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Conserved domains on  [gi|90111444|ref|NP_416976|]
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hydrogenase 4 component A [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 4-170 6.14e-61

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: 187.08  E-value: 6.14e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444   4 FVVAEPLWCTGCNTCLAACSDVH--------KTQGLQQHPRLALAKTSTITAPVVCHHCEEAPCLQVCPVNAISQRDDAI 75
Cdd:cd10554   1 FVIADPDKCIGCRTCEVACAAAHsgkgifeaGTDGLPFLPRLRVVKTGEVTAPVQCRQCEDAPCANVCPVGAISQEDGVV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  76 QLNESLCIGCKLCAVVCPFGAISAsgsrpvnahaqyvfqaegslkdgeenAPTQHALLRWEPGVQTVAVKCDLCDFLPEG 155
Cdd:cd10554  81 QVDEERCIGCKLCVLACPFGAIEM--------------------------APTTVPGVDWERGPRAVAVKCDLCAGREGG 134

                       170
                ....*....|....*
gi 90111444 156 PACVRACPNQALRLI 170
Cdd:cd10554 135 PACVEACPTKALTLV 149
 
Name Accession Description Interval E-value
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 4-170 6.14e-61

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: 187.08  E-value: 6.14e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444   4 FVVAEPLWCTGCNTCLAACSDVH--------KTQGLQQHPRLALAKTSTITAPVVCHHCEEAPCLQVCPVNAISQRDDAI 75
Cdd:cd10554   1 FVIADPDKCIGCRTCEVACAAAHsgkgifeaGTDGLPFLPRLRVVKTGEVTAPVQCRQCEDAPCANVCPVGAISQEDGVV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  76 QLNESLCIGCKLCAVVCPFGAISAsgsrpvnahaqyvfqaegslkdgeenAPTQHALLRWEPGVQTVAVKCDLCDFLPEG 155
Cdd:cd10554  81 QVDEERCIGCKLCVLACPFGAIEM--------------------------APTTVPGVDWERGPRAVAVKCDLCAGREGG 134

                       170
                ....*....|....*
gi 90111444 156 PACVRACPNQALRLI 170
Cdd:cd10554 135 PACVEACPTKALTLV 149
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
1-172 3.01e-54

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 169.45  E-value: 3.01e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444   1 MNRFVVAEPLWCTGCNTCLAACSDVH-KTQGLQQHPRLALAKTSTITAPVVCHHCEEAPCLQVCPVNAISQRDDAIQLNE 79
Cdd:COG1142   1 MNKFIIADPEKCIGCRTCEAACAVAHeGEEGEPFLPRIRVVRKAGVSAPVQCRHCEDAPCAEVCPVGAITRDDGAVVVDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  80 SLCIGCKLCAVVCPFGAISASGSRPvnahaqyvfqaegslkdgeenaptqhallrwepgvQTVAVKCDLCDFLPEGPACV 159
Cdd:COG1142  81 EKCIGCGLCVLACPFGAITMVGEKS-----------------------------------RAVAVKCDLCGGREGGPACV 125

                       170
                ....*....|...
gi 90111444 160 RACPNQALRLITG 172
Cdd:COG1142 126 EACPTGALRLVDV 138
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 1-187 4.06e-43

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 152.59  E-value: 4.06e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444    1 MNRFVVAEPLWCTGCNTCLAAC-----SDVHKTQGLQQHPRLALAKTSTITAPVVCHHCEEAPCLQVCPVNAISQRDDAI 75
Cdd:PRK12769   1 MNRFIMANSQQCLGCHACEIACvmahnDEQHVLSQHHFHPRITVIKHQQQRSAVTCHHCEDAPCARSCPNGAISHVDDSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444   76 QLNESLCIGCKLCAVVCPFGAISAsgsrpvnahaqyvfqaegslkdgeENAPTQHALlrwepgVQTVAVKCDLCDFLPEG 155
Cdd:PRK12769  81 QVNQQKCIGCKSCVVACPFGTMQI------------------------VLTPVAAGK------VKATAHKCDLCAGRENG 130

                        170       180       190
                 ....*....|....*....|....*....|..
gi 90111444  156 PACVRACPNQALRLITGDSLQRQMKEKQRLAA 187
Cdd:PRK12769 131 PACVENCPADALQLVTEQALSGMAKSRRLRTA 162
flavo_MJ0208 TIGR02700
archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of ...
 51-97 9.54e-08

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: 50.64  E-value: 9.54e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 90111444    51 CHHCEEapCLQVCPVNAISQRDDAIQLNESLCIGCKLCAVVCPFGAI 97
Cdd:TIGR02700 150 CKGCGI--CVDACPRSAIDMVDGKAFIRLLKCVGCGKCKEACPYNAI 194
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 48-169 4.51e-07

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: 46.47  E-value: 4.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444    48 PVVCHHCEEAPCLQVCPVNAISQRDD--AIQLNESLCIGCKLCAVVCPFGAIsasgsrpvnahaqyvfqaegslkdgeen 125
Cdd:pfam13247   7 PEQCRHCLNPPCKASCPVGAIYKDEEtgAVLLDEKTCRGWRECVSACPYNIP---------------------------- 58

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 90111444   126 aptqhallRWEPgVQTVAVKCDLC-DFLPEG--PACVRACPNQALRL 169
Cdd:pfam13247  59 --------RYND-ETGKAEKCDMCyDRVEAGllPACVQTCPTGAMNF 96
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 82-105 9.83e-04

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


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 38.69  E-value: 9.83e-04
                         10        20
                 ....*....|....*....|....
gi 90111444   82 CIGCKLCAVVCPFGAISASGSRPV 105
Cdd:NF038196 187 CIGCGICAKVCPVNNIEMEDGKPV 210
 
Name Accession Description Interval E-value
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 4-170 6.14e-61

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: 187.08  E-value: 6.14e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444   4 FVVAEPLWCTGCNTCLAACSDVH--------KTQGLQQHPRLALAKTSTITAPVVCHHCEEAPCLQVCPVNAISQRDDAI 75
Cdd:cd10554   1 FVIADPDKCIGCRTCEVACAAAHsgkgifeaGTDGLPFLPRLRVVKTGEVTAPVQCRQCEDAPCANVCPVGAISQEDGVV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  76 QLNESLCIGCKLCAVVCPFGAISAsgsrpvnahaqyvfqaegslkdgeenAPTQHALLRWEPGVQTVAVKCDLCDFLPEG 155
Cdd:cd10554  81 QVDEERCIGCKLCVLACPFGAIEM--------------------------APTTVPGVDWERGPRAVAVKCDLCAGREGG 134

                       170
                ....*....|....*
gi 90111444 156 PACVRACPNQALRLI 170
Cdd:cd10554 135 PACVEACPTKALTLV 149
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
1-172 3.01e-54

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 169.45  E-value: 3.01e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444   1 MNRFVVAEPLWCTGCNTCLAACSDVH-KTQGLQQHPRLALAKTSTITAPVVCHHCEEAPCLQVCPVNAISQRDDAIQLNE 79
Cdd:COG1142   1 MNKFIIADPEKCIGCRTCEAACAVAHeGEEGEPFLPRIRVVRKAGVSAPVQCRHCEDAPCAEVCPVGAITRDDGAVVVDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  80 SLCIGCKLCAVVCPFGAISASGSRPvnahaqyvfqaegslkdgeenaptqhallrwepgvQTVAVKCDLCDFLPEGPACV 159
Cdd:COG1142  81 EKCIGCGLCVLACPFGAITMVGEKS-----------------------------------RAVAVKCDLCGGREGGPACV 125

                       170
                ....*....|...
gi 90111444 160 RACPNQALRLITG 172
Cdd:COG1142 126 EACPTGALRLVDV 138
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 1-187 4.06e-43

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 152.59  E-value: 4.06e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444    1 MNRFVVAEPLWCTGCNTCLAAC-----SDVHKTQGLQQHPRLALAKTSTITAPVVCHHCEEAPCLQVCPVNAISQRDDAI 75
Cdd:PRK12769   1 MNRFIMANSQQCLGCHACEIACvmahnDEQHVLSQHHFHPRITVIKHQQQRSAVTCHHCEDAPCARSCPNGAISHVDDSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444   76 QLNESLCIGCKLCAVVCPFGAISAsgsrpvnahaqyvfqaegslkdgeENAPTQHALlrwepgVQTVAVKCDLCDFLPEG 155
Cdd:PRK12769  81 QVNQQKCIGCKSCVVACPFGTMQI------------------------VLTPVAAGK------VKATAHKCDLCAGRENG 130

                        170       180       190
                 ....*....|....*....|....*....|..
gi 90111444  156 PACVRACPNQALRLITGDSLQRQMKEKQRLAA 187
Cdd:PRK12769 131 PACVENCPADALQLVTEQALSGMAKSRRLRTA 162
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 1-187 8.67e-36

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 132.46  E-value: 8.67e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444    1 MNRFVVAEPLWCTGCNTCLAACSDVHKTQGL-QQH----PRLALAKTSTITAPVVCHHCEEAPCLQVCPVNAISQRDDAI 75
Cdd:PRK12809   1 MNKFIAAEAAECIGCHACEIACAVAHNQENWpLSHsdfrPRIHVVGKGQAANPVACHHCNNAPCVTACPVNALTFQSDSV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444   76 QLNESLCIGCKLCAVVCPFGAISAsgsrpvnahaqyvfqaegslkdgeenaptqhallrwepgVQTVAVKCDLCDFLPEG 155
Cdd:PRK12809  81 QLDEQKCIGCKRCAIACPFGVVEM---------------------------------------VDTIAQKCDLCNQRSSG 121

                        170       180       190
                 ....*....|....*....|....*....|...
gi 90111444  156 P-ACVRACPNQALRLITGDSLQRQMKEKQRLAA 187
Cdd:PRK12809 122 TqACIEVCPTQALRLMDDKGLQQIKVARQRKTA 154
PRK10330 PRK10330
electron transport protein HydN;
1-187 2.84e-31

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 112.29  E-value: 2.84e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444    1 MNRFVVAEPLWCTGCNTCLAACSDVHKTQ----GLQQH---PRLALAKTSTITAPVVCHHCEEAPCLQVCPVNAISQRDD 73
Cdd:PRK10330   1 MNRFIIADASKCIGCRTCEVACVVSHQENqdcaSLTPEtflPRIHVIKGVNVSTATVCRQCEDAPCANVCPNGAISRDKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444   74 AIQLNESLCIGCKLCAVVCPFGAISASgSRPV--NAHAQYVFQAEgslkdgeenaptqhallrwepgvQTVAVKCDLCDF 151
Cdd:PRK10330  81 FVHVMQERCIGCKTCVVACPYGAMEVV-VRPVirNSGAGLNVRAE-----------------------KAEANKCDLCNH 136

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 90111444  152 LPEGPACVRACPNQALRLITGDSLQRQMKEKQRLAA 187
Cdd:PRK10330 137 REDGPACMAACPTHALICVDRNKLEQLSAEKRRRAA 172
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 12-167 2.45e-30

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 110.04  E-value: 2.45e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  12 CTGCNTCLAACSDVHKTQG------LQQHPRLALAKTSTITAPVVCHHCEEAPCLQVCPVNAISQRDD-AIQLNESLCIG 84
Cdd:COG0437  15 CIGCRACVVACKEENNLPVgvtwrrVRRYEEGEFPNVEWLFVPVLCNHCDDPPCVKVCPTGATYKREDgIVLVDYDKCIG 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  85 CKLCAVVCPFGAIsasgsrpvnahaqyvfqaegslkdgeenaptqhallRWEPGVQtVAVKCDLC-DFLPEG--PACVRA 161
Cdd:COG0437  95 CRYCVAACPYGAP------------------------------------RFNPETG-VVEKCTFCaDRLDEGllPACVEA 137


                ....*.
gi 90111444 162 CPNQAL 167
Cdd:COG0437 138 CPTGAL 143
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 12-169 5.54e-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: 5.54e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  12 CTGCNTCLAACSDVHKTQGLQQHPR---LALAKTSTITAPVVCHHCEEAPCLQVCPVNAISQRDD-AIQLNESLCIGCKL 87
Cdd:cd04410   8 CIGCGTCEVACKQEHGLRPGPDWSRikvIEGGGLERAFLPVSCMHCEDPPCVKACPTGAIYKDEDgIVLIDEDKCIGCGS 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  88 CAVVCPFGAISasgsrpvnahaqyvfqaegslkdgeenaptqhalLRWEPGvqtVAVKCDLC-DFLPEG--PACVRACPN 164
Cdd:cd04410  88 CVEACPYGAIV----------------------------------FDPEPG---KAVKCDLCgDRLDEGlePACVKACPT 130


                ....*
gi 90111444 165 QALRL 169
Cdd:cd04410 131 GALTF 135
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 12-170 2.02e-27

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


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 100.73  E-value: 2.02e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  12 CTGCNTCLAACSDVHKTQGlqqHPRLALAKTST-----ITAPVVCHHCEEAPCLQVCPVNAISQ--RDDAIQLNESLCIG 84
Cdd:cd10550   8 CTGCRTCELACSLKHEGVF---NPSLSRIRVVRfepegLDVPVVCRQCEDAPCVEACPVGAISRdeETGAVVVDEDKCIG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  85 CKLCAVVCPFGAISasgsrpvnahaqyvFQAEGSlkdgeenaptqhallrwepgvqtVAVKCDLCDflpEGPACVRACPN 164
Cdd:cd10550  85 CGMCVEACPFGAIR--------------VDPETG-----------------------KAIKCDLCG---GDPACVKVCPT 124


                ....*.
gi 90111444 165 QALRLI 170
Cdd:cd10550 125 GALEFV 130
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 5-178 7.71e-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: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 96.96  E-value: 7.71e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444   5 VVAEPLWCTGCNTCLAACSDVHktqglQQHPRLALAKTSTITA-PVVCHHCEEAPCLQVCPVNAISQ-RDDAIQLNESLC 82
Cdd:cd16374   1 VYVDPERCIGCRACEIACAREH-----SGKPRISVEVVEDLASvPVRCRHCEDAPCMEVCPTGAIYRdEDGAVLVDPDKC 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  83 IGCKLCAVVCPFGAISASGSRpvnahaqyvfqaegslkdgeenaptqhallrwepgvqTVAVKCDLC-DFLPEG--PACV 159
Cdd:cd16374  76 IGCGMCAMACPFGVPRFDPSL-------------------------------------KVAVKCDLCiDRRREGklPACV 118

                       170
                ....*....|....*....
gi 90111444 160 RACPNQALRLITGDSLQRQ 178
Cdd:cd16374 119 EACPTGALKFGDIEELLKE 137
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 12-170 1.24e-25

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: 96.48  E-value: 1.24e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  12 CTGCNTCLAACSDVHKTQGLQQHPRL-ALAKTSTITAPVV-----CHHCEEAPCLQVCPVNAISQRDDAI-QLNESLCIG 84
Cdd:cd16371   9 CIGCKACEIACKDKNDLPPGVNWRRVyEYEGGEFPEVFAYflsmsCNHCENPACVKVCPTGAITKREDGIvVVDQDKCIG 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  85 CKLCAVVCPFGAIsasgsrpvnahaQYvfqaegslkDGEENaptqhallrwepgvqtVAVKCDLC-DFLPEG--PACVRA 161
Cdd:cd16371  89 CGYCVWACPYGAP------------QY---------NPETG----------------KMDKCDMCvDRLDEGekPACVAA 131


                ....*....
gi 90111444 162 CPNQALRLI 170
Cdd:cd16371 132 CPTRALDFG 140
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 12-167 3.03e-25

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: 96.83  E-value: 3.03e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  12 CTGCNTCLAACSDVHKTQGLQQHPRLALAKTSTITA------PVVCHHCEEAPCLQVCPVNAISQRDDAI-QLNESLCIG 84
Cdd:cd10551   8 CIGCGACVVACKAENNVPPGVFRNRVLEYEVGEYPNvkrtflPVLCNHCENPPCVKVCPTGATYKREDGIvLVDYDKCIG 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  85 CKLCAVVCPFGAISasgsrpVNAHAQYVFQAEGSLKDGeenaptqhallrwepgvqtVAVKCDLC-DFLPEG--PACVRA 161
Cdd:cd10551  88 CRYCMAACPYGARY------FNPEEPHEFGEVPVRPKG-------------------VVEKCTFCyHRLDEGllPACVEA 142


                ....*.
gi 90111444 162 CPNQAL 167
Cdd:cd10551 143 CPTGAR 148
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 11-170 2.87e-22

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: 87.70  E-value: 2.87e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  11 WCTGCNTCLAACSDVH-KTQGLQQH--------PRLALAKTSTITAPVVCHHCEEAPCLQVCPVNAIsQRDD---AIQLN 78
Cdd:cd10563   8 KCLGCKLCEVACAVAHsKSKDLIKAklekerprPRIRVEESGGRSFPLQCRHCDEPPCVKACMSGAM-HKDPetgIVIHD 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  79 ESLCIGCKLCAVVCPFGAISASGSRpvnahaqyvfqaegslkdgeenaptqhallrwepgvqTVAVKCDLC-DFlpEGPA 157
Cdd:cd10563  87 EEKCVGCWMCVMVCPYGAIRPDKER-------------------------------------KVALKCDLCpDR--ETPA 127

                       170
                ....*....|...
gi 90111444 158 CVRACPNQALRLI 170
Cdd:cd10563 128 CVEACPTGALVLE 140
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 8-178 2.65e-19

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


Pssm-ID: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 80.89  E-value: 2.65e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444   8 EPLWCTGCNTCLAACS--DVHKtqglqQHPRLAL----AKTSTITAPVVCHHCEEAPCLQVCPVNAISQRDDAIQL--NE 79
Cdd:cd16369   7 DPSRCIGCRACVAACRecGTHR-----GKSMIHVdyidRGESTQTAPTVCMHCEDPTCAEVCPADAIKVTEDGVVQsaLK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  80 SLCIGCKLCAVVCPFGAisasgsrpvnahAQYVFQAEgslkdgeenaptqhallrwepgvqtVAVKCDLC-DFLPEG--P 156
Cdd:cd16369  82 PRCIGCSNCVNACPFGV------------PKYDEERN-------------------------LMMKCDMCyDRTSVGkaP 124

                       170       180
                ....*....|....*....|..
gi 90111444 157 ACVRACPNQALRLITGDSLQRQ 178
Cdd:cd16369 125 MCASVCPSGALFYGTREEIQAL 146
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 12-170 8.18e-18

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: 76.19  E-value: 8.18e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  12 CTGCNTCLAACSDVHktqglQQHPRLALAKTS--TITAPVVCHHCEEAPCLQVCPVNAISQRDDAIQLNESLCIGCKLCA 89
Cdd:cd16367  21 CIRCDNCEKACADTH-----DGHSRLDRNGLRfgNLLVPTACRHCVDPVCMIGCPTGAIHRDDGGEVVISDACCGCGNCA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  90 VVCPFGAISAsgsrpvnahaqyvfqaegslkdgeenaptqhallrwepgvqTVAVKCDLCDFLpEGPACVRACPNQALRL 169
Cdd:cd16367  96 SACPYGAIQM-----------------------------------------VRAVKCDLCAGY-AGPACVSACPTGAAIR 133


                .
gi 90111444 170 I 170
Cdd:cd16367 134 V 134
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 12-167 1.70e-16

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: 73.20  E-value: 1.70e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  12 CTGCNTCLAACSD--------VHKTQGLQQHPRLALAKTSTIT---------------APVVCHHCEEAPCLQVCPVNAI 68
Cdd:cd16366   8 CTGCRACQVACKQwnglpaekTEFTGSYQNPPDLTAHTWTLVRfyevekpggdlswlfRKDQCMHCTDAGCLAACPTGAI 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  69 SQRD-DAIQLNESLCIGCKLCAVVCPFGAISasgsrpvnahaqyvfqaegslkdgeenaptqhalLRWEPGvqtVAVKCD 147
Cdd:cd16366  88 IRTEtGTVVVDPETCIGCGYCVNACPFDIPR----------------------------------FDEETG---RVAKCT 130

                       170       180
                ....*....|....*....|...
gi 90111444 148 LC-DFLPEG--PACVRACPNQAL 167
Cdd:cd16366 131 LCyDRISNGlqPACVKTCPTGAL 153
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 50-182 6.36e-16

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: 73.19  E-value: 6.36e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  50 VCHHCEEAPCLQVCPVNAISQRD-DAIQLNESLCIGCKLCAVVCPFGAIsasgsrpvnahaqyvfqaegslkdgEENAPT 128
Cdd:cd10560  77 VCKHCTDAGCLEACPTGAIFRTEfGTVYIQPDICNGCGYCVAACPFGVI-------------------------DRNEET 131

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 90111444 129 QHALlrwepgvqtvavKCDLC-DFLPEG--PACVRACPNQALRLITGDSLQRQMKEK 182
Cdd:cd10560 132 GRAH------------KCTLCyDRLKDGlePACAKACPTGSIQFGPLEELRERARAR 176
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
12-98 7.77e-15

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 71.98  E-value: 7.77e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  12 CTGCNTCLAACSDVHKTQGLQQHPRLALAKTSTITAPVVCHHCEeaPCLQVCPVNAISQRDDAIQLNESLCIGCKLCAVV 91
Cdd:COG4624  54 CCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCY--PCVRACPVKAIKVDDGKAEIDEEKCISCGQCVAV 131


                ....*..
gi 90111444  92 CPFGAIS 98
Cdd:COG4624 132 CPFGAIT 138
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 12-194 2.44e-14

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: 68.57  E-value: 2.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  12 CTGCNTCLAACSDVHKT-------QGLQQHPRLALAKTSTIT--APVV-------------CHHCEEAPCLQVCP-VNAI 68
Cdd:cd10558   9 CIGCKACQVACKEWNDLraevghnVGTYQNPADLSPETWTLMkfREVEdngklewlirkdgCMHCADPGCLKACPsPGAI 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  69 SQRDDAI-QLNESLCIGCKLCAVVCPFgaisasgsrpvnahaqyvfqaegslkdgeeNAPtqhallRWEPgVQTVAVKCD 147
Cdd:cd10558  89 VQYANGIvDFQSDKCIGCGYCIKGCPF------------------------------DIP------RISK-DDNKMYKCT 131

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 90111444 148 LC-DFLPEG--PACVRACPNQALRLITGDSLQRQMKEK-QRLAASWFANGG 194
Cdd:cd10558 132 LCsDRVSVGlePACVKTCPTGALHFGTKEDMLALAEKRvAALKERGYTNAG 182
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 11-168 4.75e-14

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: 67.35  E-value: 4.75e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  11 WCTGCNTCLAACSDVH---------KTQ--------GLQQHPRLALAKTSTITAPVVCHHCEEAPCLQVCPVNAISQRDD 73
Cdd:cd10552   7 KCNGCYNCFLACKDEHvgndwpgyaAPQprhghfwmRILRRERGQYPKVDVAYLPVPCNHCDNAPCIKAAKDGAVYKRDD 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  74 AI-QLNESLCIGCKLCAVVCPFGAIsasgsrpvnahaqyvFQAEgslkdgEENaptqhallrwepgvqtVAVKCDLC-DF 151
Cdd:cd10552  87 GIvIIDPEKAKGQKQLVDACPYGAI---------------YWNE------ELQ----------------VPQKCTFCaHL 129

                       170       180
                ....*....|....*....|
gi 90111444 152 LPEG---PACVRACPNQALR 168
Cdd:cd10552 130 LDDGwkePRCVQACPTGALR 149
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 12-188 6.38e-14

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: 67.24  E-value: 6.38e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  12 CTGCNTCLAACSDVHK--------TQGLQQHPRLAlAKTSTI--------------TAPVVCHHCEEAPCLQVCPVNAIS 69
Cdd:cd10561   9 CIGCRACEVACKEWNGlpaedtafGPGWDNPRDLS-AKTYTVikryevetggkgfvFVKRQCMHCLDPACVSACPVGALR 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  70 QRDDAIQL-NESLCIGCKLCAVVCPFGAISasgsrpvnahaqyvFQAEgslkdgeenaptqhallRWEPGVQtvavKCDL 148
Cdd:cd10561  88 KTPEGPVTyDEDKCIGCRYCMVACPFNIPK--------------YEWD-----------------SANPKIR----KCTM 132

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 90111444 149 C-DFLPEG--PACVRACPNQALRLITGDSLqrqMKE-KQRLAAS 188
Cdd:cd10561 133 CyDRLKEGkqPACVEACPTGALLFGKREEL---LAEaKRRIAAN 173
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 12-167 1.87e-13

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: 65.02  E-value: 1.87e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  12 CTGCNTCLAACSDVHK--------TQGLQQHPRLAlAKTSTI------TAPVV----------CHHCEEAPCLQVCPVNA 67
Cdd:cd10562   8 CTACRGCQVACKQWNQlpaektpfTGSYQNPPDLT-PNTWTLirfyehEEDNGgirwlfrkrqCMHCTDAACVKVCPTGA 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  68 ISQRDD-AIQLNESLCIGCKLCAVVCPFGAIsasgsrpvnahaQYvfqaegslkDGEENAPTqhallrwepgvqtvavKC 146
Cdd:cd10562  87 LYKTENgAVVVDEDKCIGCGYCVAACPFDVP------------RY---------DETTNKIT----------------KC 129

                       170       180
                ....*....|....*....|....
gi 90111444 147 DLC-DFLPEG--PACVRACPNQAL 167
Cdd:cd10562 130 TLCfDRIENGmqPACVKTCPTGAL 153
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 12-171 1.67e-12

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: 62.38  E-value: 1.67e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  12 CTGCNTCLAACSDVHKT-------QGLQQHPRLALAKTSTITAPVVCHHCEEAPCLQVCPVNAISQR--DDAIQLNESLC 82
Cdd:cd10553  12 CIGCLACEVHCKVKNNLpvgprlcRIFAVGPKMVGGKPRLKFVYMSCFHCENPWCVKACPTGAMQKRekDGIVYVDQELC 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  83 IGCKLCAVVCPFGAisasgsrPVnahaqyvfqaegslkdgeenaptqhallrWEPGVQTVaVKCDLC-DFLPEG--PACV 159
Cdd:cd10553  92 IGCKACIEACPWGI-------PQ-----------------------------WNPATGKV-VKCDYCmDRIDQGlkPACV 134

                       170
                ....*....|..
gi 90111444 160 RACPNQALRLIT 171
Cdd:cd10553 135 TGCTTHALSFVR 146
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 50-105 1.09e-11

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 58.13  E-value: 1.09e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 90111444  50 VCHHCEEapCLQVCPVNAISQRDDAIQLNESLCIGCKLCAVVCPFGAISASGSRPV 105
Cdd:COG4231  23 KCTGCGA--CVKVCPADAIEEGDGKAVIDPDLCIGCGSCVQVCPVDAIKLEKRVPE 76
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 3-171 1.31e-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: 59.27  E-value: 1.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444   3 RFVVAEPLWCTGCNTCLAACSDVHKTQGLQQHPRLALAKTSTITAPVVCHHCEEapCLQVCPVNAISQRDDAI-QLNESL 81
Cdd:cd16372   1 KLLVTDPEKCIGCLQCEEACSKTFFKEEDREKSCIRITETEGGYAINVCNQCGE--CIDVCPTGAITRDANGVvMINKKL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  82 CIGCKLCAVVCPFGAIsasgsrpvnahaqyvFQAEGslkdgeenaptqhallrwepgvQTVAVKCDLCDflpegpACVRA 161
Cdd:cd16372  79 CVGCLMCVGFCPEGAM---------------FKHED----------------------YPEPFKCIACG------ICVKA 115

                       170
                ....*....|
gi 90111444 162 CPNQALRLIT 171
Cdd:cd16372 116 CPTGALELVE 125
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 3-97 2.29e-11

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


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 58.82  E-value: 2.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444   3 RFVVAEPLWCTGCNTCLAACSDVHKTQG------LQQHPRLALAKTSTItapVVCHHCEEAPCLQVCPVNAISQRDD-AI 75
Cdd:cd16370   2 RLRVKDMERCIGCYSCMLACSRRVHKSAslsksaIRVRTRGGLEGGFTV---VVCRACEDPPCAEACPTGALEPRKGgGV 78

                        90       100
                ....*....|....*....|..
gi 90111444  76 QLNESLCIGCKLCAVVCPFGAI 97
Cdd:cd16370  79 VLDKEKCIGCGNCVKACIVGAI 100
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
12-96 2.79e-11

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 60.66  E-value: 2.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444   12 CTGCNTCLAACSDVHKT-QG------LQQHPRLALAKTST-ITAPVVCHHCEEAPCLQVCPVNAISQRDDAI-QLNESLC 82
Cdd:PRK14993  53 CIGCQSCTVSCTIENQTpQGafrttvNQYQVQREGSQEVTnVLLPRLCNHCDNPPCVPVCPVQATFQREDGIvVVDNKRC 132

                         90
                 ....*....|....
gi 90111444   83 IGCKLCAVVCPFGA 96
Cdd:PRK14993 133 VGCAYCVQACPYDA 146
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
51-98 5.09e-11

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 56.28  E-value: 5.09e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 90111444  51 CHHCEEapCLQVCPVNAISQRDDAIQLNESLCIGCKLCAVVCPFGAIS 98
Cdd:COG2768  13 CIGCGA--CVKVCPVGAISIEDGKAVIDPEKCIGCGACIEVCPVGAIK 58
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 40-184 2.19e-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: 57.43  E-value: 2.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  40 AKTSTITAPVVCHHCEEAPCLQVCPVNAISQRDD-AIQLNESLCIGCKLCAVVCPFGaISA--SGSRPvnahaqYVFQAE 116
Cdd:cd16368  80 GGEKEVFIPRRCMHCDNPPCAKLCPFGAARKTPEgAVYIDDDLCFGGAKCRDVCPWH-IPQrqAGVGI------YLHLAP 152

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111444 117 GSLKDGeenaptqhallrwepgvqtVAVKCDLC-DFLPEG--PACVRACPNQALRLitgdSLQRQMKEKQR 184
Cdd:cd16368 153 EYAGGG-------------------VMYKCDLCkDLLAQGkpPACIEACPKGAQYF----GPRKEMVALAR 200
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
12-188 1.98e-09

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 55.83  E-value: 1.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444   12 CTGCNTCLAACSDVHKTQGLQQHPRL--ALAKTSTITAPVV------------------------CHHCEEAPCLQVCPV 65
Cdd:PRK10882  47 CVGCQACVTKCQEINFPERNPQGEQTwdNPDKLSPYTNNIIkvwksgtgvnkdqeengyayikkqCMHCVDPNCVSVCPV 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444   66 NAISQRDDA--IQLNESLCIGCKLCAVVCPFGAISasgsrpvnahaqyvFQAEGSLkdgeenaptqhallrwePGVqtva 143
Cdd:PRK10882 127 SALTKDPKTgiVHYDKDVCTGCRYCMVACPFNVPK--------------YDYNNPF-----------------GAI---- 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 90111444  144 VKCDLCDFL-------PEGPACVRACPNQAlrLITGDSLQRQMKEKQRLAAS 188
Cdd:PRK10882 172 HKCELCNQKgverldkGGLPGCVEVCPTGA--VIFGTREELLAEAKRRLALK 221
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 59-98 3.82e-09

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 51.27  E-value: 3.82e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 90111444  59 CLQVCPVNAISQRDD-AIQLNESLCIGCKLCAVVCPFGAIS 98
Cdd:COG1149  19 CVEVCPEGAIKLDDGgAPVVDPDLCTGCGACVGVCPTGAIT 59
NapF COG1145
Ferredoxin [Energy production and conversion];
51-98 7.77e-09

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 53.96  E-value: 7.77e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 90111444  51 CHHCEEapCLQVCPVNAISQRDD--AIQLNESLCIGCKLCAVVCPFGAIS 98
Cdd:COG1145 184 CIGCGL--CVKVCPTGAIRLKDGkpQIVVDPDKCIGCGACVKVCPVGAIS 231
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 59-98 7.82e-09

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 50.43  E-value: 7.82e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 90111444  59 CLQVCPVNAISQRDDAIQLNESLCIGCKLCAVVCPFGAIS 98
Cdd:COG2221  23 CVAVCPTGAISLDDGKLVIDEEKCIGCGACIRVCPTGAIK 62
PRK09898 PRK09898
ferredoxin-like protein;
5-95 2.75e-08

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 51.76  E-value: 2.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444    5 VVAEPLWCTGCNTCLAACSDVHKTQglqQHPRLALAKTST-------------------ITAPVVCHHCEEAPCLQVCPV 65
Cdd:PRK09898  61 LVTQRARCTGCHRCEISCTNFNDGS---VGTFFSRIKIHRnyffgdngvgsggglygdlNYTADTCRQCKEPQCMNVCPI 137

                         90       100       110
                 ....*....|....*....|....*....|..
gi 90111444   66 NAIS--QRDDAIQLNESLCIGCKLCAVVCPFG 95
Cdd:PRK09898 138 GAITwqQKEGCITVDHKRCIGCSACTTACPWM 169
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 51-98 3.93e-08

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: 48.89  E-value: 3.93e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 90111444  51 CHHCeeAPCLQVCPVNAISQRDDA-IQLNESLCIGCKLCAVVCPFGAIS 98
Cdd:COG1144  32 CIGC--GLCWIVCPDGAIRVDDGKyYGIDYDYCKGCGICAEVCPVKAIE 78
flavo_MJ0208 TIGR02700
archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of ...
 51-97 9.54e-08

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: 50.64  E-value: 9.54e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 90111444    51 CHHCEEapCLQVCPVNAISQRDDAIQLNESLCIGCKLCAVVCPFGAI 97
Cdd:TIGR02700 150 CKGCGI--CVDACPRSAIDMVDGKAFIRLLKCVGCGKCKEACPYNAI 194
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
38-98 1.13e-07

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 51.01  E-value: 1.13e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111444  38 ALAKTSTITAPVV-------CHHCEEapCLQVCPVNAISQRDDA-IQLNESLCIGCKLCAVVCPFGAIS 98
Cdd:COG1148 478 LLSKGELGVEPSVaevdpekCTGCGR--CVEVCPYGAISIDEKGvAEVNPALCKGCGTCAAACPSGAIS 544
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 12-97 1.48e-07

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 48.55  E-value: 1.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  12 CTGCNTCLAACSdVHKTQGLQQHPRLALAKTSTITAPVVCHHCEEapCLQVCPVNAISQRDDA-IQLNESLCIGCKLCAV 90
Cdd:cd10549  42 CVFCGACVEVCP-TGAIELTPEGKEYVPKEKEAEIDEEKCIGCGL--CVKVCPVDAITLEDELeIVIDKEKCIGCGICAE 118


                ....*..
gi 90111444  91 VCPFGAI 97
Cdd:cd10549 119 VCPVNAI 125
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 51-98 1.61e-07

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: 46.66  E-value: 1.61e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 90111444  51 CHHCEEapCLQVCPVNAISQRDD----AIQLNESLCIGCKLCAVVCPFGAIS 98
Cdd:COG1143   4 CIGCGL--CVRVCPVDAITIEDGepgkVYVIDPDKCIGCGLCVEVCPTGAIS 53
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 51-98 2.64e-07

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: 50.17  E-value: 2.64e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 90111444  51 CHHceeaPCLQVCPVN-------AISQRDDAIQLNESLCIGCKLCAVVCPFGAIS 98
Cdd:COG1245  17 CNY----ECIKYCPVNrtgkeaiEIDEDDGKPVISEELCIGCGICVKKCPFDAIS 67
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 51-169 3.41e-07

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 47.39  E-value: 3.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  51 CHHCeeAPCLQVCPVNAIS-QRDDAIQL----NESLCIGCKLCAVVCPFGAISASGSRPVNAHA--QYVFQAEGSLKDG- 122
Cdd:cd10549   8 CIGC--GICVKACPTDAIElGPNGAIARgpeiDEDKCVFCGACVEVCPTGAIELTPEGKEYVPKekEAEIDEEKCIGCGl 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 90111444 123 -EENAPTQHALLRWEPGVQTVAVKCDLCDflpegpACVRACPNQALRL 169
Cdd:cd10549  86 cVKVCPVDAITLEDELEIVIDKEKCIGCG------ICAEVCPVNAIKL 127
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 48-169 4.51e-07

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: 46.47  E-value: 4.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444    48 PVVCHHCEEAPCLQVCPVNAISQRDD--AIQLNESLCIGCKLCAVVCPFGAIsasgsrpvnahaqyvfqaegslkdgeen 125
Cdd:pfam13247   7 PEQCRHCLNPPCKASCPVGAIYKDEEtgAVLLDEKTCRGWRECVSACPYNIP---------------------------- 58

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 90111444   126 aptqhallRWEPgVQTVAVKCDLC-DFLPEG--PACVRACPNQALRL 169
Cdd:pfam13247  59 --------RYND-ETGKAEKCDMCyDRVEAGllPACVQTCPTGAMNF 96
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 11-98 1.01e-06

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: 46.24  E-value: 1.01e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  11 WCTGCNTCLAACSdvhkTQGLQQHPRLALAKTSTI--TAPVVCHHCEEapclqVCPVNAISQRDD---------AIQLNE 79
Cdd:cd10549   7 KCIGCGICVKACP----TDAIELGPNGAIARGPEIdeDKCVFCGACVE-----VCPTGAIELTPEgkeyvpkekEAEIDE 77

                        90
                ....*....|....*....
gi 90111444  80 SLCIGCKLCAVVCPFGAIS 98
Cdd:cd10549  78 EKCIGCGLCVKVCPVDAIT 96
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
51-98 1.13e-06

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 48.27  E-value: 1.13e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 90111444   51 CHHceeaPCLQVCPVN-------AISQRDDAIQLNESLCIGCKLCAVVCPFGAIS 98
Cdd:PRK13409  17 CNY----ECIKYCPVVrtgeetiEIDEDDGKPVISEELCIGCGICVKKCPFDAIS 67
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 50-98 1.24e-06

bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 47.38  E-value: 1.24e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 90111444  50 VCHHCEEapCLQVCPVNAISQRDDAIQLNESLCIGCKLCAVVCPFGAIS 98
Cdd:cd03110  65 KCIRCGN--CERVCKFGAILEFFQKLIVDESLCEGCGACVIICPRGAIY 111
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 48-97 3.50e-06

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: 46.53  E-value: 3.50e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 90111444  48 PVVCHHCEEAPCLQVCPVNAISQRD-DAIQL-NESLCIGCKLCAVVCPFGAI 97
Cdd:cd10555 130 PRICNHCTNPACLAACPRKAIYKREeDGIVLvDQDRCRGYRYCVEACPYKKI 181
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 51-98 6.57e-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: 6.57e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 90111444  51 CHHCEEapCLQVCPVNAISQRDD---AIQLNESLCIGCKLCAVVCPFGAIS 98
Cdd:COG1146  10 CIGCGA--CVEVCPVDVLELDEEgkkALVINPEECIGCGACELVCPVGAIT 58
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 12-97 4.16e-05

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: 42.57  E-value: 4.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  12 CTGCNTCLAACSDVHKTQGLQQHPRLALAKTST----------------------ITAPVVCHHCEEAPCLQVCPVNAIS 69
Cdd:cd16365  12 CIGCQTCTVACKNAWTYRKGQEYMWWNNVETKPgggypqdwevktidnggntrffFYLQRLCNHCTNPACLAACPRGAIY 91

                        90       100       110
                ....*....|....*....|....*....|
gi 90111444  70 QR-DDAIQL-NESLCIGCKLCAVVCPFGAI 97
Cdd:cd16365  92 KReEDGIVLiDQKRCRGYRKCVEQCPYKKI 121
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 12-98 5.25e-05

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


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 41.46  E-value: 5.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  12 CTGCNTCLAACS----DVHKTQGLQQHPRLA---LAKTStitapVVCHHCEEApclqvCPVNAISQRDD-----AIQLNE 79
Cdd:cd10564  47 CTFCGACAEACPegalDPAREAPWPLRAEIGdscLALQG-----VECRSCQDA-----CPTQAIRFRPRlggiaLPELDA 116

                        90
                ....*....|....*....
gi 90111444  80 SLCIGCKLCAVVCPFGAIS 98
Cdd:cd10564 117 DACTGCGACVSVCPVGAIT 135
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
2-97 6.43e-05

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 42.61  E-value: 6.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444    2 NRFVVAEPLWCTGCNTCLAAC-SDVHKTQGLQQhpRLALAKTSTITAPVVCHHCEEA-----PCLQVCPVNAISQRDDAI 75
Cdd:PRK07118 160 NGLPVVDEDKCTGCGACVKACpRNVIELIPKSA--RVFVACNSKDKGKAVKKVCEVGcigcgKCVKACPAGAITMENNLA 237

                         90       100
                 ....*....|....*....|..
gi 90111444   76 QLNESLCIGCKLCAVVCPFGAI 97
Cdd:PRK07118 238 VIDQEKCTSCGKCVEKCPTKAI 259
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 59-98 1.87e-04

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


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 41.13  E-value: 1.87e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 90111444  59 CLQVCPVNAISQRDDAI-QLNESLCIGCKLCAVVCPFGAIS 98
Cdd:COG2878 145 CIKACPFDAIVGAAKGMhTVDEDKCTGCGLCVEACPVDCIE 185
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 75-105 2.04e-04

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 38.49  E-value: 2.04e-04
                        10        20        30
                ....*....|....*....|....*....|.
gi 90111444  75 IQLNESLCIGCKLCAVVCPFGAISASGSRPV 105
Cdd:COG2221  10 PKIDEEKCIGCGLCVAVCPTGAISLDDGKLV 40
PRK13795 PRK13795
hypothetical protein; Provisional
 59-93 2.13e-04

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 41.52  E-value: 2.13e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 90111444   59 CLQVCPVNAISqRDD---AIQLNESLCIGCKLCAVVCP 93
Cdd:PRK13795 589 CVGACPTGAIR-IEEgkrKISVDEEKCIHCGKCTEVCP 625
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 51-96 2.63e-04

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: 37.51  E-value: 2.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 90111444    51 CHHCEEapCLQVCPVNAISQRD-------DAIQLNESLCIGCKLCAVVCPFGA 96
Cdd:pfam12838   1 CIGCGA--CVAACPVGAITLDEvgekkgtKTVVIDPERCVGCGACVAVCPTGA 51
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 12-98 3.10e-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: 39.55  E-value: 3.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  12 CTGCNTCLAACSdvhkTQGLQqhPRLALAKTSTITAPVV------CHHCEEApCLQVCPVNAISQRDDAIQ--------L 77
Cdd:cd16373  16 CIRCGLCVEACP----TGVIQ--PAGLEDGLEGGRTPYLdpregpCDLCCDA-CVEVCPTGALRPLDLEEQkvkmgvavI 88

                        90       100
                ....*....|....*....|....*..
gi 90111444  78 NESLCI------GCKLCAVVCPFGAIS 98
Cdd:cd16373  89 DKDRCLawqggtDCGVCVEACPTEAIA 115
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 75-98 3.21e-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: 36.84  E-value: 3.21e-04
                          10        20
                  ....*....|....*....|....
gi 90111444    75 IQLNESLCIGCKLCAVVCPFGAIS 98
Cdd:pfam00037   1 VVIDEEKCIGCGACVEVCPVGAIT 24
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
82-98 3.22e-04

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 39.86  E-value: 3.22e-04
                         10
                 ....*....|....*..
gi 90111444   82 CIGCKLCAVVCPFGAIS 98
Cdd:PRK05888  60 CIACKLCAAICPADAIT 76
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
49-98 3.54e-04

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 39.48  E-value: 3.54e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444   49 VVCHHCEeapclQVCPVNAIS----QRDD------AIQLNESLCIGCKLCAVVCPFGAIS 98
Cdd:PRK05888  61 IACKLCA-----AICPADAITieaaEREDgrrrttRYDINFGRCIFCGFCEEACPTDAIV 115
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 75-170 3.89e-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: 3.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  75 IQLNESLCIGCKLCAVVCPFGAISASGSRpvnahaQYVFQAEgslkdgeenaptqhallrwepgvqtvavKCDLCDflpe 154
Cdd:COG1149   6 PVIDEEKCIGCGLCVEVCPEGAIKLDDGG------APVVDPD----------------------------LCTGCG---- 47

                        90
                ....*....|....*.
gi 90111444 155 gpACVRACPNQALRLI 170
Cdd:COG1149  48 --ACVGVCPTGAITLE 61
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 48-94 4.06e-04

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: 40.14  E-value: 4.06e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 90111444  48 PVVCHHCEEAPCLQVCPVNAISQR-DDAIQL-NESLCIGCKLCAVVCPF 94
Cdd:cd10556 138 PRICNHCTYPACLAACPRKAIYKReEDGIVLiDQERCRGYRECVEACPY 186
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 51-97 5.30e-04

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 40.24  E-value: 5.30e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 90111444   51 CHHCEEAP-CLQVCPVNAISQ----RDDAIqlNESLCIGCKLCAVVCPFGAI 97
Cdd:PRK12771 509 CGNCFECDnCYGACPQDAIIKlgpgRRYHF--DYDKCTGCHICADVCPCGAI 558
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
51-98 6.67e-04

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 39.66  E-value: 6.67e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 90111444  51 CHHCEEapCLQVCPVNaISQRDDAIQLNEslCIGCKLCAVVCPFGAIS 98
Cdd:COG0348 212 CIDCGL--CVKVCPMG-IDIRKGEINQSE--CINCGRCIDACPKDAIR 254
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 75-168 7.24e-04

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: 38.39  E-value: 7.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  75 IQLNESLCIGCKLCAVVCpfgAISASGSRPVNahaqyvfqaegsLKDGEENAPTQHALLRWEPGVqTVAVKCDLCDFlpe 154
Cdd:cd10563   2 IFIDEEKCLGCKLCEVAC---AVAHSKSKDLI------------KAKLEKERPRPRIRVEESGGR-SFPLQCRHCDE--- 62

                        90
                ....*....|....
gi 90111444 155 gPACVRACPNQALR 168
Cdd:cd10563  63 -PPCVKACMSGAMH 75
RnfC COG4656
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and ...
 37-93 8.13e-04

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


Pssm-ID: 443694 [Multi-domain]  Cd Length: 451  Bit Score: 39.35  E-value: 8.13e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111444  37 LALAKTSTITAPV-VCHHCeeAPCLQVCPVNAISQR----------DDAIQLNESLCIGCKLCAVVCP 93
Cdd:COG4656 351 LALTKEEVPPPEEqPCIRC--GRCVDACPMGLLPQQlywyaragdfDKAEEYNLMDCIECGCCSYVCP 416
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
51-103 8.46e-04

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 39.62  E-value: 8.46e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 90111444  51 CHHCEEAPCLQVCPVNAISQRDDAIQLNESLCIGCKLCAVVCPFGAISASGSR 103
Cdd:COG4624  62 CRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCYPCVRACPVKAIKVDDGK 114
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 82-105 9.83e-04

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


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 38.69  E-value: 9.83e-04
                         10        20
                 ....*....|....*....|....
gi 90111444   82 CIGCKLCAVVCPFGAISASGSRPV 105
Cdd:NF038196 187 CIGCGICAKVCPVNNIEMEDGKPV 210
NapF COG1145
Ferredoxin [Energy production and conversion];
78-169 1.07e-03

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 38.94  E-value: 1.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  78 NESLCIGCKLCAVVCPFGAISASGSRPvnahaQYVFQAEgslkdgeenaptqhallrwepgvqtvavKCDLCdflpegPA 157
Cdd:COG1145 180 DAEKCIGCGLCVKVCPTGAIRLKDGKP-----QIVVDPD----------------------------KCIGC------GA 220

                        90
                ....*....|..
gi 90111444 158 CVRACPNQALRL 169
Cdd:COG1145 221 CVKVCPVGAISL 232
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 48-94 1.55e-03

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: 38.50  E-value: 1.55e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 90111444  48 PVVCHHCEEAPCLQVCPVNAISQRD-DAIQL-NESLCIGCKLCAVVCPF 94
Cdd:cd10557 176 PRICNHCLNPACVAACPSGAIYKREeDGIVLiDQDRCRGWRMCVSACPY 224
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 80-179 1.68e-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: 37.62  E-value: 1.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  80 SLCIGCKLCAVVCPFGAISASGsrpvnahaqyvfqaegsLKDGEENAPTQHALLRWEPgvqtvavkCDLCdflpeGPACV 159
Cdd:cd16373  14 ALCIRCGLCVEACPTGVIQPAG-----------------LEDGLEGGRTPYLDPREGP--------CDLC-----CDACV 63

                        90       100
                ....*....|....*....|
gi 90111444 160 RACPNQALRLITGDSLQRQM 179
Cdd:cd16373  64 EVCPTGALRPLDLEEQKVKM 83
PRK06273 PRK06273
ferredoxin; Provisional
 79-112 2.87e-03

ferredoxin; Provisional


Pssm-ID: 235764 [Multi-domain]  Cd Length: 165  Bit Score: 37.00  E-value: 2.87e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 90111444   79 ESLCIGCKLCAVVCPFGAISASGSRPVNAHAQYV 112
Cdd:PRK06273  48 EELCIGCGGCANVCPTKAIEMIPVEPVKITEGYV 81
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 77-105 3.21e-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: 35.41  E-value: 3.21e-03
                        10        20
                ....*....|....*....|....*....
gi 90111444  77 LNESLCIGCKLCAVVCPFGAISASGSRPV 105
Cdd:COG1144  27 VDEDKCIGCGLCWIVCPDGAIRVDDGKYY 55
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 76-104 3.77e-03

bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 36.98  E-value: 3.77e-03
                        10        20
                ....*....|....*....|....*....
gi 90111444  76 QLNESLCIGCKLCAVVCPFGAISASGSRP 104
Cdd:cd03110  60 FIDQEKCIRCGNCERVCKFGAILEFFQKL 88
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
59-177 4.50e-03

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 36.96  E-value: 4.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444  59 CLQVCPVNAIS---QRDDAIQL--NESLCIGCKLCAVVCPFGAISASGsrpvnahaqYVFQAEgslkdgeenaptqhall 133
Cdd:COG0348 184 CRYLCPYGAFQgllSDLSTLRVryDRGDCIDCGLCVKVCPMGIDIRKG---------EINQSE----------------- 237

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 90111444 134 rwepgvqtvavkCDLCDflpegpACVRACPNQALRLITGDSLQR 177
Cdd:COG0348 238 ------------CINCG------RCIDACPKDAIRFSSRGEKTR 263
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
78-98 4.77e-03

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 34.71  E-value: 4.77e-03
                        10        20
                ....*....|....*....|.
gi 90111444  78 NESLCIGCKLCAVVCPFGAIS 98
Cdd:COG2768   9 DEEKCIGCGACVKVCPVGAIS 29
PRK00783 PRK00783
DNA-directed RNA polymerase subunit D; Provisional
 51-120 5.32e-03

DNA-directed RNA polymerase subunit D; Provisional


Pssm-ID: 234837 [Multi-domain]  Cd Length: 263  Bit Score: 36.79  E-value: 5.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111444   51 CHHCEEapCLQVCPVNAISQRDDAIQLNESL-CIGCKLCAVVCPFGAISasgsrpVNAHA-QYVFQAE--GSLK 120
Cdd:PRK00783 171 CDECEK--CVEACPRGVLELKEGKLVVTDLLnCSLCKLCERACPGKAIR------VSDDEnKFIFTVEsdGSLP 236
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 59-98 5.52e-03

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: 36.31  E-value: 5.52e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 90111444    59 CLQVCPVNAISQRDDAIQ-LNESLCIGCKLCAVVCPFGAIS 98
Cdd:TIGR01944 121 CIQACPVDAIVGAAKAMHtVIADECTGCDLCVEPCPTDCIE 161
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
59-97 6.79e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 36.45  E-value: 6.79e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 90111444   59 CLQVCPVNAISQRDDAIQLNESLCIGCKLCAVVCPFGAI 97
Cdd:PRK07118 147 CVAACPFDAIHIENGLPVVDEDKCTGCGACVKACPRNVI 185
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 82-98 7.03e-03

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: 35.08  E-value: 7.03e-03
                          10
                  ....*....|....*..
gi 90111444    82 CIGCKLCAVVCPFGAIS 98
Cdd:TIGR01971  45 CIGCTLCAAVCPADAIR 61
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 47-98 7.66e-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: 36.13  E-value: 7.66e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 90111444  47 APVVCHHCEEAPC-------LQVCPVNAIsqrdDAIQLNESLCIGCKLCAVVCPFGAIS 98
Cdd:COG2878 101 AVVRCNGGCEKAKpkyeydgIKDCRAAVI----GGPKGCEYGCIGCGDCIKACPFDAIV 155
PRK10194 PRK10194
ferredoxin-type protein NapF;
12-99 9.47e-03

ferredoxin-type protein NapF;


Pssm-ID: 182296 [Multi-domain]  Cd Length: 163  Bit Score: 35.38  E-value: 9.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111444   12 CTGCNTCLAACSDvhkTQGLQQHPR-----LALAKTSTITAPVVCHHCEEApclqvCPVNAISQRDD-----AIQLNESL 81
Cdd:PRK10194  68 CSFCYACAQACPE---SLFSPRHTRawdlqFTIGDACLAYQSVECRRCQDS-----CEPMAIIFRPTlsgiyQPQLNSQL 139

                         90
                 ....*....|....*...
gi 90111444   82 CIGCKLCAVVCPFGAISA 99
Cdd:PRK10194 140 CNGCGACAASCPVSAITA 157
 
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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