACVMAHNDEQHVLSQHH---FHPRITVIKHQQQRSAVTCHHCEDAPCARSCPNGAISHVDDS-IQVNQQK 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495957535  91 CVACKMCIAACPYGTISLDTigmpdlsgsdaETLAQRARREVAVRCDMCRAwrEENGKkitACMEACPVRALSMVEPDG 169
Cdd:PRK12769  87 CIGCKSCVVACPFGTMQIVL-----------TPVAAGKVKATAHKCDLCAG--RENGP---ACVENCPADALQLVTEQA 149
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 5-162 8.51e-27

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: 99.25  E-value: 8.51e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535   5 IQVVPDKCRACRRCEVACIAAHHGMSFKEAMKHRDVL-VARVQVVKAEGFKTTVRCHQCDPAPCCNVCPTGALQQ-EEDG 82
Cdd:cd10563    2 IFIDEEKCLGCKLCEVACAVAHSKSKDLIKAKLEKERpRPRIRVEESGGRSFPLQCRHCDEPPCVKACMSGAMHKdPETG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  83 RITMRVQFCVACKMCIAACPYGTISLDTigmpdlsgsdaetlaqraRREVAVRCDMCRawreenGKKITACMEACPVRAL 162
Cdd:cd10563   82 IVIHDEEKCVGCWMCVMVCPYGAIRPDK------------------ERKVALKCDLCP------DRETPACVEACPTGAL 137
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 9-168 2.16e-26

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 99.64  E-value: 2.16e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535   9 PDKCRACRRCEVACIAAHHGmsfKEAMKHRDVLVARV-QVVKAEGFKTTVRCHQCDPAPCCNVCPTGALQQEEDGRITMR 87
Cdd:COG0437   12 LTKCIGCRACVVACKEENNL---PVGVTWRRVRRYEEgEFPNVEWLFVPVLCNHCDDPPCVKVCPTGATYKREDGIVLVD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  88 VQFCVACKMCIAACPYGTISLDtigmpdlsgsdaetlaqrARREVAVRCDMCrAWREENGKKiTACMEACPVRALSMVEP 167
Cdd:COG0437   89 YDKCIGCRYCVAACPYGAPRFN------------------PETGVVEKCTFC-ADRLDEGLL-PACVEACPTGALVFGDL 148


                 .
gi 495957535 168 D 168
Cdd:COG0437  149 D 149
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 10-165 1.87e-25

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: 95.92  E-value: 1.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  10 DKCRACRRCEVACIAAHHGMSFKEAMKhrdvlVARVQVVKAEGFKTTVRCHQCDPAPCCNVCPTGALQQEEDGRITMRVQ 89
Cdd:cd04410    6 DRCIGCGTCEVACKQEHGLRPGPDWSR-----IKVIEGGGLERAFLPVSCMHCEDPPCVKACPTGAIYKDEDGIVLIDED 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495957535  90 FCVACKMCIAACPYGTISLDtigmpdlsgsdaetlaqrARREVAVRCDMCrAWREENGKKiTACMEACPVRALSMV 165
Cdd:cd04410   81 KCIGCGSCVEACPYGAIVFD------------------PEPGKAVKCDLC-GDRLDEGLE-PACVKACPTGALTFG 136
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 10-162 2.17e-23

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: 91.82  E-value: 2.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  10 DKCRACRRCEVACIAAHH---GMSFkeamkhrdvlvARVQVVKAEGFKTT------VRCHQCDPAPCCNVCPTGALQQEE 80
Cdd:cd10551    6 RKCIGCGACVVACKAENNvppGVFR-----------NRVLEYEVGEYPNVkrtflpVLCNHCENPPCVKVCPTGATYKRE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  81 DGRITMRVQFCVACKMCIAACPYGTISLDTIGMPDlsgsdaETLAQRARREVAVRCDMCrAWREENGKKiTACMEACPVR 160
Cdd:cd10551   75 DGIVLVDYDKCIGCRYCMAACPYGARYFNPEEPHE------FGEVPVRPKGVVEKCTFC-YHRLDEGLL-PACVEACPTG 146


                 ..
gi 495957535 161 AL 162
Cdd:cd10551  147 AR 148
PRK10330 PRK10330
electron transport protein HydN;
1-168 2.13e-22

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 89.18  E-value: 2.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535   1 MLEHIQVVPDKCRACRRCEVACIAAHHGMSFKEAMKHRDVLvARVQVVKAEGFKTTVRCHQCDPAPCCNVCPTGALQQEE 80
Cdd:PRK10330   1 MNRFIIADASKCIGCRTCEVACVVSHQENQDCASLTPETFL-PRIHVIKGVNVSTATVCRQCEDAPCANVCPNGAISRDK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  81 DGRITMRvQFCVACKMCIAACPYGTISLDTIGMPDLSGSDAETLAQRARrevAVRCDMCRAwREENgkkiTACMEACPVR 160
Cdd:PRK10330  80 GFVHVMQ-ERCIGCKTCVVACPYGAMEVVVRPVIRNSGAGLNVRAEKAE---ANKCDLCNH-REDG----PACMAACPTH 150


                 ....*...
gi 495957535 161 ALSMVEPD 168
Cdd:PRK10330 151 ALICVDRN 158
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 5-165 2.26e-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: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 84.94  E-value: 2.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535   5 IQVVPDKCRACRRCEVACIAAHHGMsFKEAMkhrdvlvARVQVVK--AEGFKTTVRCHQCDPAPCCNVCPTGAL-QQEED 81
Cdd:cd10550    1 LVVDPEKCTGCRTCELACSLKHEGV-FNPSL-------SRIRVVRfePEGLDVPVVCRQCEDAPCVEACPVGAIsRDEET 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  82 GRITMRVQFCVACKMCIAACPYGTISLDtigmpdlsgsdaetlaqrARREVAVRCDMCrawreeNGKkiTACMEACPVRA 161
Cdd:cd10550   73 GAVVVDEDKCIGCGMCVEACPFGAIRVD------------------PETGKAIKCDLC------GGD--PACVKVCPTGA 126


                 ....
gi 495957535 162 LSMV 165
Cdd:cd10550  127 LEFV 130
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 11-193 4.70e-21

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 90.08  E-value: 4.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  11 KCRACRRCEVACIAAHHGMSFkeAMKHRDVLvARVQVVKAEGFKTTVRCHQCDPAPCCNVCPTGALQQEEDGrITMRVQF 90
Cdd:PRK12809  11 ECIGCHACEIACAVAHNQENW--PLSHSDFR-PRIHVVGKGQAANPVACHHCNNAPCVTACPVNALTFQSDS-VQLDEQK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  91 CVACKMCIAACPYGTISLdtigmpdlsgsdAETLAQrarrevavRCDMCRawREENGKKitACMEACPVRALSMVEPDGt 170
Cdd:PRK12809  87 CIGCKRCAIACPFGVVEM------------VDTIAQ--------KCDLCN--QRSSGTQ--ACIEVCPTQALRLMDDKG- 141

                        170       180
                 ....*....|....*....|...
gi 495957535 171 VVEVPQPEKKTVAEAKASPTETP 193
Cdd:PRK12809 142 LQQIKVARQRKTAAGKASSDAQP 164
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 10-162 7.42e-19

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: 78.76  E-value: 7.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  10 DKCRACRRCEVACIAAHHgmsfkeamkhRDVLVARVQVV--------KAEGFKTTVRCHQCDPAPCCNVCPTGALQQEED 81
Cdd:cd16371    7 ERCIGCKACEIACKDKND----------LPPGVNWRRVYeyeggefpEVFAYFLSMSCNHCENPACVKVCPTGAITKRED 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  82 GRITMRVQFCVACKMCIAACPYGTISLDtigmpdlsgsdaetlaqrARREVAVRCDMCRAwREENGKKiTACMEACPVRA 161
Cdd:cd16371   77 GIVVVDQDKCIGCGYCVWACPYGAPQYN------------------PETGKMDKCDMCVD-RLDEGEK-PACVAACPTRA 136


                 .
gi 495957535 162 L 162
Cdd:cd16371  137 L 137
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 11-162 3.00e-14

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: 67.04  E-value: 3.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  11 KCRACRRCEVACIAAHH-----------GMSFKEAMKHRDVLVARVQVVKAEG------FKTTvrCHQCDPAPCCNVCPT 73
Cdd:cd16366    7 RCTGCRACQVACKQWNGlpaekteftgsYQNPPDLTAHTWTLVRFYEVEKPGGdlswlfRKDQ--CMHCTDAGCLAACPT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  74 GALQQEEDGRITMRVQFCVACKMCIAACPYGTISLDtigmpdlsgsdaetlaqrARREVAVRCDMCRAwREENGkKITAC 153
Cdd:cd16366   85 GAIIRTETGTVVVDPETCIGCGYCVNACPFDIPRFD------------------EETGRVAKCTLCYD-RISNG-LQPAC 144


                 ....*....
gi 495957535 154 MEACPVRAL 162
Cdd:cd16366  145 VKTCPTGAL 153
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 4-165 6.23e-13

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: 63.15  E-value: 6.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535   4 HIQVVPDKCRACRRCEVACiaahhgmsfkeAMKHRDVLVARVQVVKAEGFKTT----------VRCHQCDPAPCCNVCPT 73
Cdd:cd10553    4 YLYHDSKRCIGCLACEVHC-----------KVKNNLPVGPRLCRIFAVGPKMVggkprlkfvyMSCFHCENPWCVKACPT 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  74 GALQQ-EEDGRITMRVQFCVACKMCIAACPYGTISLDtigmpdlsgsdaetlaqrARREVAVRCDMCRAwREENGKKiTA 152
Cdd:cd10553   73 GAMQKrEKDGIVYVDQELCIGCKACIEACPWGIPQWN------------------PATGKVVKCDYCMD-RIDQGLK-PA 132

                        170
                 ....*....|...
gi 495957535 153 CMEACPVRALSMV 165
Cdd:cd10553  133 CVTGCTTHALSFV 145
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 11-162 1.44e-12

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: 63.39  E-value: 1.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  11 KCRACRRCEVACIAAHHG----MSFKEAMKHRDVLVAR----VQVVKAEGFKTTVRC--HQC----DPApCCNVCPTGAL 76
Cdd:cd10561    8 RCIGCRACEVACKEWNGLpaedTAFGPGWDNPRDLSAKtytvIKRYEVETGGKGFVFvkRQCmhclDPA-CVSACPVGAL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  77 QQEEDGRITMRVQFCVACKMCIAACPYgtisldtiGMPDLSGSDAETLAQrarrevavRCDMCRAwREENGkKITACMEA 156
Cdd:cd10561   87 RKTPEGPVTYDEDKCIGCRYCMVACPF--------NIPKYEWDSANPKIR--------KCTMCYD-RLKEG-KQPACVEA 148


                 ....*.
gi 495957535 157 CPVRAL 162
Cdd:cd10561  149 CPTGAL 154
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 9-168 4.66e-12

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


Pssm-ID: 319889 [Multi-domain]  Cd Length: 138  Bit Score: 60.78  E-value: 4.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535   9 PDKCRACRRCEVACIAAHHGMSfkeAMKHRDVLVARVQVVKAegfkttvrCHQCDPAPCCNVCPTGALQQEEDGRITMRV 88
Cdd:cd16367   18 LDRCIRCDNCEKACADTHDGHS---RLDRNGLRFGNLLVPTA--------CRHCVDPVCMIGCPTGAIHRDDGGEVVISD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  89 QfCVACKMCIAACPYGTISLdtigmpdlsgsdaetlaqrarrEVAVRCDMCRAWREengkkiTACMEACPVRALSMVEPD 168
Cdd:cd16367   87 A-CCGCGNCASACPYGAIQM----------------------VRAVKCDLCAGYAG------PACVSACPTGAAIRVNPE 137
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 9-162 7.92e-12

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: 60.78  E-value: 7.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535   9 PDKCRACRRCEVACIAAHHGMSFKEAMK-----HRDV-----LVARVQVVKAEGFKTT-----VRCHQCDPAPCCNVCPT 73
Cdd:cd10562    5 TSKCTACRGCQVACKQWNQLPAEKTPFTgsyqnPPDLtpntwTLIRFYEHEEDNGGIRwlfrkRQCMHCTDAACVKVCPT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  74 GALQQEEDGRITMRVQFCVACKMCIAACPYGTISLDtigmpdlsgsdaetlaqrARREVAVRCDMCRAwREENGKKiTAC 153
Cdd:cd10562   85 GALYKTENGAVVVDEDKCIGCGYCVAACPFDVPRYD------------------ETTNKITKCTLCFD-RIENGMQ-PAC 144


                 ....*....
gi 495957535 154 MEACPVRAL 162
Cdd:cd10562  145 VKTCPTGAL 153
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 10-168 9.43e-11

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: 58.11  E-value: 9.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  10 DKCRACRRCEVACIAAHHGMSFKEAMK------HRDVLVARV---QVVKAEGFKTTVRCHQCDPAPCCNVCPTGALQQEE 80
Cdd:cd10552    6 AKCNGCYNCFLACKDEHVGNDWPGYAApqprhgHFWMRILRRergQYPKVDVAYLPVPCNHCDNAPCIKAAKDGAVYKRD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  81 DGRITMRVQFCVACKMCIAACPYGTISLDtigmpdlsgsDAETLAQrarrevavRCDMCrAWREENGKKITACMEACPVR 160
Cdd:cd10552   86 DGIVIIDPEKAKGQKQLVDACPYGAIYWN----------EELQVPQ--------KCTFC-AHLLDDGWKEPRCVQACPTG 146


                 ....*...
gi 495957535 161 ALSMVEPD 168
Cdd:cd10552  147 ALRFGKLE 154
PRK09898 PRK09898
ferredoxin-like protein;
11-166 1.87e-10

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 57.92  E-value: 1.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  11 KCRACRRCEVACIAAHHGM--SFKEAMK-HRDVLVARVQVVKAEGFK-----TTVRCHQCDPAPCCNVCPTGALQ-QEED 81
Cdd:PRK09898  67 RCTGCHRCEISCTNFNDGSvgTFFSRIKiHRNYFFGDNGVGSGGGLYgdlnyTADTCRQCKEPQCMNVCPIGAITwQQKE 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  82 GRITMRVQFCVACKMCIAACPYgtisldtiGMPDLSGSDAETlaqrarrevaVRCDMCrawreengkkiTACMEACPVRA 161
Cdd:PRK09898 147 GCITVDHKRCIGCSACTTACPW--------MMATVNTESKKS----------SKCVLC-----------GECANACPTGA 197


                 ....*
gi 495957535 162 LSMVE 166
Cdd:PRK09898 198 LKIIE 202
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 11-158 5.22e-10

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: 56.63  E-value: 5.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  11 KCRACRRCEVACIAAHH---------GMSFKeamKHRDV------LVARVQVVKAEGFKTTVR----------CHQCDPA 65
Cdd:cd10560    8 ICIGCKACEVACKQWNQlpadgydfsGMSYD---NTGDLsastwrHVKFIERPTEDGPANEGGdlqwlfmsdvCKHCTDA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  66 PCCNVCPTGALQQEEDGRITMRVQFCVACKMCIAACPYGTIsldtigmpdlsgsdaetlAQRARREVAVRCDMCraWREE 145
Cdd:cd10560   85 GCLEACPTGAIFRTEFGTVYIQPDICNGCGYCVAACPFGVI------------------DRNEETGRAHKCTLC--YDRL 144

                        170
                 ....*....|...
gi 495957535 146 NGKKITACMEACP 158
Cdd:cd10560  145 KDGLEPACAKACP 157
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 9-106 1.30e-09

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: 53.88  E-value: 1.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535   9 PDKCRACRRCEVACIAAHhgmsFKEAMKHRdvlvARVQVVKAEGFKTTVRCHQCdpAPCCNVCPTGALQQEEDGRITMRV 88
Cdd:cd16372    7 PEKCIGCLQCEEACSKTF----FKEEDREK----SCIRITETEGGYAINVCNQC--GECIDVCPTGAITRDANGVVMINK 76

                         90
                 ....*....|....*...
gi 495957535  89 QFCVACKMCIAACPYGTI 106
Cdd:cd16372   77 KLCVGCLMCVGFCPEGAM 94
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 58-163 5.02e-09

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: 53.58  E-value: 5.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  58 RCHQCDPAPCCNVCPTGALQQEEDGRITMRVQFCVACKMCIAACPYGT------ISLDTIGMPDLSGSDaetlaqrarre 131
Cdd:cd16368   90 RCMHCDNPPCAKLCPFGAARKTPEGAVYIDDDLCFGGAKCRDVCPWHIpqrqagVGIYLHLAPEYAGGG----------- 158

                         90       100       110
                 ....*....|....*....|....*....|..
gi 495957535 132 VAVRCDMCRAwREENGKKiTACMEACPVRALS 163
Cdd:cd16368  159 VMYKCDLCKD-LLAQGKP-PACIEACPKGAQY 188
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 9-177 9.81e-09

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: 52.39  E-value: 9.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535   9 PDKCRACRRCEVAC--IAAHHGMSfkeaMKHRDvLVARVQVVKAegfkTTVRCHQCDPAPCCNVCPTGALQQEEDGRI-T 85
Cdd:cd16369    8 PSRCIGCRACVAACreCGTHRGKS----MIHVD-YIDRGESTQT----APTVCMHCEDPTCAEVCPADAIKVTEDGVVqS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  86 MRVQFCVACKMCIAACPYGTISLDTigmpdlsgsdaetlaqraRREVAVRCDMCRAwREENGKKiTACMEACPVRALSMV 165
Cdd:cd16369   79 ALKPRCIGCSNCVNACPFGVPKYDE------------------ERNLMMKCDMCYD-RTSVGKA-PMCASVCPSGALFYG 138

                        170
                 ....*....|..
gi 495957535 166 EPDGTVVEVPQP 177
Cdd:cd16369  139 TREEIQALRPGS 150
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 9-109 1.39e-08

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


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 51.12  E-value: 1.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535   9 PDKCRACRRCEVACIAAHHGMSFKEAmkhrdvlvARVQVVKAEGFK---TTVRCHQCDPAPCCNVCPTGALQQEEDGRIT 85
Cdd:cd16370    8 MERCIGCYSCMLACSRRVHKSASLSK--------SAIRVRTRGGLEggfTVVVCRACEDPPCAEACPTGALEPRKGGGVV 79

                         90       100
                 ....*....|....*....|....
gi 495957535  86 MRVQFCVACKMCIAACPYGTISLD 109
Cdd:cd16370   80 LDKEKCIGCGNCVKACIVGAIFWD 103
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 9-163 2.62e-08

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: 51.62  E-value: 2.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535   9 PDKCRACRRCEVAC---------IAAHHGMSFKEA---------MKHRDVlvarVQVVKAEGFKTTVRCHQCDPAPCCNV 70
Cdd:cd10558    6 VSKCIGCKACQVACkewndlraeVGHNVGTYQNPAdlspetwtlMKFREV----EDNGKLEWLIRKDGCMHCADPGCLKA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  71 CPT-GALQQEEDGRITMRVQFCVACKMCIAACPYGTisldtigmPDLSGSDAEtlaqrarrevAVRCDMCRAwREENGKK 149
Cdd:cd10558   82 CPSpGAIVQYANGIVDFQSDKCIGCGYCIKGCPFDI--------PRISKDDNK----------MYKCTLCSD-RVSVGLE 142

                        170
                 ....*....|....
gi 495957535 150 iTACMEACPVRALS 163
Cdd:cd10558  143 -PACVKTCPTGALH 155
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 59-166 3.29e-08

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: 49.55  E-value: 3.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535   59 CHQCDPAPCCNVCPTGAL-QQEEDGRITMRVQFCVACKMCIAACPYGTISLDtigmpDLSGsdaetlaqrarreVAVRCD 137
Cdd:pfam13247  10 CRHCLNPPCKASCPVGAIyKDEETGAVLLDEKTCRGWRECVSACPYNIPRYN-----DETG-------------KAEKCD 71

                          90       100
                  ....*....|....*....|....*....
gi 495957535  138 MCRAwREENGKKiTACMEACPVRALSMVE 166
Cdd:pfam13247  72 MCYD-RVEAGLL-PACVQTCPTGAMNFGD 98
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 58-172 1.21e-07

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 48.55  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  58 RCHQCdpAPCCNVCPTGALQQEEDGRITMRVQF----CVACKMCIAACPYGTISLDTIGMPDLSgsdaetlaqrARREVA 133
Cdd:cd10549    7 KCIGC--GICVKACPTDAIELGPNGAIARGPEIdedkCVFCGACVEVCPTGAIELTPEGKEYVP----------KEKEAE 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 495957535 134 VRCDMCRawreengkKITACMEACPVRALSMVEPDGTVV 172
Cdd:cd10549   75 IDEEKCI--------GCGLCVKVCPVDAITLEDELEIVI 105
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
59-103 1.60e-07

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 49.87  E-value: 1.60e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 495957535  59 CHQCDPAPCCNVCPTGALQQEEDGRITMRVQFCVACKMCIAACPY 103
Cdd:PRK14993 100 CNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPY 144
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 10-170 2.14e-06

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: 46.42  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  10 DKCRACRRCEVACIAAHHGMSFKEAMKHRDVLVA---------RVQVVKAEG-----FKTTVRCHQCDPAPCCNVCPTGA 75
Cdd:cd16365   10 NKCIGCQTCTVACKNAWTYRKGQEYMWWNNVETKpgggypqdwEVKTIDNGGntrffFYLQRLCNHCTNPACLAACPRGA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  76 L-QQEEDGRITMRVQFCVACKMCIAACPYGTISLdtigmpdlsgsdaetlaqRARREVAVRCDMCRAWREenGKKITACM 154
Cdd:cd16365   90 IyKREEDGIVLIDQKRCRGYRKCVEQCPYKKIYF------------------NGLSRVSEKCIACYPRIE--GGDPTRCM 149

                        170
                 ....*....|....*...
gi 495957535 155 EACP--VRALSMVEPDGT 170
Cdd:cd16365  150 SACVgrIRLQGFLDDNPK 167
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
34-161 6.56e-06

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 45.43  E-value: 6.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  34 AMKHRDVLVARVQVVKAEgfkttvrCHQC-DPApCCNVCPTGALQQE-EDGRITMRVQFCVACKMCIAACPYGTISLDTi 111
Cdd:PRK10882  94 TGVNKDQEENGYAYIKKQ-------CMHCvDPN-CVSVCPVSALTKDpKTGIVHYDKDVCTGCRYCMVACPFNVPKYDY- 164

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495957535 112 gmpdlsgsdAETLAQrarrevAVRCDMCRAWREE--NGKKITACMEACPVRA 161
Cdd:PRK10882 165 ---------NNPFGA------IHKCELCNQKGVErlDKGGLPGCVEVCPTGA 201
FixX COG2440
Ferredoxin-like protein FixX [Energy production and conversion];
62-107 1.37e-05

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


Pssm-ID: 441981 [Multi-domain]  Cd Length: 87  Bit Score: 42.11  E-value: 1.37e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 495957535  62 CDPAPCCNVCPTGALQQEEDGRITMRVQFCVACKMCIAACPYGTIS 107
Cdd:COG2440   27 CLAKPCTRYCPAGVYEIVGDGRLQINYENCLECGTCRIKCPTQNIT 72
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
9-107 1.52e-05

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 44.63  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535   9 PDKCRACRRCEVACIAAHhgmSFKEAMKHRDVLVARVQVVKAEGfkttvRCHQCDPapCCNVCPTGALQqEEDGRITMRV 88
Cdd:COG4624   51 CPRCCLCCCCCCRCCVAI---SCIQVRGIIIIDKRGPSIIRDKE-----KCKNCYP--CVRACPVKAIK-VDDGKAEIDE 119

                         90
                 ....*....|....*....
gi 495957535  89 QFCVACKMCIAACPYGTIS 107
Cdd:COG4624  120 EKCISCGQCVAVCPFGAIT 138
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
91-164 1.61e-05

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 44.47  E-value: 1.61e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495957535  91 CVACKMCIAACPYGTISLDTIGMPdlsgsdaetlaqrarrEV-AVRCDMCrawreenGkkitACMEACPVRALSM 164
Cdd:COG1148  498 CTGCGRCVEVCPYGAISIDEKGVA----------------EVnPALCKGC-------G----TCAAACPSGAISL 545
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
58-108 3.94e-05

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 43.31  E-value: 3.94e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495957535  58 RCHQCdpAPCCNVCPTGALQQEEDGRITMRVQFCVACKMCIAACPYGTISL 108
Cdd:COG1148  497 KCTGC--GRCVEVCPYGAISIDEKGVAEVNPALCKGCGTCAAACPSGAISL 545
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 59-103 6.76e-05

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: 42.73  E-value: 6.76e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 495957535  59 CHQC-DPApCCNVCPTGAL-QQEEDGRITMRVQFCVACKMCIAACPY 103
Cdd:cd10557  179 CNHClNPA-CVAACPSGAIyKREEDGIVLIDQDRCRGWRMCVSACPY 224
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 59-161 1.21e-04

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: 41.90  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  59 CHQCDPAPCCNVCPTGAL-QQEEDGRITMRVQFCVACKMCIAACPYGTISLDTIgmpdlsgsdaetlaqrarREVAVRCD 137
Cdd:cd10555  133 CNHCTNPACLAACPRKAIyKREEDGIVLVDQDRCRGYRYCVEACPYKKIYFNPV------------------EQKSEKCI 194

                         90       100
                 ....*....|....*....|....
gi 495957535 138 MCRAWREEngKKITACMEACPVRA 161
Cdd:cd10555  195 FCYPRIEK--GVAPACARQCVGRI 216
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 67-108 2.67e-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: 37.79  E-value: 2.67e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 495957535  67 CCNVCPTGALQQEEDGRITMRVQFCVACKMCIAACPYGTISL 108
Cdd:COG1149   19 CVEVCPEGAIKLDDGGAPVVDPDLCTGCGACVGVCPTGAITL 60
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 57-166 3.72e-04

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 39.16  E-value: 3.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  57 VRCHQCdpapcCNVCPTGALQQE--EDG-------RITMRVQFCVAC-KMCIAACPYGTISLDTIGmpdlsgsdaetlAQ 126
Cdd:cd16373   17 IRCGLC-----VEACPTGVIQPAglEDGleggrtpYLDPREGPCDLCcDACVEVCPTGALRPLDLE------------EQ 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 495957535 127 RARREVAV-RCDMCRAWREenGKKITACMEACPVRALSMVE 166
Cdd:cd16373   80 KVKMGVAViDKDRCLAWQG--GTDCGVCVEACPTEAIAIVL 118
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
91-166 3.77e-04

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 39.48  E-value: 3.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  91 CVACKMCIAACPYGTISLDTIGMPDlsgsdaetlaqrARREVAV------RCDMCRawreengkkitACMEACPVRALSM 164
Cdd:PRK05888  60 CIACKLCAAICPADAITIEAAERED------------GRRRTTRydinfgRCIFCG-----------FCEEACPTDAIVE 116


                 ..
gi 495957535 165 VE 166
Cdd:PRK05888 117 TP 118
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
57-110 9.27e-04

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 38.89  E-value: 9.27e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495957535  57 VRCHQCDpapccNVCPTGAlqqeeDGRITMRVQF-CVACKMCIAACPYGTISLDT 110
Cdd:COG0348  213 IDCGLCV-----KVCPMGI-----DIRKGEINQSeCINCGRCIDACPKDAIRFSS 257
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 67-111 2.49e-03

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 35.41  E-value: 2.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 495957535  67 CCNVCPTGALQQEeDGRITMRVQFCVACKMCIAACPYGTISLDTI 111
Cdd:COG2221   23 CVAVCPTGAISLD-DGKLVIDEEKCIGCGACIRVCPTGAIKGEKP 66
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 1-108 2.65e-03

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 36.61  E-value: 2.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535   1 MLEHIQVVPDKCRACRRCEVACIaahhgmsfKEAMKhrdvLVARVQVVKAEGFKTTVRCHQCDP-APCCNVCPTGALQQE 79
Cdd:cd10549   31 IARGPEIDEDKCVFCGACVEVCP--------TGAIE----LTPEGKEYVPKEKEAEIDEEKCIGcGLCVKVCPVDAITLE 98

                         90       100
                 ....*....|....*....|....*....
gi 495957535  80 EDGRITMRVQFCVACKMCIAACPYGTISL 108
Cdd:cd10549   99 DELEIVIDKEKCIGCGICAEVCPVNAIKL 127
PRK13795 PRK13795
hypothetical protein; Provisional
 87-159 3.06e-03

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 37.67  E-value: 3.06e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495957535  87 RVQFCVACKMCIAACPYGTISLDtigmpdlsgsdaetlAQRARREVAV-RCDMCRawreengkkitACMEACPV 159
Cdd:PRK13795 579 RAAECVGCGVCVGACPTGAIRIE---------------EGKRKISVDEeKCIHCG-----------KCTEVCPV 626
PRK13795 PRK13795
hypothetical protein; Provisional
 30-102 4.45e-03

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 37.28  E-value: 4.45e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495957535  30 SFKEAMKHRDVLVARVQVVKAegfkttVRCHQCDPapCCNVCPTGALQQEEDGR-ITMRVQFCVACKMCIAACP 102
Cdd:PRK13795 560 SEDKEAAASLFKDAARLLRRA------AECVGCGV--CVGACPTGAIRIEEGKRkISVDEEKCIHCGKCTEVCP 625
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
58-117 5.01e-03

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 34.71  E-value: 5.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495957535  58 RCHQCDPapCCNVCPTGALQqEEDGRITMRVQFCVACKMCIAACPYGTISLDTIGMPDLS 117
Cdd:COG2768   12 KCIGCGA--CVKVCPVGAIS-IEDGKAVIDPEKCIGCGACIEVCPVGAIKIEWEEDEEFQ 68
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 58-115 5.88e-03

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 37.07  E-value: 5.88e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495957535  58 RCH--QCDpAPCCNVCP---TGA---LQQEEDGRITMRVQFCVACKMCIAACPYGTISLdtIGMPD 115
Cdd:COG1245   11 RCQpkKCN-YECIKYCPvnrTGKeaiEIDEDDGKPVISEELCIGCGICVKKCPFDAISI--VNLPE 73
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 59-103 7.64e-03

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: 36.28  E-value: 7.64e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 495957535  59 CHQCDPAPCCNVCPTGAL-QQEEDGRITMRVQFCVACKMCIAACPY 103
Cdd:cd10556  141 CNHCTYPACLAACPRKAIyKREEDGIVLIDQERCRGYRECVEACPY 186
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
9-87 9.79e-03

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 36.08  E-value: 9.79e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495957535   9 PDKCRACRRCEVACIAAHHgmsfkEAMKHRDVLVARVQVVKAEgfktTVRCHQcdpapCCNVCPTgalqqeeDGRITMR 87
Cdd:PRK08318 341 QDKCIGCGRCYIACEDTSH-----QAIEWDEDGTRTPEVIEEE----CVGCNL-----CAHVCPV-------EGCITMG 398
 
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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