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Conserved domains on  [gi|2279651085|ref|WP_256329667|]
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4Fe-4S dicluster domain-containing protein [Variovorax sp. YR634]

Protein Classification

HybA family protein( domain architecture ID 11418228)

HybA family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 31-231 4.34e-88

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


:

Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 258.72  E-value: 4.34e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  31 KQLALVIDLNVCVGCHACVTSCKQWNTsgsagpladerpyaaNPTGTFFNRVQTYEAGAFPVTETIHFPKSCLHCEDPPC 110
Cdd:COG0437     4 KRYGMVIDLTKCIGCRACVVACKEENN---------------LPVGVTWRRVRRYEEGEFPNVEWLFVPVLCNHCDDPPC 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 111 VPVCPTGASYKRkEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRIydeqlpKEDRKPACVKACPTG 190
Cdd:COG0437    69 VKVCPTGATYKR-EDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRL------DEGLLPACVEACPTG 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2279651085 191 ARIFGDVKDPDSEVSKAIRERGGYQLMPEWETSPANQYLPR 231
Cdd:COG0437   142 ALVFGDLDDPESEVSKRLAELPAYRLLPELGTKPSVYYLPK 182
 
Name Accession Description Interval E-value
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 31-231 4.34e-88

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 258.72  E-value: 4.34e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  31 KQLALVIDLNVCVGCHACVTSCKQWNTsgsagpladerpyaaNPTGTFFNRVQTYEAGAFPVTETIHFPKSCLHCEDPPC 110
Cdd:COG0437     4 KRYGMVIDLTKCIGCRACVVACKEENN---------------LPVGVTWRRVRRYEEGEFPNVEWLFVPVLCNHCDDPPC 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 111 VPVCPTGASYKRkEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRIydeqlpKEDRKPACVKACPTG 190
Cdd:COG0437    69 VKVCPTGATYKR-EDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRL------DEGLLPACVEACPTG 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2279651085 191 ARIFGDVKDPDSEVSKAIRERGGYQLMPEWETSPANQYLPR 231
Cdd:COG0437   142 ALVFGDLDDPESEVSKRLAELPAYRLLPELGTKPSVYYLPK 182
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 35-229 4.73e-88

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: 258.62  E-value: 4.73e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  35 LVIDLNVCVGCHACVTSCKQWNTSgsagpladerpyaanPTGTFFNRVQTYEAGAFPVTETIHFPKSCLHCEDPPCVPVC 114
Cdd:cd10551     1 MVIDLRKCIGCGACVVACKAENNV---------------PPGVFRNRVLEYEVGEYPNVKRTFLPVLCNHCENPPCVKVC 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 115 PTGASYKRkEDGIVLVDYDKCIGCKYCAWACPYGARELDEE------------RQVMTKCTLCVDRIydeqlpKEDRKPA 182
Cdd:cd10551    66 PTGATYKR-EDGIVLVDYDKCIGCRYCMAACPYGARYFNPEephefgevpvrpKGVVEKCTFCYHRL------DEGLLPA 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2279651085 183 CVKACPTGARIFGDVKDPDSEVSKAIRERGGYQLMPEWETSPANQYL 229
Cdd:cd10551   139 CVEACPTGARIFGDLDDPNSEVSKLLAERRAYVLKPELGTKPKVYYI 185
DMSO_dmsB TIGR02951
DMSO reductase, iron-sulfur subunit; This family consists of the iron-sulfur subunit, or chain ...
 32-197 4.04e-50

DMSO reductase, iron-sulfur subunit; This family consists of the iron-sulfur subunit, or chain B, of an enzyme called the anaerobic dimethyl sulfoxide reductase. Chains A and B are catalytic, while chain C is a membrane anchor.


Pssm-ID: 131996 [Multi-domain]  Cd Length: 161  Bit Score: 161.44  E-value: 4.04e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  32 QLALVIDLNVCVGCHACVTSCKQWNTSgsagpladerpyaanPTGTFFNRVQTYEAGAF--------PVTETIHFPKSCL 103
Cdd:TIGR02951   1 QYGFYVDQTRCSGCKTCQIACKDKNDL---------------EVGVLFRRVYEYEGGGWteegegfhPDVFAYYISISCN 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 104 HCEDPPCVPVCPTGASYKRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRIydeqlpKEDRKPAC 183
Cdd:TIGR02951  66 HCADPACVKNCPTGAMYKREEDGLVLVDQDKCIGCRYCVWACPYGAPQYDPQQGVMGKCDGCYDRV------EKGLRPAC 139

                         170
                  ....*....|....
gi 2279651085 184 VKACPTGARIFGDV 197
Cdd:TIGR02951 140 VDACPMRALDFGPI 153
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
30-229 1.50e-46

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 155.03  E-value: 1.50e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  30 AKQLALVIDLNVCVGCHACVTSCKQWNtsgsagpladerpyaANPTGTFFNRVQTYE---AGAFPVTETIhFPKSCLHCE 106
Cdd:PRK14993   41 RHRYAMLIDLRRCIGCQSCTVSCTIEN---------------QTPQGAFRTTVNQYQvqrEGSQEVTNVL-LPRLCNHCD 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 107 DPPCVPVCPTGASYKRKeDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRIYDEQLpkedrkPACVKA 186
Cdd:PRK14993  105 NPPCVPVCPVQATFQRE-DGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLL------PACVES 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2279651085 187 CPTGARIFGDVKDPDSEVSKAIRERGG--YQLMPEWETSPANQYL 229
Cdd:PRK14993  178 CVGGARIIGDIKDPHSRIATMLHQHRDaiKVLKPENGTSPHVFYL 222
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 98-197 7.47e-30

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


Pssm-ID: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 107.33  E-value: 7.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  98 FPKSCLHCEDPPCVPVCPTGASYKRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRIydeqlpKE 177
Cdd:pfam13247   6 FPEQCRHCLNPPCKASCPVGAIYKDEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRV------EA 79

                          90       100
                  ....*....|....*....|
gi 2279651085 178 DRKPACVKACPTGARIFGDV 197
Cdd:pfam13247  80 GLLPACVQTCPTGAMNFGDR 99
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 133-191 9.09e-05

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: 42.54  E-value: 9.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 133 DKCIGCKYCAWACPYGARELDEERQV-MTKCTLCVdriydeqlpkedrkpACVKACPTGA 191
Cdd:NF038196  185 DKCIGCGICAKVCPVNNIEMEDGKPVwGHNCTHCL---------------ACIHRCPKEA 229
 
Name Accession Description Interval E-value
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 31-231 4.34e-88

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 258.72  E-value: 4.34e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  31 KQLALVIDLNVCVGCHACVTSCKQWNTsgsagpladerpyaaNPTGTFFNRVQTYEAGAFPVTETIHFPKSCLHCEDPPC 110
Cdd:COG0437     4 KRYGMVIDLTKCIGCRACVVACKEENN---------------LPVGVTWRRVRRYEEGEFPNVEWLFVPVLCNHCDDPPC 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 111 VPVCPTGASYKRkEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRIydeqlpKEDRKPACVKACPTG 190
Cdd:COG0437    69 VKVCPTGATYKR-EDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRL------DEGLLPACVEACPTG 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2279651085 191 ARIFGDVKDPDSEVSKAIRERGGYQLMPEWETSPANQYLPR 231
Cdd:COG0437   142 ALVFGDLDDPESEVSKRLAELPAYRLLPELGTKPSVYYLPK 182
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 35-229 4.73e-88

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: 258.62  E-value: 4.73e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  35 LVIDLNVCVGCHACVTSCKQWNTSgsagpladerpyaanPTGTFFNRVQTYEAGAFPVTETIHFPKSCLHCEDPPCVPVC 114
Cdd:cd10551     1 MVIDLRKCIGCGACVVACKAENNV---------------PPGVFRNRVLEYEVGEYPNVKRTFLPVLCNHCENPPCVKVC 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 115 PTGASYKRkEDGIVLVDYDKCIGCKYCAWACPYGARELDEE------------RQVMTKCTLCVDRIydeqlpKEDRKPA 182
Cdd:cd10551    66 PTGATYKR-EDGIVLVDYDKCIGCRYCMAACPYGARYFNPEephefgevpvrpKGVVEKCTFCYHRL------DEGLLPA 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2279651085 183 CVKACPTGARIFGDVKDPDSEVSKAIRERGGYQLMPEWETSPANQYL 229
Cdd:cd10551   139 CVEACPTGARIFGDLDDPNSEVSKLLAERRAYVLKPELGTKPKVYYI 185
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 36-195 3.24e-57

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: 178.52  E-value: 3.24e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  36 VIDLNVCVGCHACVTSCKQWNtsgsagpladerpyaANPTGTFFNRVQTYEAGAFPVTETIHFPKSCLHCEDPPCVPVCP 115
Cdd:cd16371     3 YFDQERCIGCKACEIACKDKN---------------DLPPGVNWRRVYEYEGGEFPEVFAYFLSMSCNHCENPACVKVCP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 116 TGASYKRkEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRIydeqlpKEDRKPACVKACPTGARIFG 195
Cdd:cd16371    68 TGAITKR-EDGIVVVDQDKCIGCGYCVWACPYGAPQYNPETGKMDKCDMCVDRL------DEGEKPACVAACPTRALDFG 140
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 35-195 2.18e-51

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: 163.71  E-value: 2.18e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  35 LVIDLNVCVGCHACVTSCKQWNTsgsagpladerpyaaNPTGTFFNRVQTYEagaFPVTETIHFPKSCLHCEDPPCVPVC 114
Cdd:cd04410     1 LVVDLDRCIGCGTCEVACKQEHG---------------LRPGPDWSRIKVIE---GGGLERAFLPVSCMHCEDPPCVKAC 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 115 PTGASYKRkEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRIydeqlpKEDRKPACVKACPTGARIF 194
Cdd:cd04410    63 PTGAIYKD-EDGIVLIDEDKCIGCGSCVEACPYGAIVFDPEPGKAVKCDLCGDRL------DEGLEPACVKACPTGALTF 135


                  .
gi 2279651085 195 G 195
Cdd:cd04410   136 G 136
DMSO_dmsB TIGR02951
DMSO reductase, iron-sulfur subunit; This family consists of the iron-sulfur subunit, or chain ...
 32-197 4.04e-50

DMSO reductase, iron-sulfur subunit; This family consists of the iron-sulfur subunit, or chain B, of an enzyme called the anaerobic dimethyl sulfoxide reductase. Chains A and B are catalytic, while chain C is a membrane anchor.


Pssm-ID: 131996 [Multi-domain]  Cd Length: 161  Bit Score: 161.44  E-value: 4.04e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  32 QLALVIDLNVCVGCHACVTSCKQWNTSgsagpladerpyaanPTGTFFNRVQTYEAGAF--------PVTETIHFPKSCL 103
Cdd:TIGR02951   1 QYGFYVDQTRCSGCKTCQIACKDKNDL---------------EVGVLFRRVYEYEGGGWteegegfhPDVFAYYISISCN 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 104 HCEDPPCVPVCPTGASYKRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRIydeqlpKEDRKPAC 183
Cdd:TIGR02951  66 HCADPACVKNCPTGAMYKREEDGLVLVDQDKCIGCRYCVWACPYGAPQYDPQQGVMGKCDGCYDRV------EKGLRPAC 139

                         170
                  ....*....|....
gi 2279651085 184 VKACPTGARIFGDV 197
Cdd:TIGR02951 140 VDACPMRALDFGPI 153
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 34-199 5.01e-47

the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 (Hyd-2), an enzyme that catalyzes the reversible oxidation of H2 to protons and electrons. Hyd-2 is membrane-associated and forms an unusual heterotetrameric [NiFe]-hydrogenase in that it lacks the typical cytochrome b membrane anchor subunit that transfers electrons to the quinone pool. The electron transfer subunit of Hyd-2 (HybA) which is predicted to contain four iron-sulfur clusters, is essential for electron transfer from Hyd-2 to menaquinone/demethylmenaquinone (MQ/DMQ) to couple hydrogen oxidation to fumarate reduction.


Pssm-ID: 319883 [Multi-domain]  Cd Length: 196  Bit Score: 154.68  E-value: 5.01e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  34 ALVIDLNVCVGCHACVTSCKQWNtSGSAGPLADERPYAANP--TGTFFNRVQTYEAGAFPVTETiHFPKSCLHCEDPPCV 111
Cdd:cd10561     1 GVLYDTTRCIGCRACEVACKEWN-GLPAEDTAFGPGWDNPRdlSAKTYTVIKRYEVETGGKGFV-FVKRQCMHCLDPACV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 112 PVCPTGASYKRKEdGIVLVDYDKCIGCKYCAWACPYG--ARELDEERQVMTKCTLCVDRIydeqlpKEDRKPACVKACPT 189
Cdd:cd10561    79 SACPVGALRKTPE-GPVTYDEDKCIGCRYCMVACPFNipKYEWDSANPKIRKCTMCYDRL------KEGKQPACVEACPT 151

                         170
                  ....*....|
gi 2279651085 190 GARIFGDVKD 199
Cdd:cd10561   152 GALLFGKREE 161
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
30-229 1.50e-46

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 155.03  E-value: 1.50e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  30 AKQLALVIDLNVCVGCHACVTSCKQWNtsgsagpladerpyaANPTGTFFNRVQTYE---AGAFPVTETIhFPKSCLHCE 106
Cdd:PRK14993   41 RHRYAMLIDLRRCIGCQSCTVSCTIEN---------------QTPQGAFRTTVNQYQvqrEGSQEVTNVL-LPRLCNHCD 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 107 DPPCVPVCPTGASYKRKeDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRIYDEQLpkedrkPACVKA 186
Cdd:PRK14993  105 NPPCVPVCPVQATFQRE-DGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLL------PACVES 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2279651085 187 CPTGARIFGDVKDPDSEVSKAIRERGG--YQLMPEWETSPANQYL 229
Cdd:PRK14993  178 CVGGARIIGDIKDPHSRIATMLHQHRDaiKVLKPENGTSPHVFYL 222
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 35-229 1.86e-42

N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This family includes the beta subunit of pyrogallol-phloroglucinol transhydroxylase (TH), a cytoplasmic molybdenum (Mo) enzyme from anaerobic microorganisms like Pelobacter acidigallici and Desulfitobacterium hafniense which catalyzes the conversion of pyrogallol to phloroglucinol, an important building block of plant polymers. TH belongs to the DMSO reductase (DMSOR) family; it is a heterodimer consisting of a large alpha catalytic subunit and a small beta FeS subunit. The beta subunit has two domains with the N-terminal domain containing three [4Fe-4S] centers and a seven-stranded, mainly antiparallel beta-barrel domain. In the anaerobic bacterium Pelobacter acidigallici, gallic acid, pyrogallol, phloroglucinol, or phloroglucinol carboxylic acid are fermented to three molecules of acetate (plus CO2), and TH is the key enzyme in the fermentation pathway, which converts pyrogallol to phloroglucinol in the absence of O2.


Pssm-ID: 319874 [Multi-domain]  Cd Length: 186  Bit Score: 142.46  E-value: 1.86e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  35 LVIDLNVCVGCHACVTSCKQwNTSGSAGPladerPYAAN--PTGTFFNRVQTYEAGAFPVTETIHFPKSCLHCEDPPCVP 112
Cdd:cd10552     1 LVIDVAKCNGCYNCFLACKD-EHVGNDWP-----GYAAPqpRHGHFWMRILRRERGQYPKVDVAYLPVPCNHCDNAPCIK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 113 VCPTGASYKRkEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRiydeqLPKEDRKPACVKACPTGAR 192
Cdd:cd10552    75 AAKDGAVYKR-DDGIVIIDPEKAKGQKQLVDACPYGAIYWNEELQVPQKCTFCAHL-----LDDGWKEPRCVQACPTGAL 148

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2279651085 193 IFGDVKDPDSEvsKAIRERGGYQLMPEWETSPANQYL 229
Cdd:cd10552   149 RFGKLEDEEMA--AKAAEEGLEVLHPELGTKPRVYYK 183
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 37-195 8.72e-42

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: 139.84  E-value: 8.72e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  37 IDLNVCVGCHACVTSCKQWN-TSGSAGPLADERPYAANPTGTFFNRVQTYEAGAFPVTETIHFPK-SCLHCEDPPCVPVC 114
Cdd:cd16366     3 VDTSRCTGCRACQVACKQWNgLPAEKTEFTGSYQNPPDLTAHTWTLVRFYEVEKPGGDLSWLFRKdQCMHCTDAGCLAAC 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 115 PTGASYKRkEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRIydeqlpKEDRKPACVKACPTGARIF 194
Cdd:cd16366    83 PTGAIIRT-ETGTVVVDPETCIGCGYCVNACPFDIPRFDEETGRVAKCTLCYDRI------SNGLQPACVKTCPTGALTF 155


                  .
gi 2279651085 195 G 195
Cdd:cd16366   156 G 156
cyt_nit_nrfC TIGR03149
cytochrome c nitrite reductase, Fe-S protein; Members of this protein family are the Fe-S ...
 23-224 1.51e-41

cytochrome c nitrite reductase, Fe-S protein; Members of this protein family are the Fe-S protein, NrfC, of a cytochrome c nitrite reductase system for which the pentaheme cytochrome c protein, NrfB (family TIGR03146) is an unambiguous marker. Members of this protein family show similarity to other ferredoxin-like proteins, including a subunit of a polysulfide reductase. [Energy metabolism, Electron transport]


Pssm-ID: 274451 [Multi-domain]  Cd Length: 225  Bit Score: 141.46  E-value: 1.51e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  23 AAQGETLAKQLALVIDLNVCVGCHACVTSCKQWNTSgsagpladerpyaanPTG-TFFNRVQTYEAGAFPVTETIHFPKS 101
Cdd:TIGR03149  29 AKEDKDKTKRYGMVHDETACIGCTACMDACREVNKV---------------PEGvSRLEIIRSEPYGEFPDVEYRFFRKS 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 102 CLHCEDPPCVPVCPTGASYKRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRIYdeqlpKEDRKP 181
Cdd:TIGR03149  94 CQHCDNAPCVAVCPTGASFKDEETGIVDVHKDLCVGCQYCIAACPYRVRFIHPVTKSADKCNFCRDTNL-----AEGKLP 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2279651085 182 ACVKACPTGARIFGDVKDPDSEVSKAIRERGGYQLMPEWETSP 224
Cdd:TIGR03149 169 ACVESCPTKALTFGDLNDPNSEVSQKLKQKPVYRTKVELGTKP 211
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 37-196 3.80e-41

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: 138.20  E-value: 3.80e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  37 IDLNVCVGCHACVTSCKQWNTSgSAGPLADERPYAANP--TGTFFNRVQTYE-AGAFPVTETIHFPKSCLHCEDPPCVPV 113
Cdd:cd10562     3 VDTSKCTACRGCQVACKQWNQL-PAEKTPFTGSYQNPPdlTPNTWTLIRFYEhEEDNGGIRWLFRKRQCMHCTDAACVKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 114 CPTGASYKrKEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRIydeqlpKEDRKPACVKACPTGARI 193
Cdd:cd10562    82 CPTGALYK-TENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCFDRI------ENGMQPACVKTCPTGALT 154


                  ...
gi 2279651085 194 FGD 196
Cdd:cd10562   155 FGD 157
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 42-195 6.84e-39

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: 132.10  E-value: 6.84e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  42 CVGCHACVTSCKQWNtsgsagpladerpyaANPTGTFFNRVQTYE---AGAFPVTETIHFPksCLHCEDPPCVPVCPTGA 118
Cdd:cd10553    12 CIGCLACEVHCKVKN---------------NLPVGPRLCRIFAVGpkmVGGKPRLKFVYMS--CFHCENPWCVKACPTGA 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2279651085 119 SYKRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRIydeqlpKEDRKPACVKACPTGARIFG 195
Cdd:cd10553    75 MQKREKDGIVYVDQELCIGCKACIEACPWGIPQWNPATGKVVKCDYCMDRI------DQGLKPACVTGCTTHALSFV 145
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 35-209 1.84e-38

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


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 130.86  E-value: 1.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  35 LVIDLNVCVGCHACVTSCKQWNTSGSagpladerpyaanptgtffnRVQTYEAGafpvtETIHFPKSCLHCEDPPCVPVC 114
Cdd:cd16374     1 VYVDPERCIGCRACEIACAREHSGKP--------------------RISVEVVE-----DLASVPVRCRHCEDAPCMEVC 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 115 PTGASYkRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRIydeqlpKEDRKPACVKACPTGARIF 194
Cdd:cd16374    56 PTGAIY-RDEDGAVLVDPDKCIGCGMCAMACPFGVPRFDPSLKVAVKCDLCIDRR------REGKLPACVEACPTGALKF 128

                         170
                  ....*....|....*
gi 2279651085 195 GDVKdpdsEVSKAIR 209
Cdd:cd16374   129 GDIE----ELLKEKR 139
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 31-230 2.76e-37

beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene dehydrogenase (EBDH, EC 1.17.99.2), a member of the DMSO reductase family. EBDH oxidizes the hydrocarbon ethylbenzene to (S)-1-phenylethanol. It is a heterotrimer, with the alpha subunit containing the catalytic center with a molybdenum held by two molybdopterin-guanine dinucleotides, the beta subunit containing four iron-sulfur clusters (the electron transfer subunit) and the gamma subunit containing a methionine and a lysine as axial heme ligands. During catalysis, electrons produced by substrate oxidation are transferred to a heme in the gamma subunit and then presumably to a separate cytochrome involved in nitrate respiration.


Pssm-ID: 319877 [Multi-domain]  Cd Length: 316  Bit Score: 132.81  E-value: 2.76e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  31 KQLALVIDLNVCVGCHACVTSCKQ------------WN---TSGSAG-----------------------PLADE--RPY 70
Cdd:cd10555     3 RQLAMVMDLNKCIGCQTCTVACKTlwtnrngreymyWNnveTQPGKGypknwekkgggfkdkgelkpgiiPTLEDygVPW 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  71 AANPTGTFFN----RVQTYE---------------AGAFPVTETIHFPKSCLHCEDPPCVPVCPTGASYKRKEDGIVLVD 131
Cdd:cd10555    83 EYNHEEELFEgkggRVRPSPkgdptwgpnwdedqgAGEYPNSYYFYLPRICNHCTNPACLAACPRKAIYKREEDGIVLVD 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 132 YDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRIyDEQLPkedrkPACVKACPTGARIFGDVKDPDSEVSKAIREr 211
Cdd:cd10555   163 QDRCRGYRYCVEACPYKKIYFNPVEQKSEKCIFCYPRI-EKGVA-----PACARQCVGRIRFVGYLDDEESPVYKLVKK- 235

                         250       260
                  ....*....|....*....|...
gi 2279651085 212 ggYQ----LMPEWETSPANQYLP 230
Cdd:cd10555   236 --WKvalpLHPEYGTEPNVFYVP 256
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
1-199 5.11e-36

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 129.79  E-value: 5.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085   1 MKAAAPSPQPSPASGRGSNTVRAAQGEtlakqLALVIDLNVCVGCHACVTSCKQWNtsGSAGPLADERPYAANP--TGTF 78
Cdd:PRK10882   11 SAGALLAGALPSVSHAAAENRPPIPGA-----LGMLYDSTLCVGCQACVTKCQEIN--FPERNPQGEQTWDNPDklSPYT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  79 FNRVQTYEAGAF-----PVTETIHFPKSCLHCEDPPCVPVCPTGASYKRKEDGIVLVDYDKCIGCKYCAWACPYGARELD 153
Cdd:PRK10882   84 NNIIKVWKSGTGvnkdqEENGYAYIKKQCMHCVDPNCVSVCPVSALTKDPKTGIVHYDKDVCTGCRYCMVACPFNVPKYD 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2279651085 154 EERQV--MTKCTLC----VDRIYDEQLpkedrkPACVKACPTGARIFGDVKD 199
Cdd:PRK10882  164 YNNPFgaIHKCELCnqkgVERLDKGGL------PGCVEVCPTGAVIFGTREE 209
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 34-212 2.16e-35

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: 125.19  E-value: 2.16e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  34 ALVIDLNVCVGCHACVTSCKQWNtsgsagplaDERPYAANPTGTFFN----RVQTYEAGAFpvTETIHFPK--------S 101
Cdd:cd10558     1 AKLIDVSKCIGCKACQVACKEWN---------DLRAEVGHNVGTYQNpadlSPETWTLMKF--REVEDNGKlewlirkdG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 102 CLHCEDPPCVPVCPTGASYKRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRIYDEQlpkedrKP 181
Cdd:cd10558    70 CMHCADPGCLKACPSPGAIVQYANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVGL------EP 143

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2279651085 182 ACVKACPTGARIFGDVKDPDSEVSK---AIRERG 212
Cdd:cd10558   144 ACVKTCPTGALHFGTKEDMLALAEKrvaALKERG 177
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 34-199 1.23e-34

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: 123.65  E-value: 1.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  34 ALVIDLNVCVGCHACVTSCKQWNTSGSAGPLADERPYAANP--TGTFFNRVQTYEAgaFPVTETIHFPK---------SC 102
Cdd:cd10560     1 GFFTDTSICIGCKACEVACKQWNQLPADGYDFSGMSYDNTGdlSASTWRHVKFIER--PTEDGPANEGGdlqwlfmsdVC 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 103 LHCEDPPCVPVCPTGASYkRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRIydeqlpKEDRKPA 182
Cdd:cd10560    79 KHCTDAGCLEACPTGAIF-RTEFGTVYIQPDICNGCGYCVAACPFGVIDRNEETGRAHKCTLCYDRL------KDGLEPA 151

                         170
                  ....*....|....*..
gi 2279651085 183 CVKACPTGARIFGDVKD 199
Cdd:cd10560   152 CAKACPTGSIQFGPLEE 168
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 35-191 2.98e-34

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: 119.60  E-value: 2.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  35 LVIDLNVCVGCHACVTSCKQWNTSgsagpladerpyAANPTgtfFNRVQTYEAGAfpvtETIHFPKSCLHCEDPPCVPVC 114
Cdd:cd10550     1 LVVDPEKCTGCRTCELACSLKHEG------------VFNPS---LSRIRVVRFEP----EGLDVPVVCRQCEDAPCVEAC 61

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2279651085 115 PTGASYKRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCvdriydeqlpkeDRKPACVKACPTGA 191
Cdd:cd10550    62 PVGAISRDEETGAVVVDEDKCIGCGMCVEACPFGAIRVDPETGKAIKCDLC------------GGDPACVKVCPTGA 126
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 31-230 2.11e-33

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


Pssm-ID: 319887 [Multi-domain]  Cd Length: 201  Bit Score: 119.61  E-value: 2.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  31 KQLALVIDLNVCVGCHACVTSCKQWNTSGSAGPLAderpyaanptgtFFNRVQTYEAGAFPVT---------ETIHF--- 98
Cdd:cd16365     1 KQFAAVFNLNKCIGCQTCTVACKNAWTYRKGQEYM------------WWNNVETKPGGGYPQDwevktidngGNTRFffy 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  99 -PKSCLHCEDPPCVPVCPTGASYKRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRIydeqlpkE 177
Cdd:cd16365    69 lQRLCNHCTNPACLAACPRGAIYKREEDGIVLIDQKRCRGYRKCVEQCPYKKIYFNGLSRVSEKCIACYPRI-------E 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2279651085 178 DRKP-ACVKACPTGARIFGDVKD-PDSEVSKAIRE-RGGYQLMPEWETSPANQYLP 230
Cdd:cd16365   142 GGDPtRCMSACVGRIRLQGFLDDnPKSPVTKLIRHwKVALPLHPEYGTEPNIYYVP 197
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 35-195 3.47e-33

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: 117.36  E-value: 3.47e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  35 LVIDLNVCVGCHACVTSCKQWNtSGSAGPLaderpYAANPTGTFFNRVQTYEAGAFPvtetihFPKSCLHCEDPPCVPVC 114
Cdd:cd10563     2 IFIDEEKCLGCKLCEVACAVAH-SKSKDLI-----KAKLEKERPRPRIRVEESGGRS------FPLQCRHCDEPPCVKAC 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 115 PTGASYKRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRiydeqlpkedRKPACVKACPTGARIF 194
Cdd:cd10563    70 MSGAMHKDPETGIVIHDEEKCVGCWMCVMVCPYGAIRPDKERKVALKCDLCPDR----------ETPACVEACPTGALVL 139


                  .
gi 2279651085 195 G 195
Cdd:cd10563   140 E 140
FDH-beta TIGR01582
formate dehydrogenase, beta subunit, Fe-S containing; This model represents the beta subunit ...
 16-212 1.73e-30

formate dehydrogenase, beta subunit, Fe-S containing; This model represents the beta subunit of the gamma-proteobacterial formate dehydrogenase. This subunit contains four 4Fe-4S clusters and is involved in transmitting electrons from the alpha subunit (TIGR01553) at the periplasmic space to the gamma subunit which spans the cytoplasmic membrane. In addition to the gamma proteobacteria, a sequence from Aquifex aolicus falls within the scope of this model. This appears to be the case for the alpha, gamma and epsilon (accessory protein TIGR01562) chains as well. [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]


Pssm-ID: 273705 [Multi-domain]  Cd Length: 283  Bit Score: 114.24  E-value: 1.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  16 RGSNTVRAAQGETLAKQLALVIDLNVCVGCHACVTSCKQWNTSGSaGPLADERPYAANP--------TGTFFNRVQTYEA 87
Cdd:TIGR01582   5 LSATKEPDPSVKTYPTELAKLIDVSSCIGCKACQAACQEWNDTTP-PILSRKVGGYQNPpdllpetfTLMRFKEGEESDG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  88 GAFPVTEtihfpKSCLHCEDPPCVPVCPTGASYKRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVD 167
Cdd:TIGR01582  84 LEWLIRK-----DGCMHCREPGCLKACPAPGAIIQYQNGIVDFDHSKCIGCGYCIVGCPFNIPRYDKVDNRPYKCTLCID 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2279651085 168 RIYDEQlpkedrKPACVKACPTGARIFG---DVKDPDSEVSKAIRERG 212
Cdd:TIGR01582 159 RVSVGQ------EPACVKTCPTNAISFGfkeDMKERAEKRVADLKSRG 200
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 98-197 7.47e-30

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


Pssm-ID: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 107.33  E-value: 7.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  98 FPKSCLHCEDPPCVPVCPTGASYKRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRIydeqlpKE 177
Cdd:pfam13247   6 FPEQCRHCLNPPCKASCPVGAIYKDEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRV------EA 79

                          90       100
                  ....*....|....*....|
gi 2279651085 178 DRKPACVKACPTGARIFGDV 197
Cdd:pfam13247  80 GLLPACVQTCPTGAMNFGDR 99
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
35-191 1.33e-29

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 107.82  E-value: 1.33e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  35 LVIDLNVCVGCHACVTSCKQWNTSGSAGPladerpyaanptgtFFNRVQTYEagafpvTETIHFPKSCLHCEDPPCVPVC 114
Cdd:COG1142     5 IIADPEKCIGCRTCEAACAVAHEGEEGEP--------------FLPRIRVVR------KAGVSAPVQCRHCEDAPCAEVC 64

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2279651085 115 PTGASYKrkEDGIVLVDYDKCIGCKYCAWACPYGARELDEE--RQVMTKCTLCVDRiydeqlpkeDRKPACVKACPTGA 191
Cdd:COG1142    65 PVGAITR--DDGAVVVDEEKCIGCGLCVLACPFGAITMVGEksRAVAVKCDLCGGR---------EGGPACVEACPTGA 132
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 35-196 2.07e-29

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


Pssm-ID: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 108.63  E-value: 2.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  35 LVIDLNVCVGCHACVTSCKQWNTSGsagplADERPYAanptgTFFNRVQTyeagafpvTETihFPKSCLHCEDPPCVPVC 114
Cdd:cd16369     4 FFIDPSRCIGCRACVAACRECGTHR-----GKSMIHV-----DYIDRGES--------TQT--APTVCMHCEDPTCAEVC 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 115 PTGAsYKRKEDGIVL-VDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRIydeqlpKEDRKPACVKACPTGARI 193
Cdd:cd16369    64 PADA-IKVTEDGVVQsALKPRCIGCSNCVNACPFGVPKYDEERNLMMKCDMCYDRT------SVGKAPMCASVCPSGALF 136


                  ...
gi 2279651085 194 FGD 196
Cdd:cd16369   137 YGT 139
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 36-191 5.01e-29

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: 106.57  E-value: 5.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  36 VIDLNVCVGCHACVTSCKQWNTSGSAgpladerPYAANPTGTFFNRVQTYEagafpvTETIHFPKSCLHCEDPPCVPVCP 115
Cdd:cd10554     3 IADPDKCIGCRTCEVACAAAHSGKGI-------FEAGTDGLPFLPRLRVVK------TGEVTAPVQCRQCEDAPCANVCP 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 116 TGASYKrkEDGIVLVDYDKCIGCKYCAWACPYGAREL-----------DEERQVMTKCTLCVDRiydeqlpkeDRKPACV 184
Cdd:cd10554    70 VGAISQ--EDGVVQVDEERCIGCKLCVLACPFGAIEMapttvpgvdweRGPRAVAVKCDLCAGR---------EGGPACV 138


                  ....*..
gi 2279651085 185 KACPTGA 191
Cdd:cd10554   139 EACPTKA 145
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 33-199 2.28e-27

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


Pssm-ID: 319890 [Multi-domain]  Cd Length: 200  Bit Score: 104.04  E-value: 2.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  33 LALVIDLNVCVGCH-----ACVTSCKQWNTSGSAGPLADE-RPYAANPTG------------------TFFNRVQTYEAG 88
Cdd:cd16368     1 LATLIDLTKCDGCPgesipACVRACREKNQARFPEPVSKPiQPYWPRKRIedwsdkrdvtdrltpynwLYVQKLTVDTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  89 AfpvTETIHFPKSCLHCEDPPCVPVCPTGASYKRKEdGIVLVDYDKCIGCKYCAWACPYGAreldEERQ----------- 157
Cdd:cd16368    81 G---EKEVFIPRRCMHCDNPPCAKLCPFGAARKTPE-GAVYIDDDLCFGGAKCRDVCPWHI----PQRQagvgiylhlap 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2279651085 158 ------VMTKCTLCVDRIydeqlpKEDRKPACVKACPTGARIFGDVKD 199
Cdd:cd16368   153 eyagggVMYKCDLCKDLL------AQGKPPACIEACPKGAQYFGPRKE 194
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 34-199 2.73e-23

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: 91.60  E-value: 2.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  34 ALVIDLNVCVGCHACVTSCkqwntsgsagpladERPYAANPTgtfFNRVQtyeagafPVTETIHFPKSCLHCEDPPCVPV 113
Cdd:cd16367    13 LLVIDLDRCIRCDNCEKAC--------------ADTHDGHSR---LDRNG-------LRFGNLLVPTACRHCVDPVCMIG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 114 CPTGAsYKRKEDGIVLVDyDKCIGCKYCAWACPYGARELdeerQVMTKCTLCVDriYDEqlpkedrkPACVKACPTGARI 193
Cdd:cd16367    69 CPTGA-IHRDDGGEVVIS-DACCGCGNCASACPYGAIQM----VRAVKCDLCAG--YAG--------PACVSACPTGAAI 132


                  ....*.
gi 2279651085 194 FGDVKD 199
Cdd:cd16367   133 RVNPEE 138
PRK09898 PRK09898
ferredoxin-like protein;
35-191 4.49e-23

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 92.98  E-value: 4.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  35 LVIDLNVCVGCHACVTSCKQWNtSGSAGPLADERPYAANptgtFFNRVQTYEAGAFPVTETIHFPKSCLHCEDPPCVPVC 114
Cdd:PRK09898   61 LVTQRARCTGCHRCEISCTNFN-DGSVGTFFSRIKIHRN----YFFGDNGVGSGGGLYGDLNYTADTCRQCKEPQCMNVC 135

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2279651085 115 PTGASYKRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCvdriydeqlpkedrkPACVKACPTGA 191
Cdd:PRK09898  136 PIGAITWQQKEGCITVDHKRCIGCSACTTACPWMMATVNTESKKSSKCVLC---------------GECANACPTGA 197
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 34-210 1.44e-22

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


Pssm-ID: 319881 [Multi-domain]  Cd Length: 200  Bit Score: 91.34  E-value: 1.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  34 ALVIDLNVCVGCHACVTSCKQWNtsGSAGPLADERPYAANP---TGTFFNRVQTYEA-GAFPVTETIHFPKSCLHCEDPP 109
Cdd:cd10559     1 SFLIDTTRCTACRGCQVACKQWN--QLPAEQTKNTGSHQNPpdlSANTYKLVRFNEVrNENGKPDWLFFPDQCRHCVTPP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 110 CVPVCP--TGASYKRKEDGIVL-------VDYDKCIGckycawACPYGARELDEERQVMTKCTLCVDRIydeqlpKEDRK 180
Cdd:cd10559    79 CKDAADmvPGAVIQDEATGAVVftektaeLDFDDVLS------ACPYNIPRKNEATGRIVKCDMCIDRV------SNGLQ 146

                         170       180       190
                  ....*....|....*....|....*....|
gi 2279651085 181 PACVKACPTGARIFGDVKDPDSEVSKAIRE 210
Cdd:cd10559   147 PACVKACPTGAMNFGDRDEMLAMASKRLEE 176
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 31-230 1.73e-21

Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate reductase (SER), a member of the DMSO reductase family. SER catalyzes the reduction of selenate to selenite in bacterial species that can obtain energy by respiring anaerobically with selenate as the terminal electron acceptor. The enzyme comprises three subunits SerABC, forming a heterotrimer, with the catalytic component (alpha-subunit), iron-sulfur protein (beta-subunit) and monomeric b-type heme-containing gamma subunit. Beta subunit contains coordinating one [3Fe-4S] cluster and three [4Fe-4S] clusters and functions as electron carrier.


Pssm-ID: 319878 [Multi-domain]  Cd Length: 287  Bit Score: 90.21  E-value: 1.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  31 KQLALVIDLNVCVGCHACVTSCKQWNTSGSAGPL-----ADERPYAANPTG----TFFNR--VQTYEAGAF--------- 90
Cdd:cd10556    10 KQFAMVFDTNKCIACQTCTMACKSTWTSGKGQEYmwwnnVETKPYGGYPLGwdvrLLDEEggQTWAEGGVYegktifeaa 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  91 ----------------------------PVTETIHF------------PKSCLHCEDPPCVPVCPTGASYKRKEDGIVLV 130
Cdd:cd10556    90 aageqvlgyrpededwrypnigedevngERTPDTGSslpphpiwffylPRICNHCTYPACLAACPRKAIYKREEDGIVLI 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 131 DYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCVDRIydeqlpKEDRKPACVKACPTGARIFGDVKDPDSEVSKAIRE 210
Cdd:cd10556   170 DQERCRGYRECVEACPYKKPMYNPTTRVSEKCIGCYPRI------EEGDQTQCVSACIGKIRLQGFINTPPDARWADDRD 243

                         250       260       270
                  ....*....|....*....|....*....|
gi 2279651085 211 RGGY----------QLMPEWETSPANQYLP 230
Cdd:cd10556   244 NPIDflvhikkvalPLYPQFGTEPNVYYIP 273
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 42-243 8.76e-21

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 90.58  E-value: 8.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  42 CVGCHACVTSCKQWNTSGSAgPLADERpyaanptgtFFNRVQTYEAGAfpvtetIHFPKSCLHCEDPPCVPVCPTGAsYK 121
Cdd:PRK12769   12 CLGCHACEIACVMAHNDEQH-VLSQHH---------FHPRITVIKHQQ------QRSAVTCHHCEDAPCARSCPNGA-IS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 122 RKEDGIVLVDyDKCIGCKYCAWACPYGAREL-------DEERQVMTKCTLCVDRiydeqlpkeDRKPACVKACPTGARIF 194
Cdd:PRK12769   75 HVDDSIQVNQ-QKCIGCKSCVVACPFGTMQIvltpvaaGKVKATAHKCDLCAGR---------ENGPACVENCPADALQL 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2279651085 195 GDvKDPDSEVSKAIRERGGYQLMPEWETS-PANQYLPRHITQAPQATDAR 243
Cdd:PRK12769  145 VT-EQALSGMAKSRRLRTARQEHQPWHAStAAQEMPAMSKVEQMQATPPR 193
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 99-187 1.12e-19

beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes nitrate reductase A, a member of the DMSO reductase family. The respiratory nitrate reductase complex (NarGHI) from E. coli is a heterotrimer, with the catalytic subunit (NarG) with a molybdo-bis (molybdopterin guanine dinucleotide) cofactor and an [Fe-S] cluster, the electron transfer subunit (NarH) with four [Fe-S] clusters, and the integral membrane subunit (NarI) with two b-type hemes. Nitrate reductase A often forms a respiratory chain with the formate dehydrogenase via the lipid soluble quinol pool. Electron transfer from formate to nitrate is coupled to proton translocation across the cytoplasmic membrane generating proton motive force by a redox loop mechanism. Demethylmenaquinol (DMKH2) has been shown to be a good substrate for NarGHI in nitrate respiration in E. coli.


Pssm-ID: 319879 [Multi-domain]  Cd Length: 363  Bit Score: 86.65  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  99 PKSCLHCEDPPCVPVCPTGASYKRKEDGIVLVDYDKCIGCKYCAWACPY---------GAREldeerqvmtKCTLCVDRI 169
Cdd:cd10557   176 PRICNHCLNPACVAACPSGAIYKREEDGIVLIDQDRCRGWRMCVSACPYkkvyynwktGKSE---------KCIFCYPRL 246

                          90
                  ....*....|....*...
gi 2279651085 170 YDEQlpkedrKPACVKAC 187
Cdd:cd10557   247 EAGQ------PTVCSETC 258
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 97-169 5.29e-19

Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 440755 [Multi-domain]  Cd Length: 485  Bit Score: 85.24  E-value: 5.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  97 HFPKSCLHCEDPPCVPVCPTGASYKRKEDGIVLVDYDKCIGCKYCAWACPY---------GAREldeerqvmtKCTLCVD 167
Cdd:COG1140   177 YLPRICEHCLNPACVASCPSGAIYKREEDGIVLVDQDKCRGWRMCVSGCPYkkvyfnwktGKAE---------KCIFCYP 247


                  ..
gi 2279651085 168 RI 169
Cdd:COG1140   248 RI 249
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 35-213 5.32e-17

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 79.68  E-value: 5.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  35 LVIDLNVCVGCHACVTSC------KQWNTSGSagplaDERPYaanpTGTFFNRVQTYeagafpvtetihfPKSCLHCEDP 108
Cdd:PRK12809    5 IAAEAAECIGCHACEIACavahnqENWPLSHS-----DFRPR----IHVVGKGQAAN-------------PVACHHCNNA 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 109 PCVPVCPTGASYKRKEDgiVLVDYDKCIGCKYCAWACPYGARELDEerQVMTKCTLCVDRIYDEQlpkedrkpACVKACP 188
Cdd:PRK12809   63 PCVTACPVNALTFQSDS--VQLDEQKCIGCKRCAIACPFGVVEMVD--TIAQKCDLCNQRSSGTQ--------ACIEVCP 130

                         170       180
                  ....*....|....*....|....*.
gi 2279651085 189 TGA-RIFGDVKDPDSEVSKAIRERGG 213
Cdd:PRK12809  131 TQAlRLMDDKGLQQIKVARQRKTAAG 156
PRK10330 PRK10330
electron transport protein HydN;
35-193 6.29e-16

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 73.00  E-value: 6.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  35 LVIDLNVCVGCHACVTSCKQWNTsgsagplaDERPYAANPTGTFFNRVQTYEaGAFPVTETIhfpksCLHCEDPPCVPVC 114
Cdd:PRK10330    5 IIADASKCIGCRTCEVACVVSHQ--------ENQDCASLTPETFLPRIHVIK-GVNVSTATV-----CRQCEDAPCANVC 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 115 PTGASykRKEDGIVLVDYDKCIGCKYCAWACPYGAREL---------------DEERQVMTKCTLCVDRiydeqlpkeDR 179
Cdd:PRK10330   71 PNGAI--SRDKGFVHVMQERCIGCKTCVVACPYGAMEVvvrpvirnsgaglnvRAEKAEANKCDLCNHR---------ED 139

                         170
                  ....*....|....
gi 2279651085 180 KPACVKACPTGARI 193
Cdd:PRK10330  140 GPACMAACPTHALI 153
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 36-190 3.68e-15

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


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 69.61  E-value: 3.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  36 VIDLNVCVGCHACVTSC-KQWNTSGSAGPLAderpyaanptgtffNRVQTYE--AGAFPVTetihfpkSCLHCEDPPCVP 112
Cdd:cd16370     5 VKDMERCIGCYSCMLACsRRVHKSASLSKSA--------------IRVRTRGglEGGFTVV-------VCRACEDPPCAE 63

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2279651085 113 VCPTGASYKRKEDGIVLvDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCvdriydeqlpkedrkPACVKACPTG 190
Cdd:cd16370    64 ACPTGALEPRKGGGVVL-DKEKCIGCGNCVKACIVGAIFWDEETNKPIICIHC---------------GYCARYCPHD 125
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 35-191 3.60e-13

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


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 64.28  E-value: 3.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  35 LVIDLNVCVGCHACVTSCKQwntsgsagpladerpyaanptgTFFnRVQTYEAGAFPVTETIHFPK--SCLHCEDppCVP 112
Cdd:cd16372     3 LVTDPEKCIGCLQCEEACSK----------------------TFF-KEEDREKSCIRITETEGGYAinVCNQCGE--CID 57

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2279651085 113 VCPTGASYKRKEdGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCvdriydeqlpkedrkPACVKACPTGA 191
Cdd:cd16372    58 VCPTGAITRDAN-GVVMINKKLCVGCLMCVGFCPEGAMFKHEDYPEPFKCIAC---------------GICVKACPTGA 120
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 96-191 7.99e-10

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: 55.10  E-value: 7.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  96 IHFPKSCLHCEDppCVPVCPTGASYKRKEDGIVL---VDYDKCIGCKYCAWACPYGARELDEERQVMTK----------- 161
Cdd:cd10549     2 KYDPEKCIGCGI--CVKACPTDAIELGPNGAIARgpeIDEDKCVFCGACVEVCPTGAIELTPEGKEYVPkekeaeideek 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2279651085 162 ---CTLCVD-------RIYDEQLPKEDRKP-----ACVKACPTGA 191
Cdd:cd10549    80 cigCGLCVKvcpvdaiTLEDELEIVIDKEKcigcgICAEVCPVNA 124
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
99-155 2.40e-09

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 52.43  E-value: 2.40e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2279651085  99 PKSCLHCEDppCVPVCPTGASYKrkEDGIVLVDYDKCIGCKYCAWACPYGARELDEE 155
Cdd:COG2768    10 EEKCIGCGA--CVKVCPVGAISI--EDGKAVIDPEKCIGCGACIEVCPVGAIKIEWE 62
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 101-155 1.01e-08

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 55.27  E-value: 1.01e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2279651085 101 SCLHC-EDPPCVPVCPTGASYKRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEE 155
Cdd:PRK12771  508 SCGNCfECDNCYGACPQDAIIKLGPGRRYHFDYDKCTGCHICADVCPCGAIEMGPG 563
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
130-191 1.35e-08

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 54.87  E-value: 1.35e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2279651085 130 VDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCvdriydeqlpkeDRKPACVKACPTGA 191
Cdd:COG1148   493 VDPEKCTGCGRCVEVCPYGAISIDEKGVAEVNPALC------------KGCGTCAAACPSGA 542
FeFe_hydrog_B1 TIGR04105
[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups.
 109-149 2.89e-08

[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups.


Pssm-ID: 274983 [Multi-domain]  Cd Length: 462  Bit Score: 53.75  E-value: 2.89e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2279651085 109 PCVPVCPTGAsYKRKEDGIVLVDYDKCIGCKYCAWACPYGA 149
Cdd:TIGR04105 165 PCEKACPVGA-ISSDEDGRAVIDYDKCISCGACMVACPFGA 204
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 110-156 1.51e-07

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 47.42  E-value: 1.51e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2279651085 110 CVPVCPTGAsYKRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEER 156
Cdd:COG1149    19 CVEVCPEGA-IKLDDGGAPVVDPDLCTGCGACVGVCPTGAITLEERE 64
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
110-191 4.12e-07

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 49.68  E-value: 4.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 110 CVPVCPTGASY---KRKEDGIVLVDYDKCIGCKYCAWACPYGArELDEERQVMTKCTLCVDriydeqlpkedrkpaCVKA 186
Cdd:COG0348   184 CRYLCPYGAFQgllSDLSTLRVRYDRGDCIDCGLCVKVCPMGI-DIRKGEINQSECINCGR---------------CIDA 247


                  ....*
gi 2279651085 187 CPTGA 191
Cdd:COG0348   248 CPKDA 252
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 127-191 5.34e-07

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 45.87  E-value: 5.34e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2279651085 127 IVLVDYDKCIGCKYCAWACPYGARELDEERQVM---TKCTLCVdriydeqlpkedrkpACVKACPTGA 191
Cdd:COG1149     5 IPVIDEEKCIGCGLCVEVCPEGAIKLDDGGAPVvdpDLCTGCG---------------ACVGVCPTGA 57
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
123-201 7.05e-07

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 45.49  E-value: 7.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 123 KEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMT--KCTLCvdriydeqlpkedrkPACVKACPTGARIFGDVKDP 200
Cdd:COG2768     1 HSLGKPYVDEEKCIGCGACVKVCPVGAISIEDGKAVIDpeKCIGC---------------GACIEVCPVGAIKIEWEEDE 65


                  .
gi 2279651085 201 D 201
Cdd:COG2768    66 E 66
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 110-158 7.62e-07

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 45.43  E-value: 7.62e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2279651085 110 CVPVCPTGASykRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQV 158
Cdd:COG2221    23 CVAVCPTGAI--SLDDGKLVIDEEKCIGCGACIRVCPTGAIKGEKPKKF 69
NapF COG1145
Ferredoxin [Energy production and conversion];
99-191 8.18e-07

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 48.57  E-value: 8.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  99 PKSCLHCEDPPCVPVCPTGASYKRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMT----KCTLCvdriydeql 174
Cdd:COG1145   148 GAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVCPTGAIRLKDGKPQIVvdpdKCIGC--------- 218

                          90
                  ....*....|....*..
gi 2279651085 175 pkedrkPACVKACPTGA 191
Cdd:COG1145   219 ------GACVKVCPVGA 229
FixX COG2440
Ferredoxin-like protein FixX [Energy production and conversion];
104-149 8.34e-07

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


Pssm-ID: 441981 [Multi-domain]  Cd Length: 87  Bit Score: 45.96  E-value: 8.34e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2279651085 104 HCEDPPCVPVCPTGAsYKRKEDGIVLVDYDKCIGCKYCAWACPYGA 149
Cdd:COG2440    26 RCLAKPCTRYCPAGV-YEIVGDGRLQINYENCLECGTCRIKCPTQN 70
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
102-211 1.09e-06

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 48.87  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 102 CLHCEDPPCVPVCPTGAsyKRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVM--TKCTLCvdriydeqlpkedr 179
Cdd:COG4624    62 CRCCVAISCIQVRGIII--IDKRGPSIIRDKEKCKNCYPCVRACPVKAIKVDDGKAEIdeEKCISC-------------- 125

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2279651085 180 kPACVKACPTGARIfgdVKDPDSEVSKAIRER 211
Cdd:COG4624   126 -GQCVAVCPFGAIT---EKSDIEKVKKALKDP 153
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 126-191 1.49e-06

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 44.70  E-value: 1.49e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2279651085 126 GIVLVDYDKCIGCKYCAWACPYGARELDEERQVMT-----KCTLCvdriydeqlpkedrkPACVKACPTGA 191
Cdd:COG1146     1 MMPVIDTDKCIGCGACVEVCPVDVLELDEEGKKALvinpeECIGC---------------GACELVCPVGA 56
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
95-150 1.57e-06

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 48.48  E-value: 1.57e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2279651085  95 TIHFPKSCLHCEdpPCVPVCPTGASykRKEDGIVLVDYDKCIGCKYCAWACPYGAR 150
Cdd:COG4624    86 IIRDKEKCKNCY--PCVRACPVKAI--KVDDGKAEIDEEKCISCGQCVAVCPFGAI 137
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 102-155 1.85e-06

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: 44.66  E-value: 1.85e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2279651085 102 CLHCEdpPCVPVCPTGAsYKRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEE 155
Cdd:COG1144    32 CIGCG--LCWIVCPDGA-IRVDDGKYYGIDYDYCKGCGICAEVCPVKAIEMVPE 82
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 39-189 3.06e-06

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: 45.71  E-value: 3.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  39 LNVCVGCHACVTSCkqwntsgsagpladerpyaanPTGTFfnRVQTYEAGAFPV-TETIHFPKS-CLHCEDPpCVPVCPT 116
Cdd:cd16373    13 LALCIRCGLCVEAC---------------------PTGVI--QPAGLEDGLEGGrTPYLDPREGpCDLCCDA-CVEVCPT 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 117 GA-SYKRKED-----GIVLVDYDKCI------GCKYCAWACPYGARELDEERQVM------TKCTLCvdriydeqlpked 178
Cdd:cd16373    69 GAlRPLDLEEqkvkmGVAVIDKDRCLawqggtDCGVCVEACPTEAIAIVLEDDVLrpvvdeDKCVGC------------- 135

                         170
                  ....*....|.
gi 2279651085 179 rkPACVKACPT 189
Cdd:cd16373   136 --GLCEYVCPV 144
NapF COG1145
Ferredoxin [Energy production and conversion];
99-155 4.58e-06

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 46.25  E-value: 4.58e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2279651085  99 PKSCLHCEdpPCVPVCPTGASYKRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEE 155
Cdd:COG1145   181 AEKCIGCG--LCVKVCPTGAIRLKDGKPQIVVDPDKCIGCGACVKVCPVGAISLEPK 235
napG PRK09476
quinol dehydrogenase periplasmic component; Provisional
 23-146 1.20e-05

quinol dehydrogenase periplasmic component; Provisional


Pssm-ID: 236534 [Multi-domain]  Cd Length: 254  Bit Score: 45.00  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  23 AAQGETLAKQLAL----VID----LNVCVGCHACVTSCKqWNTsgsagpLADERPYAANPTGTFFnrvqtYEAGAFPvte 94
Cdd:PRK09476   34 LQQQQARASGVALrppgALNendfLSACIRCGLCVQACP-YDT------LKLATLASGLSAGTPY-----FVARDIP--- 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2279651085  95 tihfpksCLHCEDPPCVPVCPTGASYKRKED------GI-VLVDYDKCIG-----CKYCAWACP 146
Cdd:PRK09476   99 -------CEMCEDIPCVKACPSGALDRELVDiddarmGLaVLVDQENCLNfqglrCDVCYRVCP 155
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 133-191 1.23e-05

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 42.04  E-value: 1.23e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2279651085 133 DKCIGCKYCAWACPYGARELDEERQV------MTKCTLCVdriydeqlpkedrkpACVKACPTGA 191
Cdd:COG1143     2 DKCIGCGLCVRVCPVDAITIEDGEPGkvyvidPDKCIGCG---------------LCVEVCPTGA 51
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
122-191 1.70e-05

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 43.72  E-value: 1.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 122 RKEDGivlvdYDKCIGCKYCAWACP------YGARELDEERQV------MTKCTLCvdriydeQLpkedrkpaCVKACPT 189
Cdd:PRK05888   52 RDPNG-----EERCIACKLCAAICPadaitiEAAEREDGRRRTtrydinFGRCIFC-------GF--------CEEACPT 111


                  ..
gi 2279651085 190 GA 191
Cdd:PRK05888  112 DA 113
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
110-157 2.12e-05

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 42.24  E-value: 2.12e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2279651085 110 CVPVCPTGASYKrKEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQ 157
Cdd:PRK09623   59 CWKFCPEPAIYI-KEDGYVAIDYDYCKGCGICANECPTKAITMVKEEK 105
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 99-149 2.97e-05

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 40.85  E-value: 2.97e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2279651085  99 PKSCLHCEDppCVPVCPTGAsYKRKEDGI--VLVDYDKCIGCKYCAWACPYGA 149
Cdd:COG1146     7 TDKCIGCGA--CVEVCPVDV-LELDEEGKkaLVINPEECIGCGACELVCPVGA 56
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 102-154 3.49e-05

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 40.88  E-value: 3.49e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2279651085 102 CLHCEDppCVPVCPTGASY--KRKEDGIVLVDYDKCIGCKYCAWACPYGARELDE 154
Cdd:COG1143     4 CIGCGL--CVRVCPVDAITieDGEPGKVYVIDPDKCIGCGLCVEVCPTGAISMTP 56
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
110-149 4.89e-05

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 44.08  E-value: 4.89e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2279651085 110 CVPVCPTGAsYKRKEDGIVLVDYDKCIGCKYCAWACPYGA 149
Cdd:COG1148   504 CVEVCPYGA-ISIDEKGVAEVNPALCKGCGTCAAACPSGA 542
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 128-191 5.30e-05

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 40.41  E-value: 5.30e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2279651085 128 VLVDYDKCIGCKYCAWACPYGARELDEERQV--MTKCTLCVdriydeqlpkedrkpACVKACPTGA 191
Cdd:COG4231    17 YVIDEDKCTGCGACVKVCPADAIEEGDGKAVidPDLCIGCG---------------SCVQVCPVDA 67
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 102-155 6.27e-05

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 40.41  E-value: 6.27e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2279651085 102 CLHCEDppCVPVCPTGAsyKRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEE 155
Cdd:COG4231    24 CTGCGA--CVKVCPADA--IEEGDGKAVIDPDLCIGCGSCVQVCPVDAIKLEKR 73
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
101-191 6.33e-05

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 43.00  E-value: 6.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 101 SCLHCEDppCVPVCPTGASykRKEDGIVLVDYDKCIGCKYCAWACPYGAREL-DEERQVMTKCTlcvdriyDEQLPKEDR 179
Cdd:PRK07118  140 GCLGLGS--CVAACPFDAI--HIENGLPVVDEDKCTGCGACVKACPRNVIELiPKSARVFVACN-------SKDKGKAVK 208

                          90       100
                  ....*....|....*....|.
gi 2279651085 180 KP---------ACVKACPTGA 191
Cdd:PRK07118  209 KVcevgcigcgKCVKACPAGA 229
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 133-191 9.09e-05

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: 42.54  E-value: 9.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085 133 DKCIGCKYCAWACPYGARELDEERQV-MTKCTLCVdriydeqlpkedrkpACVKACPTGA 191
Cdd:NF038196  185 DKCIGCGICAKVCPVNNIEMEDGKPVwGHNCTHCL---------------ACIHRCPKEA 229
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 99-146 9.22e-05

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: 39.16  E-value: 9.22e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2279651085  99 PKSCLHCEDppCVPVCPT-----GASYKRKEDGIVLVDYDKCIGCKYCAWACP 146
Cdd:pfam13237   6 PDKCIGCGR--CTAACPAgltrvGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 130-191 1.04e-04

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 39.65  E-value: 1.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2279651085 130 VDYDKCIGCKYCAWACPYGARELDEERQV--MTKCTLCvdriydeqlpkedrkPACVKACPTGA 191
Cdd:COG2221    12 IDEEKCIGCGLCVAVCPTGAISLDDGKLVidEEKCIGC---------------GACIRVCPTGA 60
PRK00783 PRK00783
DNA-directed RNA polymerase subunit D; Provisional
 96-155 1.30e-04

DNA-directed RNA polymerase subunit D; Provisional


Pssm-ID: 234837 [Multi-domain]  Cd Length: 263  Bit Score: 42.18  E-value: 1.30e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  96 IHFPKSCLHCEDppCVPVCPTGAsYKRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEE 155
Cdd:PRK00783  165 IEVSEDCDECEK--CVEACPRGV-LELKEGKLVVTDLLNCSLCKLCERACPGKAIRVSDD 221
PRK13795 PRK13795
hypothetical protein; Provisional
 110-146 1.74e-04

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 42.29  E-value: 1.74e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2279651085 110 CVPVCPTGASYKRKEDGIVLVDYDKCIGCKYCAWACP 146
Cdd:PRK13795  589 CVGACPTGAIRIEEGKRKISVDEEKCIHCGKCTEVCP 625
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 102-146 1.85e-04

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


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 41.52  E-value: 1.85e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2279651085 102 CLHCEDppCVPVCPTGASYKrKEDGIVLVDYDKCIGCKYCAWACP 146
Cdd:COG2878   139 CIGCGD--CIKACPFDAIVG-AAKGMHTVDEDKCTGCGLCVEACP 180
Fer COG1141
Ferredoxin [Energy production and conversion];
128-191 1.89e-04

Ferredoxin [Energy production and conversion];


Pssm-ID: 440756 [Multi-domain]  Cd Length: 63  Bit Score: 38.71  E-value: 1.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2279651085 128 VLVDYDKCIGCKYCAWACPyGARELDEERQVmtkctlcvdRIYDEQLPKEDRKPA--CVKACPTGA 191
Cdd:COG1141     3 VTVDRDTCIGCGLCVALAP-EVFELDDDGKA---------VVLDEEVPEELEEDVreAADACPVGA 58
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 130-191 2.05e-04

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: 38.88  E-value: 2.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2279651085 130 VDYDKCIGCKYCAWACPYGARELDEERQV---MTKCTLCvdriydeqlpkedrkPACVKACPTGA 191
Cdd:COG1144    27 VDEDKCIGCGLCWIVCPDGAIRVDDGKYYgidYDYCKGC---------------GICAEVCPVKA 76
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 128-151 2.81e-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: 37.23  E-value: 2.81e-04
                          10        20
                  ....*....|....*....|....
gi 2279651085 128 VLVDYDKCIGCKYCAWACPYGARE 151
Cdd:pfam00037   1 VVIDEEKCIGCGACVEVCPVGAIT 24
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 102-149 3.12e-04

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 37.51  E-value: 3.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2279651085 102 CLHCEDppCVPVCPTGA-----SYKRKEDGIVLVDYDKCIGCKYCAWACPYGA 149
Cdd:pfam12838   1 CIGCGA--CVAACPVGAitldeVGEKKGTKTVVIDPERCVGCGACVAVCPTGA 51
porD PRK09625
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
 56-146 3.25e-04

pyruvate flavodoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 236596 [Multi-domain]  Cd Length: 133  Bit Score: 39.73  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651085  56 NTSGSAGPLADERPYAANPTgtffnrvQTYEAGAFPVTETIHFPKSCLHCEDppCVPVCPTgASYKRKEDGIVLVDYDKC 135
Cdd:PRK09625   22 NAQSEMEKHNEERHYTEQSS-------FTTSVAHWRVEKPVHNNEICINCFN--CWVYCPD-AAILSRDKKLKGVDYSHC 91

                          90
                  ....*....|.
gi 2279651085 136 IGCKYCAWACP 146
Cdd:PRK09625   92 KGCGVCVEVCP 102
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 126-191 3.46e-04

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 39.43  E-value: 3.46e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2279651085 126 GIVLVDYDKCIGCKYCAWACPYGARE-LDEERQVMTKCTLCVdriYDEQlpkedrkpaCVKACPTGA 191
Cdd:PRK08348   35 GKILYDVDKCVGCRMCVTVCPAGVFVyLPEIRKVALWTGRCV---FCGQ---------CVDVCPTGA 89
Fer4_6 pfam12837
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 127-149 5.50e-04

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: 36.44  E-value: 5.50e-04
                          10        20
                  ....*....|....*....|...
gi 2279651085 127 IVLVDYDKCIGCKYCAWACPYGA 149
Cdd:pfam12837   1 VVEVDPDKCIGCGRCVVVCPYGA 23
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 99-155 8.70e-04

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: 40.15  E-value: 8.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2279651085  99 PKSCLHcedpPCVPVCP---TG--ASYKRKEDGIVLVDYDKCIGCKYCAWACPYGA-------RELDEE 155
Cdd:COG1245    14 PKKCNY----ECIKYCPvnrTGkeAIEIDEDDGKPVISEELCIGCGICVKKCPFDAisivnlpEELEED 78
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 135-191 8.81e-04

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 36.35  E-value: 8.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2279651085 135 CIGCKYCAWACPYGARELDEERQV---------MTKCTLCvdriydeqlpkedrkPACVKACPTGA 191
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKkgtktvvidPERCVGC---------------GACVAVCPTGA 51
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 133-191 2.77e-03

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


Pssm-ID: 273902 [Multi-domain]  Cd Length: 122  Bit Score: 36.62  E-value: 2.77e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2279651085 133 DKCIGCKYCAWACPYGARELDEER-----------QV-MTKCTLCvdriydeqlpkedrkPACVKACPTGA 191
Cdd:TIGR01971  43 EKCIGCTLCAAVCPADAIRVVPAEgedgkrrlkfyEInFGRCIFC---------------GLCEEACPTDA 98
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
127-191 3.46e-03

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 36.56  E-value: 3.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2279651085 127 IVLVDYDKCIGCKYCAWACPYGARELD-------------EERQVMTKCTLCVDRiydeqlpkedrkpACVKACPTGA 191
Cdd:COG1142     4 FIIADPEKCIGCRTCEAACAVAHEGEEgepflprirvvrkAGVSAPVQCRHCEDA-------------PCAEVCPVGA 68
Fer4_9 pfam13187
4Fe-4S dicluster domain;
134-191 4.03e-03

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 34.45  E-value: 4.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2279651085 134 KCIGCKYCAWACPYGARELDEERQVM------TKCTLCVdriydeqlpkedrkpACVKACPTGA 191
Cdd:pfam13187   1 KCTGCGACVAACPAGAIVPDLVGQTIrgdiagLACIGCG---------------ACVDACPRGA 49
Fer4_2 pfam12797
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 126-147 5.14e-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: 463711 [Multi-domain]  Cd Length: 22  Bit Score: 33.53  E-value: 5.14e-03
                          10        20
                  ....*....|....*....|..
gi 2279651085 126 GIVLVDYDKCIGCKYCAWACPY 147
Cdd:pfam12797   1 WKPLIDADKCIGCGACVSACPA 22
PRK06273 PRK06273
ferredoxin; Provisional
 98-146 5.39e-03

ferredoxin; Provisional


Pssm-ID: 235764 [Multi-domain]  Cd Length: 165  Bit Score: 36.61  E-value: 5.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2279651085  98 FPKSCLHCEDppCVPVCPTGA-------------SYKRKEdgIVLVDYDKCIGCKYCAWACP 146
Cdd:PRK06273   47 FEELCIGCGG--CANVCPTKAiemipvepvkiteGYVKTK--IPKIDYEKCVYCLYCHDFCP 104
porD PRK09624
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
 110-155 5.43e-03

pyruvate ferredoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 170017 [Multi-domain]  Cd Length: 105  Bit Score: 35.77  E-value: 5.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2279651085 110 CVPVCPTGASYkRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEE 155
Cdd:PRK09624   59 CYIYCPEPAIY-LDEEGYPVFDYDYCKGCGICANECPTKAIEMVRE 103
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
110-166 6.94e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 36.83  E-value: 6.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2279651085 110 CVPVCPTGASykRKEDGIVLVDYDKCIGCKYCAWACPYGARELDEERQVMTKCTLCV 166
Cdd:PRK07118  221 CVKACPAGAI--TMENNLAVIDQEKCTSCGKCVEKCPTKAIRILNKPPKVKEPKKAA 275
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
99-155 9.93e-03

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 36.71  E-value: 9.93e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2279651085  99 PKSCLHcedpPCVPVCP---TG--ASYKRKEDGIVLVDYDKCIGCKYCAWACPYGA-------RELDEE 155
Cdd:PRK13409   14 PKKCNY----ECIKYCPvvrTGeeTIEIDEDDGKPVISEELCIGCGICVKKCPFDAisivnlpEELEEE 78
 
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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