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Conserved domains on  [gi|446615323|ref|WP_000692669|]
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MULTISPECIES: nitrate reductase subunit beta [Bacillus]

Protein Classification

nitrate reductase subunit beta( domain architecture ID 11439033)

nitrate reductase subunit beta is a component of nitrate reductase enzyme complex that allows bacteria to use nitrate as an electron acceptor during anaerobic growth

Gene Ontology:  GO:0016020|GO:0009055|GO:0008940|GO:0051539|GO:0046872|GO:0051538|GO:0009061|GO:0042128
PubMed:  12910261|15772287

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 1-483 0e+00

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


:

Pssm-ID: 440755 [Multi-domain]  Cd Length: 485  Bit Score: 1047.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323   1 MKIKAQVGMVMNLDKCIGCHTCSVTCKNTWTNRPGAEYMYFNNVETKPGIGYPKQWEDQEKYKGGWEL-KNGEIQLKSGS 79
Cdd:COG1140    1 MKVRAQIAMVMNLDKCIGCHTCSVTCKNVWTNREGVEYMWFNNVETKPGIGYPKRWEDQEKWKGGWELdRNGKLRLRAGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323  80 KMKRLMNIFHNPDQPTIDDYFEPWNYDYETLTNSPQRKHQPVARPKSAITGEFIdKIEWGPNWEDDLAGGHITGLQDPNV 159
Cdd:COG1140   81 RLKKLANIFANPDLPEIDDYYEPWTYDYENLINAPEGDDQPVARPRSLITGEPM-KIEWGPNWDDDLGGSFEYASKDPNL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 160 KKMEEEIKTDFENVFMMYLPRICEHCMNPSCVSSCPSGAMYKREEDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKA 239
Cdd:COG1140  160 EGLQEEIYFEFENTFMFYLPRICEHCLNPACVASCPSGAIYKREEDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGKA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 240 EKCTMCFPRIEAGMPTICSETCVGRIRYIGVMLYDADKVKEAASVEDEKDLYESQLTVFLDPNDPEVAAEAKKQGIPEEW 319
Cdd:COG1140  240 EKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADRVEEAASVPDEQDLYEAQLDVFLDPHDPEVIAAARKDGIPDDW 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 320 IKAAQESPIYKMIIDWKIALPLHPEYRTMPMVWYIPPLSPIMNMVEGKGSNWQAEAIFPAIDNMRIPIQYLANLLTAGDE 399
Cdd:COG1140  320 IEAAQRSPVYKLAKEWKVALPLHPEYRTLPMVWYVPPLSPVVDAVEAGGHDGDADGLFPAIDSLRIPVEYLANLFTAGDE 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 400 SHIRLTLKKMAVMRTHMRALQINKEPNEAVLKELGLTKQDVEDMYRLLAIAKYKDRFVIPGTHREQVADLYSEQGSCGLA 479
Cdd:COG1140  400 EPVEAALRRLAAMRAYMRAKNVGGEPDEEILAAVGLTEEQAEEMYRLLAIAKYEDRFVIPTAHREQAEDLYELQGGCGFD 479


                 ....
gi 446615323 480 FAGG 483
Cdd:COG1140  480 FGGG 483
 
Name Accession Description Interval E-value
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 1-483 0e+00

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


Pssm-ID: 440755 [Multi-domain]  Cd Length: 485  Bit Score: 1047.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323   1 MKIKAQVGMVMNLDKCIGCHTCSVTCKNTWTNRPGAEYMYFNNVETKPGIGYPKQWEDQEKYKGGWEL-KNGEIQLKSGS 79
Cdd:COG1140    1 MKVRAQIAMVMNLDKCIGCHTCSVTCKNVWTNREGVEYMWFNNVETKPGIGYPKRWEDQEKWKGGWELdRNGKLRLRAGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323  80 KMKRLMNIFHNPDQPTIDDYFEPWNYDYETLTNSPQRKHQPVARPKSAITGEFIdKIEWGPNWEDDLAGGHITGLQDPNV 159
Cdd:COG1140   81 RLKKLANIFANPDLPEIDDYYEPWTYDYENLINAPEGDDQPVARPRSLITGEPM-KIEWGPNWDDDLGGSFEYASKDPNL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 160 KKMEEEIKTDFENVFMMYLPRICEHCMNPSCVSSCPSGAMYKREEDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKA 239
Cdd:COG1140  160 EGLQEEIYFEFENTFMFYLPRICEHCLNPACVASCPSGAIYKREEDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGKA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 240 EKCTMCFPRIEAGMPTICSETCVGRIRYIGVMLYDADKVKEAASVEDEKDLYESQLTVFLDPNDPEVAAEAKKQGIPEEW 319
Cdd:COG1140  240 EKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADRVEEAASVPDEQDLYEAQLDVFLDPHDPEVIAAARKDGIPDDW 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 320 IKAAQESPIYKMIIDWKIALPLHPEYRTMPMVWYIPPLSPIMNMVEGKGSNWQAEAIFPAIDNMRIPIQYLANLLTAGDE 399
Cdd:COG1140  320 IEAAQRSPVYKLAKEWKVALPLHPEYRTLPMVWYVPPLSPVVDAVEAGGHDGDADGLFPAIDSLRIPVEYLANLFTAGDE 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 400 SHIRLTLKKMAVMRTHMRALQINKEPNEAVLKELGLTKQDVEDMYRLLAIAKYKDRFVIPGTHREQVADLYSEQGSCGLA 479
Cdd:COG1140  400 EPVEAALRRLAAMRAYMRAKNVGGEPDEEILAAVGLTEEQAEEMYRLLAIAKYEDRFVIPTAHREQAEDLYELQGGCGFD 479


                 ....
gi 446615323 480 FAGG 483
Cdd:COG1140  480 FGGG 483
narH TIGR01660
nitrate reductase, beta subunit; The Nitrate reductase enzyme complex allows bacteria to use ...
 1-486 0e+00

nitrate reductase, beta subunit; The Nitrate reductase enzyme complex allows bacteria to use nitrate as an electron acceptor during anaerobic growth. The enzyme complex consists of a tetramer that has an alpha, beta and 2 gamma subunits. The alpha and beta subunits have catalytic activity and the gamma subunits attach the enzyme to the membrane and is a b-type cytochrome that receives electrons from the quinone pool and transfers them to the beta subunit. This model is specific for the beta subunit for nitrate reductase I (narH) and nitrate reductase II (narY) for gram positive and gram negative bacteria.A few thermophiles and archaea also match the model.The seed members used in this model are all experimentally characterized and include the following:SP:P11349, and SP:P19318, both E.Coli (NarH and NarY respectively), SP:P42176 from B. Subtilis, GP:11344602 from Psuedomonas fluorescens,GP:541762 from Paracoccus denitrificans, and GP:18413622 from Halomonas halodenitrificans. This model also matches Pfam pfam00037 for 4Fe-4S binding domain. [Energy metabolism, Anaerobic]


Pssm-ID: 211677 [Multi-domain]  Cd Length: 492  Bit Score: 905.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323    1 MKIKAQVGMVMNLDKCIGCHTCSVTCKNTWTNRPGAEYMYFNNVETKPGIGYPKQWEDQEKYKGGWELK-NGEIQLKSGS 79
Cdd:TIGR01660   1 MKIRSQIGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGIGYPKDWENQDKYKGGWVRKrDGKLEPRIGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323   80 KMKRLMNIFHNPDQPTIDDYFEPWNYDYETLTNSPQRKHQPVARPKSAITGEFIDKIEWGPNWEDDLAGGHITGLQDPNV 159
Cdd:TIGR01660  81 KWRVLANIFANPDLPSIDDYYEPFDFDYQHLHTAPEGKHQPTARPRSLITGERMEKIEWGPNWEDDLGGEFAKRRKDKNF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323  160 KKMEEEIKTDFENVFMMYLPRICEHCMNPSCVSSCPSGAMYKREEDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKA 239
Cdd:TIGR01660 161 DKIQKDIYGEFENTFMMYLPRLCEHCLNPACVASCPSGAIYKREEDGIVLIDQDKCRGWRMCISGCPYKKIYFNWKTGKS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323  240 EKCTMCFPRIEAGMPTICSETCVGRIRYIGVMLYDADKVKEAASVEDEKDLYESQLTVFLDPNDPEVAAEAKKQGIPEEW 319
Cdd:TIGR01660 241 EKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADKIEEAASTENEKDLYHRQLDVFLDPNDPEVIAQAKKDGIPLSV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323  320 IKAAQESPIYKMIIDWKIALPLHPEYRTMPMVWYIPPLSPIMNMVEgkGSNWQAEAIFPAIDNMRIPIQYLANLLTAGDE 399
Cdd:TIGR01660 321 IEAAQQSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQNAAE--AGKVGANGIMPDVESLRIPVRYLANLLTAGDT 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323  400 SHIRLTLKKMAVMRTHMRALQINKEPNEAVLKELGLTKQDVEDMYRLLAIAKYKDRFVIPGTHREQVADLYSEQGSCGLA 479
Cdd:TIGR01660 399 KPVLLALKRMLAMRHYMRAETVDGVVDTEVLEDVGLTEQQIEEMYRYLAIANYEDRFVIPSSHREIARDAFPERGGCGFS 478


                  ....*..
gi 446615323  480 FAGGPGS 486
Cdd:TIGR01660 479 FGDGCHG 485
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 3-366 0e+00

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: 778.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323   3 IKAQVGMVMNLDKCIGCHTCSVTCKNTWTNRPGAEYMYFNNVETKPGIGYPKQWEDQEKYKGGWELKNGEIQLKSGSKMK 82
Cdd:cd10557    1 IRAQISMVMNLDKCIGCHTCSVTCKNVWTNRKGAEYMWWNNVETKPGIGYPKQWEDQEKYRGGWVLKGGKLKLKRGGKIQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323  83 RLMNIFHNPDQPTIDDYFEPWNYDYETLTNSPQRKHQPVARPKSAITGEFIDkIEWGPNWEDDLAGGHITGLQDPNVKKM 162
Cdd:cd10557   81 KLANIFYNPKLPEIDDYYEPWTYDYENLFTAPEGDDQPVARPKSLITGEPMD-IEWGPNWDDDLAGSPEYAAEDPNLKKL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 163 EEEIKTDFENVFMMYLPRICEHCMNPSCVSSCPSGAMYKREEDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKAEKC 242
Cdd:cd10557  160 QEEIYLEFENTFMFYLPRICNHCLNPACVAACPSGAIYKREEDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSEKC 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 243 TMCFPRIEAGMPTICSETCVGRIRYIGVMLYDADKVKEAASVEDEKDLYESQLTVFLDPNDPEVAAEAKKQGIPEEWIKA 322
Cdd:cd10557  240 IFCYPRLEAGQPTVCSETCVGRIRYLGVLLYDADRILEAAAVVPEKDLVEAQLDIILDPNDPEVIAAAKANGIPDNWIEA 319

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 446615323 323 AQESPIYKMIIDWKIALPLHPEYRTMPMVWYIPPLSPIMNMVEG 366
Cdd:cd10557  320 AQRSPVYKMVKEWKIALPLHPEYRTLPMVFYVPPLSPVVAAVEA 363
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 173-271 4.79e-53

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: 173.97  E-value: 4.79e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323  173 VFMMYLPRICEHCMNPSCVSSCPSGAMYKREEDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKAEKCTMCFPRIEAG 252
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPVGAIYKDEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAG 80

                          90
                  ....*....|....*....
gi 446615323  253 MPTICSETCVGRIRYIGVM 271
Cdd:pfam13247  81 LLPACVQTCPTGAMNFGDR 99
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
178-372 2.17e-27

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 109.96  E-value: 2.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 178 LPRICEHCMNPSCVSSCPSGAMYKREeDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKAEKCTMCFPRIEAGMPTIC 257
Cdd:PRK14993  96 LPRLCNHCDNPPCVPVCPVQATFQRE-DGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPAC 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 258 SETCVGRIRYIGvmlydadkvkeaasvedekdlyesqltvflDPNDPevaaeakkqgipeewikaaqESPIYKMIIDWKI 337
Cdd:PRK14993 175 VESCVGGARIIG------------------------------DIKDP--------------------HSRIATMLHQHRD 204

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446615323 338 ALP-LHPEYRTMPMVWYIPPLSPIMNMVEGKGSN--WQ 372
Cdd:PRK14993 205 AIKvLKPENGTSPHVFYLGLDDAFVTPLMGRAQPalWQ 242
 
Name Accession Description Interval E-value
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 1-483 0e+00

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


Pssm-ID: 440755 [Multi-domain]  Cd Length: 485  Bit Score: 1047.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323   1 MKIKAQVGMVMNLDKCIGCHTCSVTCKNTWTNRPGAEYMYFNNVETKPGIGYPKQWEDQEKYKGGWEL-KNGEIQLKSGS 79
Cdd:COG1140    1 MKVRAQIAMVMNLDKCIGCHTCSVTCKNVWTNREGVEYMWFNNVETKPGIGYPKRWEDQEKWKGGWELdRNGKLRLRAGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323  80 KMKRLMNIFHNPDQPTIDDYFEPWNYDYETLTNSPQRKHQPVARPKSAITGEFIdKIEWGPNWEDDLAGGHITGLQDPNV 159
Cdd:COG1140   81 RLKKLANIFANPDLPEIDDYYEPWTYDYENLINAPEGDDQPVARPRSLITGEPM-KIEWGPNWDDDLGGSFEYASKDPNL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 160 KKMEEEIKTDFENVFMMYLPRICEHCMNPSCVSSCPSGAMYKREEDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKA 239
Cdd:COG1140  160 EGLQEEIYFEFENTFMFYLPRICEHCLNPACVASCPSGAIYKREEDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGKA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 240 EKCTMCFPRIEAGMPTICSETCVGRIRYIGVMLYDADKVKEAASVEDEKDLYESQLTVFLDPNDPEVAAEAKKQGIPEEW 319
Cdd:COG1140  240 EKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADRVEEAASVPDEQDLYEAQLDVFLDPHDPEVIAAARKDGIPDDW 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 320 IKAAQESPIYKMIIDWKIALPLHPEYRTMPMVWYIPPLSPIMNMVEGKGSNWQAEAIFPAIDNMRIPIQYLANLLTAGDE 399
Cdd:COG1140  320 IEAAQRSPVYKLAKEWKVALPLHPEYRTLPMVWYVPPLSPVVDAVEAGGHDGDADGLFPAIDSLRIPVEYLANLFTAGDE 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 400 SHIRLTLKKMAVMRTHMRALQINKEPNEAVLKELGLTKQDVEDMYRLLAIAKYKDRFVIPGTHREQVADLYSEQGSCGLA 479
Cdd:COG1140  400 EPVEAALRRLAAMRAYMRAKNVGGEPDEEILAAVGLTEEQAEEMYRLLAIAKYEDRFVIPTAHREQAEDLYELQGGCGFD 479


                 ....
gi 446615323 480 FAGG 483
Cdd:COG1140  480 FGGG 483
narH TIGR01660
nitrate reductase, beta subunit; The Nitrate reductase enzyme complex allows bacteria to use ...
 1-486 0e+00

nitrate reductase, beta subunit; The Nitrate reductase enzyme complex allows bacteria to use nitrate as an electron acceptor during anaerobic growth. The enzyme complex consists of a tetramer that has an alpha, beta and 2 gamma subunits. The alpha and beta subunits have catalytic activity and the gamma subunits attach the enzyme to the membrane and is a b-type cytochrome that receives electrons from the quinone pool and transfers them to the beta subunit. This model is specific for the beta subunit for nitrate reductase I (narH) and nitrate reductase II (narY) for gram positive and gram negative bacteria.A few thermophiles and archaea also match the model.The seed members used in this model are all experimentally characterized and include the following:SP:P11349, and SP:P19318, both E.Coli (NarH and NarY respectively), SP:P42176 from B. Subtilis, GP:11344602 from Psuedomonas fluorescens,GP:541762 from Paracoccus denitrificans, and GP:18413622 from Halomonas halodenitrificans. This model also matches Pfam pfam00037 for 4Fe-4S binding domain. [Energy metabolism, Anaerobic]


Pssm-ID: 211677 [Multi-domain]  Cd Length: 492  Bit Score: 905.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323    1 MKIKAQVGMVMNLDKCIGCHTCSVTCKNTWTNRPGAEYMYFNNVETKPGIGYPKQWEDQEKYKGGWELK-NGEIQLKSGS 79
Cdd:TIGR01660   1 MKIRSQIGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGIGYPKDWENQDKYKGGWVRKrDGKLEPRIGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323   80 KMKRLMNIFHNPDQPTIDDYFEPWNYDYETLTNSPQRKHQPVARPKSAITGEFIDKIEWGPNWEDDLAGGHITGLQDPNV 159
Cdd:TIGR01660  81 KWRVLANIFANPDLPSIDDYYEPFDFDYQHLHTAPEGKHQPTARPRSLITGERMEKIEWGPNWEDDLGGEFAKRRKDKNF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323  160 KKMEEEIKTDFENVFMMYLPRICEHCMNPSCVSSCPSGAMYKREEDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKA 239
Cdd:TIGR01660 161 DKIQKDIYGEFENTFMMYLPRLCEHCLNPACVASCPSGAIYKREEDGIVLIDQDKCRGWRMCISGCPYKKIYFNWKTGKS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323  240 EKCTMCFPRIEAGMPTICSETCVGRIRYIGVMLYDADKVKEAASVEDEKDLYESQLTVFLDPNDPEVAAEAKKQGIPEEW 319
Cdd:TIGR01660 241 EKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADKIEEAASTENEKDLYHRQLDVFLDPNDPEVIAQAKKDGIPLSV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323  320 IKAAQESPIYKMIIDWKIALPLHPEYRTMPMVWYIPPLSPIMNMVEgkGSNWQAEAIFPAIDNMRIPIQYLANLLTAGDE 399
Cdd:TIGR01660 321 IEAAQQSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQNAAE--AGKVGANGIMPDVESLRIPVRYLANLLTAGDT 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323  400 SHIRLTLKKMAVMRTHMRALQINKEPNEAVLKELGLTKQDVEDMYRLLAIAKYKDRFVIPGTHREQVADLYSEQGSCGLA 479
Cdd:TIGR01660 399 KPVLLALKRMLAMRHYMRAETVDGVVDTEVLEDVGLTEQQIEEMYRYLAIANYEDRFVIPSSHREIARDAFPERGGCGFS 478


                  ....*..
gi 446615323  480 FAGGPGS 486
Cdd:TIGR01660 479 FGDGCHG 485
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 3-366 0e+00

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: 778.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323   3 IKAQVGMVMNLDKCIGCHTCSVTCKNTWTNRPGAEYMYFNNVETKPGIGYPKQWEDQEKYKGGWELKNGEIQLKSGSKMK 82
Cdd:cd10557    1 IRAQISMVMNLDKCIGCHTCSVTCKNVWTNRKGAEYMWWNNVETKPGIGYPKQWEDQEKYRGGWVLKGGKLKLKRGGKIQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323  83 RLMNIFHNPDQPTIDDYFEPWNYDYETLTNSPQRKHQPVARPKSAITGEFIDkIEWGPNWEDDLAGGHITGLQDPNVKKM 162
Cdd:cd10557   81 KLANIFYNPKLPEIDDYYEPWTYDYENLFTAPEGDDQPVARPKSLITGEPMD-IEWGPNWDDDLAGSPEYAAEDPNLKKL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 163 EEEIKTDFENVFMMYLPRICEHCMNPSCVSSCPSGAMYKREEDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKAEKC 242
Cdd:cd10557  160 QEEIYLEFENTFMFYLPRICNHCLNPACVAACPSGAIYKREEDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSEKC 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 243 TMCFPRIEAGMPTICSETCVGRIRYIGVMLYDADKVKEAASVEDEKDLYESQLTVFLDPNDPEVAAEAKKQGIPEEWIKA 322
Cdd:cd10557  240 IFCYPRLEAGQPTVCSETCVGRIRYLGVLLYDADRILEAAAVVPEKDLVEAQLDIILDPNDPEVIAAAKANGIPDNWIEA 319

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 446615323 323 AQESPIYKMIIDWKIALPLHPEYRTMPMVWYIPPLSPIMNMVEG 366
Cdd:cd10557  320 AQRSPVYKMVKEWKIALPLHPEYRTLPMVFYVPPLSPVVAAVEA 363
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 3-401 2.28e-123

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: 362.78  E-value: 2.28e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323   3 IKAQVGMVMNLDKCIGCHTCSVTCKNTWTNRPGAEYMYFNNVETKPGIGYPKQWEDqekyKGGWELKNGEIQLksgSKMk 82
Cdd:cd10555    1 SKRQLAMVMDLNKCIGCQTCTVACKTLWTNRNGREYMYWNNVETQPGKGYPKNWEK----KGGGFKDKGELKP---GII- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323  83 rlmnifhnpdqPTIDDYFEPWNYDYE--TLTNSPQRKH-QPVARPKsaitgefidkieWGPNWEDDLAGGhitglqdpnv 159
Cdd:cd10555   73 -----------PTLEDYGVPWEYNHEeeLFEGKGGRVRpSPKGDPT------------WGPNWDEDQGAG---------- 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 160 kkmeeeiktDFENVFMMYLPRICEHCMNPSCVSSCPSGAMYKREEDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKA 239
Cdd:cd10555  120 ---------EYPNSYYFYLPRICNHCTNPACLAACPRKAIYKREEDGIVLVDQDRCRGYRYCVEACPYKKIYFNPVEQKS 190

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 240 EKCTMCFPRIEAGMPTICSETCVGRIRYIGvmlydadkvkeaasvedekdlyesqltvFLDpnDPevaaeakkqgipeew 319
Cdd:cd10555  191 EKCIFCYPRIEKGVAPACARQCVGRIRFVG----------------------------YLD--DE--------------- 225

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 320 ikaaqESPIYKMIIDWKIALPLHPEYRTMPMVWYIPPLSPIMNMVEGKgsnwqaeaifpAIDNMRIPIQYLANLLtaGDE 399
Cdd:cd10555  226 -----ESPVYKLVKKWKVALPLHPEYGTEPNVFYVPPLSPPKLGDDGE-----------PTDEPRIPLEYLESLF--GPR 287


                 ..
gi 446615323 400 SH 401
Cdd:cd10555  288 VK 289
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 6-359 2.95e-94

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: 284.09  E-value: 2.95e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323   6 QVGMVMNLDKCIGCHTCSVTCKNTWTNRPGAEYMYFNNVETKPGIGYPKQWEDQEKYKGGWELkngeiqlksgskmkrlm 85
Cdd:cd16365    2 QFAAVFNLNKCIGCQTCTVACKNAWTYRKGQEYMWWNNVETKPGGGYPQDWEVKTIDNGGNTR----------------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323  86 nifhnpdqptiddyfepwnydyetltnspqrkhqpvarpksaitgefidkiewgpnweddlagghitglqdpnvkkmeee 165
Cdd:cd16365      --------------------------------------------------------------------------------

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 166 iktdfenvFMMYLPRICEHCMNPSCVSSCPSGAMYKREEDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKAEKCTMC 245
Cdd:cd16365   65 --------FFFYLQRLCNHCTNPACLAACPRGAIYKREEDGIVLIDQKRCRGYRKCVEQCPYKKIYFNGLSRVSEKCIAC 136

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 246 FPRIEAGMPTICSETCVGRIRYIGVMLYDadkvkeaasvedekdlyesqltvfldpndpevaaeakkqgipeewikaaQE 325
Cdd:cd16365  137 YPRIEGGDPTRCMSACVGRIRLQGFLDDN-------------------------------------------------PK 167

                        330       340       350
                 ....*....|....*....|....*....|....
gi 446615323 326 SPIYKMIIDWKIALPLHPEYRTMPMVWYIPPLSP 359
Cdd:cd16365  168 SPVTKLIRHWKVALPLHPEYGTEPNIYYVPPRWA 201
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 4-356 1.50e-77

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: 244.29  E-value: 1.50e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323   4 KAQVGMVMNLDKCIGCHTCSVTCKNTWTNRPGAEYMYFNNVETKPGIGYPKQWEdqekykggwelkngeiqlksgskmkr 83
Cdd:cd10556    9 DKQFAMVFDTNKCIACQTCTMACKSTWTSGKGQEYMWWNNVETKPYGGYPLGWD-------------------------- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323  84 lMNIFHNPDQPTIDDYfepWNYDYETLtnspqrkhqPVARPKS-AITGEFIDKIEWG-PNWEDDlagghitglqDPNVKK 161
Cdd:cd10556   63 -VRLLDEEGGQTWAEG---GVYEGKTI---------FEAAAAGeQVLGYRPEDEDWRyPNIGED----------EVNGER 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 162 MEEEIKTDFEN-VFMMYLPRICEHCMNPSCVSSCPSGAMYKREEDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKAE 240
Cdd:cd10556  120 TPDTGSSLPPHpIWFFYLPRICNHCTYPACLAACPRKAIYKREEDGIVLIDQERCRGYRECVEACPYKKPMYNPTTRVSE 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 241 KCTMCFPRIEAGMPTICSETCVGRIRYIGvmlydadkvkeaasvedekdlyesqltvFLDPNDPEVAAEakkqgipeewi 320
Cdd:cd10556  200 KCIGCYPRIEEGDQTQCVSACIGKIRLQG----------------------------FINTPPDARWAD----------- 240

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 446615323 321 kaAQESPIYKMIIDWKIALPLHPEYRTMPMVWYIPP 356
Cdd:cd10556  241 --DRDNPIDFLVHIKKVALPLYPQFGTEPNVYYIPP 274
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 173-271 4.79e-53

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: 173.97  E-value: 4.79e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323  173 VFMMYLPRICEHCMNPSCVSSCPSGAMYKREEDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKAEKCTMCFPRIEAG 252
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPVGAIYKDEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAG 80

                          90
                  ....*....|....*....
gi 446615323  253 MPTICSETCVGRIRYIGVM 271
Cdd:pfam13247  81 LLPACVQTCPTGAMNFGDR 99
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 161-354 1.75e-40

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: 143.83  E-value: 1.75e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 161 KMEEEIKTDFENVFMMYLPRICEHCMNPSCVSSCPSGAMYKReEDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQ----- 235
Cdd:cd10551   32 RVLEYEVGEYPNVKRTFLPVLCNHCENPPCVKVCPTGATYKR-EDGIVLVDYDKCIGCRYCMAACPYGARYFNPEephef 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 236 -------TNKAEKCTMCFPRIEAGMPTICSETCVGRIRYIGvmlydadkvkeaasvedekdlyesqltvflDPNDPevaa 308
Cdd:cd10551  111 gevpvrpKGVVEKCTFCYHRLDEGLLPACVEACPTGARIFG------------------------------DLDDP---- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446615323 309 eakkqgipeewikaaqESPIYKMIIDWKiALPLHPEYRTMPMVWYI 354
Cdd:cd10551  157 ----------------NSEVSKLLAERR-AYVLKPELGTKPKVYYI 185
Nitr_red_bet_C pfam14711
Respiratory nitrate reductase beta C-terminal; This domain occurs near the C-terminus of the ...
 357-436 6.52e-37

Respiratory nitrate reductase beta C-terminal; This domain occurs near the C-terminus of the respiratory nitrate reductase beta chain. The nitrate reductase complex is a dimer of heterotrimers each consisting of an alpha, beta and gamma chain. This domain plays a role in the interactions between subunits and shielding of the Fe-S clusters


Pssm-ID: 434148 [Multi-domain]  Cd Length: 81  Bit Score: 130.70  E-value: 6.52e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323  357 LSPIMNMVEGKGSNWQAEAIFPAIDNMRIPIQYLANLLTAGDESHIRLTLKKMAVMRTHMRALQINKEPNEAVLKELGLT 436
Cdd:pfam14711   1 LSPVVDAAEAGGHDEDADGLFPAIDSLRIPVEYLANLLTAGDTEPVRRALRRLAAMRAYMRAKNVGGEPDESILEAVGLT 80
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 169-296 4.00e-36

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 131.99  E-value: 4.00e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 169 DFENVFMMYLPRICEHCMNPSCVSSCPSGAMYKREeDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKAEKCTMCFPR 248
Cdd:COG0437   47 EFPNVEWLFVPVLCNHCDDPPCVKVCPTGATYKRE-DGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADR 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446615323 249 IEAGMPTICSETCVGRIRYIGVMLYDADKVKEAASVEDEKDLYESQLT 296
Cdd:COG0437  126 LDEGLLPACVEACPTGALVFGDLDDPESEVSKRLAELPAYRLLPELGT 173
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 169-269 7.03e-33

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


Pssm-ID: 319870 [Multi-domain]  Cd Length: 136  Bit Score: 121.73  E-value: 7.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 169 DFENVFMMYLPRICEHCMNPSCVSSCPSGAMYKREeDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKAEKCTMCFPR 248
Cdd:cd04410   37 EGGGLERAFLPVSCMHCEDPPCVKACPTGAIYKDE-DGIVLIDEDKCIGCGSCVEACPYGAIVFDPEPGKAVKCDLCGDR 115

                         90       100
                 ....*....|....*....|.
gi 446615323 249 IEAGMPTICSETCVGRIRYIG 269
Cdd:cd04410  116 LDEGLEPACVKACPTGALTFG 136
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 159-264 4.09e-31

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: 116.89  E-value: 4.09e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 159 VKKMEEEiktDFENVFMMYLPRICEHCMNPSCVSSCPSGAMYKReEDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNK 238
Cdd:cd16371   34 VYEYEGG---EFPEVFAYFLSMSCNHCENPACVKVCPTGAITKR-EDGIVVVDQDKCIGCGYCVWACPYGAPQYNPETGK 109

                         90       100
                 ....*....|....*....|....*.
gi 446615323 239 AEKCTMCFPRIEAGMPTICSETCVGR 264
Cdd:cd16371  110 MDKCDMCVDRLDEGEKPACVAACPTR 135
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
178-372 2.17e-27

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 109.96  E-value: 2.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 178 LPRICEHCMNPSCVSSCPSGAMYKREeDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKAEKCTMCFPRIEAGMPTIC 257
Cdd:PRK14993  96 LPRLCNHCDNPPCVPVCPVQATFQRE-DGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPAC 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 258 SETCVGRIRYIGvmlydadkvkeaasvedekdlyesqltvflDPNDPevaaeakkqgipeewikaaqESPIYKMIIDWKI 337
Cdd:PRK14993 175 VESCVGGARIIG------------------------------DIKDP--------------------HSRIATMLHQHRD 204

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446615323 338 ALP-LHPEYRTMPMVWYIPPLSPIMNMVEGKGSN--WQ 372
Cdd:PRK14993 205 AIKvLKPENGTSPHVFYLGLDDAFVTPLMGRAQPalWQ 242
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 164-262 9.79e-26

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: 102.86  E-value: 9.79e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 164 EEIKTDFENVFMMYLPRICEHCMNPSCVSSCPSGAMYkREEDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKAEKCT 243
Cdd:cd16366   52 YEVEKPGGDLSWLFRKDQCMHCTDAGCLAACPTGAII-RTETGTVVVDPETCIGCGYCVNACPFDIPRFDEETGRVAKCT 130

                         90
                 ....*....|....*....
gi 446615323 244 MCFPRIEAGMPTICSETCV 262
Cdd:cd16366  131 LCYDRISNGLQPACVKTCP 149
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 182-261 3.12e-24

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: 98.53  E-value: 3.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 182 CEHCMNPSCVSSCPSGAMYKrEEDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKAEKCTMCFPRIEAGMPTICSETC 261
Cdd:cd10562   70 CMHCTDAACVKVCPTGALYK-TENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCFDRIENGMQPACVKTC 148
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 175-261 6.91e-23

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: 94.35  E-value: 6.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 175 MMYLPRICEHCMNPSCVSSCPSGAMYKREEDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKAEKCTMCFPRIEAGMP 254
Cdd:cd10553   51 LKFVYMSCFHCENPWCVKACPTGAMQKREKDGIVYVDQELCIGCKACIEACPWGIPQWNPATGKVVKCDYCMDRIDQGLK 130


                 ....*..
gi 446615323 255 TICSETC 261
Cdd:cd10553  131 PACVTGC 137
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 182-261 9.05e-23

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


Pssm-ID: 319883 [Multi-domain]  Cd Length: 196  Bit Score: 95.74  E-value: 9.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 182 CEHCMNPSCVSSCPSGAMYKREEdGIVLVDQNACRAWRFCVSSCPYKKVYFNWqtNKAE----KCTMCFPRIEAGMPTIC 257
Cdd:cd10561   69 CMHCLDPACVSACPVGALRKTPE-GPVTYDEDKCIGCRYCMVACPFNIPKYEW--DSANpkirKCTMCYDRLKEGKQPAC 145


                 ....
gi 446615323 258 SETC 261
Cdd:cd10561  146 VEAC 149
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 177-353 2.97e-21

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: 91.23  E-value: 2.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 177 YLPRICEHCMNPSCVSSCPSGAMYKREeDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKAEKCTMCFPRIEAG--MP 254
Cdd:cd10552   59 YLPVPCNHCDNAPCIKAAKDGAVYKRD-DGIVIIDPEKAKGQKQLVDACPYGAIYWNEELQVPQKCTFCAHLLDDGwkEP 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 255 TiCSETC-VGRIRyigvmlydadkvkeaasvedekdlyesqltvFLDPNDPEVAAEAKKQGipeewikaaqespiykmii 333
Cdd:cd10552  138 R-CVQACpTGALR-------------------------------FGKLEDEEMAAKAAEEG------------------- 166

                        170       180
                 ....*....|....*....|
gi 446615323 334 dwkiALPLHPEYRTMPMVWY 353
Cdd:cd10552  167 ----LEVLHPELGTKPRVYY 182
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 182-261 6.50e-19

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: 85.52  E-value: 6.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 182 CEHCMNPSCVSSCPSGAMYKREEDGIVlVDQNACRAWRFCVSSCPYKKVYFNWQTNKAEKCTMCFPRIEAGMPTICSETC 261
Cdd:cd10560   78 CKHCTDAGCLEACPTGAIFRTEFGTVY-IQPDICNGCGYCVAACPFGVIDRNEETGRAHKCTLCYDRLKDGLEPACAKAC 156
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 166-245 9.05e-19

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


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 82.24  E-value: 9.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 166 IKTDFENVFmmYLPRICEHCMNPSCVSSCPSGAMYKREEDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKAEKCTMC 245
Cdd:cd10550   35 VVRFEPEGL--DVPVVCRQCEDAPCVEACPVGAISRDEETGAVVVDEDKCIGCGMCVEACPFGAIRVDPETGKAIKCDLC 112
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 177-248 1.24e-17

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: 79.22  E-value: 1.24e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446615323 177 YLPRICEHCMNPSCVSSCPSGAMYKREEDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKAEKCTMCFPR 248
Cdd:cd10563   52 SFPLQCRHCDEPPCVKACMSGAMHKDPETGIVIHDEEKCVGCWMCVMVCPYGAIRPDKERKVALKCDLCPDR 123
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
177-261 3.54e-17

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 82.41  E-value: 3.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 177 YLPRICEHCMNPSCVSSCPSGAMYKREEDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQ--TNKAEKCTMC----FPRIE 250
Cdd:PRK10882 107 YIKKQCMHCVDPNCVSVCPVSALTKDPKTGIVHYDKDVCTGCRYCMVACPFNVPKYDYNnpFGAIHKCELCnqkgVERLD 186

                         90
                 ....*....|.
gi 446615323 251 AGMPTICSETC 261
Cdd:PRK10882 187 KGGLPGCVEVC 197
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 176-261 1.66e-16

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: 76.16  E-value: 1.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 176 MYLPRICEHCMNPSCVSSCPSGAMYkREEDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKAEKCTMCFPRIEAGMPT 255
Cdd:cd16374   37 ASVPVRCRHCEDAPCMEVCPTGAIY-RDEDGAVLVDPDKCIGCGMCAMACPFGVPRFDPSLKVAVKCDLCIDRRREGKLP 115


                 ....*.
gi 446615323 256 ICSETC 261
Cdd:cd16374  116 ACVEAC 121
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 182-261 4.52e-14

The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS subunit of formate dehydrogenase-N (FDH-N), a member of the DMSO reductase family. FDH-N is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. Thus, FDH-N is a major component of nitrate respiration of Escherichia coli. This integral membrane enzyme forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups.


Pssm-ID: 319880 [Multi-domain]  Cd Length: 208  Bit Score: 70.88  E-value: 4.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 182 CEHCMNPSCVSSCPS-GAMYKREeDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKAEKCTMCFPRIEAGMPTICSET 260
Cdd:cd10558   70 CMHCADPGCLKACPSpGAIVQYA-NGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVGLEPACVKT 148


                 .
gi 446615323 261 C 261
Cdd:cd10558  149 C 149
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 178-268 2.88e-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: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 67.80  E-value: 2.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 178 LPRICEHCMNPSCVSSCPSGAMyKREEDGIVL-VDQNACRAWRFCVSSCPYKKVYFNWQTNKAEKCTMCFPRIEAGMPTI 256
Cdd:cd16369   47 APTVCMHCEDPTCAEVCPADAI-KVTEDGVVQsALKPRCIGCSNCVNACPFGVPKYDEERNLMMKCDMCYDRTSVGKAPM 125

                         90
                 ....*....|...
gi 446615323 257 CSETC-VGRIRYI 268
Cdd:cd16369  126 CASVCpSGALFYG 138
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 177-269 8.65e-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: 319890 [Multi-domain]  Cd Length: 200  Bit Score: 67.06  E-value: 8.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 177 YLPRICEHCMNPSCVSSCPSGAMYKREEdGIVLVDQNACRAWRFCVSSCP------------YKKVYFNWQTNKAE-KCT 243
Cdd:cd16368   86 FIPRRCMHCDNPPCAKLCPFGAARKTPE-GAVYIDDDLCFGGAKCRDVCPwhipqrqagvgiYLHLAPEYAGGGVMyKCD 164

                         90       100
                 ....*....|....*....|....*.
gi 446615323 244 MCFPRIEAGMPTICSETCVGRIRYIG 269
Cdd:cd16368  165 LCKDLLAQGKPPACIEACPKGAQYFG 190
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 173-261 3.34e-12

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: 65.53  E-value: 3.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 173 VFMMYLPRICEHCMNPSCVSSCPS--GAMYKREEDGIVLVDQNACRAWRFCV-SSCPYKKVYFNWQTNKAEKCTMCFPRI 249
Cdd:cd10559   62 PDWLFFPDQCRHCVTPPCKDAADMvpGAVIQDEATGAVVFTEKTAELDFDDVlSACPYNIPRKNEATGRIVKCDMCIDRV 141

                         90
                 ....*....|..
gi 446615323 250 EAGMPTICSETC 261
Cdd:cd10559  142 SNGLQPACVKAC 153
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
176-261 1.50e-11

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 61.98  E-value: 1.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 176 MYLPRICEHCMNPSCVSSCPSGAMYKreEDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNK--AEKCTMCFPRieAGM 253
Cdd:COG1142   46 VSAPVQCRHCEDAPCAEVCPVGAITR--DDGAVVVDEEKCIGCGLCVLACPFGAITMVGEKSRavAVKCDLCGGR--EGG 121


                 ....*...
gi 446615323 254 PtICSETC 261
Cdd:COG1142  122 P-ACVEAC 128
PRK09898 PRK09898
ferredoxin-like protein;
175-245 7.02e-11

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 61.78  E-value: 7.02e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446615323 175 MMYLPRICEHCMNPSCVSSCPSGAMYKREEDGIVLVDQNACRAWRFCVSSCPYKKVYFNWQTNKAEKCTMC 245
Cdd:PRK09898 116 LNYTADTCRQCKEPQCMNVCPIGAITWQQKEGCITVDHKRCIGCSACTTACPWMMATVNTESKKSSKCVLC 186
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 180-245 2.26e-09

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: 55.36  E-value: 2.26e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446615323 180 RICEHCMNPSCVSSCPSGAMYKREEDGIVLvDQNACRAWRFCVSSCPYKKVYFNWQTNKAEKCTMC 245
Cdd:cd16370   51 VVCRACEDPPCAEACPTGALEPRKGGGVVL-DKEKCIGCGNCVKACIVGAIFWDEETNKPIICIHC 115
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 178-246 1.16e-08

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


Pssm-ID: 319889 [Multi-domain]  Cd Length: 138  Bit Score: 53.47  E-value: 1.16e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446615323 178 LPRICEHCMNPSCVSSCPSGAMyKREEDGIVLVDqNACRAWRFCVSSCPYKKVyfnwQTNKAEKCTMCF 246
Cdd:cd16367   53 VPTACRHCVDPVCMIGCPTGAI-HRDDGGEVVIS-DACCGCGNCASACPYGAI----QMVRAVKCDLCA 115
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 177-261 3.75e-06

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 49.36  E-value: 3.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 177 YLPRI-------------CEHCMNPSCVSSCPSGAMyKREEDGIVLVdQNACRAWRFCVSSCPY-------KKVYFNWQT 236
Cdd:PRK12769  38 FHPRItvikhqqqrsavtCHHCEDAPCARSCPNGAI-SHVDDSIQVN-QQKCIGCKSCVVACPFgtmqivlTPVAAGKVK 115

                         90       100
                 ....*....|....*....|....*
gi 446615323 237 NKAEKCTMCFPRiEAGmpTICSETC 261
Cdd:PRK12769 116 ATAHKCDLCAGR-ENG--PACVENC 137
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 179-317 6.73e-06

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 48.87  E-value: 6.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 179 PRICEHCMNPSCVSSCPSGAMYKREEDgiVLVDQNACRAWRFCVSSCPYKKVyfNWQTNKAEKCTMCFPRiEAGMPTiCS 258
Cdd:PRK12809  53 PVACHHCNNAPCVTACPVNALTFQSDS--VQLDEQKCIGCKRCAIACPFGVV--EMVDTIAQKCDLCNQR-SSGTQA-CI 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446615323 259 ETCVGR-IRYI---GVMLYDADKVKEAASVEDEKDLYESQLTVFLDPND----PEVAAEAKKQGIPE 317
Cdd:PRK12809 127 EVCPTQaLRLMddkGLQQIKVARQRKTAAGKASSDAQPSRSAALLPVNSrkgaDKISASERKTHFGE 193
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 182-263 9.89e-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: 9.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 182 CEHCMNpSCVSSCPSGA---MYKREED---GIVLVDQNACRAW------RFCVSSCPYKKVYFnwqtnkaekctmcFPRI 249
Cdd:cd16373   55 CDLCCD-ACVEVCPTGAlrpLDLEEQKvkmGVAVIDKDRCLAWqggtdcGVCVEACPTEAIAI-------------VLED 120

                         90
                 ....*....|....
gi 446615323 250 EAGMPTICSETCVG 263
Cdd:cd16373  121 DVLRPVVDEDKCVG 134
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
182-234 9.48e-05

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 40.87  E-value: 9.48e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446615323 182 CEHCMnpSCVSSCPSGAMYkrEEDGIVLVDQNACRAWRFCVSSCPYKKVYFNW 234
Cdd:COG2768   13 CIGCG--ACVKVCPVGAIS--IEDGKAVIDPEKCIGCGACIEVCPVGAIKIEW 61
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 179-226 1.04e-04

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


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 39.93  E-value: 1.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446615323  179 PRICEHCMNpsCVSSCPSGAM-----YKREEDGIVLVDQNACRAWRFCVSSCP 226
Cdd:pfam13237   6 PDKCIGCGR--CTAACPAGLTrvgaiVERLEGEAVRIGVWKCIGCGACVEACP 56
NapF COG1145
Ferredoxin [Energy production and conversion];
156-228 3.83e-04

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 42.02  E-value: 3.83e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446615323 156 DPNVKKMEEEIKTDFENVFMMYLPRICEHCMNpsCVSSCPSGAMYKREEDGIVLVDQNACRAWRFCVSSCPYK 228
Cdd:COG1145  158 ISGGKKIEEELKIAIKKAKAVIDAEKCIGCGL--CVKVCPTGAIRLKDGKPQIVVDPDKCIGCGACVKVCPVG 228
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 182-228 1.29e-03

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 36.74  E-value: 1.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446615323  182 CEHCMNpsCVSSCPSGAMYKREED-----GIVLVDQNACRAWRFCVSSCPYK 228
Cdd:pfam12838   1 CIGCGA--CVAACPVGAITLDEVGekkgtKTVVIDPERCVGCGACVAVCPTG 50
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 179-231 1.50e-03

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 37.33  E-value: 1.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446615323 179 PRICEHCMnpSCVSSCPSGAMYkrEEDGIVLVDQNACRAWRFCVSSCPYKKVY 231
Cdd:COG4231   21 EDKCTGCG--ACVKVCPADAIE--EGDGKAVIDPDLCIGCGSCVQVCPVDAIK 69
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 175-228 1.76e-03

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 37.01  E-value: 1.76e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446615323 175 MMYLPRI----CEHCMnpSCVSSCPSGAMyKREEDGIVLVDQNACRAWRFCVSSCPYK 228
Cdd:COG1149    2 KRKIPVIdeekCIGCG--LCVEVCPEGAI-KLDDGGAPVVDPDLCTGCGACVGVCPTG 56
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
189-226 2.12e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 39.92  E-value: 2.12e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446615323 189 SCVSSCPSGAMykREEDGIVLVDQNACRAWRFCVSSCP 226
Cdd:PRK07118 146 SCVAACPFDAI--HIENGLPVVDEDKCTGCGACVKACP 181
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
190-228 2.68e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 39.53  E-value: 2.68e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 446615323 190 CVSSCPSGAMykREEDGIVLVDQNACRAWRFCVSSCPYK 228
Cdd:PRK07118 221 CVKACPAGAI--TMENNLAVIDQEKCTSCGKCVEKCPTK 257
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 176-226 4.98e-03

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 35.80  E-value: 4.98e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446615323 176 MYLPRI----CEHCmnPSCVSSCPSGAMykREEDGIVLVDQNACRAWRFCVSSCP 226
Cdd:COG2221    7 TWPPKIdeekCIGC--GLCVAVCPTGAI--SLDDGKLVIDEEKCIGCGACIRVCP 57
napG PRK09476
quinol dehydrogenase periplasmic component; Provisional
 182-263 5.80e-03

quinol dehydrogenase periplasmic component; Provisional


Pssm-ID: 236534 [Multi-domain]  Cd Length: 254  Bit Score: 38.45  E-value: 5.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446615323 182 CEHCMNPSCVSSCPSGAMYKREED------GI-VLVDQNACRAWR-----FCVSSCP---------YKKvyfNWQTNKAE 240
Cdd:PRK09476  99 CEMCEDIPCVKACPSGALDRELVDiddarmGLaVLVDQENCLNFQglrcdVCYRVCPlidkaitleLER---NERTGKHA 175

                         90       100
                 ....*....|....*....|...
gi 446615323 241 KCtmcfprieagMPTICSETCVG 263
Cdd:PRK09476 176 FF----------LPTVHSDACTG 188
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 182-226 7.25e-03

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 35.07  E-value: 7.25e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446615323 182 CEHCMnpSCVSSCPSGAMYKREEDGIVLV-DQNACRAWRFCVSSCP 226
Cdd:COG1146   10 CIGCG--ACVEVCPVDVLELDEEGKKALViNPEECIGCGACELVCP 53
 
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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