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Conserved domains on  [gi|2787368098|ref|WP_370455141|]
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MULTISPECIES: 4Fe-4S dicluster domain-containing protein [unclassified Eggerthella]

Protein Classification

4Fe-4S dicluster domain-containing protein( domain architecture ID 11586797)

4Fe-4S dicluster domain-containing protein such as Salmonella enterica thiosulfate reductase electron transfer subunit PhsB, a component of the PhsABC thiosulfate reductase that catalyzes the reduction of thiosulfate to sulfite and hydrogen sulfide, with menaquinol as the sole electron donor

Gene Ontology:  GO:0016491|GO:0046872|GO:0051539
SCOP:  3000020

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 6-206 3.94e-102

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: 292.51  E-value: 3.94e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   6 FAIDTKRCIGCHTCSVSCRIENNLPEGTWWNRVLTKGgesmdtpEGTFPDATMSYITVACQHCENPACVKVCPVGATYKD 85
Cdd:cd10551     1 MVIDLRKCIGCGACVVACKAENNVPPGVFRNRVLEYE-------VGEYPNVKRTFLPVLCNHCENPPCVKVCPTGATYKR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  86 PDtGVVRQDYDKCIGCRMCMAACPYvGVRSFNWEEPAHYIgfdsgdaDVPEHQKHTVEKCTFCWHRLAKGEDPMCVKTCL 165
Cdd:cd10551    74 ED-GIVLVDYDKCIGCRYCMAACPY-GARYFNPEEPHEFG-------EVPVRPKGVVEKCTFCYHRLDEGLLPACVEACP 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2787368098 166 ARARVWGDLDDPESEVSKLIRERKVMQLLPEKDTKPSVYYL 206
Cdd:cd10551   145 TGARIFGDLDDPNSEVSKLLAERRAYVLKPELGTKPKVYYI 185
 
Name Accession Description Interval E-value
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 6-206 3.94e-102

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: 292.51  E-value: 3.94e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   6 FAIDTKRCIGCHTCSVSCRIENNLPEGTWWNRVLTKGgesmdtpEGTFPDATMSYITVACQHCENPACVKVCPVGATYKD 85
Cdd:cd10551     1 MVIDLRKCIGCGACVVACKAENNVPPGVFRNRVLEYE-------VGEYPNVKRTFLPVLCNHCENPPCVKVCPTGATYKR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  86 PDtGVVRQDYDKCIGCRMCMAACPYvGVRSFNWEEPAHYIgfdsgdaDVPEHQKHTVEKCTFCWHRLAKGEDPMCVKTCL 165
Cdd:cd10551    74 ED-GIVLVDYDKCIGCRYCMAACPY-GARYFNPEEPHEFG-------EVPVRPKGVVEKCTFCYHRLDEGLLPACVEACP 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2787368098 166 ARARVWGDLDDPESEVSKLIRERKVMQLLPEKDTKPSVYYL 206
Cdd:cd10551   145 TGARIFGDLDDPNSEVSKLLAERRAYVLKPELGTKPKVYYI 185
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 1-206 1.41e-83

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 245.63  E-value: 1.41e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   1 MMRYGFAIDTKRCIGCHTCSVSCRIENNLPEGTWWNRVLTKggesmdtPEGTFPDATMSYITVACQHCENPACVKVCPVG 80
Cdd:COG0437     3 MKRYGMVIDLTKCIGCRACVVACKEENNLPVGVTWRRVRRY-------EEGEFPNVEWLFVPVLCNHCDDPPCVKVCPTG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  81 ATYKDPDtGVVRQDYDKCIGCRMCMAACPYvGVRSFNWEepahyigfdsgdadvpehqKHTVEKCTFCWHRLAKGEDPMC 160
Cdd:COG0437    76 ATYKRED-GIVLVDYDKCIGCRYCVAACPY-GAPRFNPE-------------------TGVVEKCTFCADRLDEGLLPAC 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2787368098 161 VKTCLARARVWGDLDDPESEVSKLIRERKVMQLLPEKDTKPSVYYL 206
Cdd:COG0437   135 VEACPTGALVFGDLDDPESEVSKRLAELPAYRLLPELGTKPSVYYL 180
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
3-206 1.97e-48

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 158.50  E-value: 1.97e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   3 RYGFAIDTKRCIGCHTCSVSCRIENNLPEGTWWNRVLtkggESMDTPEGTfPDATMSYITVACQHCENPACVKVCPVGAT 82
Cdd:PRK14993   43 RYAMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVN----QYQVQREGS-QEVTNVLLPRLCNHCDNPPCVPVCPVQAT 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  83 YKDPDtGVVRQDYDKCIGCRMCMAACPYvgvrsfnweepahyigfdsgDADVPEHQKHTVEKCTFCWHRLAKGEDPMCVK 162
Cdd:PRK14993  118 FQRED-GIVVVDNKRCVGCAYCVQACPY--------------------DARFINHETQTADKCTFCVHRLEAGLLPACVE 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2787368098 163 TCLARARVWGDLDDPESEVSKLIRERK--VMQLLPEKDTKPSVYYL 206
Cdd:PRK14993  177 SCVGGARIIGDIKDPHSRIATMLHQHRdaIKVLKPENGTSPHVFYL 222
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 65-174 7.66e-24

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: 90.77  E-value: 7.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  65 CQHCENPACVKVCPVGATYKDPDTGVVRQDYDKCIGCRMCMAACPYVGVRsFNWEepahyigfdsgdadvpehqKHTVEK 144
Cdd:pfam13247  10 CRHCLNPPCKASCPVGAIYKDEETGAVLLDEKTCRGWRECVSACPYNIPR-YNDE-------------------TGKAEK 69

                          90       100       110
                  ....*....|....*....|....*....|
gi 2787368098 145 CTFCWHRLAKGEDPMCVKTCLARARVWGDL 174
Cdd:pfam13247  70 CDMCYDRVEAGLLPACVQTCPTGAMNFGDR 99
FeFe_hydrog_B1 TIGR04105
[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups.
 73-110 1.58e-08

[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups.


Pssm-ID: 274983 [Multi-domain]  Cd Length: 462  Bit Score: 53.75  E-value: 1.58e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2787368098  73 CVKVCPVGATYKDPDtGVVRQDYDKCIGCRMCMAACPY 110
Cdd:TIGR04105 166 CEKACPVGAISSDED-GRAVIDYDKCISCGACMVACPF 202
 
Name Accession Description Interval E-value
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 6-206 3.94e-102

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: 292.51  E-value: 3.94e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   6 FAIDTKRCIGCHTCSVSCRIENNLPEGTWWNRVLTKGgesmdtpEGTFPDATMSYITVACQHCENPACVKVCPVGATYKD 85
Cdd:cd10551     1 MVIDLRKCIGCGACVVACKAENNVPPGVFRNRVLEYE-------VGEYPNVKRTFLPVLCNHCENPPCVKVCPTGATYKR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  86 PDtGVVRQDYDKCIGCRMCMAACPYvGVRSFNWEEPAHYIgfdsgdaDVPEHQKHTVEKCTFCWHRLAKGEDPMCVKTCL 165
Cdd:cd10551    74 ED-GIVLVDYDKCIGCRYCMAACPY-GARYFNPEEPHEFG-------EVPVRPKGVVEKCTFCYHRLDEGLLPACVEACP 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2787368098 166 ARARVWGDLDDPESEVSKLIRERKVMQLLPEKDTKPSVYYL 206
Cdd:cd10551   145 TGARIFGDLDDPNSEVSKLLAERRAYVLKPELGTKPKVYYI 185
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 1-206 1.41e-83

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 245.63  E-value: 1.41e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   1 MMRYGFAIDTKRCIGCHTCSVSCRIENNLPEGTWWNRVLTKggesmdtPEGTFPDATMSYITVACQHCENPACVKVCPVG 80
Cdd:COG0437     3 MKRYGMVIDLTKCIGCRACVVACKEENNLPVGVTWRRVRRY-------EEGEFPNVEWLFVPVLCNHCDDPPCVKVCPTG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  81 ATYKDPDtGVVRQDYDKCIGCRMCMAACPYvGVRSFNWEepahyigfdsgdadvpehqKHTVEKCTFCWHRLAKGEDPMC 160
Cdd:COG0437    76 ATYKRED-GIVLVDYDKCIGCRYCVAACPY-GAPRFNPE-------------------TGVVEKCTFCADRLDEGLLPAC 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2787368098 161 VKTCLARARVWGDLDDPESEVSKLIRERKVMQLLPEKDTKPSVYYL 206
Cdd:COG0437   135 VEACPTGALVFGDLDDPESEVSKRLAELPAYRLLPELGTKPSVYYL 180
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 5-168 1.56e-51

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: 162.73  E-value: 1.56e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   5 GFAIDTKRCIGCHTCSVSCRIENNLPEGTWWNRVLTKGGesmdtpeGTFPDATMSYITVACQHCENPACVKVCPVGATYK 84
Cdd:cd16371     1 GFYFDQERCIGCKACEIACKDKNDLPPGVNWRRVYEYEG-------GEFPEVFAYFLSMSCNHCENPACVKVCPTGAITK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  85 DPDtGVVRQDYDKCIGCRMCMAACPYvGVRSFNweepahyigfdsgdadvpeHQKHTVEKCTFCWHRLAKGEDPMCVKTC 164
Cdd:cd16371    74 RED-GIVVVDQDKCIGCGYCVWACPY-GAPQYN-------------------PETGKMDKCDMCVDRLDEGEKPACVAAC 132


                  ....
gi 2787368098 165 LARA 168
Cdd:cd16371   133 PTRA 136
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
3-206 1.97e-48

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 158.50  E-value: 1.97e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   3 RYGFAIDTKRCIGCHTCSVSCRIENNLPEGTWWNRVLtkggESMDTPEGTfPDATMSYITVACQHCENPACVKVCPVGAT 82
Cdd:PRK14993   43 RYAMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVN----QYQVQREGS-QEVTNVLLPRLCNHCDNPPCVPVCPVQAT 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  83 YKDPDtGVVRQDYDKCIGCRMCMAACPYvgvrsfnweepahyigfdsgDADVPEHQKHTVEKCTFCWHRLAKGEDPMCVK 162
Cdd:PRK14993  118 FQRED-GIVVVDNKRCVGCAYCVQACPY--------------------DARFINHETQTADKCTFCVHRLEAGLLPACVE 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2787368098 163 TCLARARVWGDLDDPESEVSKLIRERK--VMQLLPEKDTKPSVYYL 206
Cdd:PRK14993  177 SCVGGARIIGDIKDPHSRIATMLHQHRdaIKVLKPENGTSPHVFYL 222
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 6-172 2.53e-44

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: 144.45  E-value: 2.53e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   6 FAIDTKRCIGCHTCSVSCRIENNLPEGTWWNRVltkggesmdtPEGTFPDATMSYITVACQHCENPACVKVCPVGATYKD 85
Cdd:cd04410     1 LVVDLDRCIGCGTCEVACKQEHGLRPGPDWSRI----------KVIEGGGLERAFLPVSCMHCEDPPCVKACPTGAIYKD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  86 PDtGVVRQDYDKCIGCRMCMAACPYvGVRSFNWEepahyigfdsgdadvpehqKHTVEKCTFCWHRLAKGEDPMCVKTCL 165
Cdd:cd04410    71 ED-GIVLIDEDKCIGCGSCVEACPY-GAIVFDPE-------------------PGKAVKCDLCGDRLDEGLEPACVKACP 129


                  ....*..
gi 2787368098 166 ARARVWG 172
Cdd:cd04410   130 TGALTFG 136
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 5-176 2.92e-42

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


Pssm-ID: 319883 [Multi-domain]  Cd Length: 196  Bit Score: 140.81  E-value: 2.92e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   5 GFAIDTKRCIGCHTCSVSCRIENNLPEGTwwnrvlTKGGESMDTPEGT--------------FPDATMSYITVACQHCEN 70
Cdd:cd10561     1 GVLYDTTRCIGCRACEVACKEWNGLPAED------TAFGPGWDNPRDLsaktytvikryeveTGGKGFVFVKRQCMHCLD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  71 PACVKVCPVGATYKDPdTGVVRQDYDKCIGCRMCMAACPYvGVRSFNWEEPAhyigfdsgdadvPEhqkhtVEKCTFCWH 150
Cdd:cd10561    75 PACVSACPVGALRKTP-EGPVTYDEDKCIGCRYCMVACPF-NIPKYEWDSAN------------PK-----IRKCTMCYD 135

                         170       180
                  ....*....|....*....|....*.
gi 2787368098 151 RLAKGEDPMCVKTCLARARVWGDLDD 176
Cdd:cd10561   136 RLKEGKQPACVEACPTGALLFGKREE 161
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 3-206 1.57e-38

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: 131.55  E-value: 1.57e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   3 RYGFAIDTKRCIGCHTCSVSCRIENNLPEGT---WWNRVLTKGG-------ESMDTPEGTFPdATMSYITVACQHCENPA 72
Cdd:cd16365     2 QFAAVFNLNKCIGCQTCTVACKNAWTYRKGQeymWWNNVETKPGggypqdwEVKTIDNGGNT-RFFFYLQRLCNHCTNPA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  73 CVKVCPVGATYKDPDTGVVRQDYDKCIGCRMCMAACPYVGVRsFNWeepahyigfdsgdadvpehQKHTVEKCTFCWHRL 152
Cdd:cd16365    81 CLAACPRGAIYKREEDGIVLIDQKRCRGYRKCVEQCPYKKIY-FNG-------------------LSRVSEKCIACYPRI 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2787368098 153 AKGEDPMCVKTCLARARVWGDLDD-PESEVSKLIRERKV-MQLLPEKDTKPSVYYL 206
Cdd:cd16365   141 EGGDPTRCMSACVGRIRLQGFLDDnPKSPVTKLIRHWKVaLPLHPEYGTEPNIYYV 196
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 8-205 3.07e-38

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: 133.97  E-value: 3.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   8 IDTKRCIGCHTCSVSCRIENNLPEGT---WWNRVLTKGG-------ESM------------------------------- 46
Cdd:cd10555     9 MDLNKCIGCQTCTVACKTLWTNRNGReymYWNNVETQPGkgypknwEKKgggfkdkgelkpgiiptledygvpweynhee 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  47 --------------------------DTPEGTFPDATMSYITVACQHCENPACVKVCPVGATYKDPDTGVVRQDYDKCIG 100
Cdd:cd10555    89 elfegkggrvrpspkgdptwgpnwdeDQGAGEYPNSYYFYLPRICNHCTNPACLAACPRKAIYKREEDGIVLVDQDRCRG 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098 101 CRMCMAACPYvGVRSFNweepahyigfdsgdadvpeHQKHTVEKCTFCWHRLAKGEDPMCVKTCLARARVWGDLDDPESE 180
Cdd:cd10555   169 YRYCVEACPY-KKIYFN-------------------PVEQKSEKCIFCYPRIEKGVAPACARQCVGRIRFVGYLDDEESP 228

                         250       260
                  ....*....|....*....|....*.
gi 2787368098 181 VSKLIRERKV-MQLLPEKDTKPSVYY 205
Cdd:cd10555   229 VYKLVKKWKVaLPLHPEYGTEPNVFY 254
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 6-206 2.32e-34

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: 120.51  E-value: 2.32e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   6 FAIDTKRCIGCHTCSVSCRIE---NNLP--------EGTWWNRVLTKggesmdtPEGTFPDATMSYITVACQHCENPACV 74
Cdd:cd10552     1 LVIDVAKCNGCYNCFLACKDEhvgNDWPgyaapqprHGHFWMRILRR-------ERGQYPKVDVAYLPVPCNHCDNAPCI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  75 KVCPVGATYKDPDtGVVRQDYDKCIGCRMCMAACPYvGVRSFNWEEpahyigfdsgdaDVPehqkhtvEKCTFCWHRLAK 154
Cdd:cd10552    74 KAAKDGAVYKRDD-GIVIIDPEKAKGQKQLVDACPY-GAIYWNEEL------------QVP-------QKCTFCAHLLDD 132

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2787368098 155 GED-PMCVKTCLARARVWGDLDDPESEVSKLIRERKVMQllPEKDTKPSVYYL 206
Cdd:cd10552   133 GWKePRCVQACPTGALRFGKLEDEEMAAKAAEEGLEVLH--PELGTKPRVYYK 183
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 3-168 4.12e-33

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: 115.92  E-value: 4.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   3 RYGFAIDTKRCIGCHTCSVSCRIENNLPEGTWWNRVLTKGgesmdtPEGTFPDATMSYITVACQHCENPACVKVCPVGAT 82
Cdd:cd10553     2 KYYLYHDSKRCIGCLACEVHCKVKNNLPVGPRLCRIFAVG------PKMVGGKPRLKFVYMSCFHCENPWCVKACPTGAM 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  83 YKDPDTGVVRQDYDKCIGCRMCMAACPYvGVRSFNWEEpahyigfdsgdadvpehqkHTVEKCTFCWHRLAKGEDPMCVK 162
Cdd:cd10553    76 QKREKDGIVYVDQELCIGCKACIEACPW-GIPQWNPAT-------------------GKVVKCDYCMDRIDQGLKPACVT 135


                  ....*.
gi 2787368098 163 TCLARA 168
Cdd:cd10553   136 GCTTHA 141
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 6-172 2.64e-32

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: 114.42  E-value: 2.64e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   6 FAIDTKRCIGCHTCSVSCRIENNLPEG--------------TW--WNRVLTKGGEsmdTPEGtfpDATMSYITVACQHCE 69
Cdd:cd16366     1 FLVDTSRCTGCRACQVACKQWNGLPAEkteftgsyqnppdlTAhtWTLVRFYEVE---KPGG---DLSWLFRKDQCMHCT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  70 NPACVKVCPVGATYKDPdTGVVRQDYDKCIGCRMCMAACPYvGVRSFNWEEPahyigfdsgdadvpehqkhTVEKCTFCW 149
Cdd:cd16366    75 DAGCLAACPTGAIIRTE-TGTVVVDPETCIGCGYCVNACPF-DIPRFDEETG-------------------RVAKCTLCY 133

                         170       180
                  ....*....|....*....|...
gi 2787368098 150 HRLAKGEDPMCVKTCLARARVWG 172
Cdd:cd16366   134 DRISNGLQPACVKTCPTGALTFG 156
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
9-172 3.17e-30

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 113.23  E-value: 3.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   9 DTKRCIGCHTCSVSCRIENNLP-----EGTWWN--------RVLTK-----GGESMDTPEGTFpdatmSYITVACQHCEN 70
Cdd:PRK10882   43 DSTLCVGCQACVTKCQEINFPErnpqgEQTWDNpdklspytNNIIKvwksgTGVNKDQEENGY-----AYIKKQCMHCVD 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  71 PACVKVCPVGATYKDPDTGVVRQDYDKCIGCRMCMAACPYvGVRSFNWEEPAHYIGfdsgdadvpehqkhtveKCTFCWH 150
Cdd:PRK10882  118 PNCVSVCPVSALTKDPKTGIVHYDKDVCTGCRYCMVACPF-NVPKYDYNNPFGAIH-----------------KCELCNQ 179

                         170       180
                  ....*....|....*....|....*.
gi 2787368098 151 ----RLAKGEDPMCVKTCLARARVWG 172
Cdd:PRK10882  180 kgveRLDKGGLPGCVEVCPTGAVIFG 205
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 8-176 1.20e-29

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: 107.39  E-value: 1.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   8 IDTKRCIGCHTCSVSCRIENNLPEgtwwnrVLTKGGESMDTPEGTFPDaTMSYITV-----------------ACQHCEN 70
Cdd:cd10562     3 VDTSKCTACRGCQVACKQWNQLPA------EKTPFTGSYQNPPDLTPN-TWTLIRFyeheednggirwlfrkrQCMHCTD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  71 PACVKVCPVGATYKDpDTGVVRQDYDKCIGCRMCMAACPYvgvrsfnweepahyigfdsgdaDVPEHQKHT--VEKCTFC 148
Cdd:cd10562    76 AACVKVCPTGALYKT-ENGAVVVDEDKCIGCGYCVAACPF----------------------DVPRYDETTnkITKCTLC 132

                         170       180
                  ....*....|....*....|....*...
gi 2787368098 149 WHRLAKGEDPMCVKTCLARARVWGDLDD 176
Cdd:cd10562   133 FDRIENGMQPACVKTCPTGALTFGDRDE 160
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 5-176 6.57e-28

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: 104.78  E-value: 6.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   5 GFAIDTKRCIGCHTCSVSCRIENNLPE-----------------GTWWNRVltKGGESMDTPEGTFPDATMSYITV--AC 65
Cdd:cd10560     1 GFFTDTSICIGCKACEVACKQWNQLPAdgydfsgmsydntgdlsASTWRHV--KFIERPTEDGPANEGGDLQWLFMsdVC 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  66 QHCENPACVKVCPVGATYKDPDTGVVRQDyDKCIGCRMCMAACPYvGVRSFNweepahyigfdsgdadvpeHQKHTVEKC 145
Cdd:cd10560    79 KHCTDAGCLEACPTGAIFRTEFGTVYIQP-DICNGCGYCVAACPF-GVIDRN-------------------EETGRAHKC 137

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2787368098 146 TFCWHRLAKGEDPMCVKTCLARARVWGDLDD 176
Cdd:cd10560   138 TLCYDRLKDGLEPACAKACPTGSIQFGPLEE 168
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 53-205 2.80e-27

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: 106.29  E-value: 2.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  53 FPDATMSYITVACQHCENPACVKVCPVGATYKDPDTGVVRQDYDKCIGCRMCMAACPYVGVrSFNWeepahyigfDSGDA 132
Cdd:cd10557   167 FENTFMFYLPRICNHCLNPACVAACPSGAIYKREEDGIVLIDQDRCRGWRMCVSACPYKKV-YYNW---------KTGKS 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098 133 dvpehqkhtvEKCTFCWHRLAKGEDPMCVKTCLARARVWG----DLD--------------------------DPE---- 178
Cdd:cd10557   237 ----------EKCIFCYPRLEAGQPTVCSETCVGRIRYLGvllyDADrileaaavvpekdlveaqldiildpnDPEviaa 306

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2787368098 179 ----------------SEVSKLIRERKV-MQLLPEKDTKPSVYY 205
Cdd:cd10557   307 akangipdnwieaaqrSPVYKMVKEWKIaLPLHPEYRTLPMVFY 350
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 8-164 1.33e-26

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: 98.80  E-value: 1.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   8 IDTKRCIGCHTCSVSC---------------RIENNLPEGTwwnrvltkggesmdtpegtfpdatmsYITVACQHCENPA 72
Cdd:cd10550     3 VDPEKCTGCRTCELACslkhegvfnpslsriRVVRFEPEGL--------------------------DVPVVCRQCEDAP 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  73 CVKVCPVGATYKDPDTGVVRQDYDKCIGCRMCMAACPYvGVRSFNWEepahyigfdsgdadvpehqKHTVEKCTFCwhrl 152
Cdd:cd10550    57 CVEACPVGAISRDEETGAVVVDEDKCIGCGMCVEACPF-GAIRVDPE-------------------TGKAIKCDLC---- 112

                         170
                  ....*....|..
gi 2787368098 153 akGEDPMCVKTC 164
Cdd:cd10550   113 --GGDPACVKVC 122
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 8-189 2.95e-26

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: 100.15  E-value: 2.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   8 IDTKRCIGCHTCSVSCRIENNLPEgtwwnRVLTKGGeSMDTPegtfPDATMSYITV-------------------ACQHC 68
Cdd:cd10558     4 IDVSKCIGCKACQVACKEWNDLRA-----EVGHNVG-TYQNP----ADLSPETWTLmkfrevedngklewlirkdGCMHC 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  69 ENPACVKVCP-VGATYKDPDtGVVRQDYDKCIGCRMCMAACPYvgvrsfnweepahyigfdsgdaDVP--EHQKHTVEKC 145
Cdd:cd10558    74 ADPGCLKACPsPGAIVQYAN-GIVDFQSDKCIGCGYCIKGCPF----------------------DIPriSKDDNKMYKC 130

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2787368098 146 TFCWHRLAKGEDPMCVKTCLARARVWGDLDDPESEVSKLIRERK 189
Cdd:cd10558   131 TLCSDRVSVGLEPACVKTCPTGALHFGTKEDMLALAEKRVAALK 174
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 8-164 7.49e-25

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: 94.63  E-value: 7.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   8 IDTKRCIGCHTCSVSCRIENNLPEGTWWNRVLTKGGESMDTPEGTFPdatmSYITVACQHCENPACVKVCPVGATYKDPD 87
Cdd:cd10563     4 IDEEKCLGCKLCEVACAVAHSKSKDLIKAKLEKERPRPRIRVEESGG----RSFPLQCRHCDEPPCVKACMSGAMHKDPE 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2787368098  88 TGVVRQDYDKCIGCRMCMAACPYVGVRsfnweepahyigfdsgdadvPEHQKHTVEKCTFCWHRlakgEDPMCVKTC 164
Cdd:cd10563    80 TGIVIHDEEKCVGCWMCVMVCPYGAIR--------------------PDKERKVALKCDLCPDR----ETPACVEAC 132
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 51-169 2.45e-24

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


Pssm-ID: 440755 [Multi-domain]  Cd Length: 485  Bit Score: 99.11  E-value: 2.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  51 GTFPDATMSYITVACQHCENPACVKVCPVGATYKDPDTGVVRQDYDKCIGCRMCMAACPYVGVrSFNWEepahyigfdSG 130
Cdd:COG1140   168 FEFENTFMFYLPRICEHCLNPACVASCPSGAIYKREEDGIVLVDQDKCRGWRMCVSGCPYKKV-YFNWK---------TG 237

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2787368098 131 DAdvpehqkhtvEKCTFCWHRLAKGEDPMCVKTCLARAR 169
Cdd:COG1140   238 KA----------EKCIFCYPRIEAGQPTVCSETCVGRIR 266
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 8-176 3.48e-24

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: 92.72  E-value: 3.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   8 IDTKRCIGCHTCSVSCRIENNlpeGTWWNRVLTKGGEsmdtpegtfpdatmSYITVACQHCENPACVKVCPVGATYKDPD 87
Cdd:cd16374     3 VDPERCIGCRACEIACAREHS---GKPRISVEVVEDL--------------ASVPVRCRHCEDAPCMEVCPTGAIYRDED 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  88 tGVVRQDYDKCIGCRMCMAACPYvGVRSFnweepahyigfdsgdadvpEHQKHTVEKCTFCWHRLAKGEDPMCVKTCLAR 167
Cdd:cd16374    66 -GAVLVDPDKCIGCGMCAMACPF-GVPRF-------------------DPSLKVAVKCDLCIDRRREGKLPACVEACPTG 124


                  ....*....
gi 2787368098 168 ARVWGDLDD 176
Cdd:cd16374   125 ALKFGDIEE 133
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 65-174 7.66e-24

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: 90.77  E-value: 7.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  65 CQHCENPACVKVCPVGATYKDPDTGVVRQDYDKCIGCRMCMAACPYVGVRsFNWEepahyigfdsgdadvpehqKHTVEK 144
Cdd:pfam13247  10 CRHCLNPPCKASCPVGAIYKDEETGAVLLDEKTCRGWRECVSACPYNIPR-YNDE-------------------TGKAEK 69

                          90       100       110
                  ....*....|....*....|....*....|
gi 2787368098 145 CTFCWHRLAKGEDPMCVKTCLARARVWGDL 174
Cdd:pfam13247  70 CDMCYDRVEAGLLPACVQTCPTGAMNFGDR 99
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 6-180 1.44e-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: 92.07  E-value: 1.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   6 FAIDTKRCIGCHTCSVSCRiennlpegtwwnRVLTKGGESMDTPEGTFPDATMSYITVACQHCENPACVKVCPVGATYKD 85
Cdd:cd16369     4 FFIDPSRCIGCRACVAACR------------ECGTHRGKSMIHVDYIDRGESTQTAPTVCMHCEDPTCAEVCPADAIKVT 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  86 PDtGVVRQ-DYDKCIGCRMCMAACPYvGVRSFNWEEPAHYigfdsgdadvpehqkhtveKCTFCWHRLAKGEDPMCVKTC 164
Cdd:cd16369    72 ED-GVVQSaLKPRCIGCSNCVNACPF-GVPKYDEERNLMM-------------------KCDMCYDRTSVGKAPMCASVC 130

                         170
                  ....*....|....*.
gi 2787368098 165 LARARVWGDLDDPESE 180
Cdd:cd16369   131 PSGALFYGTREEIQAL 146
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
2-168 2.58e-22

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 87.79  E-value: 2.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   2 MRYGFAIDTKRCIGCHTCSVSCRIENNLPEGTW---WNRVLTKGGESMdtpegtfpdatmsyiTVACQHCENPACVKVCP 78
Cdd:COG1142     1 MNKFIIADPEKCIGCRTCEAACAVAHEGEEGEPflpRIRVVRKAGVSA---------------PVQCRHCEDAPCAEVCP 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  79 VGATYKDPDTGVVrqDYDKCIGCRMCMAACPYvGvrsfnweepAHYIgfdsgdadVPEHQKHTVEKCTFCWHRlakGEDP 158
Cdd:COG1142    66 VGAITRDDGAVVV--DEEKCIGCGLCVLACPF-G---------AITM--------VGEKSRAVAVKCDLCGGR---EGGP 122

                         170
                  ....*....|
gi 2787368098 159 MCVKTCLARA 168
Cdd:COG1142   123 ACVEACPTGA 132
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 4-206 3.38e-22

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: 91.37  E-value: 3.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   4 YGFAIDTKRCIGCHTCSVSCRIENNLPEG---TWWNRVLTK--GG------------------------ESMDTPEGT-- 52
Cdd:cd10556    12 FAMVFDTNKCIACQTCTMACKSTWTSGKGqeyMWWNNVETKpyGGyplgwdvrlldeeggqtwaeggvyEGKTIFEAAaa 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  53 ---------------FP----------------------DATMSYITVACQHCENPACVKVCPVGATYKDPDTGVVRQDY 95
Cdd:cd10556    92 geqvlgyrpededwrYPnigedevngertpdtgsslpphPIWFFYLPRICNHCTYPACLAACPRKAIYKREEDGIVLIDQ 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  96 DKCIGCRMCMAACPYVGVrSFNWEEpahyigfdsgdadvpehqkHTVEKCTFCWHRLAKGEDPMCVKTCLARARVWGDL- 174
Cdd:cd10556   172 ERCRGYRECVEACPYKKP-MYNPTT-------------------RVSEKCIGCYPRIEEGDQTQCVSACIGKIRLQGFIn 231

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2787368098 175 --------DDPESEVSKLIRERKV-MQLLPEKDTKPSVYYL 206
Cdd:cd10556   232 tppdarwaDDRDNPIDFLVHIKKVaLPLYPQFGTEPNVYYI 272
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 9-168 3.63e-21

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: 85.39  E-value: 3.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   9 DTKRCIGCHTCSVSCRIENNlpeGTWWNRVLTKGGES------MDTPEGTFPdatmsyitVACQHCENPACVKVCPVGAT 82
Cdd:cd10554     5 DPDKCIGCRTCEVACAAAHS---GKGIFEAGTDGLPFlprlrvVKTGEVTAP--------VQCRQCEDAPCANVCPVGAI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  83 YKDPdtGVVRQDYDKCIGCRMCMAACPYVGVrsfnweEPAHYigfDSGDADVPEHQKHTVEKCTFCWHRlakGEDPMCVK 162
Cdd:cd10554    74 SQED--GVVQVDEERCIGCKLCVLACPFGAI------EMAPT---TVPGVDWERGPRAVAVKCDLCAGR---EGGPACVE 139


                  ....*.
gi 2787368098 163 TCLARA 168
Cdd:cd10554   140 ACPTKA 145
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 1-168 6.46e-19

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 84.03  E-value: 6.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   1 MMRYGFAiDTKRCIGCHTCSVSCRIENNlpegtwwnrvltkGGESMDTPEGTFPDATM-----SYITVACQHCENPACVK 75
Cdd:PRK12769    1 MNRFIMA-NSQQCLGCHACEIACVMAHN-------------DEQHVLSQHHFHPRITVikhqqQRSAVTCHHCEDAPCAR 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  76 VCPVGATYKDPDTGVVRQdyDKCIGCRMCMAACPYvGVRSFNWEEPAhyigfdsgdadvPEHQKHTVEKCTFCWHRlakG 155
Cdd:PRK12769   67 SCPNGAISHVDDSIQVNQ--QKCIGCKSCVVACPF-GTMQIVLTPVA------------AGKVKATAHKCDLCAGR---E 128

                         170
                  ....*....|...
gi 2787368098 156 EDPMCVKTCLARA 168
Cdd:PRK12769  129 NGPACVENCPADA 141
PRK09898 PRK09898
ferredoxin-like protein;
12-110 2.05e-16

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 74.10  E-value: 2.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  12 RCIGCHTCSVSCRIENNLPEGTWWNRVLTK-----GGESMDTPEGTFPDatMSYITVACQHCENPACVKVCPVGATYKDP 86
Cdd:PRK09898   67 RCTGCHRCEISCTNFNDGSVGTFFSRIKIHrnyffGDNGVGSGGGLYGD--LNYTADTCRQCKEPQCMNVCPIGAITWQQ 144

                          90       100
                  ....*....|....*....|....
gi 2787368098  87 DTGVVRQDYDKCIGCRMCMAACPY 110
Cdd:PRK09898  145 KEGCITVDHKRCIGCSACTTACPW 168
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 5-189 7.73e-15

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: 69.77  E-value: 7.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   5 GFAIDTKRCIGCHTCSVSCRIENNLP----------------EGTWWNRVltKGGESMDtpEGTFPDatMSYITVACQHC 68
Cdd:cd10559     1 SFLIDTTRCTACRGCQVACKQWNQLPaeqtkntgshqnppdlSANTYKLV--RFNEVRN--ENGKPD--WLFFPDQCRHC 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  69 ENPACVKVCPV--GATYKDPDTGVVRQDYDKCIGCRMCMA-ACPYvgvrsfnweepahyigfdsgdaDVPEHQKHT--VE 143
Cdd:cd10559    75 VTPPCKDAADMvpGAVIQDEATGAVVFTEKTAELDFDDVLsACPY----------------------NIPRKNEATgrIV 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2787368098 144 KCTFCWHRLAKGEDPMCVKTCLARARVWGDLDDPESEVSKLIRERK 189
Cdd:cd10559   133 KCDMCIDRVSNGLQPACVKACPTGAMNFGDRDEMLAMASKRLEELK 178
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 7-202 7.29e-14

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 69.28  E-value: 7.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   7 AIDTKRCIGCHTCSVSCRIENN-----LPEGTWWNRVLTKGGESMDTPegtfpdatmsyitVACQHCENPACVKVCPVGA 81
Cdd:PRK12809    6 AAEAAECIGCHACEIACAVAHNqenwpLSHSDFRPRIHVVGKGQAANP-------------VACHHCNNAPCVTACPVNA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  82 TYKDPDTgvVRQDYDKCIGCRMCMAACPYVGVrsfnweepahyigfdsgdadvpEHQKHTVEKCTFCWHRLAKGEdpMCV 161
Cdd:PRK12809   73 LTFQSDS--VQLDEQKCIGCKRCAIACPFGVV----------------------EMVDTIAQKCDLCNQRSSGTQ--ACI 126

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2787368098 162 KTCLARA-RVwgdLDDPESEVSKLIRERKVMQLLPEKDTKPS 202
Cdd:PRK12809  127 EVCPTQAlRL---MDDKGLQQIKVARQRKTAAGKASSDAQPS 165
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 65-186 9.85e-14

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


Pssm-ID: 319890 [Multi-domain]  Cd Length: 200  Bit Score: 66.68  E-value: 9.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  65 CQHCENPACVKVCPVGATYKDPdTGVVRQDYDKCIGCRMCMAACPyvgvrsfnWEEPAHYIGFDSGDADVPEHQKHTVE- 143
Cdd:cd16368    91 CMHCDNPPCAKLCPFGAARKTP-EGAVYIDDDLCFGGAKCRDVCP--------WHIPQRQAGVGIYLHLAPEYAGGGVMy 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2787368098 144 KCTFCWHRLAKGEDPMCVKTCLARARVWGdlddPESEVSKLIR 186
Cdd:cd16368   162 KCDLCKDLLAQGKPPACIEACPKGAQYFG----PRKEMVALAR 200
PRK10330 PRK10330
electron transport protein HydN;
1-178 2.23e-13

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 65.68  E-value: 2.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   1 MMRYGFAiDTKRCIGCHTCSVSCRIEN-------NLPEGTWWNRVLTKGGESMDTpegtfpdatmsyiTVACQHCENPAC 73
Cdd:PRK10330    1 MNRFIIA-DASKCIGCRTCEVACVVSHqenqdcaSLTPETFLPRIHVIKGVNVST-------------ATVCRQCEDAPC 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  74 VKVCPVGATYKDPDTGVVRQDydKCIGCRMCMAACPYVGVrsfnwEEPAHYIGFDSGDADVPEHQKHTVEKCTFCWHRla 153
Cdd:PRK10330   67 ANVCPNGAISRDKGFVHVMQE--RCIGCKTCVVACPYGAM-----EVVVRPVIRNSGAGLNVRAEKAEANKCDLCNHR-- 137

                         170       180
                  ....*....|....*....|....*
gi 2787368098 154 kGEDPMCVKTCLARARVWGDLDDPE 178
Cdd:PRK10330  138 -EDGPACMAACPTHALICVDRNKLE 161
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 8-110 4.76e-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: 319889 [Multi-domain]  Cd Length: 138  Bit Score: 58.09  E-value: 4.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   8 IDTKRCIGCHTCSVSCriennlpegtwwnrVLTKGGESMDTPEGTFPDATMsyITVACQHCENPACVKVCPVGATYKDpD 87
Cdd:cd16367    16 IDLDRCIRCDNCEKAC--------------ADTHDGHSRLDRNGLRFGNLL--VPTACRHCVDPVCMIGCPTGAIHRD-D 78

                          90       100
                  ....*....|....*....|...
gi 2787368098  88 TGVVRQDyDKCIGCRMCMAACPY 110
Cdd:cd16367    79 GGEVVIS-DACCGCGNCASACPY 100
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 6-109 1.15e-10

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: 56.90  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   6 FAIDTKRCIGCHTCSVSC--RIENNLPEGTWWNRVLTKGGEsmdtpEGTFpdatmsyITVACQHCENPACVKVCPVGATY 83
Cdd:cd16370     4 RVKDMERCIGCYSCMLACsrRVHKSASLSKSAIRVRTRGGL-----EGGF-------TVVVCRACEDPPCAEACPTGALE 71

                          90       100
                  ....*....|....*....|....*.
gi 2787368098  84 KDPDTGVVrQDYDKCIGCRMCMAACP 109
Cdd:cd16370    72 PRKGGGVV-LDKEKCIGCGNCVKACI 96
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
61-122 7.49e-09

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 50.50  E-value: 7.49e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2787368098  61 ITVACQHCEnpACVKVCPVGATYkdPDTGVVRQDYDKCIGCRMCMAACPyVGVRSFNWEEPA 122
Cdd:COG2768     9 DEEKCIGCG--ACVKVCPVGAIS--IEDGKAVIDPEKCIGCGACIEVCP-VGAIKIEWEEDE 65
FeFe_hydrog_B1 TIGR04105
[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups.
 73-110 1.58e-08

[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups.


Pssm-ID: 274983 [Multi-domain]  Cd Length: 462  Bit Score: 53.75  E-value: 1.58e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2787368098  73 CVKVCPVGATYKDPDtGVVRQDYDKCIGCRMCMAACPY 110
Cdd:TIGR04105 166 CEKACPVGAISSDED-GRAVIDYDKCISCGACMVACPF 202
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 8-110 1.86e-08

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


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 50.80  E-value: 1.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   8 IDTKRCIGCHTCSVSCRIENNLPEGTWWNRVLTKGGESMdtpegtfpdatmsYITVACQHCENpaCVKVCPVGATYKDPD 87
Cdd:cd16372     5 TDPEKCIGCLQCEEACSKTFFKEEDREKSCIRITETEGG-------------YAINVCNQCGE--CIDVCPTGAITRDAN 69

                          90       100
                  ....*....|....*....|...
gi 2787368098  88 tGVVRQDYDKCIGCRMCMAACPY 110
Cdd:cd16372    70 -GVVMINKKLCVGCLMCVGFCPE 91
PRK13795 PRK13795
hypothetical protein; Provisional
 73-111 2.37e-08

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 53.07  E-value: 2.37e-08
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2787368098  73 CVKVCPVGATYKDPDTGVVRQDYDKCIGCRMCMAACPYV 111
Cdd:PRK13795  589 CVGACPTGAIRIEEGKRKISVDEEKCIHCGKCTEVCPVV 627
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 65-109 8.75e-08

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 51.41  E-value: 8.75e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2787368098  65 CQHCENpaCVKVCPVGATYKDPDTGVVRQDYDKCIGCRMCMAACP 109
Cdd:PRK12771  512 CFECDN--CYGACPQDAIIKLGPGRRYHFDYDKCTGCHICADVCP 554
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 2-109 1.86e-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: 48.16  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   2 MRYGFAIDTKRCIGCHTCSVSCRIEnnlpegtwwnrVLTkggesMDTPEGTFPDATMSYIT--VACQHCEnpACVKVCPV 79
Cdd:cd10549    31 IARGPEIDEDKCVFCGACVEVCPTG-----------AIE-----LTPEGKEYVPKEKEAEIdeEKCIGCG--LCVKVCPV 92

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2787368098  80 GA-TYKDPDTGVVrqDYDKCIGCRMCMAACP 109
Cdd:cd10549    93 DAiTLEDELEIVI--DKEKCIGCGICAEVCP 121
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
59-114 5.10e-07

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 48.91  E-value: 5.10e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2787368098  59 SYITVACQHCEnpACVKVCPVGAtykDPDTGVVRQDydKCIGCRMCMAACPYVGVR 114
Cdd:COG0348   206 RYDRGDCIDCG--LCVKVCPMGI---DIRKGEINQS--ECINCGRCIDACPKDAIR 254
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
8-109 8.95e-07

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 48.48  E-value: 8.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   8 IDTKRCIGCHTCSVSCRIENNLPEGTWWNRVLTKGGESMDTPEgtfpdatmsyitvACQHCENpaCVKVCPVGATykDPD 87
Cdd:COG4624    49 SCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSIIRDKE-------------KCKNCYP--CVRACPVKAI--KVD 111

                          90       100
                  ....*....|....*....|..
gi 2787368098  88 TGVVRQDYDKCIGCRMCMAACP 109
Cdd:COG4624   112 DGKAEIDEEKCISCGQCVAVCP 133
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 64-109 1.22e-06

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 44.66  E-value: 1.22e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2787368098  64 ACQHCenPACVKVCPVGATykDPDTGVVRQDYDKCIGCRMCMAACP 109
Cdd:COG2221    16 KCIGC--GLCVAVCPTGAI--SLDDGKLVIDEEKCIGCGACIRVCP 57
NapF COG1145
Ferredoxin [Energy production and conversion];
65-110 1.71e-06

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 47.02  E-value: 1.71e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2787368098  65 CQHCEnpACVKVCPVGATYKDPDTGVVRQDYDKCIGCRMCMAACPY 110
Cdd:COG1145   184 CIGCG--LCVKVCPTGAIRLKDGKPQIVVDPDKCIGCGACVKVCPV 227
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 73-109 4.05e-06

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: 46.14  E-value: 4.05e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2787368098  73 CVKVCPVGATYKDPDtGVVRQDYDKCIGCRMCMAACP 109
Cdd:COG2878   145 CIKACPFDAIVGAAK-GMHTVDEDKCTGCGLCVEACP 180
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 11-113 4.14e-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: 44.94  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  11 KRCIGCHTCSVSCriennlPEGTWWNRVLTKGGESMDTPegtfpdaTMSYITVACQHCENpACVKVCPVGA------TYK 84
Cdd:cd16373    14 ALCIRCGLCVEAC------PTGVIQPAGLEDGLEGGRTP-------YLDPREGPCDLCCD-ACVEVCPTGAlrpldlEEQ 79

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2787368098  85 DPDTGVVRQDYDKCI------GCRMCMAACPYVGV 113
Cdd:cd16373    80 KVKMGVAVIDKDRCLawqggtDCGVCVEACPTEAI 114
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 72-109 1.07e-05

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 43.15  E-value: 1.07e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2787368098  72 ACVKVCPVGATYKDPDTGVVRQ---DYDKCIGCRMCMAACP 109
Cdd:cd10549    13 ICVKACPTDAIELGPNGAIARGpeiDEDKCVFCGACVEVCP 53
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 65-109 1.31e-05

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 41.65  E-value: 1.31e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2787368098  65 CQHCEnpACVKVCPVGATY--KDPDTGVVRQDYDKCIGCRMCMAACP 109
Cdd:COG1143     4 CIGCG--LCVRVCPVDAITieDGEPGKVYVIDPDKCIGCGLCVEVCP 48
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
12-178 1.47e-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: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  12 RCIGCHTCSVSCRIENNLPEGTWWNRVLTKGGESM----DTPEGTFPDATMSYITVACQHCENpACVKVCPVGATYKDPD 87
Cdd:COG4624     4 LLRACCCCCIEEGDELLLLEEAERVLRIIILEALLpehvDDDSACSCCPRCCLCCCCCCRCCV-AISCIQVRGIIIIDKR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  88 TGVVRQDYDKCIGCRMCMAACPYvgvrsfnweepaHYIGFDSGDADVPEhqkhtvEKCTFCwhrlakGedpMCVKTCLAR 167
Cdd:COG4624    83 GPSIIRDKEKCKNCYPCVRACPV------------KAIKVDDGKAEIDE------EKCISC------G---QCVAVCPFG 135

                         170
                  ....*....|....*....
gi 2787368098 168 A--------RVWGDLDDPE 178
Cdd:COG4624   136 AiteksdieKVKKALKDPE 154
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
73-110 1.69e-05

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 44.28  E-value: 1.69e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2787368098  73 CVKVCPVGATY---KDPDTGVVRQDYDKCIGCRMCMAACPY 110
Cdd:COG0348   184 CRYLCPYGAFQgllSDLSTLRVRYDRGDCIDCGLCVKVCPM 224
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 58-109 2.39e-05

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


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 40.70  E-value: 2.39e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2787368098  58 MSYITVACQHCENpaCVKVCP-----VGATYKDPDTGVVRQDYDKCIGCRMCMAACP 109
Cdd:pfam13237   2 VVIDPDKCIGCGR--CTAACPagltrVGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 65-110 3.39e-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: 40.20  E-value: 3.39e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2787368098  65 CQHCEnpACVKVCPVGATYKDPD-----TGVVRQDYDKCIGCRMCMAACPY 110
Cdd:pfam12838   1 CIGCG--ACVAACPVGAITLDEVgekkgTKTVVIDPERCVGCGACVAVCPT 49
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 65-109 4.54e-05

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 40.08  E-value: 4.54e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2787368098  65 CQHCEnpACVKVCPVGATYKDPDTGVVRQ-DYDKCIGCRMCMAACP 109
Cdd:COG1146    10 CIGCG--ACVEVCPVDVLELDEEGKKALViNPEECIGCGACELVCP 53
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
8-109 1.36e-04

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 41.46  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098   8 IDTKRCIGCHTCSVSCriennlPEGTWwnrVLTKGGE-------SMDTPEgtfpdATMSYITVACQHCEnpACVKVCPVG 80
Cdd:PRK07118  165 VDEDKCTGCGACVKAC------PRNVI---ELIPKSArvfvacnSKDKGK-----AVKKVCEVGCIGCG--KCVKACPAG 228

                          90       100
                  ....*....|....*....|....*....
gi 2787368098  81 ATykDPDTGVVRQDYDKCIGCRMCMAACP 109
Cdd:PRK07118  229 AI--TMENNLAVIDQEKCTSCGKCVEKCP 255
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 65-109 1.55e-04

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 38.87  E-value: 1.55e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2787368098  65 CQHCEnpACVKVCPVGATYKDPDTGVVRQDydKCIGCRMCMAACP 109
Cdd:COG4231    24 CTGCG--ACVKVCPADAIEEGDGKAVIDPD--LCIGCGSCVQVCP 64
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 65-109 2.06e-04

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: 38.88  E-value: 2.06e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2787368098  65 CQHCENpaCVKVCPVGAtYKDPDTGVVRQDYDKCIGCRMCMAACP 109
Cdd:COG1144    32 CIGCGL--CWIVCPDGA-IRVDDGKYYGIDYDYCKGCGICAEVCP 73
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
65-109 3.44e-04

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 40.61  E-value: 3.44e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2787368098  65 CQHCEnpACVKVCPVGATYKDPDtGVVRQDYDKCIGCRMCMAACP 109
Cdd:COG1148   498 CTGCG--RCVEVCPYGAISIDEK-GVAEVNPALCKGCGTCAAACP 539
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
73-109 7.49e-04

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 37.62  E-value: 7.49e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2787368098  73 CVKVCPVGATYKDPDtGVVRQDYDKCIGCRMCMAACP 109
Cdd:PRK09623   59 CWKFCPEPAIYIKED-GYVAIDYDYCKGCGICANECP 94
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
73-109 7.51e-04

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 39.53  E-value: 7.51e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2787368098  73 CVKVCPVGATYKDPDTGVVrqDYDKCIGCRMCMAACP 109
Cdd:PRK07118  147 CVAACPFDAIHIENGLPVV--DEDKCTGCGACVKACP 181
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 72-109 1.27e-03

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 38.01  E-value: 1.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2787368098  72 ACVKVCPVG--ATYKDPDTGVVRQDYDKCIGCRMCMAACP 109
Cdd:cd16373   104 VCVEACPTEaiAIVLEDDVLRPVVDEDKCVGCGLCEYVCP 143
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 65-109 1.53e-03

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 35.86  E-value: 1.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2787368098  65 CQHCEnpACVKVCPVGATYKDpDTGVVRQDYDKCIGCRMCMAACP 109
Cdd:COG1149    13 CIGCG--LCVEVCPEGAIKLD-DGGAPVVDPDLCTGCGACVGVCP 54
Fer4_9 pfam13187
4Fe-4S dicluster domain;
72-110 3.75e-03

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 34.45  E-value: 3.75e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2787368098  72 ACVKVCPVGATYKDPDTGVVR--QDYDKCIGCRMCMAACPY 110
Cdd:pfam13187   7 ACVAACPAGAIVPDLVGQTIRgdIAGLACIGCGACVDACPR 47
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 73-110 4.39e-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: 37.46  E-value: 4.39e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2787368098  73 CVKVCPV-----GATYKDPDTGVVRQDYDKCIGCRMCMAACPY 110
Cdd:COG1245    21 CIKYCPVnrtgkEAIEIDEDDGKPVISEELCIGCGICVKKCPF 63
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 91-148 4.74e-03

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: 34.15  E-value: 4.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2787368098  91 VRQDYDKCIGCRMCMAACPYVGVRSFNWEEpahyigfdsgdADVPEHQKHTVEKCTFC 148
Cdd:pfam13237   2 VVIDPDKCIGCGRCTAACPAGLTRVGAIVE-----------RLEGEAVRIGVWKCIGC 48
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 89-109 8.67e-03

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 34.81  E-value: 8.67e-03
                          10        20
                  ....*....|....*....|.
gi 2787368098  89 GVVRQDYDKCIGCRMCMAACP 109
Cdd:PRK08348   35 GKILYDVDKCVGCRMCVTVCP 55
PRK10194 PRK10194
ferredoxin-type protein NapF;
13-117 9.72e-03

ferredoxin-type protein NapF;


Pssm-ID: 182296 [Multi-domain]  Cd Length: 163  Bit Score: 35.38  E-value: 9.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787368098  13 CIGCHTCSVSCRIENNLPEGT-WWNRVLTKGgesmdtpegtfpDATMSYITVACQHCENpACVkvcPVGATYKDPDTGVV 91
Cdd:PRK10194   68 CSFCYACAQACPESLFSPRHTrAWDLQFTIG------------DACLAYQSVECRRCQD-SCE---PMAIIFRPTLSGIY 131

                          90       100
                  ....*....|....*....|....*...
gi 2787368098  92 RQDYDK--CIGCRMCMAACPYVGVRSFN 117
Cdd:PRK10194  132 QPQLNSqlCNGCGACAASCPVSAITAEY 159
 
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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