NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|882617|gb|AAA69234|]
View 

formate hydrogenlyase subunit 2 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 4-167 6.35e-62

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: 189.39  E-value: 6.35e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     4 FVIADSTLCIGCHTCEAACSETHRQH--------GLQSMPRLRVMLNEKESAPQLCHHCEDAPCAVVCPVNAITRVDGAV 75
Cdd:cd10554   1 FVIADPDKCIGCRTCEVACAAAHSGKgifeagtdGLPFLPRLRVVKTGEVTAPVQCRQCEDAPCANVCPVGAISQEDGVV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    76 QLNESLCVSCKLCGIACPFGAIEFSGSRPLDIpanantpkappappaparvstllDWVPGIRAIAVKCDLCSFDEQGPAC 155
Cdd:cd10554  81 QVDEERCIGCKLCVLACPFGAIEMAPTTVPGV-----------------------DWERGPRAVAVKCDLCAGREGGPAC 137

                       170
                ....*....|..
gi 882617   156 VRMCPTKALHLV 167
Cdd:cd10554 138 VEACPTKALTLV 149
 
Name Accession Description Interval E-value
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 4-167 6.35e-62

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: 189.39  E-value: 6.35e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     4 FVIADSTLCIGCHTCEAACSETHRQH--------GLQSMPRLRVMLNEKESAPQLCHHCEDAPCAVVCPVNAITRVDGAV 75
Cdd:cd10554   1 FVIADPDKCIGCRTCEVACAAAHSGKgifeagtdGLPFLPRLRVVKTGEVTAPVQCRQCEDAPCANVCPVGAISQEDGVV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    76 QLNESLCVSCKLCGIACPFGAIEFSGSRPLDIpanantpkappappaparvstllDWVPGIRAIAVKCDLCSFDEQGPAC 155
Cdd:cd10554  81 QVDEERCIGCKLCVLACPFGAIEMAPTTVPGV-----------------------DWERGPRAVAVKCDLCAGREGGPAC 137

                       170
                ....*....|..
gi 882617   156 VRMCPTKALHLV 167
Cdd:cd10554 138 VEACPTKALTLV 149
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
1-168 1.04e-55

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 173.30  E-value: 1.04e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     1 MNRFVIADSTLCIGCHTCEAACSETHRQ-HGLQSMPRLRVMLNEKESAPQLCHHCEDAPCAVVCPVNAITRVDGAVQLNE 79
Cdd:COG1142   1 MNKFIIADPEKCIGCRTCEAACAVAHEGeEGEPFLPRIRVVRKAGVSAPVQCRHCEDAPCAEVCPVGAITRDDGAVVVDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    80 SLCVSCKLCGIACPFGAIEFSGSRPldipanantpkappappaparvstlldwvpgiRAIAVKCDLCSFDEQGPACVRMC 159
Cdd:COG1142  81 EKCIGCGLCVLACPFGAITMVGEKS--------------------------------RAVAVKCDLCGGREGGPACVEAC 128


                ....*....
gi 882617   160 PTKALHLVD 168
Cdd:COG1142 129 PTGALRLVD 137
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 1-183 2.19e-45

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 158.76  E-value: 2.19e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617      1 MNRFVIADSTLCIGCHTCEAAC--SETHRQHGLQS---MPRLRVMLNEKESAPQLCHHCEDAPCAVVCPVNAITRVDGAV 75
Cdd:PRK12769   1 MNRFIMANSQQCLGCHACEIACvmAHNDEQHVLSQhhfHPRITVIKHQQQRSAVTCHHCEDAPCARSCPNGAISHVDDSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     76 QLNESLCVSCKLCGIACPFGAIEFSGSrpldiPANANTpkappappaparvstlldwvpgIRAIAVKCDLCSFDEQGPAC 155
Cdd:PRK12769  81 QVNQQKCIGCKSCVVACPFGTMQIVLT-----PVAAGK----------------------VKATAHKCDLCAGRENGPAC 133

                        170       180
                 ....*....|....*....|....*...
gi 882617    156 VRMCPTKALHLVDNTDIARVSKRKRELT 183
Cdd:PRK12769 134 VENCPADALQLVTEQALSGMAKSRRLRT 161
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 48-168 3.08e-11

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: 57.64  E-value: 3.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617      48 PQLCHHCEDAPCAVVCPVNAITR--VDGAVQLNESLCVSCKLCGIACPFGAIEFsgsrpldipanantpkappappapar 125
Cdd:pfam13247   7 PEQCRHCLNPPCKASCPVGAIYKdeETGAVLLDEKTCRGWRECVSACPYNIPRY-------------------------- 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 882617     126 vstllDWVPGIraiAVKCDLC-SFDEQG--PACVRMCPTKALHLVD 168
Cdd:pfam13247  61 -----NDETGK---AEKCDMCyDRVEAGllPACVQTCPTGAMNFGD 98
flavo_MJ0208 TIGR02700
archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of ...
 51-97 3.93e-06

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


Pssm-ID: 131747 [Multi-domain]  Cd Length: 234  Bit Score: 46.02  E-value: 3.93e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 882617      51 CHHCEDapCAVVCPVNAITRVDGAVQLNESLCVSCKLCGIACPFGAI 97
Cdd:TIGR02700 150 CKGCGI--CVDACPRSAIDMVDGKAFIRLLKCVGCGKCKEACPYNAI 194
 
Name Accession Description Interval E-value
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 4-167 6.35e-62

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: 189.39  E-value: 6.35e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     4 FVIADSTLCIGCHTCEAACSETHRQH--------GLQSMPRLRVMLNEKESAPQLCHHCEDAPCAVVCPVNAITRVDGAV 75
Cdd:cd10554   1 FVIADPDKCIGCRTCEVACAAAHSGKgifeagtdGLPFLPRLRVVKTGEVTAPVQCRQCEDAPCANVCPVGAISQEDGVV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    76 QLNESLCVSCKLCGIACPFGAIEFSGSRPLDIpanantpkappappaparvstllDWVPGIRAIAVKCDLCSFDEQGPAC 155
Cdd:cd10554  81 QVDEERCIGCKLCVLACPFGAIEMAPTTVPGV-----------------------DWERGPRAVAVKCDLCAGREGGPAC 137

                       170
                ....*....|..
gi 882617   156 VRMCPTKALHLV 167
Cdd:cd10554 138 VEACPTKALTLV 149
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
1-168 1.04e-55

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 173.30  E-value: 1.04e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     1 MNRFVIADSTLCIGCHTCEAACSETHRQ-HGLQSMPRLRVMLNEKESAPQLCHHCEDAPCAVVCPVNAITRVDGAVQLNE 79
Cdd:COG1142   1 MNKFIIADPEKCIGCRTCEAACAVAHEGeEGEPFLPRIRVVRKAGVSAPVQCRHCEDAPCAEVCPVGAITRDDGAVVVDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    80 SLCVSCKLCGIACPFGAIEFSGSRPldipanantpkappappaparvstlldwvpgiRAIAVKCDLCSFDEQGPACVRMC 159
Cdd:COG1142  81 EKCIGCGLCVLACPFGAITMVGEKS--------------------------------RAVAVKCDLCGGREGGPACVEAC 128


                ....*....
gi 882617   160 PTKALHLVD 168
Cdd:COG1142 129 PTGALRLVD 137
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 1-183 2.19e-45

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 158.76  E-value: 2.19e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617      1 MNRFVIADSTLCIGCHTCEAAC--SETHRQHGLQS---MPRLRVMLNEKESAPQLCHHCEDAPCAVVCPVNAITRVDGAV 75
Cdd:PRK12769   1 MNRFIMANSQQCLGCHACEIACvmAHNDEQHVLSQhhfHPRITVIKHQQQRSAVTCHHCEDAPCARSCPNGAISHVDDSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     76 QLNESLCVSCKLCGIACPFGAIEFSGSrpldiPANANTpkappappaparvstlldwvpgIRAIAVKCDLCSFDEQGPAC 155
Cdd:PRK12769  81 QVNQQKCIGCKSCVVACPFGTMQIVLT-----PVAAGK----------------------VKATAHKCDLCAGRENGPAC 133

                        170       180
                 ....*....|....*....|....*...
gi 882617    156 VRMCPTKALHLVDNTDIARVSKRKRELT 183
Cdd:PRK12769 134 VENCPADALQLVTEQALSGMAKSRRLRT 161
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 1-182 1.72e-38

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 139.78  E-value: 1.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617      1 MNRFVIADSTLCIGCHTCEAACSETHRQHGLQS-----MPRLRVMLNEKESAPQLCHHCEDAPCAVVCPVNAITRVDGAV 75
Cdd:PRK12809   1 MNKFIAAEAAECIGCHACEIACAVAHNQENWPLshsdfRPRIHVVGKGQAANPVACHHCNNAPCVTACPVNALTFQSDSV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     76 QLNESLCVSCKLCGIACPFGAIEFsgsrpldipanantpkappappaparvstlldwvpgIRAIAVKCDLCSFDEQGP-A 154
Cdd:PRK12809  81 QLDEQKCIGCKRCAIACPFGVVEM------------------------------------VDTIAQKCDLCNQRSSGTqA 124

                        170       180
                 ....*....|....*....|....*...
gi 882617    155 CVRMCPTKALHLVDNTDIARVsKRKREL 182
Cdd:PRK12809 125 CIEVCPTQALRLMDDKGLQQI-KVARQR 151
PRK10330 PRK10330
electron transport protein HydN;
1-180 1.16e-35

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 123.46  E-value: 1.16e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617      1 MNRFVIADSTLCIGCHTCEAACSETHRQHGLQS-------MPRLRVMLNEKESAPQLCHHCEDAPCAVVCPVNAITRVDG 73
Cdd:PRK10330   1 MNRFIIADASKCIGCRTCEVACVVSHQENQDCAsltpetfLPRIHVIKGVNVSTATVCRQCEDAPCANVCPNGAISRDKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     74 AVQLNESLCVSCKLCGIACPFGAIEFSgSRPLdipanantpkappappapARVSTLLDWVPGIRAIAVKCDLCSFDEQGP 153
Cdd:PRK10330  81 FVHVMQERCIGCKTCVVACPYGAMEVV-VRPV------------------IRNSGAGLNVRAEKAEANKCDLCNHREDGP 141

                        170       180
                 ....*....|....*....|....*..
gi 882617    154 ACVRMCPTKALHLVDNTDIARVSKRKR 180
Cdd:PRK10330 142 ACMAACPTHALICVDRNKLEQLSAEKR 168
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 1-182 3.55e-35

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 122.36  E-value: 3.55e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     1 MNRFVIaDSTLCIGCHTCEAACSETHrqHGLQSMPRLRVMLNEKESAPQ--------LCHHCEDAPCAVVCPVNAIT-RV 71
Cdd:COG0437   5 RYGMVI-DLTKCIGCRACVVACKEEN--NLPVGVTWRRVRRYEEGEFPNvewlfvpvLCNHCDDPPCVKVCPTGATYkRE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    72 DGAVQLNESLCVSCKLCGIACPFGAIEFSGSRPldipanantpkappappaparvstlldwvpgiraIAVKCDLCS---F 148
Cdd:COG0437  82 DGIVLVDYDKCIGCRYCVAACPYGAPRFNPETG----------------------------------VVEKCTFCAdrlD 127

                       170       180       190
                ....*....|....*....|....*....|....*
gi 882617   149 DEQGPACVRMCPTKALHLVD-NTDIARVSKRKREL 182
Cdd:COG0437 128 EGLLPACVEACPTGALVFGDlDDPESEVSKRLAEL 162
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 8-167 2.49e-33

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: 115.95  E-value: 2.49e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     8 DSTLCIGCHTCEAACSETH---RQHGLQSMPRLRVMLNEKESAPQLCHHCEDAPCAVVCPVNAITRV-DGAVQLNESLCV 83
Cdd:cd04410   4 DLDRCIGCGTCEVACKQEHglrPGPDWSRIKVIEGGGLERAFLPVSCMHCEDPPCVKACPTGAIYKDeDGIVLIDEDKCI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    84 SCKLCGIACPFGAIEFsgsrpldipanantpkappappaparvstllDWVPGiraIAVKCDLC---SFDEQGPACVRMCP 160
Cdd:cd04410  84 GCGSCVEACPYGAIVF-------------------------------DPEPG---KAVKCDLCgdrLDEGLEPACVKACP 129


                ....*..
gi 882617   161 TKALHLV 167
Cdd:cd04410 130 TGALTFG 136
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 5-167 4.22e-32

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: 112.67  E-value: 4.22e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     5 VIADSTLCIGCHTCEAACSETHRQHGLQSMPRLRVMLNEKE--SAPQLCHHCEDAPCAVVCPVNAITR--VDGAVQLNES 80
Cdd:cd10550   1 LVVDPEKCTGCRTCELACSLKHEGVFNPSLSRIRVVRFEPEglDVPVVCRQCEDAPCVEACPVGAISRdeETGAVVVDED 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    81 LCVSCKLCGIACPFGAIEFsgsrpldipanantpkappappaparvstllDWVpgiRAIAVKCDLCSFDeqgPACVRMCP 160
Cdd:cd10550  81 KCIGCGMCVEACPFGAIRV-------------------------------DPE---TGKAIKCDLCGGD---PACVKVCP 123


                ....*..
gi 882617   161 TKALHLV 167
Cdd:cd10550 124 TGALEFV 130
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 5-180 1.21e-28

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


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 104.28  E-value: 1.21e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     5 VIADSTLCIGCHTCEAACSETHRQHglqsmPRLRVML-NEKESAPQLCHHCEDAPCAVVCPVNAITR-VDGAVQLNESLC 82
Cdd:cd16374   1 VYVDPERCIGCRACEIACAREHSGK-----PRISVEVvEDLASVPVRCRHCEDAPCMEVCPTGAIYRdEDGAVLVDPDKC 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    83 VSCKLCGIACPFGAIEFSGSRPldipanantpkappappaparvstlldwvpgiraIAVKCDLCS---FDEQGPACVRMC 159
Cdd:cd16374  76 IGCGMCAMACPFGVPRFDPSLK----------------------------------VAVKCDLCIdrrREGKLPACVEAC 121

                       170       180
                ....*....|....*....|.
gi 882617   160 PTKALHLvdnTDIARVSKRKR 180
Cdd:cd16374 122 PTGALKF---GDIEELLKEKR 139
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 5-167 4.08e-28

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: 102.72  E-value: 4.08e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     5 VIADSTLCIGCHTCEAACSETHRQHG---------LQSMPRLRVMLNEKESAPQLCHHCEDAPCAVVCPVNAITR--VDG 73
Cdd:cd10563   2 IFIDEEKCLGCKLCEVACAVAHSKSKdlikaklekERPRPRIRVEESGGRSFPLQCRHCDEPPCVKACMSGAMHKdpETG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    74 AVQLNESLCVSCKLCGIACPFGAIefsgsrpldIPANANTpkappappaparvstlldwvpgiraIAVKCDLCsFDEQGP 153
Cdd:cd10563  82 IVIHDEEKCVGCWMCVMVCPYGAI---------RPDKERK-------------------------VALKCDLC-PDRETP 126

                       170
                ....*....|....
gi 882617   154 ACVRMCPTKALHLV 167
Cdd:cd10563 127 ACVEACPTGALVLE 140
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 8-164 4.21e-28

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


Pssm-ID: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 102.64  E-value: 4.21e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     8 DSTLCIGCHTCEAACSETHrqhGLQSMPRLR-VMLNEKESAPQL--------CHHCEDAPCAVVCPVNAIT-RVDGAVQL 77
Cdd:cd16371   5 DQERCIGCKACEIACKDKN---DLPPGVNWRrVYEYEGGEFPEVfayflsmsCNHCENPACVKVCPTGAITkREDGIVVV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    78 NESLCVSCKLCGIACPFGAIEFSGSRPldipanantpkappappaparvstlldwvpgiraIAVKCDLCsFD--EQG--P 153
Cdd:cd16371  82 DQDKCIGCGYCVWACPYGAPQYNPETG----------------------------------KMDKCDMC-VDrlDEGekP 126

                       170
                ....*....|.
gi 882617   154 ACVRMCPTKAL 164
Cdd:cd16371 127 ACVAACPTRAL 137
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 4-181 2.92e-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: 2.92e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     4 FVIaDSTLCIGCHTCEAACSETHRQhgLQSMPRLRVMLNEKESA--------PQLCHHCEDAPCAVVCPVNAIT-RVDGA 74
Cdd:cd10551   1 MVI-DLRKCIGCGACVVACKAENNV--PPGVFRNRVLEYEVGEYpnvkrtflPVLCNHCENPPCVKVCPTGATYkREDGI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    75 VQLNESLCVSCKLCGIACPFGAIEFSGSRPLDIPANantpkappappaparvstlldwVPGIRAIAVKCDLCS-FDEQG- 152
Cdd:cd10551  78 VLVDYDKCIGCRYCMAACPYGARYFNPEEPHEFGEV----------------------PVRPKGVVEKCTFCYhRLDEGl 135

                       170       180       190
                ....*....|....*....|....*....|.
gi 882617   153 -PACVRMCPTKALHLVD-NTDIARVSKRKRE 181
Cdd:cd10551 136 lPACVEACPTGARIFGDlDDPNSEVSKLLAE 166
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 8-164 2.64e-23

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: 91.89  E-value: 2.64e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     8 DSTLCIGCHTCEAACSETHR--------QHGLQSMPRL------RVMLNEKESAP-------QLCHHCEDAPCAVVCPVN 66
Cdd:cd10561   5 DTTRCIGCRACEVACKEWNGlpaedtafGPGWDNPRDLsaktytVIKRYEVETGGkgfvfvkRQCMHCLDPACVSACPVG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    67 AITRV-DGAVQLNESLCVSCKLCGIACPFGAIEFSGSRPLdipanantpkappappaparvstlldwvPGIRaiavKCDL 145
Cdd:cd10561  85 ALRKTpEGPVTYDEDKCIGCRYCMVACPFNIPKYEWDSAN----------------------------PKIR----KCTM 132

                       170       180
                ....*....|....*....|...
gi 882617   146 CsFD--EQG--PACVRMCPTKAL 164
Cdd:cd10561 133 C-YDrlKEGkqPACVEACPTGAL 154
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 12-192 3.47e-22

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


Pssm-ID: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 88.60  E-value: 3.47e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    12 CIGCHTCEAACSE--THRQhglQSMPRLRvMLNEKES---APQLCHHCEDAPCAVVCPVNAITRV-DGAVQL-NESLCVS 84
Cdd:cd16369  11 CIGCRACVAACREcgTHRG---KSMIHVD-YIDRGEStqtAPTVCMHCEDPTCAEVCPADAIKVTeDGVVQSaLKPRCIG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    85 CKLCGIACPFGaiefsgsrpldipanantpkappappaparvstlldwVPGI---RAIAVKCDLC---SFDEQGPACVRM 158
Cdd:cd16369  87 CSNCVNACPFG-------------------------------------VPKYdeeRNLMMKCDMCydrTSVGKAPMCASV 129

                       170       180       190
                ....*....|....*....|....*....|....*
gi 882617   159 CPTKALHLVDNTDIArvSKRKRELTFNT-DFGDLT 192
Cdd:cd16369 130 CPSGALFYGTREEIQ--ALRPGSTPVNTfVFGPQE 162
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 2-168 2.09e-20

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


Pssm-ID: 319889 [Multi-domain]  Cd Length: 138  Bit Score: 82.74  E-value: 2.09e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     2 NRFVIADSTLCIGCHTCEAACSETHRQHglqsmPRL--RVMLNEKESAPQLCHHCEDAPCAVVCPVNAITRVD-GAVQLN 78
Cdd:cd16367  11 TNLLVIDLDRCIRCDNCEKACADTHDGH-----SRLdrNGLRFGNLLVPTACRHCVDPVCMIGCPTGAIHRDDgGEVVIS 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    79 ESlCVSCKLCGIACPFGAIEFsgsrpldipanantpkappappaparvstlldwvpgirAIAVKCDLCSfDEQGPACVRM 158
Cdd:cd16367  86 DA-CCGCGNCASACPYGAIQM--------------------------------------VRAVKCDLCA-GYAGPACVSA 125

                       170
                ....*....|
gi 882617   159 CPTKALHLVD 168
Cdd:cd16367 126 CPTGAAIRVN 135
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 8-182 7.85e-20

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: 83.21  E-value: 7.85e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     8 DSTLCIGCHTCEAACSE--------THRQHGLQSMPRLR-----VM-LNEKESAPQL--------CHHCEDAPCAVVCP- 64
Cdd:cd10558   5 DVSKCIGCKACQVACKEwndlraevGHNVGTYQNPADLSpetwtLMkFREVEDNGKLewlirkdgCMHCADPGCLKACPs 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    65 VNAI-TRVDGAVQLNESLCVSCKLCGIACPFgaiefsgsrplDIPanantpkappappapaRVSTLLdwvpgirAIAVKC 143
Cdd:cd10558  85 PGAIvQYANGIVDFQSDKCIGCGYCIKGCPF-----------DIP----------------RISKDD-------NKMYKC 130

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 882617   144 DLCS---FDEQGPACVRMCPTKALHLVDNTD-IARVSKRKREL 182
Cdd:cd10558 131 TLCSdrvSVGLEPACVKTCPTGALHFGTKEDmLALAEKRVAAL 173
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 8-165 4.33e-19

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


Pssm-ID: 319888 [Multi-domain]  Cd Length: 156  Bit Score: 79.75  E-value: 4.33e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     8 DSTLCIGCHTCEAACSE--------THRQHGLQSMPRL------RVMLNEKE---------SAPQLCHHCEDAPCAVVCP 64
Cdd:cd16366   4 DTSRCTGCRACQVACKQwnglpaekTEFTGSYQNPPDLtahtwtLVRFYEVEkpggdlswlFRKDQCMHCTDAGCLAACP 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    65 VNAITRVD-GAVQLNESLCVSCKLCGIACPFGAIEFSGSRPLdipanantpkappappaparvstlldwvpgiraiAVKC 143
Cdd:cd16366  84 TGAIIRTEtGTVVVDPETCIGCGYCVNACPFDIPRFDEETGR----------------------------------VAKC 129

                       170       180
                ....*....|....*....|....*.
gi 882617   144 DLCsFDEQG----PACVRMCPTKALH 165
Cdd:cd16366 130 TLC-YDRISnglqPACVKTCPTGALT 154
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 8-172 3.38e-18

uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes the beta-subunit of formate dehydrogenases that are as yet uncharacterized. Members of the DMSO reductase family include formate dehydrogenase N and O (FDH-N, FDH-O) and tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N, a major component of nitrate respiration of Escherichia coli, is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. It forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.


Pssm-ID: 319884 [Multi-domain]  Cd Length: 161  Bit Score: 77.73  E-value: 3.38e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     8 DSTLCIGCHTCEAACSE--------THRQHGLQSMP------RLRVMLNEKESAP---------QLCHHCEDAPCAVVCP 64
Cdd:cd10562   4 DTSKCTACRGCQVACKQwnqlpaekTPFTGSYQNPPdltpntWTLIRFYEHEEDNggirwlfrkRQCMHCTDAACVKVCP 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    65 VNAITRVD-GAVQLNESLCVSCKLCGIACPFGAIEFSGSRPldipanantpkappappaparvstlldwvpgiraIAVKC 143
Cdd:cd10562  84 TGALYKTEnGAVVVDEDKCIGCGYCVAACPFDVPRYDETTN----------------------------------KITKC 129

                       170       180       190
                ....*....|....*....|....*....|...
gi 882617   144 DLCsFD--EQG--PACVRMCPTKALHLVDNTDI 172
Cdd:cd10562 130 TLC-FDriENGmqPACVKTCPTGALTFGDRDEL 161
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 8-164 8.85e-17

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: 75.50  E-value: 8.85e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     8 DSTLCIGCHTCEAACSE--------------THRQHG------------LQSMPRLRVMLNEKES----APQLCHHCEDA 57
Cdd:cd10560   5 DTSICIGCKACEVACKQwnqlpadgydfsgmSYDNTGdlsastwrhvkfIERPTEDGPANEGGDLqwlfMSDVCKHCTDA 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    58 PCAVVCPVNAITRVD-GAVQLNESLCVSCKLCGIACPFGAIEFsgsrpldipaNANTPKappappaparvstlldwvpgi 136
Cdd:cd10560  85 GCLEACPTGAIFRTEfGTVYIQPDICNGCGYCVAACPFGVIDR----------NEETGR--------------------- 133

                       170       180       190
                ....*....|....*....|....*....|..
gi 882617   137 raiAVKCDLCsFDEQG----PACVRMCPTKAL 164
Cdd:cd10560 134 ---AHKCTLC-YDRLKdglePACAKACPTGSI 161
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 8-167 3.31e-16

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


Pssm-ID: 319875 [Multi-domain]  Cd Length: 146  Bit Score: 72.01  E-value: 3.31e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     8 DSTLCIGCHTCEAACSEthrQHGLQSMPRL----RVMLNEKESAPQL------CHHCEDAPCAVVCPVNAITR--VDGAV 75
Cdd:cd10553   8 DSKRCIGCLACEVHCKV---KNNLPVGPRLcrifAVGPKMVGGKPRLkfvymsCFHCENPWCVKACPTGAMQKreKDGIV 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    76 QLNESLCVSCKLCGIACPFGAIEFSGSRpldipanantpkappappaparvstlldwvpgirAIAVKCDLCSFD-EQG-- 152
Cdd:cd10553  85 YVDQELCIGCKACIEACPWGIPQWNPAT----------------------------------GKVVKCDYCMDRiDQGlk 130

                       170
                ....*....|....*
gi 882617   153 PACVRMCPTKALHLV 167
Cdd:cd10553 131 PACVTGCTTHALSFV 145
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 3-104 1.55e-15

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: 69.67  E-value: 1.55e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     3 RFVIADSTLCIGCHTCEAACSETHRQHGLQSMPRLRVMLNEKESAPQLCHHCedAPCAVVCPVNAITR-VDGAVQLNESL 81
Cdd:cd16372   1 KLLVTDPEKCIGCLQCEEACSKTFFKEEDREKSCIRITETEGGYAINVCNQC--GECIDVCPTGAITRdANGVVMINKKL 78

                        90       100
                ....*....|....*....|...
gi 882617    82 CVSCKLCGIACPFGAIEFSGSRP 104
Cdd:cd16372  79 CVGCLMCVGFCPEGAMFKHEDYP 101
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
8-163 2.43e-15

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 72.78  E-value: 2.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617      8 DSTLCIGCHTCEAACSET------HRQHGLQSMP--------------RLRVMLNEKESA------PQLCHHCEDAPCAV 61
Cdd:PRK10882  43 DSTLCVGCQACVTKCQEInfpernPQGEQTWDNPdklspytnniikvwKSGTGVNKDQEEngyayiKKQCMHCVDPNCVS 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     62 VCPVNAITR--VDGAVQLNESLCVSCKLCGIACPFGAIEFSGSRPLdipanantpkappappaparvstlldwvPGIrai 139
Cdd:PRK10882 123 VCPVSALTKdpKTGIVHYDKDVCTGCRYCMVACPFNVPKYDYNNPF----------------------------GAI--- 171

                        170       180       190
                 ....*....|....*....|....*....|.
gi 882617    140 aVKCDLCS-------FDEQGPACVRMCPTKA 163
Cdd:PRK10882 172 -HKCELCNqkgverlDKGGLPGCVEVCPTGA 201
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 4-181 1.99e-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: 68.12  E-value: 1.99e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     4 FVIaDSTLCIGCHTCEAAC------------SETHRQHGLQSM-----PRLRVMLNEKESAPQLCHHCEDAPCAVVCPVN 66
Cdd:cd10552   1 LVI-DVAKCNGCYNCFLACkdehvgndwpgyAAPQPRHGHFWMrilrrERGQYPKVDVAYLPVPCNHCDNAPCIKAAKDG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    67 AIT-RVDGAVQLNESLCVSCKLCGIACPFGAIEFsgSRPLDIPAnantpkappappaparvstlldwvpgiraiavKCDL 145
Cdd:cd10552  80 AVYkRDDGIVIIDPEKAKGQKQLVDACPYGAIYW--NEELQVPQ--------------------------------KCTF 125

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 882617   146 CSF----DEQGPACVRMCPTKALHLVDNTDIARVSKRKRE 181
Cdd:cd10552 126 CAHllddGWKEPRCVQACPTGALRFGKLEDEEMAAKAAEE 165
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 3-99 1.85e-13

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: 64.22  E-value: 1.85e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     3 RFVIADSTLCIGCHTCEAACSETHRQHGLQSMPRLRVMLN---EKESAPQLCHHCEDAPCAVVCPVNAIT-RVDGAVQLN 78
Cdd:cd16370   2 RLRVKDMERCIGCYSCMLACSRRVHKSASLSKSAIRVRTRgglEGGFTVVVCRACEDPPCAEACPTGALEpRKGGGVVLD 81

                        90       100
                ....*....|....*....|.
gi 882617    79 ESLCVSCKLCGIACPFGAIEF 99
Cdd:cd16370  82 KEKCIGCGNCVKACIVGAIFW 102
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
12-96 1.24e-11

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 61.81  E-value: 1.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     12 CIGCHTCEAACS---ETHRQHGLQSMPRLRVMLNEKESA-----PQLCHHCEDAPCAVVCPVNA-ITRVDGAVQLNESLC 82
Cdd:PRK14993  53 CIGCQSCTVSCTienQTPQGAFRTTVNQYQVQREGSQEVtnvllPRLCNHCDNPPCVPVCPVQAtFQREDGIVVVDNKRC 132

                         90
                 ....*....|....
gi 882617     83 VSCKLCGIACPFGA 96
Cdd:PRK14993 133 VGCAYCVQACPYDA 146
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
12-97 1.99e-11

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 61.97  E-value: 1.99e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    12 CIGCHTCEAACSETHRQHGLQSMPRLRVMLNEKESAPQLCHHCEdaPCAVVCPVNAITRVDGAVQLNESLCVSCKLCGIA 91
Cdd:COG4624  54 CCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCY--PCVRACPVKAIKVDDGKAEIDEEKCISCGQCVAV 131


                ....*.
gi 882617    92 CPFGAI 97
Cdd:COG4624 132 CPFGAI 137
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 48-168 3.08e-11

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: 57.64  E-value: 3.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617      48 PQLCHHCEDAPCAVVCPVNAITR--VDGAVQLNESLCVSCKLCGIACPFGAIEFsgsrpldipanantpkappappapar 125
Cdd:pfam13247   7 PEQCRHCLNPPCKASCPVGAIYKdeETGAVLLDEKTCRGWRECVSACPYNIPRY-------------------------- 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 882617     126 vstllDWVPGIraiAVKCDLC-SFDEQG--PACVRMCPTKALHLVD 168
Cdd:pfam13247  61 -----NDETGK---AEKCDMCyDRVEAGllPACVQTCPTGAMNFGD 98
PRK09898 PRK09898
ferredoxin-like protein;
5-172 1.28e-09

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 55.61  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617      5 VIADSTLCIGCHTCEAACSETHRQHGLQSMPRLRVMLN----------------EKESAPQLCHHCEDAPCAVVCPVNAI 68
Cdd:PRK09898  61 LVTQRARCTGCHRCEISCTNFNDGSVGTFFSRIKIHRNyffgdngvgsggglygDLNYTADTCRQCKEPQCMNVCPIGAI 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     69 T--RVDGAVQLNESLCVSCKLCGIACPFGAiefsgsrpldipANANTPKAPpappaparvstlldwvpgiraiAVKCDLC 146
Cdd:PRK09898 141 TwqQKEGCITVDHKRCIGCSACTTACPWMM------------ATVNTESKK----------------------SSKCVLC 186

                        170       180
                 ....*....|....*....|....*.
gi 882617    147 SfdeqgpACVRMCPTKALHLVDNTDI 172
Cdd:PRK09898 187 G------ECANACPTGALKIIEWKDI 206
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 48-163 1.46e-08

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


Pssm-ID: 319890 [Multi-domain]  Cd Length: 200  Bit Score: 52.42  E-value: 1.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    48 PQLCHHCEDAPCAVVCPVNAIT-RVDGAVQLNESLCVSCKLCGIACPFGaiefsgsrpldIPAnantpkappappAPARV 126
Cdd:cd16368  88 PRRCMHCDNPPCAKLCPFGAARkTPEGAVYIDDDLCFGGAKCRDVCPWH-----------IPQ------------RQAGV 144

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 882617   127 STLLDWVPGIRAIAV--KCDLCS---FDEQGPACVRMCPTKA 163
Cdd:cd16368 145 GIYLHLAPEYAGGGVmyKCDLCKdllAQGKPPACIEACPKGA 186
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 48-104 1.62e-08

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 49.66  E-value: 1.62e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 882617    48 PQLCHHCEDapCAVVCPVNAITRVDGAVQLNESLCVSCKLCGIACPFGAIEFSGSRP 104
Cdd:COG4231  21 EDKCTGCGA--CVKVCPADAIEEGDGKAVIDPDLCIGCGSCVQVCPVDAIKLEKRVP 75
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 48-99 2.48e-08

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 48.96  E-value: 2.48e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 882617    48 PQLCHHCEDapCAVVCPVNAITRVDG-AVQLNESLCVSCKLCGIACPFGAIEF 99
Cdd:COG1149  10 EEKCIGCGL--CVEVCPEGAIKLDDGgAPVVDPDLCTGCGACVGVCPTGAITL 60
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
48-99 3.03e-08

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 48.96  E-value: 3.03e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 882617    48 PQLCHHCEDapCAVVCPVNAITRVDGAVQLNESLCVSCKLCGIACPFGAIEF 99
Cdd:COG2768  10 EEKCIGCGA--CVKVCPVGAISIEDGKAVIDPEKCIGCGACIEVCPVGAIKI 59
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 1-100 5.74e-08

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 49.70  E-value: 5.74e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     1 MNRFVIADSTLCIGCHTCEAACS----ETHRQHGLQSMPRLRVMLNEKesapqLCHHCEDapCAVVCPVNAITRVDGA-V 75
Cdd:cd10549  31 IARGPEIDEDKCVFCGACVEVCPtgaiELTPEGKEYVPKEKEAEIDEE-----KCIGCGL--CVKVCPVDAITLEDELeI 103

                        90       100
                ....*....|....*....|....*
gi 882617    76 QLNESLCVSCKLCGIACPFGAIEFS 100
Cdd:cd10549 104 VIDKEKCIGCGICAEVCPVNAIKLV 128
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 48-172 1.69e-07

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 48.16  E-value: 1.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    48 PQLCHHCedAPCAVVCPVNAITRVDG-----AVQLNESLCVSCKLCGIACPFGAIEFSGSRPLDIPAnantpkappappa 122
Cdd:cd10549   5 PEKCIGC--GICVKACPTDAIELGPNgaiarGPEIDEDKCVFCGACVEVCPTGAIELTPEGKEYVPK------------- 69

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 882617   123 paRVSTLLDwvpgiraiAVKCDLCSfdeqgpACVRMCPTKALHLVDNTDI 172
Cdd:cd10549  70 --EKEAEID--------EEKCIGCG------LCVKVCPVDAITLEDELEI 103
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 48-165 3.04e-07

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: 49.61  E-value: 3.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    48 PQLCHHCEDAPCAVVCPVNAITR--VDGAVQLNESLCVSCKLCGIACPFGAIEFsgsrpldipanaNTpkappappapar 125
Cdd:cd10555 130 PRICNHCTNPACLAACPRKAIYKreEDGIVLVDQDRCRGYRYCVEACPYKKIYF------------NP------------ 185

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 882617   126 vstlldwvpgIRAIAVKCDLCsFD--EQG--PACVRMCPTKALH 165
Cdd:cd10555 186 ----------VEQKSEKCIFC-YPriEKGvaPACARQCVGRIRF 218
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 59-98 6.46e-07

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 45.04  E-value: 6.46e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 882617    59 CAVVCPVNAITRVDGAVQLNESLCVSCKLCGIACPFGAIE 98
Cdd:COG2221  23 CVAVCPTGAISLDDGKLVIDEEKCIGCGACIRVCPTGAIK 62
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
48-101 7.68e-07

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 48.70  E-value: 7.68e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 882617    48 PQLCHHCEdaPCAVVCPVNAITRVDGAV-QLNESLCVSCKLCGIACPFGAIEFSG 101
Cdd:COG1148 495 PEKCTGCG--RCVEVCPYGAISIDEKGVaEVNPALCKGCGTCAAACPSGAISLKG 547
NapF COG1145
Ferredoxin [Energy production and conversion];
48-99 1.82e-06

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 47.02  E-value: 1.82e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 882617    48 PQLCHHCEdaPCAVVCPVNAITRVDGAVQL--NESLCVSCKLCGIACPFGAIEF 99
Cdd:COG1145 181 AEKCIGCG--LCVKVCPTGAIRLKDGKPQIvvDPDKCIGCGACVKVCPVGAISL 232
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 8-182 2.38e-06

tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit of Tungsten-containing formate dehydrogenase (W-FDH), a member of the DMSO reductase family. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.


Pssm-ID: 319881 [Multi-domain]  Cd Length: 200  Bit Score: 46.27  E-value: 2.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     8 DSTLCIGCHTCEAACSETHRQHGLQSM--------PRL------RVMLNEKESA---------PQLCHHCEDAPCAVVCP 64
Cdd:cd10559   5 DTTRCTACRGCQVACKQWNQLPAEQTKntgshqnpPDLsantykLVRFNEVRNEngkpdwlffPDQCRHCVTPPCKDAAD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    65 V--NAITRVD--GAVQLNESLCVSC-KLCGIACPFgaiefsgsrplDIP-ANANTPKAppappaparvstlldwvpgira 138
Cdd:cd10559  85 MvpGAVIQDEatGAVVFTEKTAELDfDDVLSACPY-----------NIPrKNEATGRI---------------------- 131

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 882617   139 iaVKCDLCsFDE----QGPACVRMCPTKALHLVDNTDI-ARVSKRKREL 182
Cdd:cd10559 132 --VKCDMC-IDRvsngLQPACVKACPTGAMNFGDRDEMlAMASKRLEEL 177
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 12-101 2.69e-06

beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several DMSO reductase superfamily, including nitrate reductase A, ethylbenzene dehydrogenase and selenate reductase. DMSO Reductase (DMSOR) family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. . The beta subunits of DMSOR contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system. Nitrate reductase A contains three subunits (the catalytic subunit NarG, the catalytic subunit NarH with four [Fe-S] clusters, and integral membrane subunit NarI) and often forms a respiratory chain with the formate dehydrogenase via the lipid soluble quinol pool. Ethylbenzene dehydrogenase oxidizes the hydrocarbon ethylbenzene to (S)-1-phenylethanol. Selenate reductase catalyzes reduction of selenate to selenite in bacterial species that can obtain energy by respiring anaerobically with selenate as the terminal electron acceptor.


Pssm-ID: 319887 [Multi-domain]  Cd Length: 201  Bit Score: 46.04  E-value: 2.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    12 CIGCHTCEAACSE--THRQhGLQSMPRLRVMLNEKESAPQ---------------------LCHHCEDAPCAVVCPVNAI 68
Cdd:cd16365  12 CIGCQTCTVACKNawTYRK-GQEYMWWNNVETKPGGGYPQdwevktidnggntrfffylqrLCNHCTNPACLAACPRGAI 90

                        90       100       110
                ....*....|....*....|....*....|....*
gi 882617    69 TRV--DGAVQLNESLCVSCKLCGIACPFGAIEFSG 101
Cdd:cd16365  91 YKReeDGIVLIDQKRCRGYRKCVEQCPYKKIYFNG 125
flavo_MJ0208 TIGR02700
archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of ...
 51-97 3.93e-06

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


Pssm-ID: 131747 [Multi-domain]  Cd Length: 234  Bit Score: 46.02  E-value: 3.93e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 882617      51 CHHCEDapCAVVCPVNAITRVDGAVQLNESLCVSCKLCGIACPFGAI 97
Cdd:TIGR02700 150 CKGCGI--CVDACPRSAIDMVDGKAFIRLLKCVGCGKCKEACPYNAI 194
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 48-100 4.68e-06

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: 42.81  E-value: 4.68e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 882617    48 PQLCHHCEDapCAVVCPVNAITRVDG----AVQLNESLCVSCKLCGIACPFGAIEFS 100
Cdd:COG1143   1 EDKCIGCGL--CVRVCPVDAITIEDGepgkVYVIDPDKCIGCGLCVEVCPTGAISMT 55
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 48-106 6.92e-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: 6.92e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 882617    48 PQLCHHCEDapCAVVCPVNAITRVDG---AVQLNESLCVSCKLCGIACPFGAIEFSGSRPLD 106
Cdd:COG1146   7 TDKCIGCGA--CVEVCPVDVLELDEEgkkALVINPEECIGCGACELVCPVGAITVEDDEPEE 66
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 48-98 7.60e-06

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: 45.55  E-value: 7.60e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 882617    48 PQLCHHcedaPCAVVCPVN-----AIT--RVDGAVQLNESLCVSCKLCGIACPFGAIE 98
Cdd:COG1245  14 PKKCNY----ECIKYCPVNrtgkeAIEidEDDGKPVISEELCIGCGICVKKCPFDAIS 67
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 51-98 2.40e-05

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


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 41.19  E-value: 2.40e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 882617    51 CHHCedAPCAVVCPVNAITRVDGA-VQLNESLCVSCKLCGIACPFGAIE 98
Cdd:COG1144  32 CIGC--GLCWIVCPDGAIRVDDGKyYGIDYDYCKGCGICAEVCPVKAIE 78
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 48-94 5.42e-05

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: 42.83  E-value: 5.42e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 882617    48 PQLCHHCEDAPCAVVCPVNAITR--VDGAVQLNESLCVSCKLCGIACPF 94
Cdd:cd10556 138 PRICNHCTYPACLAACPRKAIYKreEDGIVLIDQERCRGYRECVEACPY 186
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
2-98 5.65e-05

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 42.61  E-value: 5.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617      2 NRFVIADSTLCIGCHTCEAACSethrQHGLQSMP---RLRVMLNEKESAPQLCHHCEDA-----PCAVVCPVNAITRVDG 73
Cdd:PRK07118 160 NGLPVVDEDKCTGCGACVKACP----RNVIELIPksaRVFVACNSKDKGKAVKKVCEVGcigcgKCVKACPAGAITMENN 235

                         90       100
                 ....*....|....*....|....*
gi 882617     74 AVQLNESLCVSCKLCGIACPFGAIE 98
Cdd:PRK07118 236 LAVIDQEKCTSCGKCVEKCPTKAIR 260
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 47-99 7.70e-05

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: 41.99  E-value: 7.70e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 882617    47 APQLCHHCEDapCAVVCPVNAITRVDGAVQLNESLCVSCKLCGIACPFGAIEF 99
Cdd:cd03110  62 DQEKCIRCGN--CERVCKFGAILEFFQKLIVDESLCEGCGACVIICPRGAIYL 112
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
59-99 1.09e-04

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 41.84  E-value: 1.09e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 882617     59 CAVVCPVNAITRVDGAVQLNESLCVSCKLCGIACPFGAIEF 99
Cdd:PRK07118 147 CVAACPFDAIHIENGLPVVDEDKCTGCGACVKACPRNVIEL 187
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
48-98 1.59e-04

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 41.72  E-value: 1.59e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 882617     48 PQLCHHcedaPCAVVCPVN-----AIT--RVDGAVQLNESLCVSCKLCGIACPFGAIE 98
Cdd:PRK13409  14 PKKCNY----ECIKYCPVVrtgeeTIEidEDDGKPVISEELCIGCGICVKKCPFDAIS 67
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 11-98 2.31e-04

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 39.93  E-value: 2.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    11 LCIGCHTCEAACSE-----THRQHGLQSM--PRlrvmLNEKESApqlCHHCEDApCAVVCPVNAITRVD--------GAV 75
Cdd:cd16373  15 LCIRCGLCVEACPTgviqpAGLEDGLEGGrtPY----LDPREGP---CDLCCDA-CVEVCPTGALRPLDleeqkvkmGVA 86

                        90       100
                ....*....|....*....|....*....
gi 882617    76 QLNESLCVS------CKLCGIACPFGAIE 98
Cdd:cd16373  87 VIDKDRCLAwqggtdCGVCVEACPTEAIA 115
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 51-96 4.55e-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: 36.74  E-value: 4.55e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 882617      51 CHHCEDapCAVVCPVNAITRVD-------GAVQLNESLCVSCKLCGIACPFGA 96
Cdd:pfam12838   1 CIGCGA--CVAACPVGAITLDEvgekkgtKTVVIDPERCVGCGACVAVCPTGA 51
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 50-98 6.14e-04

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 39.86  E-value: 6.14e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 882617     50 LCHHCEDapCAVVCPVNAITRVD--GAVQLNESLCVSCKLCGIACPFGAIE 98
Cdd:PRK12771 511 NCFECDN--CYGACPQDAIIKLGpgRRYHFDYDKCTGCHICADVCPCGAIE 559
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 48-99 6.77e-04

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: 39.65  E-value: 6.77e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 882617    48 PQLCHHCEDAPCAVVCPVNAITR--VDGAVQLNESLCVSCKLCGIACPFGAIEF 99
Cdd:cd10557 176 PRICNHCLNPACVAACPSGAIYKreEDGIVLIDQDRCRGWRMCVSACPYKKVYY 229
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 8-69 2.33e-03

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 35.47  E-value: 2.33e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 882617     8 DSTLCIGCHTCEAACSEthrqHGLQSMPRLRVMLNekesaPQLCHHCEDapCAVVCPVNAIT 69
Cdd:COG1149   9 DEEKCIGCGLCVEVCPE----GAIKLDDGGAPVVD-----PDLCTGCGA--CVGVCPTGAIT 59
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
51-171 2.93e-03

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 37.70  E-value: 2.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    51 CHHCEDAPCAVVCPVNAITRVDGAVQLNESLCVSCKLCGIACPFGAIEFSGSRpldipanantpkappappaparvstll 130
Cdd:COG4624  62 CRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCYPCVRACPVKAIKVDDGK--------------------------- 114

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 882617   131 dwvpgIRAIAVKCDLCsfdeqGpACVRMCPTKALHLVDNTD 171
Cdd:COG4624 115 -----AEIDEEKCISC-----G-QCVAVCPFGAITEKSDIE 144
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 64-169 3.11e-03

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 36.35  E-value: 3.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617     64 PVNAITRVDGAVQLNESLCVSCKLCGIACPFGAIEFsgsrpldipanantpkappappaparvstlldwVPGIRAIAVKC 143
Cdd:PRK08348  26 PVPVPEDFRGKILYDVDKCVGCRMCVTVCPAGVFVY---------------------------------LPEIRKVALWT 72

                         90       100
                 ....*....|....*....|....*.
gi 882617    144 DLCSFDEQgpaCVRMCPTKALHLVDN 169
Cdd:PRK08348  73 GRCVFCGQ---CVDVCPTGALQMSDD 95
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
 48-100 3.38e-03

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 36.93  E-value: 3.38e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 882617     48 PQLCHHCedAPCAVVCPVNAIT------RVDGAVQLNESLCVSCKLCGIACPFGAIEFS 100
Cdd:PRK12387  37 PQQCIGC--AACVNACPSNALTvetdlaTGELAWEFNLGRCIFCGRCEEVCPTAAIKLS 93
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
76-99 4.30e-03

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 37.53  E-value: 4.30e-03
                        10        20
                ....*....|....*....|....
gi 882617    76 QLNESLCVSCKLCGIACPFGAIEF 99
Cdd:COG1148 492 EVDPEKCTGCGRCVEVCPYGAISI 515
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 8-72 5.01e-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: 36.59  E-value: 5.01e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 882617     8 DSTLCIGCHTCEAACsethRQHGLQSMPrlrvmlNEKESAPQLCHHCedAPCAVVCPVNAITRVD 72
Cdd:cd03110  62 DQEKCIRCGNCERVC----KFGAILEFF------QKLIVDESLCEGC--GACVIICPRGAIYLKD 114
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
59-97 5.37e-03

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 36.01  E-value: 5.37e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 882617     59 CAVVCPVNAIT-----RVDG-----AVQLNESLCVSCKLCGIACPFGAI 97
Cdd:PRK05888  66 CAAICPADAITieaaeREDGrrrttRYDINFGRCIFCGFCEEACPTDAI 114
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 11-99 6.26e-03

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


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 35.68  E-value: 6.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882617    11 LCIGCHTCEAACSETHRQHGLQSMPRLRVMLNEkesapqlCHHCEDapCAVVCPVNAITRVDGA-----VQLNESlC--- 82
Cdd:cd10564  14 LCTRCGDCVEACPEGIIVRGDGGFPELDFSRGE-------CTFCGA--CAEACPEGALDPAREApwplrAEIGDS-Clal 83

                        90
                ....*....|....*....
gi 882617    83 --VSCKLCGIACPFGAIEF 99
Cdd:cd10564  84 qgVECRSCQDACPTQAIRF 102
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
51-100 6.60e-03

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 36.58  E-value: 6.60e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 882617    51 CHHCEDapCAVVCPVNAITRvDGAVQLNEslCVSCKLCGIACPFGAIEFS 100
Cdd:COG0348 212 CIDCGL--CVKVCPMGIDIR-KGEINQSE--CINCGRCIDACPKDAIRFS 256
RDH TIGR02486
reductive dehalogenase; This model represents a family of corrin and 8-iron Fe-S ...
 82-112 7.61e-03

reductive dehalogenase; This model represents a family of corrin and 8-iron Fe-S cluster-containing reductive dehalogenases found primarily in halorespiring microorganisms such as dehalococcoides ethenogenes which contains as many as 17 enzymes of this type with varying substrate ranges. One example of a characterized species is the tetrachloroethene reductive dehalogenase (1.97.1.8) which also acts on trichloroethene converting it to dichloroethene.


Pssm-ID: 274158  Cd Length: 314  Bit Score: 36.26  E-value: 7.61e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 882617      82 CVSCKLCGIACPFGAIEFSGSRPLDIPANAN 112
Cdd:TIGR02486 207 CETCGKCADECPSGAISKGGEPTWDPEDSNG 237
PRK13795 PRK13795
hypothetical protein; Provisional
 59-93 9.04e-03

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 36.51  E-value: 9.04e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 882617     59 CAVVCPVNAITRVDG--AVQLNESLCVSCKLCGIACP 93
Cdd:PRK13795 589 CVGACPTGAIRIEEGkrKISVDEEKCIHCGKCTEVCP 625
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH