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Conserved domains on  [gi|1783788852|ref|WP_156643552|]
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sulfate reduction electron transfer complex DsrMKJOP subunit DsrO [Lentibacillus sp. JNUCC-1]

Protein Classification

Ferredoxin_N and PsrB domain-containing protein( domain architecture ID 11726329)

Ferredoxin_N and PsrB domain-containing protein

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 ...
 90-293 3.58e-110

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: 316.78  E-value: 3.58e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  90 MVIDLQKCVGCDSCTVACKSENRTPPGISYNVVLEEEIGEFPNLAKVNLPMPCMHCDKPPCVQVCPVKATFKLDNGIVTI 169
Cdd:cd10551     1 MVIDLRKCIGCGACVVACKAENNVPPGVFRNRVLEYEVGEYPNVKRTFLPVLCNHCENPPCVKVCPTGATYKREDGIVLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 170 DNDRCIGCRYCIIACPYGARSFDFGESYEDEmlsfndvtspeygiergerGKRKSPIGTVRKCNFCLHRLERGEEPACVE 249
Cdd:cd10551    81 DYDKCIGCRYCMAACPYGARYFNPEEPHEFG-------------------EVPVRPKGVVEKCTFCYHRLDEGLLPACVE 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1783788852 250 TCIGDARFFGDLNDPNSTVSKLANSPRAFRLKSELGAGPNVIYL 293
Cdd:cd10551   142 ACPTGARIFGDLDDPNSEVSKLLAERRAYVLKPELGTKPKVYYI 185
Ferredoxin_N super family cl25219
N-terminal region of 4Fe-4S ferredoxin iron-sulfur binding; Ferredoxin_N is a short domain ...
 20-68 3.24e-13

N-terminal region of 4Fe-4S ferredoxin iron-sulfur binding; Ferredoxin_N is a short domain that is often found at the N-terminus of 4Fe-4S ferredoxin iron-sulfur binding domain proteins from Archaea and a few bacteria.


The actual alignment was detected with superfamily member pfam16947:

Pssm-ID: 407169  Cd Length: 65  Bit Score: 63.20  E-value: 3.24e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1783788852  20 DAKTELDQSPYSTQLGMDMADDARRVVAGNLDIKAFHKKYHSSLLGEFG 68
Cdd:pfam16947  10 EAEEMLDDTEYDAELGMEMARDAMRVTKGELSEAEFHEKYHEDVVAEFG 58
 
Name Accession Description Interval E-value
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 90-293 3.58e-110

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: 316.78  E-value: 3.58e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  90 MVIDLQKCVGCDSCTVACKSENRTPPGISYNVVLEEEIGEFPNLAKVNLPMPCMHCDKPPCVQVCPVKATFKLDNGIVTI 169
Cdd:cd10551     1 MVIDLRKCIGCGACVVACKAENNVPPGVFRNRVLEYEVGEYPNVKRTFLPVLCNHCENPPCVKVCPTGATYKREDGIVLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 170 DNDRCIGCRYCIIACPYGARSFDFGESYEDEmlsfndvtspeygiergerGKRKSPIGTVRKCNFCLHRLERGEEPACVE 249
Cdd:cd10551    81 DYDKCIGCRYCMAACPYGARYFNPEEPHEFG-------------------EVPVRPKGVVEKCTFCYHRLDEGLLPACVE 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1783788852 250 TCIGDARFFGDLNDPNSTVSKLANSPRAFRLKSELGAGPNVIYL 293
Cdd:cd10551   142 ACPTGARIFGDLDDPNSEVSKLLAERRAYVLKPELGTKPKVYYI 185
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 83-293 1.31e-87

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 259.49  E-value: 1.31e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  83 KKGVKWGMVIDLQKCVGCDSCTVACKSENRTPPGISYNVVLEEEIGEFPNLAKVNLPMPCMHCDKPPCVQVCPVKATFKL 162
Cdd:COG0437     1 LSMKRYGMVIDLTKCIGCRACVVACKEENNLPVGVTWRRVRRYEEGEFPNVEWLFVPVLCNHCDDPPCVKVCPTGATYKR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 163 DNGIVTIDNDRCIGCRYCIIACPYGARSFDfgesyedemlsfndvtspeygiergergkrkSPIGTVRKCNFCLHRLERG 242
Cdd:COG0437    81 EDGIVLVDYDKCIGCRYCVAACPYGAPRFN-------------------------------PETGVVEKCTFCADRLDEG 129

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1783788852 243 EEPACVETCIGDARFFGDLNDPNSTVSKLANSPRAFRLKSELGAGPNVIYL 293
Cdd:COG0437   130 LLPACVEACPTGALVFGDLDDPESEVSKRLAELPAYRLLPELGTKPSVYYL 180
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
74-293 1.81e-61

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 195.09  E-value: 1.81e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  74 EPIDEEGNTKKgvKWGMVIDLQKCVGCDSCTVACKSENRTPPGISYNVVLEEEIGEFPNLAKVN--LPMPCMHCDKPPCV 151
Cdd:PRK14993   32 SPERHEGSPRH--RYAMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQYQVQREGSQEVTNvlLPRLCNHCDNPPCV 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 152 QVCPVKATFKLDNGIVTIDNDRCIGCRYCIIACPYGARsfdfgesyedemlSFNDVTSpeygiergergkrkspigTVRK 231
Cdd:PRK14993  110 PVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDAR-------------FINHETQ------------------TADK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1783788852 232 CNFCLHRLERGEEPACVETCIGDARFFGDLNDPNSTVSKLANSPRAFR--LKSELGAGPNVIYL 293
Cdd:PRK14993  159 CTFCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRIATMLHQHRDAIkvLKPENGTSPHVFYL 222
FDH3_beta NF038355
formate dehydrogenase FDH3 subunit beta; Members of this family are the beta subunit of the ...
 93-260 2.18e-31

formate dehydrogenase FDH3 subunit beta; Members of this family are the beta subunit of the FDH3 type of formate dehydrogenase as found in Methylorubrum (Methylobacterium) extorquens.


Pssm-ID: 439648 [Multi-domain]  Cd Length: 180  Bit Score: 115.16  E-value: 2.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  93 DLQKCVGCDSCTVACKSENRTPPGISYNVVL---EEEIGEFpnlakvNLPMPCMHCDKPPCVQVCPVKATFKLDNGIVTI 169
Cdd:NF038355    8 DTERCIECNGCVVACKNAHELPWGINRRRVVtlnDGVPGEK------SISVACMHCTDAPCAAVCPVDCFYIRADGIVLH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 170 DNDRCIGCRYCIIACPYGARSFdfgesyedemlsfndvtsPEYGIeRGERGKrkspigtVRKCNFCL------------- 236
Cdd:NF038355   82 DKDKCIGCGYCLYACPFGAPQF------------------PKDGA-FGARGK-------MDKCTFCAggpeetnseaere 135

                         170       180
                  ....*....|....*....|....*...
gi 1783788852 237 ----HRLERGEEPACVETCIGDARFFGD 260
Cdd:NF038355  136 kygqNRIAEGKLPLCAEMCSTKALLAGD 163
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 138-261 6.24e-23

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: 90.39  E-value: 6.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 138 LPMPCMHCDKPPCVQVCPVKATFK-LDNGIVTIDNDRCIGCRYCIIACPYGArsfdfgesyedemLSFNDVTspeygier 216
Cdd:pfam13247   6 FPEQCRHCLNPPCKASCPVGAIYKdEETGAVLLDEKTCRGWRECVSACPYNI-------------PRYNDET-------- 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1783788852 217 gergkrkspiGTVRKCNFCLHRLERGEEPACVETCIGDARFFGDL 261
Cdd:pfam13247  65 ----------GKAEKCDMCYDRVEAGLLPACVQTCPTGAMNFGDR 99
Ferredoxin_N pfam16947
N-terminal region of 4Fe-4S ferredoxin iron-sulfur binding; Ferredoxin_N is a short domain ...
 20-68 3.24e-13

N-terminal region of 4Fe-4S ferredoxin iron-sulfur binding; Ferredoxin_N is a short domain that is often found at the N-terminus of 4Fe-4S ferredoxin iron-sulfur binding domain proteins from Archaea and a few bacteria.


Pssm-ID: 407169  Cd Length: 65  Bit Score: 63.20  E-value: 3.24e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1783788852  20 DAKTELDQSPYSTQLGMDMADDARRVVAGNLDIKAFHKKYHSSLLGEFG 68
Cdd:pfam16947  10 EAEEMLDDTEYDAELGMEMARDAMRVTKGELSEAEFHEKYHEDVVAEFG 58
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 142-185 1.34e-04

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


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 41.71  E-value: 1.34e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1783788852 142 CMHCDKppCVQVCPVKATFKLDNGIVTIDNDRCIGCRYCIIACP 185
Cdd:TIGR01944 115 CIGCTK--CIQACPVDAIVGAAKAMHTVIADECTGCDLCVEPCP 156
 
Name Accession Description Interval E-value
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 90-293 3.58e-110

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: 316.78  E-value: 3.58e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  90 MVIDLQKCVGCDSCTVACKSENRTPPGISYNVVLEEEIGEFPNLAKVNLPMPCMHCDKPPCVQVCPVKATFKLDNGIVTI 169
Cdd:cd10551     1 MVIDLRKCIGCGACVVACKAENNVPPGVFRNRVLEYEVGEYPNVKRTFLPVLCNHCENPPCVKVCPTGATYKREDGIVLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 170 DNDRCIGCRYCIIACPYGARSFDFGESYEDEmlsfndvtspeygiergerGKRKSPIGTVRKCNFCLHRLERGEEPACVE 249
Cdd:cd10551    81 DYDKCIGCRYCMAACPYGARYFNPEEPHEFG-------------------EVPVRPKGVVEKCTFCYHRLDEGLLPACVE 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1783788852 250 TCIGDARFFGDLNDPNSTVSKLANSPRAFRLKSELGAGPNVIYL 293
Cdd:cd10551   142 ACPTGARIFGDLDDPNSEVSKLLAERRAYVLKPELGTKPKVYYI 185
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 83-293 1.31e-87

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 259.49  E-value: 1.31e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  83 KKGVKWGMVIDLQKCVGCDSCTVACKSENRTPPGISYNVVLEEEIGEFPNLAKVNLPMPCMHCDKPPCVQVCPVKATFKL 162
Cdd:COG0437     1 LSMKRYGMVIDLTKCIGCRACVVACKEENNLPVGVTWRRVRRYEEGEFPNVEWLFVPVLCNHCDDPPCVKVCPTGATYKR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 163 DNGIVTIDNDRCIGCRYCIIACPYGARSFDfgesyedemlsfndvtspeygiergergkrkSPIGTVRKCNFCLHRLERG 242
Cdd:COG0437    81 EDGIVLVDYDKCIGCRYCVAACPYGAPRFN-------------------------------PETGVVEKCTFCADRLDEG 129

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1783788852 243 EEPACVETCIGDARFFGDLNDPNSTVSKLANSPRAFRLKSELGAGPNVIYL 293
Cdd:COG0437   130 LLPACVEACPTGALVFGDLDDPESEVSKRLAELPAYRLLPELGTKPSVYYL 180
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
74-293 1.81e-61

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 195.09  E-value: 1.81e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  74 EPIDEEGNTKKgvKWGMVIDLQKCVGCDSCTVACKSENRTPPGISYNVVLEEEIGEFPNLAKVN--LPMPCMHCDKPPCV 151
Cdd:PRK14993   32 SPERHEGSPRH--RYAMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQYQVQREGSQEVTNvlLPRLCNHCDNPPCV 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 152 QVCPVKATFKLDNGIVTIDNDRCIGCRYCIIACPYGARsfdfgesyedemlSFNDVTSpeygiergergkrkspigTVRK 231
Cdd:PRK14993  110 PVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDAR-------------FINHETQ------------------TADK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1783788852 232 CNFCLHRLERGEEPACVETCIGDARFFGDLNDPNSTVSKLANSPRAFR--LKSELGAGPNVIYL 293
Cdd:PRK14993  159 CTFCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRIATMLHQHRDAIkvLKPENGTSPHVFYL 222
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 89-255 2.67e-56

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: 178.14  E-value: 2.67e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  89 GMVIDLQKCVGCDSCTVACKSENRTPPGISYNVVLEEEIGEFPNLAKVNLPMPCMHCDKPPCVQVCPVKATFKLDNGIVT 168
Cdd:cd16371     1 GFYFDQERCIGCKACEIACKDKNDLPPGVNWRRVYEYEGGEFPEVFAYFLSMSCNHCENPACVKVCPTGAITKREDGIVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 169 IDNDRCIGCRYCIIACPYGARSFDfgesyedemlsfndvtspeygierGERGKrkspigtVRKCNFCLHRLERGEEPACV 248
Cdd:cd16371    81 VDQDKCIGCGYCVWACPYGAPQYN------------------------PETGK-------MDKCDMCVDRLDEGEKPACV 129


                  ....*..
gi 1783788852 249 ETCIGDA 255
Cdd:cd16371   130 AACPTRA 136
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 90-259 5.33e-47

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: 154.08  E-value: 5.33e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  90 MVIDLQKCVGCDSCTVACKSENRTPPGISYNVVLEEEIGEFPNlakVNLPMPCMHCDKPPCVQVCPVKATFKLDNGIVTI 169
Cdd:cd04410     1 LVVDLDRCIGCGTCEVACKQEHGLRPGPDWSRIKVIEGGGLER---AFLPVSCMHCEDPPCVKACPTGAIYKDEDGIVLI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 170 DNDRCIGCRYCIIACPYGARSFDFGEsyedemlsfndvtspeygiergergkrkspiGTVRKCNFCLHRLERGEEPACVE 249
Cdd:cd04410    78 DEDKCIGCGSCVEACPYGAIVFDPEP-------------------------------GKAVKCDLCGDRLDEGLEPACVK 126

                         170
                  ....*....|
gi 1783788852 250 TCIGDARFFG 259
Cdd:cd04410   127 ACPTGALTFG 136
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 89-260 8.55e-46

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: 153.14  E-value: 8.55e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  89 GMVIDLQKCVGCDSCTVACKSENRTPP----------------GISYNVVLEEEIGEfPNLAKVNLPMPCMHCDKPPCVQ 152
Cdd:cd10561     1 GVLYDTTRCIGCRACEVACKEWNGLPAedtafgpgwdnprdlsAKTYTVIKRYEVET-GGKGFVFVKRQCMHCLDPACVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 153 VCPVKATFKLDNGIVTIDNDRCIGCRYCIIACPYGARSFDFGesyedemlsfndvtspeygiergergkrkSPIGTVRKC 232
Cdd:cd10561    80 ACPVGALRKTPEGPVTYDEDKCIGCRYCMVACPFNIPKYEWD-----------------------------SANPKIRKC 130

                         170       180
                  ....*....|....*....|....*...
gi 1783788852 233 NFCLHRLERGEEPACVETCIGDARFFGD 260
Cdd:cd10561   131 TMCYDRLKEGKQPACVEACPTGALLFGK 158
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 89-292 6.74e-40

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: 141.29  E-value: 6.74e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  89 GMVIDLQKCVGCDSCTVACKS----------------------------------------------------------- 109
Cdd:cd10555     6 AMVMDLNKCIGCQTCTVACKTlwtnrngreymywnnvetqpgkgypknwekkgggfkdkgelkpgiiptledygvpweyn 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 110 -ENRTPPGISYNVVLEEEI--------------GEFPNLAKVNLPMPCMHCDKPPCVQVCPVKATFKLD-NGIVTIDNDR 173
Cdd:cd10555    86 hEEELFEGKGGRVRPSPKGdptwgpnwdedqgaGEYPNSYYFYLPRICNHCTNPACLAACPRKAIYKREeDGIVLVDQDR 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 174 CIGCRYCIIACPYGArsfdfgesyedemLSFNDVtspeygiergergkrkspIGTVRKCNFCLHRLERGEEPACVETCIG 253
Cdd:cd10555   166 CRGYRYCVEACPYKK-------------IYFNPV------------------EQKSEKCIFCYPRIEKGVAPACARQCVG 214

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1783788852 254 DARFFGDLNDPNSTVSKLANSPR-AFRLKSELGAGPNVIY 292
Cdd:cd10555   215 RIRFVGYLDDEESPVYKLVKKWKvALPLHPEYGTEPNVFY 254
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 92-263 5.53e-38

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: 130.86  E-value: 5.53e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  92 IDLQKCVGCDSCTVACKSENRTPPGISynvvleeeIGEFPNLAkvNLPMPCMHCDKPPCVQVCPVKATFKLDNGIVTIDN 171
Cdd:cd16374     3 VDPERCIGCRACEIACAREHSGKPRIS--------VEVVEDLA--SVPVRCRHCEDAPCMEVCPTGAIYRDEDGAVLVDP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 172 DRCIGCRYCIIACPYGARSFDfgesyedemlsfndvtsPEYGIergergkrkspigtVRKCNFCLHRLERGEEPACVETC 251
Cdd:cd16374    73 DKCIGCGMCAMACPFGVPRFD-----------------PSLKV--------------AVKCDLCIDRRREGKLPACVEAC 121

                         170
                  ....*....|..
gi 1783788852 252 IGDARFFGDLND 263
Cdd:cd16374   122 PTGALKFGDIEE 133
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 90-293 2.70e-37

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: 130.91  E-value: 2.70e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  90 MVIDLQKCVGCDSCTVACKSE---NRTPP--------GISYNVVLEEEIGEFPNLAKVNLPMPCMHCDKPPCVQVCPVKA 158
Cdd:cd10552     1 LVIDVAKCNGCYNCFLACKDEhvgNDWPGyaapqprhGHFWMRILRRERGQYPKVDVAYLPVPCNHCDNAPCIKAAKDGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 159 TFKLDNGIVTIDNDRCIGCRYCIIACPYGARSFDfgesyEDEMLSfndvtspeygiergergkrkspigtvRKCNFCLHR 238
Cdd:cd10552    81 VYKRDDGIVIIDPEKAKGQKQLVDACPYGAIYWN-----EELQVP--------------------------QKCTFCAHL 129

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1783788852 239 LERGE-EPACVETCIGDARFFGDLNDPNSTvsKLANSPRAFRLKSELGAGPNVIYL 293
Cdd:cd10552   130 LDDGWkEPRCVQACPTGALRFGKLEDEEMA--AKAAEEGLEVLHPELGTKPRVYYK 183
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 93-259 5.50e-35

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: 123.63  E-value: 5.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  93 DLQKCVGCDSCTVACKSENRTPPGISYNVVLEEEIGEFPNLAKV-NLPMPCMHCDKPPCVQVCPVKATFKLD-NGIVTID 170
Cdd:cd10553     8 DSKRCIGCLACEVHCKVKNNLPVGPRLCRIFAVGPKMVGGKPRLkFVYMSCFHCENPWCVKACPTGAMQKREkDGIVYVD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 171 NDRCIGCRYCIIACPYGARSFDfgesyedemlsfndvtspeygiergergkrkSPIGTVRKCNFCLHRLERGEEPACVET 250
Cdd:cd10553    88 QELCIGCKACIEACPWGIPQWN-------------------------------PATGKVVKCDYCMDRIDQGLKPACVTG 136


                  ....*....
gi 1783788852 251 CIGDARFFG 259
Cdd:cd10553   137 CTTHALSFV 145
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 90-259 2.16e-34

beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family contains beta FeS subunits of several dehydrogenases in the DMSO reductase superfamily, including formate dehydrogenase N (FDH-N), tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N is a major component of nitrate respiration of Escherichia coli; it catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate to a cytochrome. W-FDH contains a tungsten instead of molybdenum at the catalytic center and seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate.


Pssm-ID: 319888 [Multi-domain]  Cd Length: 156  Bit Score: 122.51  E-value: 2.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  90 MVIDLQKCVGCDSCTVACKSENRTPPGISYN------------------VVLEEEIGEfPNLAKVNLPMPCMHCDKPPCV 151
Cdd:cd16366     1 FLVDTSRCTGCRACQVACKQWNGLPAEKTEFtgsyqnppdltahtwtlvRFYEVEKPG-GDLSWLFRKDQCMHCTDAGCL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 152 QVCPVKATFKLDNGIVTIDNDRCIGCRYCIIACPYGArsfdfgesyedemlsfndvtsPEYGIERgergkrkspiGTVRK 231
Cdd:cd16366    80 AACPTGAIIRTETGTVVVDPETCIGCGYCVNACPFDI---------------------PRFDEET----------GRVAK 128

                         170       180
                  ....*....|....*....|....*...
gi 1783788852 232 CNFCLHRLERGEEPACVETCIGDARFFG 259
Cdd:cd16366   129 CTLCYDRISNGLQPACVKTCPTGALTFG 156
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 89-293 9.09e-34

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: 122.31  E-value: 9.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  89 GMVIDLQKCVGCDSCTVACKSENRTPPGISY---NVVLEEEIGEFP----NLAKVN---------LPMPCMHCDKPPCVQ 152
Cdd:cd16365     4 AAVFNLNKCIGCQTCTVACKNAWTYRKGQEYmwwNNVETKPGGGYPqdweVKTIDNggntrfffyLQRLCNHCTNPACLA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 153 VCPVKATFKL-DNGIVTIDNDRCIGCRYCIIACPYGArsfdfgesyedemLSFNDVTspeygiergergkrkspiGTVRK 231
Cdd:cd16365    84 ACPRGAIYKReEDGIVLIDQKRCRGYRKCVEQCPYKK-------------IYFNGLS------------------RVSEK 132

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1783788852 232 CNFCLHRLERGEEPACVETCIGDARFFGDLND-PNSTVSKLANSPR-AFRLKSELGAGPNVIYL 293
Cdd:cd16365   133 CIACYPRIEGGDPTRCMSACVGRIRLQGFLDDnPKSPVTKLIRHWKvALPLHPEYGTEPNIYYV 196
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 90-260 9.79e-34

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: 120.87  E-value: 9.79e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  90 MVIDLQKCVGCDSCTVACKSEN-------------RTPPGIS---YNVVLEEEigEFPNLAKVNLPM---PCMHCDKPPC 150
Cdd:cd10562     1 MLVDTSKCTACRGCQVACKQWNqlpaektpftgsyQNPPDLTpntWTLIRFYE--HEEDNGGIRWLFrkrQCMHCTDAAC 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 151 VQVCPVKATFKLDNGIVTIDNDRCIGCRYCIIACPYGArsfdfgesyedemlsfndvtsPEYGiergergkrkSPIGTVR 230
Cdd:cd10562    79 VKVCPTGALYKTENGAVVVDEDKCIGCGYCVAACPFDV---------------------PRYD----------ETTNKIT 127

                         170       180       190
                  ....*....|....*....|....*....|
gi 1783788852 231 KCNFCLHRLERGEEPACVETCIGDARFFGD 260
Cdd:cd10562   128 KCTLCFDRIENGMQPACVKTCPTGALTFGD 157
FDH3_beta NF038355
formate dehydrogenase FDH3 subunit beta; Members of this family are the beta subunit of the ...
 93-260 2.18e-31

formate dehydrogenase FDH3 subunit beta; Members of this family are the beta subunit of the FDH3 type of formate dehydrogenase as found in Methylorubrum (Methylobacterium) extorquens.


Pssm-ID: 439648 [Multi-domain]  Cd Length: 180  Bit Score: 115.16  E-value: 2.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  93 DLQKCVGCDSCTVACKSENRTPPGISYNVVL---EEEIGEFpnlakvNLPMPCMHCDKPPCVQVCPVKATFKLDNGIVTI 169
Cdd:NF038355    8 DTERCIECNGCVVACKNAHELPWGINRRRVVtlnDGVPGEK------SISVACMHCTDAPCAAVCPVDCFYIRADGIVLH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 170 DNDRCIGCRYCIIACPYGARSFdfgesyedemlsfndvtsPEYGIeRGERGKrkspigtVRKCNFCL------------- 236
Cdd:NF038355   82 DKDKCIGCGYCLYACPFGAPQF------------------PKDGA-FGARGK-------MDKCTFCAggpeetnseaere 135

                         170       180
                  ....*....|....*....|....*...
gi 1783788852 237 ----HRLERGEEPACVETCIGDARFFGD 260
Cdd:NF038355  136 kygqNRIAEGKLPLCAEMCSTKALLAGD 163
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
89-259 4.28e-30

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 115.54  E-value: 4.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  89 GMVIDLQKCVGCDSCTVACKSENRTPP---------------GISYNVvleeeIGEFPNLAKVNLPMP----------CM 143
Cdd:PRK10882   39 GMLYDSTLCVGCQACVTKCQEINFPERnpqgeqtwdnpdklsPYTNNI-----IKVWKSGTGVNKDQEengyayikkqCM 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 144 HCDKPPCVQVCPVKATFK-LDNGIVTIDNDRCIGCRYCIIACPYGARSFDfgesYEdemlsfndvtspeygiergergkr 222
Cdd:PRK10882  114 HCVDPNCVSVCPVSALTKdPKTGIVHYDKDVCTGCRYCMVACPFNVPKYD----YN------------------------ 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1783788852 223 kSPIGTVRKCNFCLH----RLERGEEPACVETCIGDARFFG 259
Cdd:PRK10882  166 -NPFGAIHKCELCNQkgveRLDKGGLPGCVEVCPTGAVIFG 205
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 90-262 3.38e-28

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: 106.70  E-value: 3.38e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  90 MVIDLQKCVGCDSCTVACkSENRTPPGISYNVVLEEEIGEFPNLAkvnlPMPCMHCDKPPCVQVCPVKATFKLDNGIV-T 168
Cdd:cd16369     4 FFIDPSRCIGCRACVAAC-RECGTHRGKSMIHVDYIDRGESTQTA----PTVCMHCEDPTCAEVCPADAIKVTEDGVVqS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 169 IDNDRCIGCRYCIIACPYGARSFDFGesyEDEMLsfndvtspeygiergergkrkspigtvrKCNFCLHRLERGEEPACV 248
Cdd:cd16369    79 ALKPRCIGCSNCVNACPFGVPKYDEE---RNLMM----------------------------KCDMCYDRTSVGKAPMCA 127

                         170
                  ....*....|....
gi 1783788852 249 ETCIGDARFFGDLN 262
Cdd:cd16369   128 SVCPSGALFYGTRE 141
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 91-251 8.50e-28

HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 105.03  E-value: 8.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  91 VIDLQKCVGCDSCTVACKSENRtppGISYNVVLEEEIGEFPNL-----AKVNLPMPCMHCDKPPCVQVCPVKATFKlDNG 165
Cdd:cd10554     3 IADPDKCIGCRTCEVACAAAHS---GKGIFEAGTDGLPFLPRLrvvktGEVTAPVQCRQCEDAPCANVCPVGAISQ-EDG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 166 IVTIDNDRCIGCRYCIIACPYGARSFDFgesyedemlsfndVTSPEYGIERGERGKrkspigtVRKCNFClhrLERGEEP 245
Cdd:cd10554    79 VVQVDEERCIGCKLCVLACPFGAIEMAP-------------TTVPGVDWERGPRAV-------AVKCDLC---AGREGGP 135


                  ....*.
gi 1783788852 246 ACVETC 251
Cdd:cd10554   136 ACVEAC 141
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 92-263 1.23e-27

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: 106.32  E-value: 1.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  92 IDLQKCVGCDSCTVACKSENRTPPGISYNVVLEE-------------EIGEFPNLAKVNLPM---PCMHCDKPPCVQVCP 155
Cdd:cd10558     4 IDVSKCIGCKACQVACKEWNDLRAEVGHNVGTYQnpadlspetwtlmKFREVEDNGKLEWLIrkdGCMHCADPGCLKACP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 156 -VKATFKLDNGIVTIDNDRCIGCRYCIIACPygarsFDfgesyedemlsfndvtspeygIERGERGKRKspigtVRKCNF 234
Cdd:cd10558    84 sPGAIVQYANGIVDFQSDKCIGCGYCIKGCP-----FD---------------------IPRISKDDNK-----MYKCTL 132

                         170       180
                  ....*....|....*....|....*....
gi 1783788852 235 CLHRLERGEEPACVETCIGDARFFGDLND 263
Cdd:cd10558   133 CSDRVSVGLEPACVKTCPTGALHFGTKED 161
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 89-263 3.78e-26

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: 102.85  E-value: 3.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  89 GMVIDLQKCVGCDSCTVACKSENRTP------PGISYN------------VVLEEEIGEFPNLAKVN----LPMP--CMH 144
Cdd:cd10560     1 GFFTDTSICIGCKACEVACKQWNQLPadgydfSGMSYDntgdlsastwrhVKFIERPTEDGPANEGGdlqwLFMSdvCKH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 145 CDKPPCVQVCPVKATFKLDNGIVTIDNDRCIGCRYCIIACPYGArsfdfgesyedemlsfndvtspeygIERGERGkrks 224
Cdd:cd10560    81 CTDAGCLEACPTGAIFRTEFGTVYIQPDICNGCGYCVAACPFGV-------------------------IDRNEET---- 131

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1783788852 225 piGTVRKCNFCLHRLERGEEPACVETCIGDARFFGDLND 263
Cdd:cd10560   132 --GRAHKCTLCYDRLKDGLEPACAKACPTGSIQFGPLEE 168
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
91-251 3.13e-25

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 97.81  E-value: 3.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  91 VIDLQKCVGCDSCTVAC---KSENRTPPGISYNVVLEEeigefpnlAKVNLPMPCMHCDKPPCVQVCPVKATFKlDNGIV 167
Cdd:COG1142     6 IADPEKCIGCRTCEAACavaHEGEEGEPFLPRIRVVRK--------AGVSAPVQCRHCEDAPCAEVCPVGAITR-DDGAV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 168 TIDNDRCIGCRYCIIACPYGArsfdfgesyedemlsfndvtspeygIERGERGKRKSPIgtvrKCNFCLHrleRGEEPAC 247
Cdd:COG1142    77 VVDEEKCIGCGLCVLACPFGA-------------------------ITMVGEKSRAVAV----KCDLCGG---REGGPAC 124


                  ....
gi 1783788852 248 VETC 251
Cdd:COG1142   125 VEAC 128
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 92-251 1.25e-24

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: 96.17  E-value: 1.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  92 IDLQKCVGCDSCTVAC-----------KSENRTPPGISYNVVLEEEigefpnlaKVNLPMPCMHCDKPPCVQVCPVKATF 160
Cdd:cd10563     4 IDEEKCLGCKLCEVACavahskskdliKAKLEKERPRPRIRVEESG--------GRSFPLQCRHCDEPPCVKACMSGAMH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 161 K-LDNGIVTIDNDRCIGCRYCIIACPYGArsfdfgesyedemlsfndvtspeygIERGERGKRkspigtVRKCNFCLHRl 239
Cdd:cd10563    76 KdPETGIVIHDEEKCVGCWMCVMVCPYGA-------------------------IRPDKERKV------ALKCDLCPDR- 123

                         170
                  ....*....|..
gi 1783788852 240 ergEEPACVETC 251
Cdd:cd10563   124 ---ETPACVEAC 132
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 90-251 2.04e-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: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 92.64  E-value: 2.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  90 MVIDLQKCVGCDSCTVAC--KSENRTPPGIS-YNVVLEEEIGefpnlakVNLPMPCMHCDKPPCVQVCPVKA-TFKLDNG 165
Cdd:cd10550     1 LVVDPEKCTGCRTCELACslKHEGVFNPSLSrIRVVRFEPEG-------LDVPVVCRQCEDAPCVEACPVGAiSRDEETG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 166 IVTIDNDRCIGCRYCIIACPYGARSFDFGEsyedemlsfndvtspeygiergergkrkspiGTVRKCNFClhrlerGEEP 245
Cdd:cd10550    74 AVVVDEDKCIGCGMCVEACPFGAIRVDPET-------------------------------GKAIKCDLC------GGDP 116


                  ....*.
gi 1783788852 246 ACVETC 251
Cdd:cd10550   117 ACVKVC 122
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 138-261 6.24e-23

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: 90.39  E-value: 6.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 138 LPMPCMHCDKPPCVQVCPVKATFK-LDNGIVTIDNDRCIGCRYCIIACPYGArsfdfgesyedemLSFNDVTspeygier 216
Cdd:pfam13247   6 FPEQCRHCLNPPCKASCPVGAIYKdEETGAVLLDEKTCRGWRECVSACPYNI-------------PRYNDET-------- 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1783788852 217 gergkrkspiGTVRKCNFCLHRLERGEEPACVETCIGDARFFGDL 261
Cdd:pfam13247  65 ----------GKAEKCDMCYDRVEAGLLPACVQTCPTGAMNFGDR 99
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 89-272 8.17e-23

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


Pssm-ID: 319890 [Multi-domain]  Cd Length: 200  Bit Score: 93.25  E-value: 8.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  89 GMVIDLQKCVGCD-----SCTVACKSEN--RTPPGIS---------------------------YN------VVLEEEIG 128
Cdd:cd16368     2 ATLIDLTKCDGCPgesipACVRACREKNqaRFPEPVSkpiqpywprkriedwsdkrdvtdrltpYNwlyvqkLTVDTAGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 129 EfpnlAKVNLPMPCMHCDKPPCVQVCPVKATFKLDNGIVTIDNDRCIGCRYCIIACPYGARSFDFGESYEDEMLsfndvt 208
Cdd:cd16368    82 E----KEVFIPRRCMHCDNPPCAKLCPFGAARKTPEGAVYIDDDLCFGGAKCRDVCPWHIPQRQAGVGIYLHLA------ 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1783788852 209 sPEYGiergerGKrkspiGTVRKCNFCLHRLERGEEPACVETCIGDARFFGdlndPNSTVSKLA 272
Cdd:cd16368   152 -PEYA------GG-----GVMYKCDLCKDLLAQGKPPACIEACPKGAQYFG----PRKEMVALA 199
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 123-259 1.29e-21

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: 93.19  E-value: 1.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 123 LEEEI-GEFPNLAKVNLPMPCMHCDKPPCVQVCPVKATFKLD-NGIVTIDNDRCIGCRYCIIACPYgarsfdfGESYede 200
Cdd:cd10557   159 LQEEIyLEFENTFMFYLPRICNHCLNPACVAACPSGAIYKREeDGIVLIDQDRCRGWRMCVSACPY-------KKVY--- 228

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1783788852 201 mlsFNDVTspeygiergergkrkspiGTVRKCNFCLHRLERGEEPACVETCIGDARFFG 259
Cdd:cd10557   229 ---YNWKT------------------GKSEKCIFCYPRLEAGQPTVCSETCVGRIRYLG 266
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 87-293 2.49e-21

Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate reductase (SER), a member of the DMSO reductase family. SER catalyzes the reduction of selenate to selenite in bacterial species that can obtain energy by respiring anaerobically with selenate as the terminal electron acceptor. The enzyme comprises three subunits SerABC, forming a heterotrimer, with the catalytic component (alpha-subunit), iron-sulfur protein (beta-subunit) and monomeric b-type heme-containing gamma subunit. Beta subunit contains coordinating one [3Fe-4S] cluster and three [4Fe-4S] clusters and functions as electron carrier.


Pssm-ID: 319878 [Multi-domain]  Cd Length: 287  Bit Score: 90.98  E-value: 2.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  87 KWGMVIDLQKCVGCDSCTVACKS-------------------------------------ENRTPPGISY---------- 119
Cdd:cd10556    11 QFAMVFDTNKCIACQTCTMACKStwtsgkgqeymwwnnvetkpyggyplgwdvrlldeegGQTWAEGGVYegktifeaaa 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 120 --NVVL----EEEIGEFPNLAKVN----------------------LPMPCMHCDKPPCVQVCPVKATFKL-DNGIVTID 170
Cdd:cd10556    91 agEQVLgyrpEDEDWRYPNIGEDEvngertpdtgsslpphpiwffyLPRICNHCTYPACLAACPRKAIYKReEDGIVLID 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 171 NDRCIGCRYCIIACPYgarsfdfgesyedemlsfndvTSPEYgieRGERGKRKSPIGtvrkcnfCLHRLERGEEPACVET 250
Cdd:cd10556   171 QERCRGYRECVEACPY---------------------KKPMY---NPTTRVSEKCIG-------CYPRIEEGDQTQCVSA 219

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1783788852 251 CIGDARFFGDLNDPNSTVSKLANSPR----------AFRLKSELGAGPNVIYL 293
Cdd:cd10556   220 CIGKIRLQGFINTPPDARWADDRDNPidflvhikkvALPLYPQFGTEPNVYYI 272
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 90-255 3.46e-18

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 84.41  E-value: 3.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  90 MVIDLQKCVGCDSCTVAC----------KSENRTPPGISynvVLEEeigefpnlAKVNLPMPCMHCDKPPCVQVCPVKAT 159
Cdd:PRK12769    5 IMANSQQCLGCHACEIACvmahndeqhvLSQHHFHPRIT---VIKH--------QQQRSAVTCHHCEDAPCARSCPNGAI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 160 FKLDNGiVTIDNDRCIGCRYCIIACPYGARSFdfgesyedemlsfndVTSPeygierGERGKRKSpigTVRKCNFClhrL 239
Cdd:PRK12769   74 SHVDDS-IQVNQQKCIGCKSCVVACPFGTMQI---------------VLTP------VAAGKVKA---TAHKCDLC---A 125

                         170
                  ....*....|....*.
gi 1783788852 240 ERGEEPACVETCIGDA 255
Cdd:PRK12769  126 GRENGPACVENCPADA 141
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 123-259 1.08e-17

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


Pssm-ID: 440755 [Multi-domain]  Cd Length: 485  Bit Score: 82.55  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 123 LEEEI-GEFPNLAKVNLPMPCMHCDKPPCVQVCPVKATFKLD-NGIVTIDNDRCIGCRYCIIACPYgarsfdfgesyedE 200
Cdd:COG1140   162 LQEEIyFEFENTFMFYLPRICEHCLNPACVASCPSGAIYKREeDGIVLVDQDKCRGWRMCVSGCPY-------------K 228

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1783788852 201 MLSFNDVTspeygiergerGKRKspigtvrKCNFCLHRLERGEEPACVETCIGDARFFG 259
Cdd:COG1140   229 KVYFNWKT-----------GKAE-------KCIFCYPRIEAGQPTVCSETCVGRIRYLG 269
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 90-188 1.27e-17

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: 77.35  E-value: 1.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  90 MVIDLQKCVGCDSCTVACKSENRTPPGISYNVvleeeigefPNLAKVNLPMPCMHCDKPPCVQVCPVKATFKLDNGIVTI 169
Cdd:cd16367    14 LVIDLDRCIRCDNCEKACADTHDGHSRLDRNG---------LRFGNLLVPTACRHCVDPVCMIGCPTGAIHRDDGGEVVI 84

                          90
                  ....*....|....*....
gi 1783788852 170 DnDRCIGCRYCIIACPYGA 188
Cdd:cd16367    85 S-DACCGCGNCASACPYGA 102
PRK10330 PRK10330
electron transport protein HydN;
90-251 2.08e-15

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 72.62  E-value: 2.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  90 MVIDLQKCVGCDSCTVAC---KSENRTPPGISYNVVLeeeigefPNL-----AKVNLPMPCMHCDKPPCVQVCPVKAtFK 161
Cdd:PRK10330    5 IIADASKCIGCRTCEVACvvsHQENQDCASLTPETFL-------PRIhvikgVNVSTATVCRQCEDAPCANVCPNGA-IS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 162 LDNGIVTIDNDRCIGCRYCIIACPYGARsfdfgesyedEMLSFNDVTSPEYGIE-RGERGKrkspigtVRKCNFCLHrle 240
Cdd:PRK10330   77 RDKGFVHVMQERCIGCKTCVVACPYGAM----------EVVVRPVIRNSGAGLNvRAEKAE-------ANKCDLCNH--- 136

                         170
                  ....*....|.
gi 1783788852 241 RGEEPACVETC 251
Cdd:PRK10330  137 REDGPACMAAC 147
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 90-188 2.68e-14

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 72.75  E-value: 2.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  90 MVIDLQKCVGCDSCTVAC-KSENRTPPGISYNVVLEEEIGEFPNLAKVnlPMPCMHCDKPPCVQVCPVKA-TFKLDNgiV 167
Cdd:PRK12809    5 IAAEAAECIGCHACEIACaVAHNQENWPLSHSDFRPRIHVVGKGQAAN--PVACHHCNNAPCVTACPVNAlTFQSDS--V 80

                          90       100
                  ....*....|....*....|.
gi 1783788852 168 TIDNDRCIGCRYCIIACPYGA 188
Cdd:PRK12809   81 QLDEQKCIGCKRCAIACPFGV 101
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 91-197 4.55e-14

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


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 67.68  E-value: 4.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  91 VIDLQKCVGCDSCTVACKSENRTPPGISYNVVLEEEIGEFPNLAKVNLpmpCMHCDKPPCVQVCPVKATFKLDNGIVTID 170
Cdd:cd16370     5 VKDMERCIGCYSCMLACSRRVHKSASLSKSAIRVRTRGGLEGGFTVVV---CRACEDPPCAEACPTGALEPRKGGGVVLD 81

                          90       100
                  ....*....|....*....|....*..
gi 1783788852 171 NDRCIGCRYCIIACPYGARSFDFGESY 197
Cdd:cd16370    82 KEKCIGCGNCVKACIVGAIFWDEETNK 108
Ferredoxin_N pfam16947
N-terminal region of 4Fe-4S ferredoxin iron-sulfur binding; Ferredoxin_N is a short domain ...
 20-68 3.24e-13

N-terminal region of 4Fe-4S ferredoxin iron-sulfur binding; Ferredoxin_N is a short domain that is often found at the N-terminus of 4Fe-4S ferredoxin iron-sulfur binding domain proteins from Archaea and a few bacteria.


Pssm-ID: 407169  Cd Length: 65  Bit Score: 63.20  E-value: 3.24e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1783788852  20 DAKTELDQSPYSTQLGMDMADDARRVVAGNLDIKAFHKKYHSSLLGEFG 68
Cdd:pfam16947  10 EAEEMLDDTEYDAELGMEMARDAMRVTKGELSEAEFHEKYHEDVVAEFG 58
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 89-263 5.56e-13

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: 66.30  E-value: 5.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  89 GMVIDLQKCVGCDSCTVACK---------SENR----TPPGISYN----VVLEEEIGEFPNLAKVNLPMPCMHCDKPPCV 151
Cdd:cd10559     1 SFLIDTTRCTACRGCQVACKqwnqlpaeqTKNTgshqNPPDLSANtyklVRFNEVRNENGKPDWLFFPDQCRHCVTPPCK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852 152 QVCPvkatfKLDNGIVtidNDRCIGcryciiACPYGARSFDfgesyedemLSFNDVTSP-EYGIERgergkRKSPIGTVR 230
Cdd:cd10559    81 DAAD-----MVPGAVI---QDEATG------AVVFTEKTAE---------LDFDDVLSAcPYNIPR-----KNEATGRIV 132

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1783788852 231 KCNFCLHRLERGEEPACVETCIGDARFFGDLND 263
Cdd:cd10559   133 KCDMCIDRVSNGLQPACVKACPTGAMNFGDRDE 165
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
97-190 6.68e-13

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 68.51  E-value: 6.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  97 CVGCDSCTVACKSENRTPPGISYNVVLEEEIGEFPNLAKVNLPMPCMHCDkpPCVQVCPVKAtFKLDNGIVTIDNDRCIG 176
Cdd:COG4624    48 CSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCY--PCVRACPVKA-IKVDDGKAEIDEEKCIS 124

                          90
                  ....*....|....
gi 1783788852 177 CRYCIIACPYGARS 190
Cdd:COG4624   125 CGQCVAVCPFGAIT 138
PRK09898 PRK09898
ferredoxin-like protein;
62-192 3.37e-12

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 64.47  E-value: 3.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  62 SLLGEFGdlFTQEPIDEE----GNTKKGVkwgMVIDLQKCVGCDSCTVACKSENRTPPG-------ISYNVVLEEE---- 126
Cdd:PRK09898   34 ALLSLLG--CKQEDIDSGtvglINTPKGV---LVTQRARCTGCHRCEISCTNFNDGSVGtffsrikIHRNYFFGDNgvgs 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1783788852 127 -IGEFPNLAKVnlPMPCMHCDKPPCVQVCPVKA-TFKLDNGIVTIDNDRCIGCRYCIIACPYGARSFD 192
Cdd:PRK09898  109 gGGLYGDLNYT--ADTCRQCKEPQCMNVCPIGAiTWQQKEGCITVDHKRCIGCSACTTACPWMMATVN 174
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
142-196 7.61e-12

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 59.74  E-value: 7.61e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1783788852 142 CMHCDKppCVQVCPVKAtFKLDNGIVTIDNDRCIGCRYCIIACPYGARSFDFGES 196
Cdd:COG2768    13 CIGCGA--CVKVCPVGA-ISIEDGKAVIDPEKCIGCGACIEVCPVGAIKIEWEED 64
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 91-188 2.63e-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: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 60.04  E-value: 2.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  91 VIDLQKCVGCDSCTVAC-----KSENRTPPGIsynVVLEEEIGEFPNLakvnlpmpCMHCDKppCVQVCPVKATFKLDNG 165
Cdd:cd16372     4 VTDPEKCIGCLQCEEACsktffKEEDREKSCI---RITETEGGYAINV--------CNQCGE--CIDVCPTGAITRDANG 70

                          90       100
                  ....*....|....*....|...
gi 1783788852 166 IVTIDNDRCIGCRYCIIACPYGA 188
Cdd:cd16372    71 VVMINKKLCVGCLMCVGFCPEGA 93
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 142-192 1.14e-10

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 56.60  E-value: 1.14e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1783788852 142 CMHCDKppCVQVCPVKAtFKLDNGIVTIDNDRCIGCRYCIIACPYGARSFD 192
Cdd:COG2221    17 CIGCGL--CVAVCPTGA-ISLDDGKLVIDEEKCIGCGACIRVCPTGAIKGE 64
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 81-188 1.94e-09

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: 54.71  E-value: 1.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  81 NTKKGVKWGMVIDLQKCVGCDSCTVAC-------KSENRTPPGISYNVVLEEEIgefpnlakvnlpmpCMHCDKppCVQV 153
Cdd:cd10549    26 GPNGAIARGPEIDEDKCVFCGACVEVCptgaielTPEGKEYVPKEKEAEIDEEK--------------CIGCGL--CVKV 89

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1783788852 154 CPVKATFKLDNGIVTIDNDRCIGCRYCIIACPYGA 188
Cdd:cd10549    90 CPVDAITLEDELEIVIDKEKCIGCGICAEVCPVNA 124
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 142-191 1.35e-08

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 50.50  E-value: 1.35e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1783788852 142 CMHCDKppCVQVCPVKATFKLDNGIVTIDNDRCIGCRYCIIACPYGARSF 191
Cdd:COG1149    13 CIGCGL--CVEVCPEGAIKLDDGGAPVVDPDLCTGCGACVGVCPTGAITL 60
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 91-188 2.54e-08

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 51.63  E-value: 2.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  91 VIDLQKCVGCDSCTVACKSEnrtppGISYNVVLEEEIGEFPNLAKvnlpmpCMHCDKppCVQVCPVKA---------TFK 161
Cdd:cd10549     2 KYDPEKCIGCGICVKACPTD-----AIELGPNGAIARGPEIDEDK------CVFCGA--CVEVCPTGAieltpegkeYVP 68

                          90       100
                  ....*....|....*....|....*..
gi 1783788852 162 LDNGIVtIDNDRCIGCRYCIIACPYGA 188
Cdd:cd10549    69 KEKEAE-IDEEKCIGCGLCVKVCPVDA 94
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 150-188 5.07e-08

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 49.27  E-value: 5.07e-08
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1783788852 150 CVQVCPVKAtFKLDNGIVTIDNDRCIGCRYCIIACPYGA 188
Cdd:COG4231    30 CVKVCPADA-IEEGDGKAVIDPDLCIGCGSCVQVCPVDA 67
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 142-188 7.05e-08

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 48.59  E-value: 7.05e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1783788852 142 CMHCDKppCVQVCPVKA---TFKLDNGIVTIDNDRCIGCRYCIIACPYGA 188
Cdd:COG1143     4 CIGCGL--CVRVCPVDAitiEDGEPGKVYVIDPDKCIGCGLCVEVCPTGA 51
NapF COG1145
Ferredoxin [Energy production and conversion];
142-191 2.69e-07

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 50.49  E-value: 2.69e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1783788852 142 CMHCDKppCVQVCPVKA-TFKLDNGIVTIDNDRCIGCRYCIIACPYGARSF 191
Cdd:COG1145   184 CIGCGL--CVKVCPTGAiRLKDGKPQIVVDPDKCIGCGACVKVCPVGAISL 232
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
91-188 8.64e-07

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 49.16  E-value: 8.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  91 VIDLQKCVGCDSCTVACksenrtPPGISYNVVLEEEI------GEFPNLAKVNLPMPCMHCDKppCVQVCPVKAtFKLDN 164
Cdd:PRK07118  164 VVDEDKCTGCGACVKAC------PRNVIELIPKSARVfvacnsKDKGKAVKKVCEVGCIGCGK--CVKACPAGA-ITMEN 234

                          90       100
                  ....*....|....*....|....
gi 1783788852 165 GIVTIDNDRCIGCRYCIIACPYGA 188
Cdd:PRK07118  235 NLAVIDQEKCTSCGKCVEKCPTKA 258
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 142-185 1.42e-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: 48.45  E-value: 1.42e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1783788852 142 CMHCDKppCVQVCPVKATFKLDNGIVTIDNDRCIGCRYCIIACP 185
Cdd:COG2878   139 CIGCGD--CIKACPFDAIVGAAKGMHTVDEDKCTGCGLCVEACP 180
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 94-197 2.25e-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: 46.48  E-value: 2.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  94 LQKCVGCDSCTVACksenrtPPGISYNVVLEEeigefpNLAKVNLPM------PCMHCDKPpCVQVCP-------VKATF 160
Cdd:cd16373    13 LALCIRCGLCVEAC------PTGVIQPAGLED------GLEGGRTPYldpregPCDLCCDA-CVEVCPtgalrplDLEEQ 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1783788852 161 KLDNGIVTIDNDRCI------GCRYCIIACPYGARSFDFGESY 197
Cdd:cd16373    80 KVKMGVAVIDKDRCLawqggtDCGVCVEACPTEAIAIVLEDDV 122
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 142-188 2.93e-06

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 43.67  E-value: 2.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1783788852 142 CMHCDKppCVQVCPVKA------TFKLDNGIVTIDNDRCIGCRYCIIACPYGA 188
Cdd:pfam12838   1 CIGCGA--CVAACPVGAitldevGEKKGTKTVVIDPERCVGCGACVAVCPTGA 51
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
142-193 4.59e-06

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 46.98  E-value: 4.59e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1783788852 142 CMHCDKppCVQVCPVKAtfKLDNGivTIDNDRCIGCRYCIIACPYGARSFDF 193
Cdd:COG0348   212 CIDCGL--CVKVCPMGI--DIRKG--EINQSECINCGRCIDACPKDAIRFSS 257
PRK13795 PRK13795
hypothetical protein; Provisional
 142-185 1.26e-05

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 46.53  E-value: 1.26e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1783788852 142 CMHCDKppCVQVCPVKAtFKLDNG--IVTIDNDRCIGCRYCIIACP 185
Cdd:PRK13795  583 CVGCGV--CVGACPTGA-IRIEEGkrKISVDEEKCIHCGKCTEVCP 625
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 142-188 1.68e-05

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


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 42.35  E-value: 1.68e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1783788852 142 CMHCDKppCVQVCPVKATFKLDNGIVTIDNDRCIGCRYCIIACPYGA 188
Cdd:COG1144    32 CIGCGL--CWIVCPDGAIRVDDGKYYGIDYDYCKGCGICAEVCPVKA 76
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
125-202 2.10e-05

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 45.62  E-value: 2.10e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1783788852 125 EEIGEFPNLAKVNlPMPCMHCDKppCVQVCPVKATFKLDNGIVTIDNDRCIGCRYCIIACPYGARSFdfgESYEDEML 202
Cdd:COG1148   482 GELGVEPSVAEVD-PEKCTGCGR--CVEVCPYGAISIDEKGVAEVNPALCKGCGTCAAACPSGAISL---KGFTDDQI 553
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 142-185 3.43e-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: 3.43e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1783788852 142 CMHCDKppCVQVCPVKAT------FKLDNGIVTIDNDRCIGCRYCIIACP 185
Cdd:pfam13237   9 CIGCGR--CTAACPAGLTrvgaivERLEGEAVRIGVWKCIGCGACVEACP 56
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 142-188 5.64e-05

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 44.48  E-value: 5.64e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1783788852 142 CMHCDKppCVQVCPVKATFKLDNGI-VTIDNDRCIGCRYCIIACPYGA 188
Cdd:PRK12771  512 CFECDN--CYGACPQDAIIKLGPGRrYHFDYDKCTGCHICADVCPCGA 557
Fer4_6 pfam12837
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 166-188 6.23e-05

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


Pssm-ID: 432822 [Multi-domain]  Cd Length: 24  Bit Score: 39.14  E-value: 6.23e-05
                          10        20
                  ....*....|....*....|...
gi 1783788852 166 IVTIDNDRCIGCRYCIIACPYGA 188
Cdd:pfam12837   1 VVEVDPDKCIGCGRCVVVCPYGA 23
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
150-187 7.36e-05

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 43.38  E-value: 7.36e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1783788852 150 CVQVCPVKAtFKLDNGIVTIDNDRCIGCRYCIIACPYG 187
Cdd:PRK07118  147 CVAACPFDA-IHIENGLPVVDEDKCTGCGACVKACPRN 183
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 142-188 9.34e-05

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 39.69  E-value: 9.34e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1783788852 142 CMHCDKppCVQVCPVKAtFKLDNG---IVTIDNDRCIGCRYCIIACPYGA 188
Cdd:COG1146    10 CIGCGA--CVEVCPVDV-LELDEEgkkALVINPEECIGCGACELVCPVGA 56
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 90-155 1.01e-04

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


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 39.54  E-value: 1.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1783788852  90 MVIDLQKCVGCDSCTVACksenrtpPGISYNVVLEEEIgeFPNLAKVNLPMPCMHCDKppCVQVCP 155
Cdd:pfam13237   2 VVIDPDKCIGCGRCTAAC-------PAGLTRVGAIVER--LEGEAVRIGVWKCIGCGA--CVEACP 56
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 142-185 1.34e-04

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


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 41.71  E-value: 1.34e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1783788852 142 CMHCDKppCVQVCPVKATFKLDNGIVTIDNDRCIGCRYCIIACP 185
Cdd:TIGR01944 115 CIGCTK--CIQACPVDAIVGAAKAMHTVIADECTGCDLCVEPCP 156
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
140-192 1.72e-04

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 42.71  E-value: 1.72e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1783788852 140 MPCMHCDKPPCVQVCPVKATFKLDNGIVTIDNDRCIGCRYCIIACPYGARSFD 192
Cdd:COG4624    59 CCCCRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCYPCVRACPVKAIKVD 111
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 167-188 1.94e-04

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


Pssm-ID: 459642 [Multi-domain]  Cd Length: 24  Bit Score: 38.00  E-value: 1.94e-04
                          10        20
                  ....*....|....*....|..
gi 1783788852 167 VTIDNDRCIGCRYCIIACPYGA 188
Cdd:pfam00037   1 VVIDEEKCIGCGACVEVCPVGA 22
NapF COG1145
Ferredoxin [Energy production and conversion];
86-188 6.04e-04

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 40.48  E-value: 6.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  86 VKWGMVIDLQKCVGCDSCTVACKSENRTPPGISYNVVLEEEIGEFPNLAKVNLPMPCMHCDKPPCVQVCPVKATFKLDN- 164
Cdd:COG1145    92 NLKAVALVLLLALAVAGAAKRLIISAVKLVAGLVVAAGEVLLVIAAALAEAGLAILGAAAPVDALAISGGKKIEEELKIa 171

                          90       100
                  ....*....|....*....|....*..
gi 1783788852 165 ---GIVTIDNDRCIGCRYCIIACPYGA 188
Cdd:COG1145   172 ikkAKAVIDAEKCIGCGLCVKVCPTGA 198
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 166-188 7.15e-04

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 37.40  E-value: 7.15e-04
                          10        20
                  ....*....|....*....|...
gi 1783788852 166 IVTIDNDRCIGCRYCIIACPYGA 188
Cdd:COG1149     5 IPVIDEEKCIGCGLCVEVCPEGA 27
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 165-188 1.37e-03

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 36.61  E-value: 1.37e-03
                          10        20
                  ....*....|....*....|....
gi 1783788852 165 GIVTIDNDRCIGCRYCIIACPYGA 188
Cdd:COG1146     1 MMPVIDTDKCIGCGACVEVCPVDV 24
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
150-187 1.42e-03

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 39.28  E-value: 1.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1783788852 150 CVQVCPVKAT----FKLDNGIVTIDNDRCIGCRYCIIACPYG 187
Cdd:COG0348   184 CRYLCPYGAFqgllSDLSTLRVRYDRGDCIDCGLCVKVCPMG 225
FixX COG2440
Ferredoxin-like protein FixX [Energy production and conversion];
144-188 1.62e-03

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


Pssm-ID: 441981 [Multi-domain]  Cd Length: 87  Bit Score: 36.72  E-value: 1.62e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1783788852 144 HCDKPPCVQVCPVkATFKLD-NGIVTIDNDRCIGCRYCIIACPYGA 188
Cdd:COG2440    26 RCLAKPCTRYCPA-GVYEIVgDGRLQINYENCLECGTCRIKCPTQN 70
PRK08764 PRK08764
Rnf electron transport complex subunit RnfB;
142-185 1.71e-03

Rnf electron transport complex subunit RnfB;


Pssm-ID: 181550 [Multi-domain]  Cd Length: 135  Bit Score: 37.98  E-value: 1.71e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1783788852 142 CMHCDKppCVQVCPVKATFKLDNGIVTIDNDRCIGCRYCIIACP 185
Cdd:PRK08764   87 CIGCTK--CIQACPVDAIVGGAKHMHTVIAPLCTGCELCVPACP 128
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 168-188 1.92e-03

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


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 36.57  E-value: 1.92e-03
                          10        20
                  ....*....|....*....|.
gi 1783788852 168 TIDNDRCIGCRYCIIACPYGA 188
Cdd:COG1144    26 VVDEDKCIGCGLCWIVCPDGA 46
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 150-185 2.29e-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: 2.29e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1783788852 150 CVQVCPVKA---TFKLDNGIVTIDNDRCIGCRYCIIACP 185
Cdd:cd16373   105 CVEACPTEAiaiVLEDDVLRPVVDEDKCVGCGLCEYVCP 143
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 150-188 2.36e-03

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


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 37.61  E-value: 2.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1783788852 150 CVQVCPVKA-TFKLDNGIV---TIDNDRCIGCRYCIIACPYGA 188
Cdd:cd10564    91 CQDACPTQAiRFRPRLGGIalpELDADACTGCGACVSVCPVGA 133
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 161-200 2.45e-03

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 36.17  E-value: 2.45e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1783788852 161 KLDNGI----VTIDNDRCIGCRYCIIACPYGARSFDFGESYEDE 200
Cdd:COG4231     7 ILDNRTtamrYVIDEDKCTGCGACVKVCPADAIEEGDGKAVIDP 50
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 97-158 3.51e-03

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 34.81  E-value: 3.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1783788852  97 CVGCDSCTVACksenrtppgiSYNVVLEEEIGEFPNLAKVNL-PMPCMHCDKppCVQVCPVKA 158
Cdd:pfam12838   1 CIGCGACVAAC----------PVGAITLDEVGEKKGTKTVVIdPERCVGCGA--CVAVCPTGA 51
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
150-202 3.52e-03

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 37.55  E-value: 3.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1783788852 150 CVQVCPVKA-----TFKLDNGIVT----IDNDRCIGCRYCIIACPYGA----RSFDFGES------YEDEML 202
Cdd:PRK05888   66 CAAICPADAitieaAEREDGRRRTtrydINFGRCIFCGFCEEACPTDAivetPDFELATEtreeliYDKEKL 137
Fer4_2 pfam12797
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 165-186 4.32e-03

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


Pssm-ID: 463711 [Multi-domain]  Cd Length: 22  Bit Score: 33.91  E-value: 4.32e-03
                          10        20
                  ....*....|....*....|..
gi 1783788852 165 GIVTIDNDRCIGCRYCIIACPY 186
Cdd:pfam12797   1 WKPLIDADKCIGCGACVSACPA 22
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
117-188 4.82e-03

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 36.08  E-value: 4.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1783788852 117 ISYNVVLEEEIGEFPNLAKVNLPMPCMHCdkPPCVQVCPVKATFKLDNGIVTIDNDRCIGCRYCIIACPYGA 188
Cdd:PRK09623   28 ISLGTTLSNFTGDWRTFMPVVDESKCVKC--YICWKFCPEPAIYIKEDGYVAIDYDYCKGCGICANECPTKA 97
Fer4_21 pfam14697
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 142-185 5.37e-03

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


Pssm-ID: 434137 [Multi-domain]  Cd Length: 59  Bit Score: 34.56  E-value: 5.37e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1783788852 142 CMHCDKppCVQVCP---VKATFKLDNGIVTIDNDRCIGCRYCIIACP 185
Cdd:pfam14697   8 CIGCGK--CYIACPdtsHQAIVGDGKRHHTVIEDECTGCNLCVSVCP 52
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 91-158 5.70e-03

HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 36.47  E-value: 5.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1783788852  91 VIDLQKCVGCDSCTVACksenrtPPGiSYNVVLEEEIGEFPNLAKVNLPMPCMHC----DKPPCVQVCPVKA 158
Cdd:cd10554    81 QVDEERCIGCKLCVLAC------PFG-AIEMAPTTVPGVDWERGPRAVAVKCDLCagreGGPACVEACPTKA 145
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 75-158 6.36e-03

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


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 35.03  E-value: 6.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783788852  75 PIDEEGNTKKGVKWGM-----VIDLQKCVGCDSCTVACKsenrtppgisYNVVLEEEIGEFpnlaKVNlPMPCMHCDKpp 149
Cdd:COG1144     5 AITEPGGTAAYKTGGWrverpVVDEDKCIGCGLCWIVCP----------DGAIRVDDGKYY----GID-YDYCKGCGI-- 67


                  ....*....
gi 1783788852 150 CVQVCPVKA 158
Cdd:COG1144    68 CAEVCPVKA 76
Fer COG1141
Ferredoxin [Energy production and conversion];
167-185 8.03e-03

Ferredoxin [Energy production and conversion];


Pssm-ID: 440756 [Multi-domain]  Cd Length: 63  Bit Score: 34.09  E-value: 8.03e-03
                          10
                  ....*....|....*....
gi 1783788852 167 VTIDNDRCIGCRYCIIACP 185
Cdd:COG1141     3 VTVDRDTCIGCGLCVALAP 21
 
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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