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Conserved domains on  [gi|517009692|ref|WP_018210970|]
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4Fe-4S dicluster domain-containing protein [Desulfitobacterium hafniense]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 8-160 6.37e-60

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: 182.46  E-value: 6.37e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692   8 FIHADLSRCLSCKSCELACGLAHAGYEIEGAAAGQMKLKPRVSVVQQGTTVALTQCRQCEDAPCVKVCPNGSLYQEEGLV 87
Cdd:cd10554    1 FVIADPDKCIGCRTCEVACAAAHSGKGIFEAGTDGLPFLPRLRVVKTGEVTAPVQCRQCEDAPCANVCPVGAISQEDGVV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517009692  88 KLNRETCIGCKLCARACPFGSITMTTEVVERADGKKNNRTKALKCDLCFSRnkeikAEGCACIQACPTKVLSL 160
Cdd:cd10554   81 QVDEERCIGCKLCVLACPFGAIEMAPTTVPGVDWERGPRAVAVKCDLCAGR-----EGGPACVEACPTKALTL 148
 
Name Accession Description Interval E-value
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 8-160 6.37e-60

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: 182.46  E-value: 6.37e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692   8 FIHADLSRCLSCKSCELACGLAHAGYEIEGAAAGQMKLKPRVSVVQQGTTVALTQCRQCEDAPCVKVCPNGSLYQEEGLV 87
Cdd:cd10554    1 FVIADPDKCIGCRTCEVACAAAHSGKGIFEAGTDGLPFLPRLRVVKTGEVTAPVQCRQCEDAPCANVCPVGAISQEDGVV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517009692  88 KLNRETCIGCKLCARACPFGSITMTTEVVERADGKKNNRTKALKCDLCFSRnkeikAEGCACIQACPTKVLSL 160
Cdd:cd10554   81 QVDEERCIGCKLCVLACPFGAIEMAPTTVPGVDWERGPRAVAVKCDLCAGR-----EGGPACVEACPTKALTL 148
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
6-160 1.89e-43

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 140.56  E-value: 1.89e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692   6 NRFIHADLSRCLSCKSCELACGLAHAGYEIEgaaagqmKLKPRVSVVQQGTTVALTQCRQCEDAPCVKVCPNGSLYQEEG 85
Cdd:COG1142    2 NKFIIADPEKCIGCRTCEAACAVAHEGEEGE-------PFLPRIRVVRKAGVSAPVQCRHCEDAPCAEVCPVGAITRDDG 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517009692  86 LVKLNRETCIGCKLCARACPFGSITMTTEVVeradgkknnRTKALKCDLCFSRnkeikAEGCACIQACPTKVLSL 160
Cdd:COG1142   75 AVVVDEEKCIGCGLCVLACPFGAITMVGEKS---------RAVAVKCDLCGGR-----EGGPACVEACPTGALRL 135
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 6-160 7.34e-39

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 139.11  E-value: 7.34e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692   6 NRFIHADLSRCLSCKSCELACGLAHAGyeiEGAAAGQMKLKPRVSVVQQGTTVALTQCRQCEDAPCVKVCPNGSLYQEEG 85
Cdd:PRK12769   2 NRFIMANSQQCLGCHACEIACVMAHND---EQHVLSQHHFHPRITVIKHQQQRSAVTCHHCEDAPCARSCPNGAISHVDD 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517009692  86 LVKLNRETCIGCKLCARACPFGSITMTTEVVERAdgkkNNRTKALKCDLCFSRnkeikAEGCACIQACPTKVLSL 160
Cdd:PRK12769  79 SIQVNQQKCIGCKSCVVACPFGTMQIVLTPVAAG----KVKATAHKCDLCAGR-----ENGPACVENCPADALQL 144
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 62-160 1.26e-13

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: 63.04  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692   62 QCRQCEDAPCVKVCPNGSLYQEE--GLVKLNRETCIGCKLCARACPFGsitmttevVERADGKKNnrtKALKCDLCFSRN 139
Cdd:pfam13247   9 QCRHCLNPPCKASCPVGAIYKDEetGAVLLDEKTCRGWRECVSACPYN--------IPRYNDETG---KAEKCDMCYDRV 77

                          90       100
                  ....*....|....*....|.
gi 517009692  140 KEIKAEgcACIQACPTKVLSL 160
Cdd:pfam13247  78 EAGLLP--ACVQTCPTGAMNF 96
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 92-156 1.52e-07

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


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 49.09  E-value: 1.52e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517009692  92 ETCIGCKLCARACPFGSITMTtevveraDGK---KNNrtkalkCDLCfsrnkeikaegCACIQACPTK 156
Cdd:NF038196 185 DKCIGCGICAKVCPVNNIEME-------DGKpvwGHN------CTHC-----------LACIHRCPKE 228
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 92-160 1.76e-06

NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes "I" subunits from the closely related F420H2 dehydrogenase and formate hydrogenlyase complexes. [Energy metabolism, Electron transport]


Pssm-ID: 273902 [Multi-domain]  Cd Length: 122  Bit Score: 44.71  E-value: 1.76e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517009692   92 ETCIGCKLCARACPFGSITMTTEvvERADGKKN------NRTKALKCDLcfsrnkeikaegcaCIQACPTKVLSL 160
Cdd:TIGR01971  43 EKCIGCTLCAAVCPADAIRVVPA--EGEDGKRRlkfyeiNFGRCIFCGL--------------CEEACPTDAIVL 101
 
Name Accession Description Interval E-value
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 8-160 6.37e-60

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: 182.46  E-value: 6.37e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692   8 FIHADLSRCLSCKSCELACGLAHAGYEIEGAAAGQMKLKPRVSVVQQGTTVALTQCRQCEDAPCVKVCPNGSLYQEEGLV 87
Cdd:cd10554    1 FVIADPDKCIGCRTCEVACAAAHSGKGIFEAGTDGLPFLPRLRVVKTGEVTAPVQCRQCEDAPCANVCPVGAISQEDGVV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517009692  88 KLNRETCIGCKLCARACPFGSITMTTEVVERADGKKNNRTKALKCDLCFSRnkeikAEGCACIQACPTKVLSL 160
Cdd:cd10554   81 QVDEERCIGCKLCVLACPFGAIEMAPTTVPGVDWERGPRAVAVKCDLCAGR-----EGGPACVEACPTKALTL 148
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
6-160 1.89e-43

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 140.56  E-value: 1.89e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692   6 NRFIHADLSRCLSCKSCELACGLAHAGYEIEgaaagqmKLKPRVSVVQQGTTVALTQCRQCEDAPCVKVCPNGSLYQEEG 85
Cdd:COG1142    2 NKFIIADPEKCIGCRTCEAACAVAHEGEEGE-------PFLPRIRVVRKAGVSAPVQCRHCEDAPCAEVCPVGAITRDDG 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517009692  86 LVKLNRETCIGCKLCARACPFGSITMTTEVVeradgkknnRTKALKCDLCFSRnkeikAEGCACIQACPTKVLSL 160
Cdd:COG1142   75 AVVVDEEKCIGCGLCVLACPFGAITMVGEKS---------RAVAVKCDLCGGR-----EGGPACVEACPTGALRL 135
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 6-160 7.34e-39

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 139.11  E-value: 7.34e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692   6 NRFIHADLSRCLSCKSCELACGLAHAGyeiEGAAAGQMKLKPRVSVVQQGTTVALTQCRQCEDAPCVKVCPNGSLYQEEG 85
Cdd:PRK12769   2 NRFIMANSQQCLGCHACEIACVMAHND---EQHVLSQHHFHPRITVIKHQQQRSAVTCHHCEDAPCARSCPNGAISHVDD 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517009692  86 LVKLNRETCIGCKLCARACPFGSITMTTEVVERAdgkkNNRTKALKCDLCFSRnkeikAEGCACIQACPTKVLSL 160
Cdd:PRK12769  79 SIQVNQQKCIGCKSCVVACPFGTMQIVLTPVAAG----KVKATAHKCDLCAGR-----ENGPACVENCPADALQL 144
PRK10330 PRK10330
electron transport protein HydN;
6-158 2.14e-34

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 118.84  E-value: 2.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692   6 NRFIHADLSRCLSCKSCELACGLAHAGYEiEGAAAGQMKLKPRVSVVQQGTTVALTQCRQCEDAPCVKVCPNGSLYQEEG 85
Cdd:PRK10330   2 NRFIIADASKCIGCRTCEVACVVSHQENQ-DCASLTPETFLPRIHVIKGVNVSTATVCRQCEDAPCANVCPNGAISRDKG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517009692  86 LVKLNRETCIGCKLCARACPFGSITMTTEVVERADGKKNN----RTKALKCDLCFSRnkeikAEGCACIQACPTKVL 158
Cdd:PRK10330  81 FVHVMQERCIGCKTCVVACPYGAMEVVVRPVIRNSGAGLNvraeKAEANKCDLCNHR-----EDGPACMAACPTHAL 152
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 9-160 3.77e-31

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: 109.27  E-value: 3.77e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692   9 IHADLSRCLSCKSCELACGLAHAGYE-IEGAAAGQMKLKPRVSVVQQGTTVALTQCRQCEDAPCVKVCPNGSLYQEE--G 85
Cdd:cd10563    2 IFIDEEKCLGCKLCEVACAVAHSKSKdLIKAKLEKERPRPRIRVEESGGRSFPLQCRHCDEPPCVKACMSGAMHKDPetG 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517009692  86 LVKLNRETCIGCKLCARACPFGSITmttevveradgKKNNRTKALKCDLCFSRnkeikaEGCACIQACPTKVLSL 160
Cdd:cd10563   82 IVIHDEEKCVGCWMCVMVCPYGAIR-----------PDKERKVALKCDLCPDR------ETPACVEACPTGALVL 139
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 6-160 2.45e-30

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 115.12  E-value: 2.45e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692   6 NRFIHADLSRCLSCKSCELACGLAHagyEIEGAAAGQMKLKPRVSVVQQGTTVALTQCRQCEDAPCVKVCPNGSLYQEEG 85
Cdd:PRK12809   2 NKFIAAEAAECIGCHACEIACAVAH---NQENWPLSHSDFRPRIHVVGKGQAANPVACHHCNNAPCVTACPVNALTFQSD 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517009692  86 LVKLNRETCIGCKLCARACPFGSITMTTEVveradgkknnrtkALKCDLCFSRNKEIKaegcACIQACPTKVLSL 160
Cdd:PRK12809  79 SVQLDEQKCIGCKRCAIACPFGVVEMVDTI-------------AQKCDLCNQRSSGTQ----ACIEVCPTQALRL 136
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 12-158 1.54e-28

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: 102.47  E-value: 1.54e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  12 DLSRCLSCKSCELACGLAHAGYEiegaaagqMKLKPRVSVVQQGTTVAL---TQCRQCEDAPCVKVCPNGSLYQ-EEGLV 87
Cdd:cd04410    4 DLDRCIGCGTCEVACKQEHGLRP--------GPDWSRIKVIEGGGLERAflpVSCMHCEDPPCVKACPTGAIYKdEDGIV 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517009692  88 KLNRETCIGCKLCARACPFGSITMTTEVVeradgkknnrtKALKCDLCFSRNKEikAEGCACIQACPTKVL 158
Cdd:cd04410   76 LIDEDKCIGCGSCVEACPYGAIVFDPEPG-----------KAVKCDLCGDRLDE--GLEPACVKACPTGAL 133
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 12-158 5.40e-28

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 102.33  E-value: 5.40e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  12 DLSRCLSCKSCELACGLAHAGyeiegaAAGQMKLkpRVSVVQQGTTVAL------TQCRQCEDAPCVKVCPNGSLYQ-EE 84
Cdd:COG0437   11 DLTKCIGCRACVVACKEENNL------PVGVTWR--RVRRYEEGEFPNVewlfvpVLCNHCDDPPCVKVCPTGATYKrED 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517009692  85 GLVKLNRETCIGCKLCARACPFGSITMttevvERADGkknnrtKALKCDLCFSRNKEikAEGCACIQACPTKVL 158
Cdd:COG0437   83 GIVLVDYDKCIGCRYCVAACPYGAPRF-----NPETG------VVEKCTFCADRLDE--GLLPACVEACPTGAL 143
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 9-160 5.77e-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: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 100.81  E-value: 5.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692   9 IHADLSRCLSCKSCELACGLAHAGyeiegaaagqmklKPRVSVVQQGTTVAL-TQCRQCEDAPCVKVCPNGSLYQ-EEGL 86
Cdd:cd16374    1 VYVDPERCIGCRACEIACAREHSG-------------KPRISVEVVEDLASVpVRCRHCEDAPCMEVCPTGAIYRdEDGA 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517009692  87 VKLNRETCIGCKLCARACPFGSITMTTEvveradgkknnRTKALKCDLCFSRNKEIKAEgcACIQACPTKVLSL 160
Cdd:cd16374   68 VLVDPDKCIGCGMCAMACPFGVPRFDPS-----------LKVAVKCDLCIDRRREGKLP--ACVEACPTGALKF 128
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 9-160 5.84e-26

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


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 95.72  E-value: 5.84e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692   9 IHADLSRCLSCKSCELACGLAHAGYEIEGAAagqmklkpRVSVVQ---QGTTVALTqCRQCEDAPCVKVCPNGSLYQEE- 84
Cdd:cd10550    1 LVVDPEKCTGCRTCELACSLKHEGVFNPSLS--------RIRVVRfepEGLDVPVV-CRQCEDAPCVEACPVGAISRDEe 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517009692  85 -GLVKLNRETCIGCKLCARACPFGSITMTTEvveradgkknnRTKALKCDLCfsrnkeiKAEGcACIQACPTKVLSL 160
Cdd:cd10550   72 tGAVVVDEDKCIGCGMCVEACPFGAIRVDPE-----------TGKAIKCDLC-------GGDP-ACVKVCPTGALEF 129
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 12-158 1.27e-24

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: 93.75  E-value: 1.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  12 DLSRCLSCKSCELACGLAHA-----------GYEIEGAAAGQMKLKPRvsvvqqgttvaltQCRQCEDAPCVKVCPNGSL 80
Cdd:cd10551    4 DLRKCIGCGACVVACKAENNvppgvfrnrvlEYEVGEYPNVKRTFLPV-------------LCNHCENPPCVKVCPTGAT 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  81 YQ-EEGLVKLNRETCIGCKLCARACPFGSITMTTEVVERADGKKNNRTK-ALKCDLCFSRNKEikAEGCACIQACPTKVL 158
Cdd:cd10551   71 YKrEDGIVLVDYDKCIGCRYCMAACPYGARYFNPEEPHEFGEVPVRPKGvVEKCTFCYHRLDE--GLLPACVEACPTGAR 148
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 12-158 5.38e-22

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


Pssm-ID: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 85.69  E-value: 5.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  12 DLSRCLSCKSCELACGLAHagyeiegaaagqmKLKP-----RVSVVQQGTTVAL------TQCRQCEDAPCVKVCPNGSL 80
Cdd:cd16371    5 DQERCIGCKACEIACKDKN-------------DLPPgvnwrRVYEYEGGEFPEVfayflsMSCNHCENPACVKVCPTGAI 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517009692  81 YQEE-GLVKLNRETCIGCKLCARACPFGSITMTTEvveradgkknnRTKALKCDLCFSRNKEikAEGCACIQACPTKVL 158
Cdd:cd16371   72 TKREdGIVVVDQDKCIGCGYCVWACPYGAPQYNPE-----------TGKMDKCDMCVDRLDE--GEKPACVAACPTRAL 137
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 12-155 4.66e-20

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: 80.81  E-value: 4.66e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  12 DLSRCLSCKSCELACGLAHAGYeiegaaagqmklkPRVsvVQQGTTVA----LTQCRQCEDAPCVKVCPNGSLYQEEGLV 87
Cdd:cd16367   17 DLDRCIRCDNCEKACADTHDGH-------------SRL--DRNGLRFGnllvPTACRHCVDPVCMIGCPTGAIHRDDGGE 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517009692  88 KLNRETCIGCKLCARACPFGSITMttevveradgkknnrTKALKCDLCFSRNkeikaeGCACIQACPT 155
Cdd:cd16367   82 VVISDACCGCGNCASACPYGAIQM---------------VRAVKCDLCAGYA------GPACVSACPT 128
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 12-159 1.37e-19

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: 81.28  E-value: 1.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  12 DLSRCLSCKSCELACGLAHAGYEIEGAAAGQMKLKPRVS-----------VVQQGTTVAL---TQCRQCEDAPCVKVCP- 76
Cdd:cd10558    5 DVSKCIGCKACQVACKEWNDLRAEVGHNVGTYQNPADLSpetwtlmkfreVEDNGKLEWLirkDGCMHCADPGCLKACPs 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  77 NGSLYQ-EEGLVKLNRETCIGCKLCARACPFGsitmttevVERADGKKNnrtKALKCDLCFSRNKEikAEGCACIQACPT 155
Cdd:cd10558   85 PGAIVQyANGIVDFQSDKCIGCGYCIKGCPFD--------IPRISKDDN---KMYKCTLCSDRVSV--GLEPACVKTCPT 151


                 ....
gi 517009692 156 KVLS 159
Cdd:cd10558  152 GALH 155
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 12-155 3.51e-19

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: 80.51  E-value: 3.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  12 DLSRCLSCKSCELAC----GLAHAGYEIEG-----------------AAAGQMKLKPRVSVVQQGTTVALT-QCRQCEDA 69
Cdd:cd10560    5 DTSICIGCKACEVACkqwnQLPADGYDFSGmsydntgdlsastwrhvKFIERPTEDGPANEGGDLQWLFMSdVCKHCTDA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  70 PCVKVCPNGSLYQEE-GLVKLNRETCIGCKLCARACPFGsitmtteVVERadGKKNNRtkALKCDLCFSRNKEikAEGCA 148
Cdd:cd10560   85 GCLEACPTGAIFRTEfGTVYIQPDICNGCGYCVAACPFG-------VIDR--NEETGR--AHKCTLCYDRLKD--GLEPA 151


                 ....*..
gi 517009692 149 CIQACPT 155
Cdd:cd10560  152 CAKACPT 158
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 12-158 5.34e-19

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: 78.60  E-value: 5.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  12 DLSRCLSCKSCELAC----GLAHAGYEIEGAAAGQMKLKP------RVSVVQQGTT-----VALTQCRQCEDAPCVKVCP 76
Cdd:cd16366    4 DTSRCTGCRACQVACkqwnGLPAEKTEFTGSYQNPPDLTAhtwtlvRFYEVEKPGGdlswlFRKDQCMHCTDAGCLAACP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  77 NGSLYQEE-GLVKLNRETCIGCKLCARACPFGSITMTTEvveradgkknnRTKALKCDLCFSRnkeiKAEGC--ACIQAC 153
Cdd:cd16366   84 TGAIIRTEtGTVVVDPETCIGCGYCVNACPFDIPRFDEE-----------TGRVAKCTLCYDR----ISNGLqpACVKTC 148


                 ....*
gi 517009692 154 PTKVL 158
Cdd:cd16366  149 PTGAL 153
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 62-155 6.48e-18

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: 75.80  E-value: 6.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  62 QCRQCEDAPCVKVCPNGSLYQ-EEGLVKLNRETCIGCKLCARACPFGsitmttevVERADGKKNnrtKALKCDLCFSRNK 140
Cdd:cd10562   69 QCMHCTDAACVKVCPTGALYKtENGAVVVDEDKCIGCGYCVAACPFD--------VPRYDETTN---KITKCTLCFDRIE 137

                         90
                 ....*....|....*
gi 517009692 141 EIKAEgcACIQACPT 155
Cdd:cd10562  138 NGMQP--ACVKTCPT 150
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 9-161 7.67e-17

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: 72.40  E-value: 7.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692   9 IHADLSRCLSCKSCELACGLAHAG------YEIEGAAAGQMKLKPRVSVVQQgttvaltQCRQCEDAPCVKVCPNGSLYQ 82
Cdd:cd10553    5 LYHDSKRCIGCLACEVHCKVKNNLpvgprlCRIFAVGPKMVGGKPRLKFVYM-------SCFHCENPWCVKACPTGAMQK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  83 EE--GLVKLNRETCIGCKLCARACPFGSITMTTEvveradgkknnRTKALKCDLCFSRNKEikAEGCACIQACPTKVLSL 160
Cdd:cd10553   78 REkdGIVYVDQELCIGCKACIEACPWGIPQWNPA-----------TGKVVKCDYCMDRIDQ--GLKPACVTGCTTHALSF 144


                 .
gi 517009692 161 S 161
Cdd:cd10553  145 V 145
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 12-158 1.01e-16

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: 72.81  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  12 DLSRCLSCKSCELACglahagyeiegAAAGQMKLKPRVSV--VQQGTTVAL--TQCRQCEDAPCVKVCP-NGSLYQEEGL 86
Cdd:cd16369    7 DPSRCIGCRACVAAC-----------RECGTHRGKSMIHVdyIDRGESTQTapTVCMHCEDPTCAEVCPaDAIKVTEDGV 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517009692  87 VKL-NRETCIGCKLCARACPFGsitmttevVERADGKKNnrtKALKCDLCFSRNKEIKAEGCAciQACPTKVL 158
Cdd:cd16369   76 VQSaLKPRCIGCSNCVNACPFG--------VPKYDEERN---LMMKCDMCYDRTSVGKAPMCA--SVCPSGAL 135
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 12-158 3.36e-16

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: 71.86  E-value: 3.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  12 DLSRCLSCKSCELACGLAHaGYEIEGAAAGQMKLKPR--------------VSVVQQGTTVALTQCRQCEDAPCVKVCPN 77
Cdd:cd10561    5 DTTRCIGCRACEVACKEWN-GLPAEDTAFGPGWDNPRdlsaktytvikryeVETGGKGFVFVKRQCMHCLDPACVSACPV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  78 GSLY-QEEGLVKLNRETCIGCKLCARACPFGsitmttevVERADGKKNNRtKALKCDLCFSRNKEIKAEgcACIQACPTK 156
Cdd:cd10561   84 GALRkTPEGPVTYDEDKCIGCRYCMVACPFN--------IPKYEWDSANP-KIRKCTMCYDRLKEGKQP--ACVEACPTG 152


                 ..
gi 517009692 157 VL 158
Cdd:cd10561  153 AL 154
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 12-158 8.55e-16

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: 70.82  E-value: 8.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  12 DLSRCLSCKSCELACGLAHAGYEIEGAAAGQ-------MKLKPRV--SVVQQGTTVALTQCRQCEDAPCVKVCPNGSLYQ 82
Cdd:cd10552    4 DVAKCNGCYNCFLACKDEHVGNDWPGYAAPQprhghfwMRILRRErgQYPKVDVAYLPVPCNHCDNAPCIKAAKDGAVYK 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517009692  83 -EEGLVKLNRETCIGCKLCARACPFGSITMttevveradgkknNRTKAL--KCDLCFSRNKEIKAEGcACIQACPTKVL 158
Cdd:cd10552   84 rDDGIVIIDPEKAKGQKQLVDACPYGAIYW-------------NEELQVpqKCTFCAHLLDDGWKEP-RCVQACPTGAL 148
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 62-160 1.26e-13

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: 63.04  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692   62 QCRQCEDAPCVKVCPNGSLYQEE--GLVKLNRETCIGCKLCARACPFGsitmttevVERADGKKNnrtKALKCDLCFSRN 139
Cdd:pfam13247   9 QCRHCLNPPCKASCPVGAIYKDEetGAVLLDEKTCRGWRECVSACPYN--------IPRYNDETG---KAEKCDMCYDRV 77

                          90       100
                  ....*....|....*....|.
gi 517009692  140 KEIKAEgcACIQACPTKVLSL 160
Cdd:pfam13247  78 EAGLLP--ACVQTCPTGAMNF 96
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
61-155 1.65e-12

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 63.53  E-value: 1.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  61 TQCRQCEDAPCVKVCPNGSLYQEE--GLVKLNRETCIGCKLCARACPFGsitmttevVERADGKKNNrTKALKCDLCFSR 138
Cdd:PRK10882 110 KQCMHCVDPNCVSVCPVSALTKDPktGIVHYDKDVCTGCRYCMVACPFN--------VPKYDYNNPF-GAIHKCELCNQK 180

                         90
                 ....*....|....*....
gi 517009692 139 NKEIKAEG--CACIQACPT 155
Cdd:PRK10882 181 GVERLDKGglPGCVEVCPT 199
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 11-114 3.12e-12

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


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 59.98  E-value: 3.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  11 ADLSRCLSCKSCELACGLAHAGYEIEGAAAGQMKLKPRVSvvqqgTTVALTQCRQCEDAPCVKVCPNGSLYQEE-GLVKL 89
Cdd:cd16370    6 KDMERCIGCYSCMLACSRRVHKSASLSKSAIRVRTRGGLE-----GGFTVVVCRACEDPPCAEACPTGALEPRKgGGVVL 80

                         90       100
                 ....*....|....*....|....*
gi 517009692  90 NRETCIGCKLCARACPFGSITMTTE 114
Cdd:cd16370   81 DKEKCIGCGNCVKACIVGAIFWDEE 105
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
12-106 3.72e-12

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 62.20  E-value: 3.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  12 DLSRCLSCKSCELACGLAHAgyeiegAAAGQMKLKPRVSVV----QQGTTVALTQ--CRQCEDAPCVKVCPNGSLYQ-EE 84
Cdd:PRK14993  49 DLRRCIGCQSCTVSCTIENQ------TPQGAFRTTVNQYQVqregSQEVTNVLLPrlCNHCDNPPCVPVCPVQATFQrED 122

                         90       100
                 ....*....|....*....|..
gi 517009692  85 GLVKLNRETCIGCKLCARACPF 106
Cdd:PRK14993 123 GIVVVDNKRCVGCAYCVQACPY 144
PRK09898 PRK09898
ferredoxin-like protein;
63-160 1.33e-10

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 57.15  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  63 CRQCEDAPCVKVCPNG--SLYQEEGLVKLNRETCIGCKLCARACPFGSITMTTEVveradgkknnrTKALKCDLCfsrnk 140
Cdd:PRK09898 123 CRQCKEPQCMNVCPIGaiTWQQKEGCITVDHKRCIGCSACTTACPWMMATVNTES-----------KKSSKCVLC----- 186

                         90       100
                 ....*....|....*....|
gi 517009692 141 eikaegCACIQACPTKVLSL 160
Cdd:PRK09898 187 ------GECANACPTGALKI 200
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 49-159 2.94e-10

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


Pssm-ID: 319890 [Multi-domain]  Cd Length: 200  Bit Score: 56.28  E-value: 2.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  49 VSVVQQGTTVALTQ-CRQCEDAPCVKVCPNGSLYQE-EGLVKLNRETCIGCKLCARACPFG------SITMTTEVVERAD 120
Cdd:cd16368   76 VDTAGGEKEVFIPRrCMHCDNPPCAKLCPFGAARKTpEGAVYIDDDLCFGGAKCRDVCPWHipqrqaGVGIYLHLAPEYA 155

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 517009692 121 GKKnnrtKALKCDLCFSRNKEIKAEgcACIQACPTKVLS 159
Cdd:cd16368  156 GGG----VMYKCDLCKDLLAQGKPP--ACIEACPKGAQY 188
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
85-155 1.29e-09

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 53.73  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  85 GLVKLNR-----ETCIGCKLCARACPFGSITMTTEvvERADGKKnnRTKA-----LKCDLC-FsrnkeikaegcaCIQAC 153
Cdd:PRK05888  46 GRHALRRdpngeERCIACKLCAAICPADAITIEAA--EREDGRR--RTTRydinfGRCIFCgF------------CEEAC 109


                 ..
gi 517009692 154 PT 155
Cdd:PRK05888 110 PT 111
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 14-160 3.52e-09

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


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 51.95  E-value: 3.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  14 SRCLSCKSCELACGLAHagYEIEGaaagqmKLKPRVSVVQQGTTVALTQCRQCedAPCVKVCPNGSLYQE-EGLVKLNRE 92
Cdd:cd16372    8 EKCIGCLQCEEACSKTF--FKEED------REKSCIRITETEGGYAINVCNQC--GECIDVCPTGAITRDaNGVVMINKK 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517009692  93 TCIGCKLCARACPFGSITMTTEVVEradgkknnrtkALKCDLCfsrnkeikaegCACIQACPTKVLSL 160
Cdd:cd16372   78 LCVGCLMCVGFCPEGAMFKHEDYPE-----------PFKCIAC-----------GICVKACPTGALEL 123
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
63-118 1.19e-08

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 49.34  E-value: 1.19e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 517009692  63 CRQCEDapCVKVCPNGSLYQEEGLVKLNRETCIGCKLCARACPFGSITMTTEVVER 118
Cdd:COG2768   13 CIGCGA--CVKVCPVGAISIEDGKAVIDPEKCIGCGACIEVCPVGAIKIEWEEDEE 66
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 63-115 6.06e-08

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 47.34  E-value: 6.06e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 517009692  63 CRQCEDapCVKVCPNGSLYQEEGLVKLNRETCIGCKLCARACPFGSITMTTEV 115
Cdd:COG4231   24 CTGCGA--CVKVCPADAIEEGDGKAVIDPDLCIGCGSCVQVCPVDAIKLEKRV 74
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
5-110 1.30e-07

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 49.64  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692   5 KNRFIHADLSRCLSCKSCELACGLAhaGYEIEGAAAGQMKLKPRVSVVQQGTTVALTQCRQCEdaPCVKVCPNGSLYQEE 84
Cdd:COG4624   37 LLPEHVDDDSACSCCPRCCLCCCCC--CRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCY--PCVRACPVKAIKVDD 112

                         90       100
                 ....*....|....*....|....*.
gi 517009692  85 GLVKLNRETCIGCKLCARACPFGSIT 110
Cdd:COG4624  113 GKAEIDEEKCISCGQCVAVCPFGAIT 138
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 92-156 1.52e-07

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


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 49.09  E-value: 1.52e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517009692  92 ETCIGCKLCARACPFGSITMTtevveraDGK---KNNrtkalkCDLCfsrnkeikaegCACIQACPTK 156
Cdd:NF038196 185 DKCIGCGICAKVCPVNNIEME-------DGKpvwGHN------CTHC-----------LACIHRCPKE 228
PRK13795 PRK13795
hypothetical protein; Provisional
 71-105 8.91e-07

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 47.30  E-value: 8.91e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 517009692  71 CVKVCPNGSLYQEEGL--VKLNRETCIGCKLCARACP 105
Cdd:PRK13795 589 CVGACPTGAIRIEEGKrkISVDEEKCIHCGKCTEVCP 625
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
71-162 1.73e-06

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 46.21  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  71 CVKVCPNGSLYqeeGL--------VKLNRETCIGCKLCARACPFGsITMttevveradgkKNNRTKALKCDLCFsrnkei 142
Cdd:COG0348  184 CRYLCPYGAFQ---GLlsdlstlrVRYDRGDCIDCGLCVKVCPMG-IDI-----------RKGEINQSECINCG------ 242

                         90       100
                 ....*....|....*....|
gi 517009692 143 kaegcACIQACPTKVLSLSL 162
Cdd:COG0348  243 -----RCIDACPKDAIRFSS 257
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 92-160 1.76e-06

NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes "I" subunits from the closely related F420H2 dehydrogenase and formate hydrogenlyase complexes. [Energy metabolism, Electron transport]


Pssm-ID: 273902 [Multi-domain]  Cd Length: 122  Bit Score: 44.71  E-value: 1.76e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517009692   92 ETCIGCKLCARACPFGSITMTTEvvERADGKKN------NRTKALKCDLcfsrnkeikaegcaCIQACPTKVLSL 160
Cdd:TIGR01971  43 EKCIGCTLCAAVCPADAIRVVPA--EGEDGKRRlkfyeiNFGRCIFCGL--------------CEEACPTDAIVL 101
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
25-111 2.36e-06

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 46.01  E-value: 2.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  25 ACGLAHAGYEIE-------GAAA--------GQMKLKPRVSVVQQgttvalTQCRQCEdaPCVKVCPNGSL-YQEEGLVK 88
Cdd:COG1148  451 LAGAAHGPKDIPesiaqatAAAAraiqllskGELGVEPSVAEVDP------EKCTGCG--RCVEVCPYGAIsIDEKGVAE 522

                         90       100
                 ....*....|....*....|...
gi 517009692  89 LNRETCIGCKLCARACPFGSITM 111
Cdd:COG1148  523 VNPALCKGCGTCAAACPSGAISL 545
napG PRK09476
quinol dehydrogenase periplasmic component; Provisional
 13-127 2.56e-06

quinol dehydrogenase periplasmic component; Provisional


Pssm-ID: 236534 [Multi-domain]  Cd Length: 254  Bit Score: 45.77  E-value: 2.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  13 LSRCLSCKSCELAC-----GLAHAGyeiEGAAAGQMKLKPRVsvvqqgttvalTQCRQCEDAPCVKVCPNGSLYQEE--- 84
Cdd:PRK09476  58 LSACIRCGLCVQACpydtlKLATLA---SGLSAGTPYFVARD-----------IPCEMCEDIPCVKACPSGALDRELvdi 123

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 517009692  85 -----GL-VKLNRETCIG-----CKLCARACPFGSITMTTEVveradgKKNNRT 127
Cdd:PRK09476 124 ddarmGLaVLVDQENCLNfqglrCDVCYRVCPLIDKAITLEL------ERNERT 171
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 71-110 2.75e-06

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 42.73  E-value: 2.75e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 517009692  71 CVKVCPNGSLYQEEGLVKLNRETCIGCKLCARACPFGSIT 110
Cdd:COG2221   23 CVAVCPTGAISLDDGKLVIDEEKCIGCGACIRVCPTGAIK 62
NapF COG1145
Ferredoxin [Energy production and conversion];
63-117 3.69e-06

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 45.48  E-value: 3.69e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 517009692  63 CRQCEdaPCVKVCPNGSLYQEEGLVKL--NRETCIGCKLCARACPFGSITMTTEVVE 117
Cdd:COG1145  184 CIGCG--LCVKVCPTGAIRLKDGKPQIvvDPDKCIGCGACVKVCPVGAISLEPKEIE 238
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 56-118 3.83e-06

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 42.39  E-value: 3.83e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517009692  56 TTVALTQCRQCEDapCVKVCPNGSLYQEEGLVKL---NRETCIGCKLCARACPFGSITMTTEVVER 118
Cdd:COG1146    3 PVIDTDKCIGCGA--CVEVCPVDVLELDEEGKKAlviNPEECIGCGACELVCPVGAITVEDDEPEE 66
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
71-112 4.44e-06

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 44.92  E-value: 4.44e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 517009692  71 CVKVCPNGSLYQEEGLVKLNRETCIGCKLCARACPFGSITMT 112
Cdd:PRK07118 147 CVAACPFDAIHIENGLPVVDEDKCTGCGACVKACPRNVIELI 188
flavo_MJ0208 TIGR02700
archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of ...
 62-115 4.44e-06

archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of archaealflavoprotein. The other, described by TIGR02699 and typified by the partially characterized AF1518 of Archaeoglobus fulgidus, is a homodimeric FMN-containing flavoprotein that accepts electrons from ferredoxin and can transfer them to various oxidoreductases. The function of this protein family is unknown. [Unknown function, General]


Pssm-ID: 131747 [Multi-domain]  Cd Length: 234  Bit Score: 44.86  E-value: 4.44e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 517009692   62 QCRQCEDapCVKVCPNGSLYQEEGLVKLNRETCIGCKLCARACPFGSITMTTEV 115
Cdd:TIGR02700 149 RCKGCGI--CVDACPRSAIDMVDGKAFIRLLKCVGCGKCKEACPYNAIHGGLEY 200
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
88-160 6.05e-06

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 44.85  E-value: 6.05e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517009692  88 KLNRETCIGCKLCARACPFGSITMttevveraDGKKNNRTKALKCdlcfsrnkeikaEGC-ACIQACPTKVLSL 160
Cdd:COG1148  492 EVDPEKCTGCGRCVEVCPYGAISI--------DEKGVAEVNPALC------------KGCgTCAAACPSGAISL 545
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
71-114 9.87e-06

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 42.24  E-value: 9.87e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 517009692  71 CVKVCPNGSLY-QEEGLVKLNRETCIGCKLCARACPFGSITMTTE 114
Cdd:PRK09623  59 CWKFCPEPAIYiKEDGYVAIDYDYCKGCGICANECPTKAITMVKE 103
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 48-110 1.06e-05

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 44.39  E-value: 1.06e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  48 RVSVVQQgttvALTQCRQCeDAPCVKVCP---NGS----LYQEEGLVKLNRETCIGCKLCARACPFGSIT 110
Cdd:COG1245    3 RIAVVDR----DRCQPKKC-NYECIKYCPvnrTGKeaieIDEDDGKPVISEELCIGCGICVKKCPFDAIS 67
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 63-113 1.62e-05

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 40.88  E-value: 1.62e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 517009692  63 CRQCEDapCVKVCPNGSLYQEEGLVK----LNRETCIGCKLCARACPFGSITMTT 113
Cdd:COG1143    4 CIGCGL--CVRVCPVDAITIEDGEPGkvyvIDPDKCIGCGLCVEVCPTGAISMTP 56
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 12-155 1.80e-05

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: 42.81  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  12 DLSRCLSCKSCELACGLAHA--GYEIEGAAAGQ---------MKLKPRVSVVQQGTTVALT----QCRQCEDAPCVKVCP 76
Cdd:cd10559    5 DTTRCTACRGCQVACKQWNQlpAEQTKNTGSHQnppdlsantYKLVRFNEVRNENGKPDWLffpdQCRHCVTPPCKDAAD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  77 --NGSLYQEE--GLVKLNRETCIGC-KLCARACPFGsitmttevVERADGKKNNRTkalKCDLCFSRnkeIKAEGC-ACI 150
Cdd:cd10559   85 mvPGAVIQDEatGAVVFTEKTAELDfDDVLSACPYN--------IPRKNEATGRIV---KCDMCIDR---VSNGLQpACV 150


                 ....*
gi 517009692 151 QACPT 155
Cdd:cd10559  151 KACPT 155
FixX COG2440
Ferredoxin-like protein FixX [Energy production and conversion];
64-110 2.74e-05

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


Pssm-ID: 441981 [Multi-domain]  Cd Length: 87  Bit Score: 40.57  E-value: 2.74e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 517009692  64 RQCEDAPCVKVCPNGsLY--QEEGLVKLNRETCIGCKLCARACPFGSIT 110
Cdd:COG2440   25 ARCLAKPCTRYCPAG-VYeiVGDGRLQINYENCLECGTCRIKCPTQNIT 72
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 63-111 2.80e-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: 40.42  E-value: 2.80e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 517009692  63 CRQCedAPCVKVCPNGSLYQEEG-LVKLNRETCIGCKLCARACPFGSITM 111
Cdd:COG1144   32 CIGC--GLCWIVCPDGAIRVDDGkYYGIDYDYCKGCGICAEVCPVKAIEM 79
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 71-111 2.82e-05

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 40.10  E-value: 2.82e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 517009692  71 CVKVCPNGSLYQEEG-LVKLNRETCIGCKLCARACPFGSITM 111
Cdd:COG1149   19 CVEVCPEGAIKLDDGgAPVVDPDLCTGCGACVGVCPTGAITL 60
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 71-161 2.87e-05

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 41.61  E-value: 2.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  71 CVKVCPNGSLYQEEGL---------VKLNRETCIGCKLCARACPFGSITMTTEVVERADGKknnrtkalKCDLCfsrnke 141
Cdd:cd10549   48 CVEVCPTGAIELTPEGkeyvpkekeAEIDEEKCIGCGLCVKVCPVDAITLEDELEIVIDKE--------KCIGC------ 113

                         90       100
                 ....*....|....*....|
gi 517009692 142 ikaegCACIQACPTKVLSLS 161
Cdd:cd10549  114 -----GICAEVCPVNAIKLV 128
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
62-114 3.13e-05

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 42.74  E-value: 3.13e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 517009692  62 QCRQCEDapCVKVCP------NGSLYQEEglvklnretCIGCKLCARACPFGSITMTTE 114
Cdd:COG0348  211 DCIDCGL--CVKVCPmgidirKGEINQSE---------CINCGRCIDACPKDAIRFSSR 258
RNAP_D cd07030
D subunit of Archaeal RNA polymerase; The D subunit of archaeal RNA polymerase (RNAP) is ...
 63-114 3.42e-05

D subunit of Archaeal RNA polymerase; The D subunit of archaeal RNA polymerase (RNAP) is involved in the assembly of RNAP subunits. RNAP is a large multi-subunit complex responsible for the synthesis of RNA. It is the principal enzyme of the transcription process, and is a final target in many regulatory pathways that control gene expression in all living cells. A single distinct RNAP complex is found in archaea, which may be responsible for the synthesis of all RNAs. The archaeal RNAP harbors homologues of all eukaryotic RNAP II subunits with two exceptions (RPB8 and RPB9). The 12 archaeal subunits are designated by letters and can be divided into three functional groups that are engaged in: (I) catalysis (A'/A", B'/B" or B); (II) assembly (L, N, D and P); and (III) auxiliary functions (F, E, H and K). The D subunit is equivalent to the RPB3 subunit of eukaryotic RNAP II. It contains two subdomains: one subdomain is similar the eukaryotic Rpb11/AC19/archaeal L subunit which is involved in dimerization, and the other is an inserted beta sheet subdomain. The assembly of the two largest archaeal RNAP subunits that provide most of the enzyme's catalytic functions depends on the presence of the archaeal D/L heterodimer.


Pssm-ID: 132908 [Multi-domain]  Cd Length: 259  Bit Score: 42.25  E-value: 3.42e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 517009692  63 CRQCEDapCVKVCPNGSLYQEEGLVK-LNRETCIGCKLCARACPFGSITMTTE 114
Cdd:cd07030  171 CDGCGK--CVEECPRGVLELEEGKVVvEDLEDCSLCKLCERACDAGAIRVGWD 221
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
71-110 3.51e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 42.87  E-value: 3.51e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 517009692  71 CVKVCP---NGS----LYQEEGLVKLNRETCIGCKLCARACPFGSIT 110
Cdd:PRK13409  21 CIKYCPvvrTGEetieIDEDDGKPVISEELCIGCGICVKKCPFDAIS 67
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 13-118 1.33e-04

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 39.93  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  13 LSRCLSCKSCELAC-----GLAHAGYEIEGAaagqmkLKPRVSVVQQGttvaltqCRQCEDApCVKVCPNGSLYQEE--- 84
Cdd:cd16373   13 LALCIRCGLCVEACptgviQPAGLEDGLEGG------RTPYLDPREGP-------CDLCCDA-CVEVCPTGALRPLDlee 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 517009692  85 -----GLVKLNRETCI------GCKLCARACPFGSITMTTEVVER 118
Cdd:cd16373   79 qkvkmGVAVIDKDRCLawqggtDCGVCVEACPTEAIAIVLEDDVL 123
PRK00783 PRK00783
DNA-directed RNA polymerase subunit D; Provisional
 63-114 1.37e-04

DNA-directed RNA polymerase subunit D; Provisional


Pssm-ID: 234837 [Multi-domain]  Cd Length: 263  Bit Score: 40.64  E-value: 1.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 517009692  63 CRQCEDapCVKVCPNGSLYQEEGLVKLNR-ETCIGCKLCARACPFGSITMTTE 114
Cdd:PRK00783 171 CDECEK--CVEACPRGVLELKEGKLVVTDlLNCSLCKLCERACPGKAIRVSDD 221
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 88-161 1.97e-04

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: 39.30  E-value: 1.97e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517009692  88 KLNRETCIGCKLCARACPFGSITMTTEVVERADGKKNnrtkALKCDLCFsrnkeikaegcACIQACPTKVLSLS 161
Cdd:cd10549    2 KYDPEKCIGCGICVKACPTDAIELGPNGAIARGPEID----EDKCVFCG-----------ACVEVCPTGAIELT 60
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 91-161 2.16e-04

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 37.80  E-value: 2.16e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517009692  91 RETCIGCKLCARACPFGSITMttevvERADGKKNNRTKALKCDLCfsrnkeikaegCACIQACPTKVLSLS 161
Cdd:COG1143    1 EDKCIGCGLCVRVCPVDAITI-----EDGEPGKVYVIDPDKCIGC-----------GLCVEVCPTGAISMT 55
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 87-160 4.13e-04

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 37.01  E-value: 4.13e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517009692  87 VKLNRETCIGCKLCARACPFGSITMttevveradgkKNNRTKALKCDLCfsrnkeikaEGC-ACIQACPTKVLSL 160
Cdd:COG1149    6 PVIDEEKCIGCGLCVEVCPEGAIKL-----------DDGGAPVVDPDLC---------TGCgACVGVCPTGAITL 60
NapF COG1145
Ferredoxin [Energy production and conversion];
83-160 4.41e-04

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 39.32  E-value: 4.41e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517009692  83 EEGLVKLNRETCIGCKLCARACPFGSITMttevverADGKKNNRTKALKCDLCFsrnkeikaegcACIQACPTKVLSL 160
Cdd:COG1145  173 KKAKAVIDAEKCIGCGLCVKVCPTGAIRL-------KDGKPQIVVDPDKCIGCG-----------ACVKVCPVGAISL 232
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 87-159 4.59e-04

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 36.95  E-value: 4.59e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517009692  87 VKLNRETCIGCKLCARACPFGSITMTTEVVEradgkknnrTKALKCDLCfsrnkeikaegCACIQACPTKVLS 159
Cdd:COG2221   10 PKIDEEKCIGCGLCVAVCPTGAISLDDGKLV---------IDEEKCIGC-----------GACIRVCPTGAIK 62
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 71-156 6.08e-04

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


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 38.82  E-value: 6.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  71 CVKVCPNGSLY-QEEGLVKLNRETCIGCKLCARACPFGSITM---TTEVVER-----ADGKKNNRTKALKCDLCF----- 136
Cdd:COG2878  145 CIKACPFDAIVgAAKGMHTVDEDKCTGCGLCVEACPVDCIEMvpvSPTVVVSswdkgKAVRKVVGCIGLCCKKCCpaaai 224

                         90       100
                 ....*....|....*....|....*.
gi 517009692 137 ------SRNKEIKAEGCACIQACPTK 156
Cdd:COG2878  225 tvnnlaAIIDYKKCTCCGCCEKCCPT 250
PRK06273 PRK06273
ferredoxin; Provisional
 84-136 7.13e-04

ferredoxin; Provisional


Pssm-ID: 235764 [Multi-domain]  Cd Length: 165  Bit Score: 38.15  E-value: 7.13e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517009692  84 EGLVKLNR----ETCIGCKLCARACPFGSITMT-TEVVERADG---KKNNRTKALKCDLCF 136
Cdd:PRK06273  37 TGTVELPKkvfeELCIGCGGCANVCPTKAIEMIpVEPVKITEGyvkTKIPKIDYEKCVYCL 97
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
71-125 1.12e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 37.99  E-value: 1.12e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 517009692  71 CVKVCPNGSLYQEEGLVKLNRETCIGCKLCARACPFGSITMTTEVVERADGKKNN 125
Cdd:PRK07118 221 CVKACPAGAITMENNLAVIDQEKCTSCGKCVEKCPTKAIRILNKPPKVKEPKKAA 275
porD PRK09624
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
 71-115 1.19e-03

pyruvate ferredoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 170017 [Multi-domain]  Cd Length: 105  Bit Score: 36.55  E-value: 1.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 517009692  71 CVKVCPNGSLY-QEEGLVKLNRETCIGCKLCARACPFGSITMTTEV 115
Cdd:PRK09624  59 CYIYCPEPAIYlDEEGYPVFDYDYCKGCGICANECPTKAIEMVRET 104
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
71-158 1.81e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 37.61  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  71 CVKVCPNGSLYqeegLVKLNRET--------------------CIGCKLCARACPFGSITMTTEVVEradgkknnrTKAL 130
Cdd:PRK07118 176 CVKACPRNVIE----LIPKSARVfvacnskdkgkavkkvcevgCIGCGKCVKACPAGAITMENNLAV---------IDQE 242

                         90       100
                 ....*....|....*....|....*...
gi 517009692 131 KCDLCfsrnkeikaegCACIQACPTKVL 158
Cdd:PRK07118 243 KCTSC-----------GKCVEKCPTKAI 259
PRK13984 PRK13984
putative oxidoreductase; Provisional
 92-161 1.92e-03

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 37.82  E-value: 1.92e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517009692  92 ETCIGCKLCARACPFGSITMT-TEVVERADGKKNNRTKALKCDLCFsrnkeikaegCA-CIQACPTKVLSLS 161
Cdd:PRK13984  45 EKCIGCGTCSKICPTDAITMVeVPDLPQEYGKKPQRPVIDYGRCSF----------CAlCVDICTTGSLKMT 106
PRK13795 PRK13795
hypothetical protein; Provisional
 72-154 2.20e-03

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 37.67  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  72 VKVCPNGSLY----QEEGLVKLNRET---------CIGCKLCARACPFGSITMTtevveraDGKKNNRTKALKCDLCFsr 138
Cdd:PRK13795 548 VKVFASGNIWarseDKEAAASLFKDAarllrraaeCVGCGVCVGACPTGAIRIE-------EGKRKISVDEEKCIHCG-- 618

                         90
                 ....*....|....*.
gi 517009692 139 nkeikaegcACIQACP 154
Cdd:PRK13795 619 ---------KCTEVCP 625
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 85-161 2.29e-03

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 35.97  E-value: 2.29e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517009692  85 GLVKLNRETCIGCKLCARACPFGSITMTTEVveradgkKNNRTKALKCDLCfsrnkeikaegCACIQACPTKVLSLS 161
Cdd:PRK08348  35 GKILYDVDKCVGCRMCVTVCPAGVFVYLPEI-------RKVALWTGRCVFC-----------GQCVDVCPTGALQMS 93
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 86-154 4.28e-03

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


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 34.15  E-value: 4.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517009692   86 LVKLNRETCIGCKLCARACPFGSITMTteVVERADGKKNNRTKALKCDLCFsrnkeikaegcACIQACP 154
Cdd:pfam13237   1 KVVIDPDKCIGCGRCTAACPAGLTRVG--AIVERLEGEAVRIGVWKCIGCG-----------ACVEACP 56
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
85-160 4.81e-03

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 34.32  E-value: 4.81e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517009692  85 GLVKLNRETCIGCKLCARACPFGSITMTTEVVERADGkknnrtkalKCDLCfsrnkeikaegCACIQACPTKVLSL 160
Cdd:COG2768    4 GKPYVDEEKCIGCGACVKVCPVGAISIEDGKAVIDPE---------KCIGC-----------GACIEVCPVGAIKI 59
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 85-160 7.03e-03

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: 35.74  E-value: 7.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  85 GLVKLNRETCIGCKLCARACPFGSITMTT----EVVEradgkknnrtkalkcDLCfsrnkeikaEGC-ACIQACPTKVLS 159
Cdd:COG2878  130 GGPKGCEYGCIGCGDCIKACPFDAIVGAAkgmhTVDE---------------DKC---------TGCgLCVEACPVDCIE 185


                 .
gi 517009692 160 L 160
Cdd:COG2878  186 M 186
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
15-155 7.28e-03

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 35.77  E-value: 7.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517009692  15 RCLSCKSCELACGLAHAGYEIEGAAAGQMKLKPRVSVVQQGTTVALTQCRQCEDAPCVKVCPNGSLYQEEGLVKLNRETC 94
Cdd:COG4624   14 EEGDELLLLEEAERVLRIIILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSIIRDKEKC 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517009692  95 IGCKLCARACPFGSItmttevveradgKKNNRTKALKCDLCFSrnkeikaegC-ACIQACPT 155
Cdd:COG4624   94 KNCYPCVRACPVKAI------------KVDDGKAEIDEEKCIS---------CgQCVAVCPF 134
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
71-114 9.23e-03

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 34.86  E-value: 9.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 517009692  71 CVKVCPNGSLY-----QEEGLVKLNR-----ETCIGCKLCARACPFGSITMTTE 114
Cdd:PRK05888  66 CAAICPADAITieaaeREDGRRRTTRydinfGRCIFCGFCEEACPTDAIVETPD 119
 
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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