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Conserved domains on  [gi|15831591|ref|NP_310364|]
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electron transport complex subunit B [Escherichia coli O157:H7 str. Sakai]

Protein Classification

electron transport complex subunit RsxB( domain architecture ID 11480380)

electron transport complex subunit RsxB is required to maintain the reduced state of SoxR; probably transfers electron from NAD(P)H to SoxR

EC:  7.-.-.-
Gene Ontology:  GO:0046872|GO:0009055|GO:0051539

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05113 PRK05113
electron transport complex protein RnfB; Provisional
 1-192 5.87e-133

electron transport complex protein RnfB; Provisional


:

Pssm-ID: 235347 [Multi-domain]  Cd Length: 191  Bit Score: 370.04  E-value: 5.87e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591    1 MNAIWIAVAAVSLLGLAFGAILGYASRRFAVEDDPVVEKIDEILPQSQCGQCGYPGCRPYAEAIScNGEKINRCAPGGEA 80
Cdd:PRK05113   1 MSAIWIAVAALSLLALVFGAILGFASRRFKVEGDPIVEKIDAILPQSQCGQCGYPGCRPYAEAIA-NGEKINKCPPGGEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591   81 VMLKIAELLNVEPQPLDGEAQELTPARMVAVIDENNCIGCTKCIQACPVDAIVGATRAMHTVMSDLCTGCNLCVDPCPTH 160
Cdd:PRK05113  80 TMLKLAELLGVEPQPLDGEAQEATPARKVAFIDEDNCIGCTKCIQACPVDAIVGATKAMHTVISDLCTGCDLCVAPCPTD 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 15831591  161 CISLQPVAETPDSWKWDLNTIPVRIIPVEHHA 192
Cdd:PRK05113 160 CIEMIPVAETPDNWKWDLNTIPVRIIPVEQHA 191
 
Name Accession Description Interval E-value
PRK05113 PRK05113
electron transport complex protein RnfB; Provisional
 1-192 5.87e-133

electron transport complex protein RnfB; Provisional


Pssm-ID: 235347 [Multi-domain]  Cd Length: 191  Bit Score: 370.04  E-value: 5.87e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591    1 MNAIWIAVAAVSLLGLAFGAILGYASRRFAVEDDPVVEKIDEILPQSQCGQCGYPGCRPYAEAIScNGEKINRCAPGGEA 80
Cdd:PRK05113   1 MSAIWIAVAALSLLALVFGAILGFASRRFKVEGDPIVEKIDAILPQSQCGQCGYPGCRPYAEAIA-NGEKINKCPPGGEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591   81 VMLKIAELLNVEPQPLDGEAQELTPARMVAVIDENNCIGCTKCIQACPVDAIVGATRAMHTVMSDLCTGCNLCVDPCPTH 160
Cdd:PRK05113  80 TMLKLAELLGVEPQPLDGEAQEATPARKVAFIDEDNCIGCTKCIQACPVDAIVGATKAMHTVISDLCTGCDLCVAPCPTD 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 15831591  161 CISLQPVAETPDSWKWDLNTIPVRIIPVEHHA 192
Cdd:PRK05113 160 CIEMIPVAETPDNWKWDLNTIPVRIIPVEQHA 191
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 3-167 1.41e-89

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


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 259.34  E-value: 1.41e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591     3 AIWIAVAAVSLLGLAFGAILGYASRRFAVEDDPVVEKIDEILPQSQCGQCGYPGCRPYAEAISCnGEKINRCAPGGEAVM 82
Cdd:TIGR01944   1 MIIAAVAALSALGLALGAILGYAARRFPVEADPIVEEIDALLPQTQCGQCGYPGCRPYAEAIAE-GEAINKCPPGGEAVI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591    83 LKIAELLNVEP--QPLDGEAQELTPaRMVAVIDENNCIGCTKCIQACPVDAIVGATRAMHTVMSDLCTGCNLCVDPCPTH 160
Cdd:TIGR01944  80 LALAELLGVEPipQPLDADAGTIQP-PMVALIDEDNCIGCTKCIQACPVDAIVGAAKAMHTVIADECTGCDLCVEPCPTD 158


                  ....*..
gi 15831591   161 CISLQPV 167
Cdd:TIGR01944 159 CIEMIPV 165
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 1-177 4.05e-81

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


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 241.44  E-value: 4.05e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591   1 MNAIWIAVAAVSLLGLAFGAILGYASRRFAVEDDPVVEKIDEILPQSQCGQCGYPGCRPYAEAISCNGEKINRCAPGGEA 80
Cdd:COG2878   1 MSTILIAVLVLGGLGLVFGLILGYASKKFKVEEDPRVEEIDALLPGANCGQCGYPGCRPYAEAIAEGEAPINLCPPGGAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591  81 VMLKIAELLNVEPQPLDGEAQEL-------TPARM----------VAVI-----DENNCIGCTKCIQACPVDAIVGATRA 138
Cdd:COG2878  81 VAEKLAELLGVEAGPLDPEVAVVrcnggceKAKPKyeydgikdcrAAVIggpkgCEYGCIGCGDCIKACPFDAIVGAAKG 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 15831591 139 MHTVMSDLCTGCNLCVDPCPTHCISLQPVAETP--DSWKWD 177
Cdd:COG2878 161 MHTVDEDKCTGCGLCVEACPVDCIEMVPVSPTVvvSSWDKG 201
Fer4_21 pfam14697
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 110-164 2.77e-18

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


Pssm-ID: 434137 [Multi-domain]  Cd Length: 59  Bit Score: 74.62  E-value: 2.77e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15831591   110 AVIDENNCIGCTKCIQACP---VDAIVGATRAMHTVMSDLCTGCNLCVDPCPTH-CISL 164
Cdd:pfam14697   1 ARIDEDTCIGCGKCYIACPdtsHQAIVGDGKRHHTVIEDECTGCNLCVSVCPVDdCITM 59
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 96-165 1.10e-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: 67.42  E-value: 1.10e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591  96 LDGEAQELTPARMVAVIDENNCIGCTKCIQACPVDAIVGATRAMHTVMSDLCTGCNLCVDPCPTHCISLQ 165
Cdd:cd10549  59 LTPEGKEYVPKEKEAEIDEEKCIGCGLCVKVCPVDAITLEDELEIVIDKEKCIGCGICAEVCPVNAIKLV 128
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 115-162 2.51e-04

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


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 40.61  E-value: 2.51e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 15831591  115 NNCIGCTKCIQACPVDAIVGATRamHTVMSDLCTGCNLCVDPCPTHCI 162
Cdd:NF038196 185 DKCIGCGICAKVCPVNNIEMEDG--KPVWGHNCTHCLACIHRCPKEAI 230
 
Name Accession Description Interval E-value
PRK05113 PRK05113
electron transport complex protein RnfB; Provisional
 1-192 5.87e-133

electron transport complex protein RnfB; Provisional


Pssm-ID: 235347 [Multi-domain]  Cd Length: 191  Bit Score: 370.04  E-value: 5.87e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591    1 MNAIWIAVAAVSLLGLAFGAILGYASRRFAVEDDPVVEKIDEILPQSQCGQCGYPGCRPYAEAIScNGEKINRCAPGGEA 80
Cdd:PRK05113   1 MSAIWIAVAALSLLALVFGAILGFASRRFKVEGDPIVEKIDAILPQSQCGQCGYPGCRPYAEAIA-NGEKINKCPPGGEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591   81 VMLKIAELLNVEPQPLDGEAQELTPARMVAVIDENNCIGCTKCIQACPVDAIVGATRAMHTVMSDLCTGCNLCVDPCPTH 160
Cdd:PRK05113  80 TMLKLAELLGVEPQPLDGEAQEATPARKVAFIDEDNCIGCTKCIQACPVDAIVGATKAMHTVISDLCTGCDLCVAPCPTD 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 15831591  161 CISLQPVAETPDSWKWDLNTIPVRIIPVEHHA 192
Cdd:PRK05113 160 CIEMIPVAETPDNWKWDLNTIPVRIIPVEQHA 191
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 3-167 1.41e-89

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


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 259.34  E-value: 1.41e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591     3 AIWIAVAAVSLLGLAFGAILGYASRRFAVEDDPVVEKIDEILPQSQCGQCGYPGCRPYAEAISCnGEKINRCAPGGEAVM 82
Cdd:TIGR01944   1 MIIAAVAALSALGLALGAILGYAARRFPVEADPIVEEIDALLPQTQCGQCGYPGCRPYAEAIAE-GEAINKCPPGGEAVI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591    83 LKIAELLNVEP--QPLDGEAQELTPaRMVAVIDENNCIGCTKCIQACPVDAIVGATRAMHTVMSDLCTGCNLCVDPCPTH 160
Cdd:TIGR01944  80 LALAELLGVEPipQPLDADAGTIQP-PMVALIDEDNCIGCTKCIQACPVDAIVGAAKAMHTVIADECTGCDLCVEPCPTD 158


                  ....*..
gi 15831591   161 CISLQPV 167
Cdd:TIGR01944 159 CIEMIPV 165
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 1-177 4.05e-81

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


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 241.44  E-value: 4.05e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591   1 MNAIWIAVAAVSLLGLAFGAILGYASRRFAVEDDPVVEKIDEILPQSQCGQCGYPGCRPYAEAISCNGEKINRCAPGGEA 80
Cdd:COG2878   1 MSTILIAVLVLGGLGLVFGLILGYASKKFKVEEDPRVEEIDALLPGANCGQCGYPGCRPYAEAIAEGEAPINLCPPGGAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591  81 VMLKIAELLNVEPQPLDGEAQEL-------TPARM----------VAVI-----DENNCIGCTKCIQACPVDAIVGATRA 138
Cdd:COG2878  81 VAEKLAELLGVEAGPLDPEVAVVrcnggceKAKPKyeydgikdcrAAVIggpkgCEYGCIGCGDCIKACPFDAIVGAAKG 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 15831591 139 MHTVMSDLCTGCNLCVDPCPTHCISLQPVAETP--DSWKWD 177
Cdd:COG2878 161 MHTVDEDKCTGCGLCVEACPVDCIEMVPVSPTVvvSSWDKG 201
PRK06991 PRK06991
electron transport complex subunit RsxB;
37-174 3.50e-60

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 188.46  E-value: 3.50e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591   37 VEKIDEILPQSQCGQCGYPGCRPYAEAISCNGEKINRCAPGGEAVMLKIAELLNVEPQPLDGEAQELTPaRMVAVIDENN 116
Cdd:PRK06991   8 ADRIEDLLPQTQCTKCGYDGCRPYAEAIAAGEANYNRCPPGGAEGIARLAALLGKPVIPLDPANGVERP-RAVAVIDEQL 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15831591  117 CIGCTKCIQACPVDAIVGATRAMHTVMSDLCTGCNLCVDPCPTHCISLQPVAETPDSW 174
Cdd:PRK06991  87 CIGCTLCMQACPVDAIVGAPKQMHTVLADLCTGCDLCVPPCPVDCIDMVPVTGERTGW 144
PRK08764 PRK08764
Rnf electron transport complex subunit RnfB;
35-165 2.76e-47

Rnf electron transport complex subunit RnfB;


Pssm-ID: 181550 [Multi-domain]  Cd Length: 135  Bit Score: 151.23  E-value: 2.76e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591   35 PVVEKIDEILPQSQCGQCGYPGCRPYAEAISCNGEKINRCAPGGEAVMLKIAELLNVEPQPLDGEAQELTPARmVAVIDE 114
Cdd:PRK08764   6 TLVERLDRLLPQTQCGQCGFDGCRPYAQAMARGEATIDRCPPGGDAGARALAQVLGVPARPYDRSRGTHKLPQ-VAWIVE 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15831591  115 NNCIGCTKCIQACPVDAIVGATRAMHTVMSDLCTGCNLCVDPCPTHCISLQ 165
Cdd:PRK08764  85 ADCIGCTKCIQACPVDAIVGGAKHMHTVIAPLCTGCELCVPACPVDCIELH 135
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
1-169 5.29e-36

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 126.97  E-value: 5.29e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591    1 MNAIWIAVAAVSLLGLAFGAILGYASRRFAVEDDPVVEKIDEILPQSQCGQCGYPGCRPYAEAISCNGEKINRCAPGGEA 80
Cdd:PRK07118   1 MNMILFAVLSLGALGLVFGILLAFASKKFAVEEDPRVEAVREVLPGANCGGCGYPGCDGYAEAVVNGDAPPNLCPVGGAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591   81 VMLKIAELLNVEPQPldgeaqeltPARMVAVI----DENN-----------------------------CIGCTKCIQAC 127
Cdd:PRK07118  81 VAEKVAEILGKEAAE---------SEPKVAVVrcqgTCDKakeryeyqgikdcaaaallfggpkgcsygCLGLGSCVAAC 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 15831591  128 PVDAIVGATRAMHtVMSDLCTGCNLCVDPCPTHCISLQPVAE 169
Cdd:PRK07118 152 PFDAIHIENGLPV-VDEDKCTGCGACVKACPRNVIELIPKSA 192
Fer4_21 pfam14697
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 110-164 2.77e-18

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


Pssm-ID: 434137 [Multi-domain]  Cd Length: 59  Bit Score: 74.62  E-value: 2.77e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15831591   110 AVIDENNCIGCTKCIQACP---VDAIVGATRAMHTVMSDLCTGCNLCVDPCPTH-CISL 164
Cdd:pfam14697   1 ARIDEDTCIGCGKCYIACPdtsHQAIVGDGKRHHTVIEDECTGCNLCVSVCPVDdCITM 59
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 96-165 1.10e-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: 67.42  E-value: 1.10e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591  96 LDGEAQELTPARMVAVIDENNCIGCTKCIQACPVDAIVGATRAMHTVMSDLCTGCNLCVDPCPTHCISLQ 165
Cdd:cd10549  59 LTPEGKEYVPKEKEAEIDEEKCIGCGLCVKVCPVDAITLEDELEIVIDKEKCIGCGICAEVCPVNAIKLV 128
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 106-166 1.42e-14

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 65.13  E-value: 1.42e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831591 106 ARMVAVIDENNCIGCTKCIQACPVDAIVGATRAMHTVMSDLCTGCNLCVDPCPTHCISLQP 166
Cdd:COG1149   2 KRKIPVIDEEKCIGCGLCVEVCPEGAIKLDDGGAPVVDPDLCTGCGACVGVCPTGAITLEE 62
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 108-164 1.16e-13

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 63.14  E-value: 1.16e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15831591 108 MVAVIDENNCIGCTKCIQACPVDAIVGATRaMHTVMSDLCTGCNLCVDPCPTHCISL 164
Cdd:COG4231  15 MRYVIDEDKCTGCGACVKVCPADAIEEGDG-KAVIDPDLCIGCGSCVQVCPVDAIKL 70
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 104-166 3.24e-13

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: 62.38  E-value: 3.24e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831591 104 TPARMVAVIDENNCIGCTKCIQACPVDAIVGATRAMHTVMSDLCTGCNLCVDPCPTHCISLQP 166
Cdd:COG1144  19 GWRVERPVVDEDKCIGCGLCWIVCPDGAIRVDDGKYYGIDYDYCKGCGICAEVCPVKAIEMVP 81
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 108-172 1.55e-11

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 57.41  E-value: 1.55e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831591 108 MVAVIDENNCIGCTKCIQACPVDAIVGATRAMHTVM--SDLCTGCNLCVDPCPTHCISLQPVAETPD 172
Cdd:COG1146   1 MMPVIDTDKCIGCGACVEVCPVDVLELDEEGKKALVinPEECIGCGACELVCPVGAITVEDDEPEEQ 67
NapF COG1145
Ferredoxin [Energy production and conversion];
54-166 7.97e-11

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 59.35  E-value: 7.97e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591  54 YPGCRPYAEAISCNGEKINRCAPGGEAVMLKIAELLNVEPQPLDGEAQELTPARMVAVIDENNCIGCTKCIQACPVDAIV 133
Cdd:COG1145 121 VAGLVVAAGEVLLVIAAALAEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVCPTGAIR 200

                        90       100       110
                ....*....|....*....|....*....|....
gi 15831591 134 -GATRAMHTVMSDLCTGCNLCVDPCPTHCISLQP 166
Cdd:COG1145 201 lKDGKPQIVVDPDKCIGCGACVKVCPVGAISLEP 234
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
99-165 8.87e-11

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 59.87  E-value: 8.87e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831591  99 EAQELTPARMVAVIDENNCIGCTKCIQACPVDAIVGATRAMHTVMSDLCTGCNLCVDPCPTHCISLQ 165
Cdd:COG1148 480 SKGELGVEPSVAEVDPEKCTGCGRCVEVCPYGAISIDEKGVAEVNPALCKGCGTCAAACPSGAISLK 546
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
108-166 1.21e-10

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 55.12  E-value: 1.21e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15831591 108 MVAVIDENNCIGCTKCIQACPVDAIVGaTRAMHTVMSDLCTGCNLCVDPCPTHCISLQP 166
Cdd:COG2768   4 GKPYVDEEKCIGCGACVKVCPVGAISI-EDGKAVIDPEKCIGCGACIEVCPVGAIKIEW 61
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
37-163 2.39e-10

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 58.50  E-value: 2.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591  37 VEKIDEILPQSQCGQCGYPGCRPYAEAISCNGEKINRCAPGGEAVMLKIAELLNVEPQPLDGEAQELTPARMVAVIDENN 116
Cdd:COG4624  13 IEEGDELLLLEEAERVLRIIILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSIIRDKEK 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15831591 117 CIGCTKCIQACPVDAIVGATRAMHtVMSDLCTGCNLCVDPCPTHCIS 163
Cdd:COG4624  93 CKNCYPCVRACPVKAIKVDDGKAE-IDEEKCISCGQCVAVCPFGAIT 138
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 114-166 2.53e-10

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: 53.98  E-value: 2.53e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15831591 114 ENNCIGCTKCIQACPVDAIV---GATRAMHTVMSDLCTGCNLCVDPCPTHCISLQP 166
Cdd:COG1143   1 EDKCIGCGLCVRVCPVDAITiedGEPGKVYVIDPDKCIGCGLCVEVCPTGAISMTP 56
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
109-177 3.67e-10

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 58.03  E-value: 3.67e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15831591  109 VAVIDENNCIGCTKCIQAC------PVDAIVGATRAMHtVMSDLCTGCNLCVDPCPT-HCISLQPVAETPDSWKWD 177
Cdd:PRK08318 336 YARIDQDKCIGCGRCYIACedtshqAIEWDEDGTRTPE-VIEEECVGCNLCAHVCPVeGCITMGEVKFGKPYANWT 410
FeS pfam04060
Putative Fe-S cluster; This family includes a domain with four conserved cysteines that ...
 44-76 1.57e-09

Putative Fe-S cluster; This family includes a domain with four conserved cysteines that probably form an Fe-S redox cluster.


Pssm-ID: 461150 [Multi-domain]  Cd Length: 33  Bit Score: 51.28  E-value: 1.57e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 15831591    44 LPQSQCGQCGYPGCRPYAEAISCNGEKINRCAP 76
Cdd:pfam04060   1 LPGTNCGACGYPGCRAFAEAVVAGEAKINDCPP 33
PRK06214 PRK06214
sulfite reductase subunit alpha;
32-84 3.66e-09

sulfite reductase subunit alpha;


Pssm-ID: 235745 [Multi-domain]  Cd Length: 530  Bit Score: 55.08  E-value: 3.66e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15831591   32 EDDPVVEKIDEILPQSQCGQCGYpGCRPYAEAISCNGEK-INRCAPGGE--AVMLK 84
Cdd:PRK06214  75 EGRPLPRKLMAAMAQQDCGQCGY-NCQDYAEAIASGEEKrLNLCAPGGKetARMLK 129
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 111-163 4.51e-09

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 50.82  E-value: 4.51e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15831591 111 VIDENNCIGCTKCIQACPVDAIVGATRAMHtVMSDLCTGCNLCVDPCPTHCIS 163
Cdd:COG2221  11 KIDEEKCIGCGLCVAVCPTGAISLDDGKLV-IDEEKCIGCGACIRVCPTGAIK 62
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 111-175 1.80e-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: 50.86  E-value: 1.80e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831591 111 VIDENNCIGCTKCIQACPVDAI----VGATRAMHTVMSDLCTGCNLCVDPCPTHCISLQPVAETPDSWK 175
Cdd:cd10549   2 KYDPEKCIGCGICVKACPTDAIelgpNGAIARGPEIDEDKCVFCGACVEVCPTGAIELTPEGKEYVPKE 70
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
112-164 3.27e-08

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 51.99  E-value: 3.27e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15831591 112 IDENNCIGCTKCIQACPVDAIVgatRAMHTVMSDlCTGCNLCVDPCPTHCISL 164
Cdd:COG0348 207 YDRGDCIDCGLCVKVCPMGIDI---RKGEINQSE-CINCGRCIDACPKDAIRF 255
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 111-164 4.14e-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: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 49.88  E-value: 4.14e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15831591 111 VIDENNCIGCTKCIQACPVDAIVGATRAMHTVMSDLCTGCNLCVDPCPTHCISL 164
Cdd:cd10550  76 VVDEDKCIGCGMCVEACPFGAIRVDPETGKAIKCDLCGGDPACVKVCPTGALEF 129
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 96-160 9.47e-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: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 49.18  E-value: 9.47e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831591  96 LDGEAQELTPARM-VAVIDENNCI------GCTKCIQACPVDAIVGATRAMH---TVMSDLCTGCNLCVDPCPTH 160
Cdd:cd16373  71 LRPLDLEEQKVKMgVAVIDKDRCLawqggtDCGVCVEACPTEAIAIVLEDDVlrpVVDEDKCVGCGLCEYVCPVE 145
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 114-179 1.60e-07

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: 48.18  E-value: 1.60e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831591   114 ENNCIGCTKCIQACPVDAI--VGATR-------AMHTVMSDLCTGCNLCVDPCPTHCISLQPVAETPDSWKWDLN 179
Cdd:TIGR01971  42 EEKCIGCTLCAAVCPADAIrvVPAEGedgkrrlKFYEINFGRCIFCGLCEEACPTDAIVLTPEFELATYTRSDLV 116
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 116-166 2.08e-07

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 49.87  E-value: 2.08e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15831591  116 NCIGCTKCIQACPVDAI--VGATRAMHTVMsDLCTGCNLCVDPCPTHCISLQP 166
Cdd:PRK12771 511 NCFECDNCYGACPQDAIikLGPGRRYHFDY-DKCTGCHICADVCPCGAIEMGP 562
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
111-164 2.12e-07

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 48.11  E-value: 2.12e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15831591 111 VIDENNCIGCTKCIQACPVDAIVGATRAMHTVMS--DLCTGCN---LCVDPCPTHCISL 164
Cdd:COG1142  77 VVDEEKCIGCGLCVLACPFGAITMVGEKSRAVAVkcDLCGGREggpACVEACPTGALRL 135
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
109-164 4.91e-07

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 46.48  E-value: 4.91e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15831591  109 VAVIDENNCIGCTKCIQACPVDAIVGATRAMHTVMSDLCTGCNLCVDPCPTHCISL 164
Cdd:PRK09623  45 MPVVDESKCVKCYICWKFCPEPAIYIKEDGYVAIDYDYCKGCGICANECPTKAITM 100
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
117-179 5.14e-07

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 47.57  E-value: 5.14e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831591  117 CIGCTKCIQACPVDAIVgatraMHTVMSD--------------LCTGCNLCVDPCPTHCISLQPVAETPDSWKWDLN 179
Cdd:PRK05888  60 CIACKLCAAICPADAIT-----IEAAEREdgrrrttrydinfgRCIFCGFCEEACPTDAIVETPDFELATETREELI 131
PRK14028 PRK14028
pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional
 111-164 8.37e-07

pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional


Pssm-ID: 172522 [Multi-domain]  Cd Length: 312  Bit Score: 48.07  E-value: 8.37e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15831591  111 VIDENNCIGCTKCIQACPVDAIVGA--------TRAMHTVMSDL----CTGCNLCVDPCPTHCISL 164
Cdd:PRK14028 243 VIDHSKCIMCRKCWLYCPDDAIIEAwreaegprGRKFRMKMIDFdyqyCKGCGVCAEVCPTGAIQM 308
Fer4_9 pfam13187
4Fe-4S dicluster domain;
116-162 9.15e-07

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 44.08  E-value: 9.15e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 15831591   116 NCIGCTKCIQACPVDAIV---GATRAMHTVMSDLCTGCNLCVDPCPTHCI 162
Cdd:pfam13187   1 KCTGCGACVAACPAGAIVpdlVGQTIRGDIAGLACIGCGACVDACPRGAI 50
porD PRK09625
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
 111-164 1.36e-06

pyruvate flavodoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 236596 [Multi-domain]  Cd Length: 133  Bit Score: 45.89  E-value: 1.36e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15831591  111 VIDENNCIGCTKCIQACPVDAIVGATRAMHTVMSDLCTGCNLCVDPCPTHCISL 164
Cdd:PRK09625  55 VHNNEICINCFNCWVYCPDAAILSRDKKLKGVDYSHCKGCGVCVEVCPTNPKSL 108
PRK13795 PRK13795
hypothetical protein; Provisional
 117-158 2.19e-06

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 46.91  E-value: 2.19e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 15831591  117 CIGCTKCIQACPVDAI-VGATRAMHTVMSDLCTGCNLCVDPCP 158
Cdd:PRK13795 583 CVGCGVCVGACPTGAIrIEEGKRKISVDEEKCIHCGKCTEVCP 625
PRK07569 PRK07569
bidirectional hydrogenase complex protein HoxU; Validated
 111-165 2.22e-06

bidirectional hydrogenase complex protein HoxU; Validated


Pssm-ID: 181037 [Multi-domain]  Cd Length: 234  Bit Score: 46.57  E-value: 2.22e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831591  111 VIDENNCIGCTKCIQACpvDAIVGAtramHT-----------VMSDL---------CTGCNLCVDPCPTHCISLQ 165
Cdd:PRK07569 142 GIDHNRCVLCTRCVRVC--DEIEGA----HTwdvagrgaksrVITDLnqpwgtsetCTSCGKCVQACPTGAIFRK 210
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 111-164 2.41e-06

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 45.08  E-value: 2.41e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831591 111 VIDENNCIGCTKCIQACPVDAI-------VGATRAMHTVM-SDLCTGCNLCVDPCPTHCISL 164
Cdd:cd10549  36 EIDEDKCVFCGACVEVCPTGAIeltpegkEYVPKEKEAEIdEEKCIGCGLCVKVCPVDAITL 97
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 97-167 3.27e-06

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


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 45.84  E-value: 3.27e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831591  97 DGEAQELTPARMVAVIDENNCIGCTKCIQACPVDAIvGATRAMHTVMSDLCTGCNLCVDPCPTHCISLQPV 167
Cdd:cd03110  46 EPEEEEDFVGGKKAFIDQEKCIRCGNCERVCKFGAI-LEFFQKLIVDESLCEGCGACVIICPRGAIYLKDR 115
CdhE COG1456
CO dehydrogenase/acetyl-CoA synthase gamma subunit (corrinoid Fe-S protein) [Energy production ...
 40-90 4.66e-06

CO dehydrogenase/acetyl-CoA synthase gamma subunit (corrinoid Fe-S protein) [Energy production and conversion];


Pssm-ID: 441065 [Multi-domain]  Cd Length: 442  Bit Score: 45.78  E-value: 4.66e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 15831591  40 IDEILPQSQCGQCGYPGCRPYAEAISCNGEKINRCAPGGEAVMLKIAELLN 90
Cdd:COG1456   8 IYKLLPKTNCKECGEPTCMAFAMKLAKGKAKLEDCPPLSEEALEKLEEALA 58
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 111-164 1.13e-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: 43.40  E-value: 1.13e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15831591 111 VIDENNCIGCTKCIQACPVDAI---------VGATRAMHTVMS--DLCTGCN---LCVDPCPTHCISL 164
Cdd:cd10554  81 QVDEERCIGCKLCVLACPFGAIemapttvpgVDWERGPRAVAVkcDLCAGREggpACVEACPTKALTL 148
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 111-165 1.40e-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: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 43.03  E-value: 1.40e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15831591 111 VIDENNCIGCTKCIQACPVDAIVGATRAMHTVMsdlCTGCNLCVDPCPTHCISLQ 165
Cdd:cd16370  79 VLDKEKCIGCGNCVKACIVGAIFWDEETNKPII---CIHCGYCARYCPHDVLAME 130
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 109-162 2.57e-05

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: 42.38  E-value: 2.57e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591 109 VAVIDENNCIGCTKCIQACPVDAIVGATRAMHTVMSDLCTGCN------LCVDPCPTHCI 162
Cdd:cd04410  74 IVLIDEDKCIGCGSCVEACPYGAIVFDPEPGKAVKCDLCGDRLdeglepACVKACPTGAL 133
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 106-164 2.59e-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: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 41.94  E-value: 2.59e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15831591 106 ARMVAVIDENNCIGCTKCIQACPVDAIVGATramHTVMSDLCTGCNLCVDPCPTHCISL 164
Cdd:cd16372  68 ANGVVMINKKLCVGCLMCVGFCPEGAMFKHE---DYPEPFKCIACGICVKACPTGALEL 123
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 115-159 3.16e-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: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 41.94  E-value: 3.16e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15831591 115 NNCIGCTKCIQACPVDAIVGATRAMHTVMSDLCTGCNLCVDPCPT 159
Cdd:cd16372  47 NVCNQCGECIDVCPTGAITRDANGVVMINKKLCVGCLMCVGFCPE 91
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 111-166 3.27e-05

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 41.74  E-value: 3.27e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15831591  111 VIDENNCIGCTKCIQACPVDAIV--GATRAMhTVMSDLCTGCNLCVDPCPTHCISLQP 166
Cdd:PRK08348  38 LYDVDKCVGCRMCVTVCPAGVFVylPEIRKV-ALWTGRCVFCGQCVDVCPTGALQMSD 94
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 117-167 5.74e-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: 41.02  E-value: 5.74e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15831591 117 CIGCTK--CIQACPVDAIV--GATRAMhTVMSDLCTGCNLCVDPCPTHCISLQPV 167
Cdd:cd10550  49 CRQCEDapCVEACPVGAISrdEETGAV-VVDEDKCIGCGMCVEACPFGAIRVDPE 102
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 117-159 6.02e-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: 39.05  E-value: 6.02e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 15831591   117 CIGCTKCIQACPVDAIVGATRAMH------TVMSDLCTGCNLCVDPCPT 159
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKkgtktvVIDPERCVGCGACVAVCPT 49
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 109-163 7.46e-05

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 42.46  E-value: 7.46e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831591 109 VAVIDENNC--IGCTK-CIQACPV-----DAIV-GATRAMHTVMSDLCTGCNLCVDPCPTHCIS 163
Cdd:COG1245   4 IAVVDRDRCqpKKCNYeCIKYCPVnrtgkEAIEiDEDDGKPVISEELCIGCGICVKKCPFDAIS 67
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 98-132 7.96e-05

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 42.46  E-value: 7.96e-05
                        10        20        30
                ....*....|....*....|....*....|....*
gi 15831591  98 GEAQELTPARMVAVIDENNCIGCTKCIQACPVDAI 132
Cdd:COG1245  32 KEAIEIDEDDGKPVISEELCIGCGICVKKCPFDAI 66
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 111-162 1.06e-04

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 41.09  E-value: 1.06e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831591 111 VIDENNCIGCTKCIQACPVDAIvgaTRAMHTVMSDLCTGCN---------LCVDPCPTHCI 162
Cdd:COG0437  86 LVDYDKCIGCRYCVAACPYGAP---RFNPETGVVEKCTFCAdrldegllpACVEACPTGAL 143
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
117-158 1.09e-04

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 39.01  E-value: 1.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831591   117 CIGCTKCIQACPVDAIVGAT---------------------RAMHTVMSDLCTGCNLCVDPCP 158
Cdd:pfam13484   1 CGSCGKCIDACPTGAIVGPEgvldarrcisyltiekkglipDELRCLLGNRCYGCDICQDVCP 63
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
109-163 1.40e-04

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 41.72  E-value: 1.40e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831591  109 VAVIDENNCIG--C-TKCIQACPV-----DAIVGATRAMHTVMS-DLCTGCNLCVDPCPTHCIS 163
Cdd:PRK13409   4 IAVVDYDRCQPkkCnYECIKYCPVvrtgeETIEIDEDDGKPVISeELCIGCGICVKKCPFDAIS 67
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 101-164 1.58e-04

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 41.55  E-value: 1.58e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591  101 QELTPARMVAVIDENNCIGCTKCIQACPvdaiVGATRAMHTVMS--DLC----TGCNLCVDPCPTHCISL 164
Cdd:PRK12809  71 NALTFQSDSVQLDEQKCIGCKRCAIACP----FGVVEMVDTIAQkcDLCnqrsSGTQACIEVCPTQALRL 136
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 103-134 1.92e-04

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 38.11  E-value: 1.92e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 15831591 103 LTPARMVAVIDENNCIGCTKCIQACPVDAIVG 134
Cdd:COG2221  32 ISLDDGKLVIDEEKCIGCGACIRVCPTGAIKG 63
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 111-158 2.11e-04

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


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 38.00  E-value: 2.11e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15831591   111 VIDENNCIGCTKCIQACP-----VDAIVGATRAMHT-VMSDLCTGCNLCVDPCP 158
Cdd:pfam13237   3 VIDPDKCIGCGRCTAACPagltrVGAIVERLEGEAVrIGVWKCIGCGACVEACP 56
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 100-166 2.50e-04

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: 39.53  E-value: 2.50e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15831591 100 AQELTPARMVAVIDEN----NCIGCTKCIQACPVDAI-----VGAtRAMHTVMSDLCTGCNLCVDPCPTHCISLQP 166
Cdd:cd10564  64 PAREAPWPLRAEIGDSclalQGVECRSCQDACPTQAIrfrprLGG-IALPELDADACTGCGACVSVCPVGAITLTP 138
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 115-162 2.51e-04

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


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 40.61  E-value: 2.51e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 15831591  115 NNCIGCTKCIQACPVDAIVGATRamHTVMSDLCTGCNLCVDPCPTHCI 162
Cdd:NF038196 185 DKCIGCGICAKVCPVNNIEMEDG--KPVWGHNCTHCLACIHRCPKEAI 230
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 111-165 3.34e-04

CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the iron-sulfur subunit of carbon monoxide dehydrogenase (CODH), found in anaerobic bacteria and archaea. Carbon monoxide dehydrogenase is a key enzyme for carbon monoxide (CO) metabolism, where CooF is the proposed mediator of electron transfer between CODH and the CO-induced hydrogenase, catalyzing the reaction that uses CO as a single carbon and energy source, and producing only H2 and CO2. The ion-sulfur subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons in the protein complex during reaction.


Pssm-ID: 319885 [Multi-domain]  Cd Length: 140  Bit Score: 39.16  E-value: 3.34e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15831591 111 VIDENNCIGCTKCIQACPVDAIVGATRAMHTVMSDLCTG--CNLCVDPCPTHCISLQ 165
Cdd:cd10563  84 IHDEEKCVGCWMCVMVCPYGAIRPDKERKVALKCDLCPDreTPACVEACPTGALVLE 140
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 111-159 3.48e-04

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: 39.31  E-value: 3.48e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591 111 VIDENNCIGCTKCIQACPVDAI--VGATRAMHTvmsdlCTGCN---------LCVDPCPT 159
Cdd:cd16366  96 VVDPETCIGCGYCVNACPFDIPrfDEETGRVAK-----CTLCYdrisnglqpACVKTCPT 150
PRK09898 PRK09898
ferredoxin-like protein;
111-166 3.51e-04

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 39.82  E-value: 3.51e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15831591  111 VIDENNCIGCTKCIQACPvdaIVGATRAMHTVMSDLCTGCNLCVDPCPTHCISLQP 166
Cdd:PRK09898 150 TVDHKRCIGCSACTTACP---WMMATVNTESKKSSKCVLCGECANACPTGALKIIE 202
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 117-158 3.68e-04

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: 40.06  E-value: 3.68e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 15831591 117 CIGCTK--CIQACPVDAIVGATRAMHTVMSDLCTGCNLCVDPCP 158
Cdd:cd10560  78 CKHCTDagCLEACPTGAIFRTEFGTVYIQPDICNGCGYCVAACP 121
porD PRK09624
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
 113-164 3.86e-04

pyruvate ferredoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 170017 [Multi-domain]  Cd Length: 105  Bit Score: 38.47  E-value: 3.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15831591  113 DENNCIGCTKCIQACPVDAIVGATRAMHTVMSDLCTGCNLCVDPCPTHCISL 164
Cdd:PRK09624  49 NRDKCVRCYLCYIYCPEPAIYLDEEGYPVFDYDYCKGCGICANECPTKAIEM 100
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 105-133 4.05e-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: 4.05e-04
                        10        20
                ....*....|....*....|....*....
gi 15831591 105 PARMVAVIDENNCIGCTKCIQACPVDAIV 133
Cdd:COG1143  25 EPGKVYVIDPDKCIGCGLCVEVCPTGAIS 53
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 114-134 4.91e-04

Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; Epoxyqueuosine reductase QueG (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441208 [Multi-domain]  Cd Length: 345  Bit Score: 39.80  E-value: 4.91e-04
                        10        20
                ....*....|....*....|.
gi 15831591 114 ENNCIGCTKCIQACPVDAIVG 134
Cdd:COG1600 183 EDHCGSCTRCLDACPTGAIVA 203
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 67-158 6.16e-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: 39.68  E-value: 6.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831591  67 NGEKINRCAPGGEAVMLKIAELLNVEPQPLDGEAQELtparmvavideNNCIGCTKCIQACPV----------------- 129
Cdd:COG0247  41 NPGKIGLLNPGVELLGDGDLHDKNLKTLPWKELLDAL-----------DACVGCGFCRAMCPSykatgdekdsprgrinl 109

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15831591 130 -------DAIVGATRAMHTVMsDLCTGCNLCVDPCP 158
Cdd:COG0247 110 lrevlegELPLDLSEEVYEVL-DLCLTCKACETACP 144
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 111-162 8.51e-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: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 37.93  E-value: 8.51e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831591 111 VIDENNCIGCTKCIQACPVDAIVGATramHTVMSDLCTGCN---------LCVDPCPTHCI 162
Cdd:cd16371  80 VVDQDKCIGCGYCVWACPYGAPQYNP---ETGKMDKCDMCVdrldegekpACVAACPTRAL 137
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 110-132 9.62e-04

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


Pssm-ID: 459642 [Multi-domain]  Cd Length: 24  Bit Score: 35.30  E-value: 9.62e-04
                          10        20
                  ....*....|....*....|...
gi 15831591   110 AVIDENNCIGCTKCIQACPVDAI 132
Cdd:pfam00037   1 VVIDEEKCIGCGACVEVCPVGAI 23
PLN00071 PLN00071
photosystem I subunit VII; Provisional
 115-165 1.06e-03

photosystem I subunit VII; Provisional


Pssm-ID: 177700 [Multi-domain]  Cd Length: 81  Bit Score: 36.46  E-value: 1.06e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15831591  115 NNCIGCTKCIQACPVDAI-------VGATRAMHTVMSDLCTGCNLCVDPCPTHCISLQ 165
Cdd:PLN00071   9 DTCIGCTQCVRACPTDVLemipwdgCKAKQIASAPRTEDCVGCKRCESACPTDFLSVR 66
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 117-178 1.08e-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: 37.76  E-value: 1.08e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831591 117 CIGCTK--CIQACPVDAIVGATRAMHTVMSDLCTGCNLCVDPCPTHCISLQpvAETPDSWKWDL 178
Cdd:cd16366  70 CMHCTDagCLAACPTGAIIRTETGTVVVDPETCIGCGYCVNACPFDIPRFD--EETGRVAKCTL 131
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
123-166 1.09e-03

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 37.71  E-value: 1.09e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 15831591 123 CIQACPVDAIVGATRAMHtVMSDLCTGCNLCVDPCPTHCISLQP 166
Cdd:COG1142  60 CAEVCPVGAITRDDGAVV-VDEEKCIGCGLCVLACPFGAITMVG 102
psaC CHL00065
photosystem I subunit VII
 115-165 1.17e-03

photosystem I subunit VII


Pssm-ID: 177005 [Multi-domain]  Cd Length: 81  Bit Score: 36.28  E-value: 1.17e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15831591  115 NNCIGCTKCIQACPVDAI-------VGATRAMHTVMSDLCTGCNLCVDPCPTHCISLQ 165
Cdd:CHL00065   9 DTCIGCTQCVRACPTDVLemipwdgCKAKQIASAPRTEDCVGCKRCESACPTDFLSVR 66
PRK13984 PRK13984
putative oxidoreductase; Provisional
 113-159 1.18e-03

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 38.98  E-value: 1.18e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15831591  113 DENNCIGCTKCIQACPVDAI-VGATRAMHTVMSDL----------CTGCNLCVDPCPT 159
Cdd:PRK13984  43 DWEKCIGCGTCSKICPTDAItMVEVPDLPQEYGKKpqrpvidygrCSFCALCVDICTT 100
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 123-175 1.23e-03

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


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 37.62  E-value: 1.23e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15831591 123 CIQACPVDAIVGATRAMHtVMSDLCTGCNLCVDPCPTHCISLQPVAETPDSWK 175
Cdd:cd10554  64 CANVCPVGAISQEDGVVQ-VDEERCIGCKLCVLACPFGAIEMAPTTVPGVDWE 115
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 111-162 1.24e-03

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: 37.67  E-value: 1.24e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831591 111 VIDENNCIGCTKCIQACPVDAIVGATRAMHtvmSDLCTGCN---------LCVDPCPTHCI 162
Cdd:cd10562  96 VVDEDKCIGCGYCVAACPFDVPRYDETTNK---ITKCTLCFdriengmqpACVKTCPTGAL 153
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
109-150 1.56e-03

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 38.32  E-value: 1.56e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 15831591  109 VAVIDENNCIGCTKCIQACPVDAivgatRAMH--TVMSDLCTGC 150
Cdd:PRK14993 124 IVVVDNKRCVGCAYCVQACPYDA-----RFINheTQTADKCTFC 162
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 117-164 1.84e-03

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: 37.28  E-value: 1.84e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15831591 117 CIGCTK--CIQACPVDAIVGATRAMHTVMSDLCTGCNLCVDPCPTHCISL 164
Cdd:cd10562  70 CMHCTDaaCVKVCPTGALYKTENGAVVVDEDKCIGCGYCVAACPFDVPRY 119
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
 116-166 2.11e-03

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 37.32  E-value: 2.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15831591  116 NCIGCTKCIQACPVDAIVGATRAMHTVMS---DL--CTGCNLCVDPCPTHCISLQP 166
Cdd:PRK12387  39 QCIGCAACVNACPSNALTVETDLATGELAwefNLgrCIFCGRCEEVCPTAAIKLSQ 94
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 112-164 2.16e-03

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: 36.96  E-value: 2.16e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15831591 112 IDENNCIGCTKCIQACPVDAIVGATRAMHTVMSDLC-----TGCN-LCVDPCPTHCISL 164
Cdd:cd10553  86 VDQELCIGCKACIEACPWGIPQWNPATGKVVKCDYCmdridQGLKpACVTGCTTHALSF 144
ndhI CHL00014
NADH dehydrogenase subunit I
 117-164 2.84e-03

NADH dehydrogenase subunit I


Pssm-ID: 214334 [Multi-domain]  Cd Length: 167  Bit Score: 36.66  E-value: 2.84e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15831591  117 CIGCTKCIQACPVDAIV---GATRAM-------HTVMSDLCTGCNLCVDPCPTHCISL 164
Cdd:CHL00014  61 CIACEVCVRVCPIDLPVvdwKLETDIrkkrllnYSIDFGVCIFCGNCVEYCPTNCLSM 118
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 111-162 3.28e-03

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: 36.74  E-value: 3.28e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831591 111 VIDENNCIGCTKCIQACPVDAI-----------VGATRAMHTVmsDLCTGCN---------LCVDPCPTHCI 162
Cdd:cd10551  79 LVDYDKCIGCRYCMAACPYGARyfnpeephefgEVPVRPKGVV--EKCTFCYhrldegllpACVEACPTGAR 148
COG4871 COG4871
Metal-binding trascriptional regulator, contains Fe-S cluster and ArsR family DNA binding ...
 35-76 3.33e-03

Metal-binding trascriptional regulator, contains Fe-S cluster and ArsR family DNA binding domain [Transcription];


Pssm-ID: 443899  Cd Length: 177  Bit Score: 36.82  E-value: 3.33e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 15831591  35 PVVEKIDEILPQSQCGQCGYPGCRPYAEAISCNGEKINRCAP 76
Cdd:COG4871 112 PGVIEIYKLLPKTNCGKCGEPTCMAFAAKLLAGEKGLDDCPP 153
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 117-169 3.38e-03

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 36.46  E-value: 3.38e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831591 117 CIGCTKCIQACPVDAIV------GATRAMHTVMS------DLCtgCNLCVDPCPTHCISLQPVAE 169
Cdd:cd16373  16 CIRCGLCVEACPTGVIQpagledGLEGGRTPYLDpregpcDLC--CDACVEVCPTGALRPLDLEE 78
Fer4_6 pfam12837
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 109-132 4.01e-03

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


Pssm-ID: 432822 [Multi-domain]  Cd Length: 24  Bit Score: 33.74  E-value: 4.01e-03
                          10        20
                  ....*....|....*....|....
gi 15831591   109 VAVIDENNCIGCTKCIQACPVDAI 132
Cdd:pfam12837   1 VVEVDPDKCIGCGRCVVVCPYGAI 24
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 116-167 4.20e-03

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: 35.83  E-value: 4.20e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15831591 116 NCIGCT--KCIQACPVDAIV----GATRamhtVMSDLCTGCNLCVDPCPTHCISLQPV 167
Cdd:cd04410  49 SCMHCEdpPCVKACPTGAIYkdedGIVL----IDEDKCIGCGSCVEACPYGAIVFDPE 102
napH PRK09477
quinol dehydrogenase membrane component; Provisional
 109-158 5.21e-03

quinol dehydrogenase membrane component; Provisional


Pssm-ID: 236535 [Multi-domain]  Cd Length: 271  Bit Score: 36.80  E-value: 5.21e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15831591  109 VAVIDENNCIGCTKCIQACP----VDAIVGATRAMHTVMSDLCTGCNLCVDPCP 158
Cdd:PRK09477 202 VKAHDRQKCTRCMDCFHVCPepqvLRPPLKGKQSPSQVTSGDCITCGRCIDVCS 255
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 131-164 8.83e-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: 8.83e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 15831591 131 AIVGATRAMhtVMSDLCTGCNLCVDPCPTHCISL 164
Cdd:COG2221   3 GIIGTWPPK--IDEEKCIGCGLCVAVCPTGAISL 34
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 110-159 8.88e-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: 319889 [Multi-domain]  Cd Length: 138  Bit Score: 34.98  E-value: 8.88e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15831591 110 AVIDENNCIGCTKCIQACPVDAI--VGATRamhtvmSDLCTGCN--LCVDPCPT 159
Cdd:cd16367  81 EVVISDACCGCGNCASACPYGAIqmVRAVK------CDLCAGYAgpACVSACPT 128
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 95-129 8.93e-03

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 35.31  E-value: 8.93e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 15831591  95 PLDGEAQELTPARMVAVIDENNCIGCTKCIQACPV 129
Cdd:cd16373 110 PTEAIAIVLEDDVLRPVVDEDKCVGCGLCEYVCPV 144
 
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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