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Conserved domains on  [gi|1248065340|ref|WP_096569281|]
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MULTISPECIES: ferredoxin-type protein NapG [Campylobacter]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
napG super family cl35838
quinol dehydrogenase periplasmic component; Provisional
 1-246 6.44e-135

quinol dehydrogenase periplasmic component; Provisional


The actual alignment was detected with superfamily member PRK09476:

Pssm-ID: 236534 [Multi-domain]  Cd Length: 254  Bit Score: 379.74  E-value: 6.44e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340   1 MKDRREFFASAFKGLCLCTAGGFLANLSLKADDDY--ALRPPGAEDEARFLSKCIRCGLCVKACPYNTLKLATLLDGAKN 78
Cdd:PRK09476    8 QNGRRRFLRDVVRTAGGLAAVGVALGLQQQQARASgvALRPPGALNENDFLSACIRCGLCVQACPYDTLKLATLASGLSA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  79 GTPFFKAREIPCYLCKDIPCIKECPTDALDKKHLEqgIESLKMGIAI-VDSASCVAHWGIQCDACYRACPLIDRALKLEL 157
Cdd:PRK09476   88 GTPYFVARDIPCEMCEDIPCVKACPSGALDRELVD--IDDARMGLAVlVDQENCLNFQGLRCDVCYRVCPLIDKAITLEL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340 158 KRNERTAKHAFLLPSVDHEVCVGCGLCELACITEKPAIHVLPREYVLGKAGSHYVKGWDQEDEDRIKDADTSKYFDAKKA 237
Cdd:PRK09476  166 ERNERTGKHAFFLPTVHSDACTGCGKCEKACVLEKAAIKVLPRSLAKGKLGHHYRKGWLEKDEGRSSNAGEIKKLDTKKA 245


                  ....*....
gi 1248065340 238 TNYLNEGEF 246
Cdd:PRK09476  246 EDYLNSGEL 254
 
Name Accession Description Interval E-value
napG PRK09476
quinol dehydrogenase periplasmic component; Provisional
 1-246 6.44e-135

quinol dehydrogenase periplasmic component; Provisional


Pssm-ID: 236534 [Multi-domain]  Cd Length: 254  Bit Score: 379.74  E-value: 6.44e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340   1 MKDRREFFASAFKGLCLCTAGGFLANLSLKADDDY--ALRPPGAEDEARFLSKCIRCGLCVKACPYNTLKLATLLDGAKN 78
Cdd:PRK09476    8 QNGRRRFLRDVVRTAGGLAAVGVALGLQQQQARASgvALRPPGALNENDFLSACIRCGLCVQACPYDTLKLATLASGLSA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  79 GTPFFKAREIPCYLCKDIPCIKECPTDALDKKHLEqgIESLKMGIAI-VDSASCVAHWGIQCDACYRACPLIDRALKLEL 157
Cdd:PRK09476   88 GTPYFVARDIPCEMCEDIPCVKACPSGALDRELVD--IDDARMGLAVlVDQENCLNFQGLRCDVCYRVCPLIDKAITLEL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340 158 KRNERTAKHAFLLPSVDHEVCVGCGLCELACITEKPAIHVLPREYVLGKAGSHYVKGWDQEDEDRIKDADTSKYFDAKKA 237
Cdd:PRK09476  166 ERNERTGKHAFFLPTVHSDACTGCGKCEKACVLEKAAIKVLPRSLAKGKLGHHYRKGWLEKDEGRSSNAGEIKKLDTKKA 245


                  ....*....
gi 1248065340 238 TNYLNEGEF 246
Cdd:PRK09476  246 EDYLNSGEL 254
mauM_napG TIGR00397
MauM/NapG family ferredoxin-type protein; MauM is involved in methylamine utilization. NapG is ...
 3-212 3.62e-57

MauM/NapG family ferredoxin-type protein; MauM is involved in methylamine utilization. NapG is associated with nitrate reductase activity. The two proteins are highly similar. [Energy metabolism, Electron transport]


Pssm-ID: 129492 [Multi-domain]  Cd Length: 213  Bit Score: 181.27  E-value: 3.62e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340   3 DRREFFASAFKGLCLCTAGGFLANLSLK---ADDDYALRPPGAEDEARFLSKCIRCGLCVKACPYNTLKLATLLDGAKNG 79
Cdd:TIGR00397   3 ERRDAFADAARAVGVACVGGFFGAALLRsrpAVAARVLRPPGALPEQDFLAACVRCGLCVEACPYDILSLASWSDPAPLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  80 TPFFKAREIPCYLCKDIPCIKECPTDALDKkhLEQGIESLKMGIAI-VDSASCVAHWGIQCDACYRACPLIDRALKLELK 158
Cdd:TIGR00397  83 TPFFTPREVPCRMCKDIPCARACPTGALDP--LLTDIRKADMGVAVlVGHETCLNYKGLNCSICVRVCPIRGEAISLKPI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1248065340 159 RNERtakHAFLLPSVDHEVCVGCGLCELACITEKPAIHVLPREYVLGKAGSHYV 212
Cdd:TIGR00397 161 ENER---GRLQIPTVDSAKCTGCGTCEKHCVLSEAAIRVLPRELGLGVPGANSA 211
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 37-199 1.47e-55

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: 175.14  E-value: 1.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  37 LRPPGAEDEARFLSKCIRCGLCVKACPYNTLKLATLLDGAKNG-TPFFKAREIPCYLCKDIpCIKECPTDALDkkHLEQG 115
Cdd:cd16373     1 LRPPGALDEEEFLALCIRCGLCVEACPTGVIQPAGLEDGLEGGrTPYLDPREGPCDLCCDA-CVEVCPTGALR--PLDLE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340 116 IESLKMGIAIVDSASCVAHWG-IQCDACYRACPLIDRALKLElkrnertakHAFLLPSVDHEVCVGCGLCELACITEKP- 193
Cdd:cd16373    78 EQKVKMGVAVIDKDRCLAWQGgTDCGVCVEACPTEAIAIVLE---------DDVLRPVVDEDKCVGCGLCEYVCPVEPPk 148


                  ....*.
gi 1248065340 194 AIHVLP 199
Cdd:cd16373   149 AIVVEP 154
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 50-108 1.21e-05

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 42.00  E-value: 1.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1248065340  50 SKCIRCGLCVKACPYNTLKLatlldgAKNGTPFFKAREIPCYLCKdiPCIKECPTDALD 108
Cdd:COG1146     8 DKCIGCGACVEVCPVDVLEL------DEEGKKALVINPEECIGCG--ACELVCPVGAIT 58
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 52-106 5.05e-05

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 39.82  E-value: 5.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1248065340  52 CIRCGLCVKACPYNTLKLATLLDGAKNGTPFFKAREipCYLCKDipCIKECPTDA 106
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKKGTKTVVIDPER--CVGCGA--CVAVCPTGA 51
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 50-117 1.10e-03

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: 39.07  E-value: 1.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1248065340  50 SKCIRCGLCVKACPYNTLKLatlldgaKNGTPFFKAReipCYLCkdIPCIKECPTDALDKKHLEQGIE 117
Cdd:NF038196  185 DKCIGCGICAKVCPVNNIEM-------EDGKPVWGHN---CTHC--LACIHRCPKEAIEYGKKTKKKG 240
 
Name Accession Description Interval E-value
napG PRK09476
quinol dehydrogenase periplasmic component; Provisional
 1-246 6.44e-135

quinol dehydrogenase periplasmic component; Provisional


Pssm-ID: 236534 [Multi-domain]  Cd Length: 254  Bit Score: 379.74  E-value: 6.44e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340   1 MKDRREFFASAFKGLCLCTAGGFLANLSLKADDDY--ALRPPGAEDEARFLSKCIRCGLCVKACPYNTLKLATLLDGAKN 78
Cdd:PRK09476    8 QNGRRRFLRDVVRTAGGLAAVGVALGLQQQQARASgvALRPPGALNENDFLSACIRCGLCVQACPYDTLKLATLASGLSA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  79 GTPFFKAREIPCYLCKDIPCIKECPTDALDKKHLEqgIESLKMGIAI-VDSASCVAHWGIQCDACYRACPLIDRALKLEL 157
Cdd:PRK09476   88 GTPYFVARDIPCEMCEDIPCVKACPSGALDRELVD--IDDARMGLAVlVDQENCLNFQGLRCDVCYRVCPLIDKAITLEL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340 158 KRNERTAKHAFLLPSVDHEVCVGCGLCELACITEKPAIHVLPREYVLGKAGSHYVKGWDQEDEDRIKDADTSKYFDAKKA 237
Cdd:PRK09476  166 ERNERTGKHAFFLPTVHSDACTGCGKCEKACVLEKAAIKVLPRSLAKGKLGHHYRKGWLEKDEGRSSNAGEIKKLDTKKA 245


                  ....*....
gi 1248065340 238 TNYLNEGEF 246
Cdd:PRK09476  246 EDYLNSGEL 254
mauM_napG TIGR00397
MauM/NapG family ferredoxin-type protein; MauM is involved in methylamine utilization. NapG is ...
 3-212 3.62e-57

MauM/NapG family ferredoxin-type protein; MauM is involved in methylamine utilization. NapG is associated with nitrate reductase activity. The two proteins are highly similar. [Energy metabolism, Electron transport]


Pssm-ID: 129492 [Multi-domain]  Cd Length: 213  Bit Score: 181.27  E-value: 3.62e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340   3 DRREFFASAFKGLCLCTAGGFLANLSLK---ADDDYALRPPGAEDEARFLSKCIRCGLCVKACPYNTLKLATLLDGAKNG 79
Cdd:TIGR00397   3 ERRDAFADAARAVGVACVGGFFGAALLRsrpAVAARVLRPPGALPEQDFLAACVRCGLCVEACPYDILSLASWSDPAPLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  80 TPFFKAREIPCYLCKDIPCIKECPTDALDKkhLEQGIESLKMGIAI-VDSASCVAHWGIQCDACYRACPLIDRALKLELK 158
Cdd:TIGR00397  83 TPFFTPREVPCRMCKDIPCARACPTGALDP--LLTDIRKADMGVAVlVGHETCLNYKGLNCSICVRVCPIRGEAISLKPI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1248065340 159 RNERtakHAFLLPSVDHEVCVGCGLCELACITEKPAIHVLPREYVLGKAGSHYV 212
Cdd:TIGR00397 161 ENER---GRLQIPTVDSAKCTGCGTCEKHCVLSEAAIRVLPRELGLGVPGANSA 211
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 37-199 1.47e-55

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: 175.14  E-value: 1.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  37 LRPPGAEDEARFLSKCIRCGLCVKACPYNTLKLATLLDGAKNG-TPFFKAREIPCYLCKDIpCIKECPTDALDkkHLEQG 115
Cdd:cd16373     1 LRPPGALDEEEFLALCIRCGLCVEACPTGVIQPAGLEDGLEGGrTPYLDPREGPCDLCCDA-CVEVCPTGALR--PLDLE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340 116 IESLKMGIAIVDSASCVAHWG-IQCDACYRACPLIDRALKLElkrnertakHAFLLPSVDHEVCVGCGLCELACITEKP- 193
Cdd:cd16373    78 EQKVKMGVAVIDKDRCLAWQGgTDCGVCVEACPTEAIAIVLE---------DDVLRPVVDEDKCVGCGLCEYVCPVEPPk 148


                  ....*.
gi 1248065340 194 AIHVLP 199
Cdd:cd16373   149 AIVVEP 154
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 38-188 2.06e-18

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: 78.82  E-value: 2.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  38 RPPGAEDEARFLSKCIRCGLCVKACPYNTLKlatLLDGaknGTPFFKAREIPCYLCKDipCIKECPTDALDKKHLEQgie 117
Cdd:cd10564     1 RPPWAVDEALFLDLCTRCGDCVEACPEGIIV---RGDG---GFPELDFSRGECTFCGA--CAEACPEGALDPAREAP--- 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1248065340 118 slkMGIAIVDSASCVAHWGIQCDACYRACPliDRALKLELKRNERTakhaflLPSVDHEVCVGCGLCELAC 188
Cdd:cd10564    70 ---WPLRAEIGDSCLALQGVECRSCQDACP--TQAIRFRPRLGGIA------LPELDADACTGCGACVSVC 129
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 51-188 3.50e-14

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: 67.04  E-value: 3.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  51 KCIRCGLCVKACPYNTLKLATLLDGAKNGTPFFKAreipCYLCKDipCIKECPTDALDKKHLEQGIESLKMGIaIVDSAS 130
Cdd:cd10549     7 KCIGCGICVKACPTDAIELGPNGAIARGPEIDEDK----CVFCGA--CVEVCPTGAIELTPEGKEYVPKEKEA-EIDEEK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1248065340 131 CvahwgIQCDACYRACPLidRALKLELKrnertakhafLLPSVDHEVCVGCGLCELAC 188
Cdd:cd10549    80 C-----IGCGLCVKVCPV--DAITLEDE----------LEIVIDKEKCIGCGICAEVC 120
PRK10194 PRK10194
ferredoxin-type protein NapF;
37-188 6.10e-11

ferredoxin-type protein NapF;


Pssm-ID: 182296 [Multi-domain]  Cd Length: 163  Bit Score: 59.27  E-value: 6.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  37 LRPPGAEDEARFLSKCIRCGLCVKACPYNTLKLATlldgakNGTPFFKAREIPCYLCKDipCIKECPTDALDKKHLEQGI 116
Cdd:PRK10194   21 IRPPWSGDESHFLTHCTRCDACINACENNILQRGA------GGYPSVNFKNNECSFCYA--CAQACPESLFSPRHTRAWD 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1248065340 117 ESLKMGIAivdsasCVAHWGIQCDACYRACPLIDRALKLELKrnertakhAFLLPSVDHEVCVGCGLCELAC 188
Cdd:PRK10194   93 LQFTIGDA------CLAYQSVECRRCQDSCEPMAIIFRPTLS--------GIYQPQLNSQLCNGCGACAASC 150
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 48-147 8.12e-11

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: 58.17  E-value: 8.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  48 FLSKCIRCGLCVKACPY-NTLKLATLLDGAK---NGTPFFKAREIPCYLCKDIPCIKECPTDALDKKhleqgieslKMGI 123
Cdd:cd04410     4 DLDRCIGCGTCEVACKQeHGLRPGPDWSRIKvieGGGLERAFLPVSCMHCEDPPCVKACPTGAIYKD---------EDGI 74

                          90       100
                  ....*....|....*....|....
gi 1248065340 124 AIVDSASCVAhwgiqCDACYRACP 147
Cdd:cd04410    75 VLIDEDKCIG-----CGSCVEACP 93
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 49-147 7.10e-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: 7.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  49 LSKCIRCGLCVKACPYNTLKLATLLDGAKNGTPFFKAREIPCYLCKDipCIKECPTDAldkkhleqgIESLKMGIAIVDS 128
Cdd:cd10549    39 EDKCVFCGACVEVCPTGAIELTPEGKEYVPKEKEAEIDEEKCIGCGL--CVKVCPVDA---------ITLEDELEIVIDK 107

                          90
                  ....*....|....*....
gi 1248065340 129 ASCvahwgIQCDACYRACP 147
Cdd:cd10549   108 EKC-----IGCGICAEVCP 121
napF TIGR00402
ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of ...
 37-126 5.31e-07

ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of the periplasmic nitrate reductase system, as in Escherichia coli. NapF interacts with the catalytic subunit, NapA, and may be an accessory protein for NapA maturation. [Energy metabolism, Electron transport]


Pssm-ID: 273060 [Multi-domain]  Cd Length: 101  Bit Score: 46.86  E-value: 5.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  37 LRPPGAEDEARFLSKCIRCGLCVKACPYNTLKLatlldgAKNGTPFFKAREIPCYLCKdiPCIKECPTDALDKKHleQGI 116
Cdd:TIGR00402  21 IRPPWSARESLFSAVCTRCGECASACENNILQL------GQQGQPTVEFDNAECDFCG--KCAEACPTNAFHPRF--PGD 90

                          90
                  ....*....|
gi 1248065340 117 ESLKMGIAIV 126
Cdd:TIGR00402  91 WLLRPQISSA 100
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 51-107 1.07e-05

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 45.89  E-value: 1.07e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1248065340  51 KCIRCGLCVKACPYNTLKLATLLDGAKNgtpfFKAREIPCYLCKDIP----CIKECPTDAL 107
Cdd:PRK12769   86 KCIGCKSCVVACPFGTMQIVLTPVAAGK----VKATAHKCDLCAGREngpaCVENCPADAL 142
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 50-147 1.10e-05

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: 43.89  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  50 SKCIRCGLCVKACPYNT--------LKLATLLDGAKNGTPFFKAREIPCYLCKDIPCIKECPTDALDKKHleqgieslKM 121
Cdd:cd10553    10 KRCIGCLACEVHCKVKNnlpvgprlCRIFAVGPKMVGGKPRLKFVYMSCFHCENPWCVKACPTGAMQKRE--------KD 81

                          90       100
                  ....*....|....*....|....*.
gi 1248065340 122 GIAIVDSASCVAhwgiqCDACYRACP 147
Cdd:cd10553    82 GIVYVDQELCIG-----CKACIEACP 102
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 50-108 1.21e-05

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 42.00  E-value: 1.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1248065340  50 SKCIRCGLCVKACPYNTLKLatlldgAKNGTPFFKAREIPCYLCKdiPCIKECPTDALD 108
Cdd:COG1146     8 DKCIGCGACVEVCPVDVLEL------DEEGKKALVINPEECIGCG--ACELVCPVGAIT 58
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 51-108 1.56e-05

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: 43.33  E-value: 1.56e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1248065340  51 KCIRCGLCVKACPYNTLKLATLLDGAkngtpfFKareipCYLCKDIP-CIKECPTDALD 108
Cdd:cd10550    81 KCIGCGMCVEACPFGAIRVDPETGKA------IK-----CDLCGGDPaCVKVCPTGALE 128
PRK09898 PRK09898
ferredoxin-like protein;
90-201 2.84e-05

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 43.67  E-value: 2.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  90 CYLCKDIPCIKECPTDALDKKHleqgieslKMGIAIVDSASCvahwgIQCDACYRACPLIDRALKLELKRNERtakhafl 169
Cdd:PRK09898  123 CRQCKEPQCMNVCPIGAITWQQ--------KEGCITVDHKRC-----IGCSACTTACPWMMATVNTESKKSSK------- 182

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1248065340 170 lpsvdhevCVGCGLCELACITEkpAIHVLPRE 201
Cdd:PRK09898  183 --------CVLCGECANACPTG--ALKIIEWK 204
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 51-107 3.71e-05

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: 42.63  E-value: 3.71e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1248065340  51 KCIRCGLCVKACPYNTLKLATLLDGAKNGTPFFKAREIPCYLC---KDIP-CIKECPTDAL 107
Cdd:cd10554    86 RCIGCKLCVLACPFGAIEMAPTTVPGVDWERGPRAVAVKCDLCagrEGGPaCVEACPTKAL 146
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 52-106 5.05e-05

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 39.82  E-value: 5.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1248065340  52 CIRCGLCVKACPYNTLKLATLLDGAKNGTPFFKAREipCYLCKDipCIKECPTDA 106
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKKGTKTVVIDPER--CVGCGA--CVAVCPTGA 51
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 49-147 5.96e-05

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: 41.91  E-value: 5.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  49 LSKCIRCGLCVKACpyntlklATLLDGAK----NGTPFFKArEIP--CYLCKDIPCIKECPTDALdkkHLEQGIEslkmg 122
Cdd:cd16367    18 LDRCIRCDNCEKAC-------ADTHDGHSrldrNGLRFGNL-LVPtaCRHCVDPVCMIGCPTGAI---HRDDGGE----- 81

                          90       100
                  ....*....|....*....|....*
gi 1248065340 123 IAIVDsascvahWGIQCDACYRACP 147
Cdd:cd16367    82 VVISD-------ACCGCGNCASACP 99
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 50-120 6.16e-05

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: 42.76  E-value: 6.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  50 SKCIRCGLCVKACPYNTLKLATLldgakngtpffKAREIPCYLCKD-------IPCIKECPTDALD-------KKHLEQG 115
Cdd:cd10558   101 DKCIGCGYCIKGCPFDIPRISKD-----------DNKMYKCTLCSDrvsvglePACVKTCPTGALHfgtkedmLALAEKR 169


                  ....*
gi 1248065340 116 IESLK 120
Cdd:cd10558   170 VAALK 174
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
50-107 1.03e-04

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 41.18  E-value: 1.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1248065340  50 SKCIRCGLCVKACPYNTLKLATLLDgakngtpffKAREIPCYLCKDIP----CIKECPTDAL 107
Cdd:COG1142    81 EKCIGCGLCVLACPFGAITMVGEKS---------RAVAVKCDLCGGREggpaCVEACPTGAL 133
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 137-202 1.37e-04

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 38.96  E-value: 1.37e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1248065340 137 IQCDACYRACPliDRALKLELKRNERTakhafllPSVDHEVCVGCGLCELACITEkpAIHVLPREY 202
Cdd:COG1143     5 IGCGLCVRVCP--VDAITIEDGEPGKV-------YVIDPDKCIGCGLCVEVCPTG--AISMTPFEL 59
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 49-147 1.42e-04

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 41.47  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  49 LSKCIRCGLCVKAC----------PYNTLKLATLLDGAKNGTPFFKareIPCYLCKDIPCIKECPTDALDKKhleqgies 118
Cdd:COG0437    12 LTKCIGCRACVVACkeennlpvgvTWRRVRRYEEGEFPNVEWLFVP---VLCNHCDDPPCVKVCPTGATYKR-------- 80

                          90       100
                  ....*....|....*....|....*....
gi 1248065340 119 lKMGIAIVDSASCVAhwgiqCDACYRACP 147
Cdd:COG0437    81 -EDGIVLVDYDKCIG-----CRYCVAACP 103
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 51-107 1.57e-04

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: 40.48  E-value: 1.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1248065340  51 KCIRCGLCVKACPYNTLKLAT--LLDGAKNGTPFF--KAREIPCYLCKDIpcikeCPTDAL 107
Cdd:TIGR01971  44 KCIGCTLCAAVCPADAIRVVPaeGEDGKRRLKFYEinFGRCIFCGLCEEA-----CPTDAI 99
NapF COG1145
Ferredoxin [Energy production and conversion];
50-113 2.15e-04

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 41.63  E-value: 2.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1248065340  50 SKCIRCGLCVKACPYNTLKLatlldgaKNGTPFFKAREIPCYLCKDipCIKECPTDALDKKHLE 113
Cdd:COG1145   182 EKCIGCGLCVKVCPTGAIRL-------KDGKPQIVVDPDKCIGCGA--CVKVCPVGAISLEPKE 236
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
50-147 2.82e-04

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 40.03  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  50 SKCIRCGLCVKACPYNTLKLATLLDGAKNGTPFFKAREIP--CYLCKDIPCIKECPTDALDKKHleqgieslkmGIAIVD 127
Cdd:COG1142    10 EKCIGCRTCEAACAVAHEGEEGEPFLPRIRVVRKAGVSAPvqCRHCEDAPCAEVCPVGAITRDD----------GAVVVD 79

                          90       100
                  ....*....|....*....|
gi 1248065340 128 SASCVAhwgiqCDACYRACP 147
Cdd:COG1142    80 EEKCIG-----CGLCVLACP 94
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 50-115 3.10e-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: 38.17  E-value: 3.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1248065340  50 SKCIRCGLCVKACPYNTLKLatlldgAKNGTPFFkaREIPCYLCKDipCIKECPTDALDKKHLEQG 115
Cdd:COG1149    11 EKCIGCGLCVEVCPEGAIKL------DDGGAPVV--DPDLCTGCGA--CVGVCPTGAITLEEREAG 66
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 120-201 3.14e-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: 38.17  E-value: 3.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340 120 KMGIAIVDSASCvahwgIQCDACYRACPLidRALKLELKRNertakhafllPSVDHEVCVGCGLCELACITEkpAIHVLP 199
Cdd:COG1149     2 KRKIPVIDEEKC-----IGCGLCVEVCPE--GAIKLDDGGA----------PVVDPDLCTGCGACVGVCPTG--AITLEE 62


                  ..
gi 1248065340 200 RE 201
Cdd:COG1149    63 RE 64
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
51-147 3.63e-04

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 41.16  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  51 KCIRCGLCVKACPYNTLKLATLLDGAKNGTPFFKAREIPCYlckdiPCIKECPTDALDKKHleqgieslkmGIAIVDSAS 130
Cdd:COG4624    57 CCCCCCRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCY-----PCVRACPVKAIKVDD----------GKAEIDEEK 121

                          90
                  ....*....|....*..
gi 1248065340 131 CvahwgIQCDACYRACP 147
Cdd:COG4624   122 C-----ISCGQCVAVCP 133
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 90-147 3.80e-04

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: 39.98  E-value: 3.80e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1248065340  90 CYLCKDIPCIKECPTDALDKkhleqgiesLKMGIAIVDSASCVAhwgiqCDACYRACP 147
Cdd:cd10562    70 CMHCTDAACVKVCPTGALYK---------TENGAVVVDEDKCIG-----CGYCVAACP 113
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 51-113 4.71e-04

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 37.42  E-value: 4.71e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1248065340  51 KCIRCGLCVKACPYNTLKLatlldGAKNGTPFFKAREIPCYLCKDipCIKECPTDALDKKHLE 113
Cdd:COG1143     3 KCIGCGLCVRVCPVDAITI-----EDGEPGKVYVIDPDKCIGCGL--CVEVCPTGAISMTPFE 58
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
51-107 5.39e-04

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 39.48  E-value: 5.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1248065340  51 KCIRCGLCVKACPYN--TLKLATLLDGAKNGTPF---FkAREIPCYLCKDIpcikeCPTDAL 107
Cdd:PRK05888   59 RCIACKLCAAICPADaiTIEAAEREDGRRRTTRYdinF-GRCIFCGFCEEA-----CPTDAI 114
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 17-175 6.54e-04

Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 40.45  E-value: 6.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  17 LCTAGGFLANLSLKADDDYALRPPGAEDEARFLSKCIRCGLCVKACPYNtlklatLLDGAKNGTPFFKAREIpcylckdi 96
Cdd:COG0247    45 IGLLNPGVELLGDGDLHDKNLKTLPWKELLDALDACVGCGFCRAMCPSY------KATGDEKDSPRGRINLL-------- 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  97 pcikecptdaldKKHLEqGIESLKMGIAIVDSA-SCVAhwgiqCDACYRACP-------LIDRALKLELKRNERTAKHAF 168
Cdd:COG0247   111 ------------REVLE-GELPLDLSEEVYEVLdLCLT-----CKACETACPsgvdiadLIAEARAQLVERGGRPLRDRL 172


                  ....*..
gi 1248065340 169 LLPSVDH 175
Cdd:COG0247   173 LRTFPDR 179
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 51-107 8.78e-04

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: 38.82  E-value: 8.78e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1248065340  51 KCIRCGLCVKACPYNTLKLATLLDGAKNgtpffkareipCYLCKD------IP-CIKECPTDAL 107
Cdd:cd10562   101 KCIGCGYCVAACPFDVPRYDETTNKITK-----------CTLCFDriengmQPaCVKTCPTGAL 153
PRK13795 PRK13795
hypothetical protein; Provisional
 50-103 1.06e-03

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 39.98  E-value: 1.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1248065340  50 SKCIRCGLCVKACPYNTLKLatlldgaKNGTPFFKAREIPCYLCKDipCIKECP 103
Cdd:PRK13795  581 AECVGCGVCVGACPTGAIRI-------EEGKRKISVDEEKCIHCGK--CTEVCP 625
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 50-117 1.10e-03

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: 39.07  E-value: 1.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1248065340  50 SKCIRCGLCVKACPYNTLKLatlldgaKNGTPFFKAReipCYLCkdIPCIKECPTDALDKKHLEQGIE 117
Cdd:NF038196  185 DKCIGCGICAKVCPVNNIEM-------EDGKPVWGHN---CTHC--LACIHRCPKEAIEYGKKTKKKG 240
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 82-147 1.49e-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: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 37.56  E-value: 1.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1248065340  82 FFKAREIP--CYLCKDIPCIKECPTDALDKkhleqgieSLKMGIAIVDSASCvahwgIQCDACYRACP 147
Cdd:cd10550    39 EPEGLDVPvvCRQCEDAPCVEACPVGAISR--------DEETGAVVVDEDKC-----IGCGMCVEACP 93
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
90-196 1.83e-03

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 39.24  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  90 CYLCKDIPCIKECPTDALDKKHleqgieslkmGIAIVDSASCvahwgIQCDACYRACPLidralkLELKRNERTAKhafl 169
Cdd:COG4624    62 CRCCVAISCIQVRGIIIIDKRG----------PSIIRDKEKC-----KNCYPCVRACPV------KAIKVDDGKAE---- 116

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1248065340 170 lpsVDHEVCVGCGLCELAC----ITEKPAIH 196
Cdd:COG4624   117 ---IDEEKCISCGQCVAVCpfgaITEKSDIE 144
NapF COG1145
Ferredoxin [Energy production and conversion];
1-201 2.10e-03

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 38.55  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340   1 MKDRREFFASAFKGLCLCTAGGFLANLSLKADDDYALRPPGAEDEARFLSKCIRCGLCVKACPYNTLKLATLLDGAKNGT 80
Cdd:COG1145    52 GILAKEAFDALKDVLGILGAIVIGIGAGEIVRVGIAAADLNLKAVALVLLLALAVAGAAKRLIISAVKLVAGLVVAAGEV 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  81 PFFKAREIPCY--LCKDIPCIKECPTDALDKKHLEQGIESLKMGIAIVDSASCvahwgIQCDACYRACPLidRALKLELK 158
Cdd:COG1145   132 LLVIAAALAEAglAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKC-----IGCGLCVKVCPT--GAIRLKDG 204

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1248065340 159 RNErtakhafllPSVDHEVCVGCGLCELACITEkpAIHVLPRE 201
Cdd:COG1145   205 KPQ---------IVVDPDKCIGCGACVKVCPVG--AISLEPKE 236
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
48-111 2.23e-03

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 38.69  E-value: 2.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1248065340  48 FLSKCIRCGLCVKACPYntlklatlldGAKNGTPFFKAREIP--CYLCKDipCIKECPTDALDKKH 111
Cdd:COG1148   494 DPEKCTGCGRCVEVCPY----------GAISIDEKGVAEVNPalCKGCGT--CAAACPSGAISLKG 547
ACS_1 cd01916
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
 137-197 3.22e-03

Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.


Pssm-ID: 238897 [Multi-domain]  Cd Length: 731  Bit Score: 38.54  E-value: 3.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1248065340 137 IQCDACYRACP---LIDRALKLelkrnertAKHAFLLPSVD-HEVCVGCGLCELACITEKPAIHV 197
Cdd:cd01916   368 TDCGWCTRACPnslRIKEAMEA--------AKEGDFSGLADlFDQCVGCGRCEQECPKEIPIINM 424
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
50-147 3.50e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 37.99  E-value: 3.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  50 SKCIRCGLCVKACPYNTLKLATllDGAK---------NGTPFFKAREIPCYLCKdiPCIKECPTDALdkkhleqgieSLK 120
Cdd:PRK07118  168 DKCTGCGACVKACPRNVIELIP--KSARvfvacnskdKGKAVKKVCEVGCIGCG--KCVKACPAGAI----------TME 233

                          90       100
                  ....*....|....*....|....*..
gi 1248065340 121 MGIAIVDSASCVAhwgiqCDACYRACP 147
Cdd:PRK07118  234 NNLAVIDQEKCTS-----CGKCVEKCP 255
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 137-196 4.20e-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: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 36.40  E-value: 4.20e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1248065340 137 IQCD--ACYRACPLidRALKLELKRNERTakhafllpsVDHEVCVGCGLCELACITEKPAIH 196
Cdd:cd10550    50 RQCEdaPCVEACPV--GAISRDEETGAVV---------VDEDKCIGCGMCVEACPFGAIRVD 100
PRK08222 PRK08222
hydrogenase 4 subunit H; Validated
 50-107 4.89e-03

hydrogenase 4 subunit H; Validated


Pssm-ID: 181301 [Multi-domain]  Cd Length: 181  Bit Score: 37.04  E-value: 4.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1248065340  50 SKCIRCGLCVKACPYNTLKLATLLDGAKNGTPFFKAREIPCYLCKDIpcikeCPTDAL 107
Cdd:PRK08222   38 SQCIACGACTCACPANALTIQTDDQQNSRTWQLYLGRCIYCGRCEEV-----CPTRAI 90
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 88-147 5.00e-03

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 37.80  E-value: 5.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  88 IPCYLCKDIPCIKECPTDALDKKHleqgieslkmgiaivDSASCVAHWGIQCDACYRACP 147
Cdd:PRK12769   54 VTCHHCEDAPCARSCPNGAISHVD---------------DSIQVNQQKCIGCKSCVVACP 98
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 50-107 5.45e-03

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 36.85  E-value: 5.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1248065340  50 SKCIRCGLCVKACPYNTLKLatlldGAKNGTPfFKareipCYLCKD------IP-CIKECPTDAL 107
Cdd:COG0437    90 DKCIGCRYCVAACPYGAPRF-----NPETGVV-EK-----CTFCADrldeglLPaCVEACPTGAL 143
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 51-107 5.77e-03

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: 36.22  E-value: 5.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1248065340  51 KCIRCGLCVKACPYNTLKLatlldGAKNGTPFfkareiPCYLCKD------IP-CIKECPTDAL 107
Cdd:cd16366   101 TCIGCGYCVNACPFDIPRF-----DEETGRVA------KCTLCYDrisnglQPaCVKTCPTGAL 153
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
50-107 6.17e-03

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 36.96  E-value: 6.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1248065340  50 SKCIRCGLCVKACPYntlklatlldGAKNGTPFFKAREipCYLCKDipCIKECPTDAL 107
Cdd:COG0348   210 GDCIDCGLCVKVCPM----------GIDIRKGEINQSE--CINCGR--CIDACPKDAI 253
PsaC COG5703
Photosystem I reaction center iron-sulfur center subunit VII, PsaC [Energy production and ...
 52-107 7.55e-03

Photosystem I reaction center iron-sulfur center subunit VII, PsaC [Energy production and conversion]; Photosystem I reaction center iron-sulfur center subunit VII, PsaC is part of the Pathway/BioSystem: Photosystem I


Pssm-ID: 444413 [Multi-domain]  Cd Length: 82  Bit Score: 34.80  E-value: 7.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1248065340  52 CIRCGLCVKACPYNTLKLATLLDGAKNGTPFFkAREIPCYLCkdIPCIKECPTDAL 107
Cdd:COG5703    11 CIGCTQCVRACPTDVLEMVPWDGCKAGQIAAS-PRTEDCVGC--KRCETACPTDFL 63
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 125-188 8.28e-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: 34.64  E-value: 8.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1248065340 125 IVDSASCvahwgIQCDACYRACPliDRALKLELKRNertakhafllPSVDHEVCVGCGLCELAC 188
Cdd:COG1144    26 VVDEDKC-----IGCGLCWIVCP--DGAIRVDDGKY----------YGIDYDYCKGCGICAEVC 72
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
123-191 9.10e-03

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 36.85  E-value: 9.10e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1248065340 123 IAIVDSASCvahwgIQCDACYRACPliD---RALKLELKRNERtakhafllPSVDHEVCVGCGLCELACITE 191
Cdd:PRK08318  336 YARIDQDKC-----IGCGRCYIACE--DtshQAIEWDEDGTRT--------PEVIEEECVGCNLCAHVCPVE 392
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 51-111 9.49e-03

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 33.87  E-value: 9.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1248065340  51 KCIRCGLCVKACPYNTLKLatlldgaKNGTPFFKAREipCYLCKDipCIKECPTDALDKKH 111
Cdd:COG2221    16 KCIGCGLCVAVCPTGAISL-------DDGKLVIDEEK--CIGCGA--CIRVCPTGAIKGEK 65
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 122-201 9.53e-03

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 33.91  E-value: 9.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340 122 GIAIVDSASCvahwgIQCDACYRACPliDRALKLELKRNERTAKHAfllpsvdhEVCVGCGLCELACITEkpAIHVLPRE 201
Cdd:COG1146     1 MMPVIDTDKC-----IGCGACVEVCP--VDVLELDEEGKKALVINP--------EECIGCGACELVCPVG--AITVEDDE 63
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 50-147 9.78e-03

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: 35.31  E-value: 9.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248065340  50 SKCIRCGLCVKAC-----PYNTLKLATLLDG---------AKNGTPFfkarEIPCYLCKDIPCIKECPTDALDKkhleqg 115
Cdd:cd10563     7 EKCLGCKLCEVACavahsKSKDLIKAKLEKErprprirveESGGRSF----PLQCRHCDEPPCVKACMSGAMHK------ 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1248065340 116 ieSLKMGIAIVDSASCVAHWgiqcdACYRACP 147
Cdd:cd10563    77 --DPETGIVIHDEEKCVGCW-----MCVMVCP 101
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
50-71 9.99e-03

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 36.58  E-value: 9.99e-03
                          10        20
                  ....*....|....*....|..
gi 1248065340  50 SKCIRCGLCVKACPYNTLKLAT 71
Cdd:COG0348   236 SECINCGRCIDACPKDAIRFSS 257
 
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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