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Conserved domains on  [gi|505383367|ref|WP_015570469|]
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MULTISPECIES: nitrate reductase subunit beta [Enterobacter]

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 ...
 1-485 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: 1062.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367   1 MKIRSQVGMVLNLDKCIGCHTCSVTCKNVWTGREGMEYAWFNNVETKPGIGYPKNWEDQDEWQGGWIRGIHGKLTPRLGG 80
Cdd:COG1140    1 MKVRAQIAMVMNLDKCIGCHTCSVTCKNVWTNREGVEYMWFNNVETKPGIGYPKRWEDQEKWKGGWELDRNGKLRLRAGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367  81 KMGVLSKIFANPVLPQIDDYYEPFTFDYQDLHRAPEGDHLPTARPRSLIDGKRMdKIEWGPNWEELLGGEFEKRARDRNF 160
Cdd:COG1140   81 RLKKLANIFANPDLPEIDDYYEPWTYDYENLINAPEGDDQPVARPRSLITGEPM-KIEWGPNWDDDLGGSFEYASKDPNL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 161 QKIQKEMYGQFENTFMMYLPRLCEHCLNPSCVATCPSGAIYKREEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKS 240
Cdd:COG1140  160 EGLQEEIYFEFENTFMFYLPRICEHCLNPACVASCPSGAIYKREEDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGKA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 241 EKCIFCYPRIESGQPTVCSETCVGRIRYLGVLLYDADRIEEAASTEHETDLYERQCDVFLNPNDPAVIEEALKQGIPQNV 320
Cdd:COG1140  240 EKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADRVEEAASVPDEQDLYEAQLDVFLDPHDPEVIAAARKDGIPDDW 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 321 IDAAQRSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQSYADAGGLP-QSDGVLPAVESLRIPVQYLANMLSAGDT 399
Cdd:COG1140  320 IEAAQRSPVYKLAKEWKVALPLHPEYRTLPMVWYVPPLSPVVDAVEAGGHDgDADGLFPAIDSLRIPVEYLANLFTAGDE 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 400 GPVLRALKRMMAMRHYKRSQTVEGVTDTRAIEEVGLTEEQVEEMYRYLAIANYEDRFVIPTSHREMARDAFPEKNGCGFT 479
Cdd:COG1140  400 EPVEAALRRLAAMRAYMRAKNVGGEPDEEILAAVGLTEEQAEEMYRLLAIAKYEDRFVIPTAHREQAEDLYELQGGCGFD 479


                 ....*.
gi 505383367 480 FGDGCH 485
Cdd:COG1140  480 FGGGCP 485
 
Name Accession Description Interval E-value
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 1-485 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: 1062.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367   1 MKIRSQVGMVLNLDKCIGCHTCSVTCKNVWTGREGMEYAWFNNVETKPGIGYPKNWEDQDEWQGGWIRGIHGKLTPRLGG 80
Cdd:COG1140    1 MKVRAQIAMVMNLDKCIGCHTCSVTCKNVWTNREGVEYMWFNNVETKPGIGYPKRWEDQEKWKGGWELDRNGKLRLRAGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367  81 KMGVLSKIFANPVLPQIDDYYEPFTFDYQDLHRAPEGDHLPTARPRSLIDGKRMdKIEWGPNWEELLGGEFEKRARDRNF 160
Cdd:COG1140   81 RLKKLANIFANPDLPEIDDYYEPWTYDYENLINAPEGDDQPVARPRSLITGEPM-KIEWGPNWDDDLGGSFEYASKDPNL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 161 QKIQKEMYGQFENTFMMYLPRLCEHCLNPSCVATCPSGAIYKREEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKS 240
Cdd:COG1140  160 EGLQEEIYFEFENTFMFYLPRICEHCLNPACVASCPSGAIYKREEDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGKA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 241 EKCIFCYPRIESGQPTVCSETCVGRIRYLGVLLYDADRIEEAASTEHETDLYERQCDVFLNPNDPAVIEEALKQGIPQNV 320
Cdd:COG1140  240 EKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADRVEEAASVPDEQDLYEAQLDVFLDPHDPEVIAAARKDGIPDDW 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 321 IDAAQRSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQSYADAGGLP-QSDGVLPAVESLRIPVQYLANMLSAGDT 399
Cdd:COG1140  320 IEAAQRSPVYKLAKEWKVALPLHPEYRTLPMVWYVPPLSPVVDAVEAGGHDgDADGLFPAIDSLRIPVEYLANLFTAGDE 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 400 GPVLRALKRMMAMRHYKRSQTVEGVTDTRAIEEVGLTEEQVEEMYRYLAIANYEDRFVIPTSHREMARDAFPEKNGCGFT 479
Cdd:COG1140  400 EPVEAALRRLAAMRAYMRAKNVGGEPDEEILAAVGLTEEQAEEMYRLLAIAKYEDRFVIPTAHREQAEDLYELQGGCGFD 479


                 ....*.
gi 505383367 480 FGDGCH 485
Cdd:COG1140  480 FGGGCP 485
narH TIGR01660
nitrate reductase, beta subunit; The Nitrate reductase enzyme complex allows bacteria to use ...
 1-494 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: 1006.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367    1 MKIRSQVGMVLNLDKCIGCHTCSVTCKNVWTGREGMEYAWFNNVETKPGIGYPKNWEDQDEWQGGWIRGIHGKLTPRLGG 80
Cdd:TIGR01660   1 MKIRSQIGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGIGYPKDWENQDKYKGGWVRKRDGKLEPRIGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367   81 KMGVLSKIFANPVLPQIDDYYEPFTFDYQDLHRAPEGDHLPTARPRSLIDGKRMDKIEWGPNWEELLGGEFEKRARDRNF 160
Cdd:TIGR01660  81 KWRVLANIFANPDLPSIDDYYEPFDFDYQHLHTAPEGKHQPTARPRSLITGERMEKIEWGPNWEDDLGGEFAKRRKDKNF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367  161 QKIQKEMYGQFENTFMMYLPRLCEHCLNPSCVATCPSGAIYKREEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKS 240
Cdd:TIGR01660 161 DKIQKDIYGEFENTFMMYLPRLCEHCLNPACVASCPSGAIYKREEDGIVLIDQDKCRGWRMCISGCPYKKIYFNWKTGKS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367  241 EKCIFCYPRIESGQPTVCSETCVGRIRYLGVLLYDADRIEEAASTEHETDLYERQCDVFLNPNDPAVIEEALKQGIPQNV 320
Cdd:TIGR01660 241 EKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADKIEEAASTENEKDLYHRQLDVFLDPNDPEVIAQAKKDGIPLSV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367  321 IDAAQRSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQSYADAGGLpQSDGVLPAVESLRIPVQYLANMLSAGDTG 400
Cdd:TIGR01660 321 IEAAQQSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQNAAEAGKV-GANGIMPDVESLRIPVRYLANLLTAGDTK 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367  401 PVLRALKRMMAMRHYKRSQTVEGVTDTRAIEEVGLTEEQVEEMYRYLAIANYEDRFVIPTSHREMARDAFPEKNGCGFTF 480
Cdd:TIGR01660 400 PVLLALKRMLAMRHYMRAETVDGVVDTEVLEDVGLTEQQIEEMYRYLAIANYEDRFVIPSSHREIARDAFPERGGCGFSF 479

                         490
                  ....*....|....
gi 505383367  481 GDGCHGSDTKfNLF 494
Cdd:TIGR01660 480 GDGCHGSDTK-NLF 492
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 3-367 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: 764.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367   3 IRSQVGMVLNLDKCIGCHTCSVTCKNVWTGREGMEYAWFNNVETKPGIGYPKNWEDQDEWQGGWIRGiHGKLTPRLGGKM 82
Cdd:cd10557    1 IRAQISMVMNLDKCIGCHTCSVTCKNVWTNRKGAEYMWWNNVETKPGIGYPKQWEDQEKYRGGWVLK-GGKLKLKRGGKI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367  83 GVLSKIFANPVLPQIDDYYEPFTFDYQDLHRAPEGDHLPTARPRSLIDGKRMDkIEWGPNWEELLGGEFEKRARDRNFQK 162
Cdd:cd10557   80 QKLANIFYNPKLPEIDDYYEPWTYDYENLFTAPEGDDQPVARPKSLITGEPMD-IEWGPNWDDDLAGSPEYAAEDPNLKK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 163 IQKEMYGQFENTFMMYLPRLCEHCLNPSCVATCPSGAIYKREEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKSEK 242
Cdd:cd10557  159 LQEEIYLEFENTFMFYLPRICNHCLNPACVAACPSGAIYKREEDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSEK 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 243 CIFCYPRIESGQPTVCSETCVGRIRYLGVLLYDADRIEEAASTEHETDLYERQCDVFLNPNDPAVIEEALKQGIPQNVID 322
Cdd:cd10557  239 CIFCYPRLEAGQPTVCSETCVGRIRYLGVLLYDADRILEAAAVVPEKDLVEAQLDIILDPNDPEVIAAAKANGIPDNWIE 318

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 505383367 323 AAQRSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQSYADA 367
Cdd:cd10557  319 AAQRSPVYKMVKEWKIALPLHPEYRTLPMVFYVPPLSPVVAAVEA 363
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 174-272 1.73e-52

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: 172.82  E-value: 1.73e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367  174 TFMMYLPRLCEHCLNPSCVATCPSGAIYKREEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKSEKCIFCYPRIESG 253
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPVGAIYKDEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAG 80

                          90
                  ....*....|....*....
gi 505383367  254 QPTVCSETCVGRIRYLGVL 272
Cdd:pfam13247  81 LLPACVQTCPTGAMNFGDR 99
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
169-291 1.57e-25

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 104.96  E-value: 1.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 169 GQFENTFMMY--------------LPRLCEHCLNPSCVATCPSGAIYKREeDGIVLIDQDKCRGWRLCISGCPYKKIYFN 234
Cdd:PRK14993  72 GAFRTTVNQYqvqregsqevtnvlLPRLCNHCDNPPCVPVCPVQATFQRE-DGIVVVDNKRCVGCAYCVQACPYDARFIN 150

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 505383367 235 WKSGKSEKCIFCYPRIESGQPTVCSETCVGRIRYLGVLLYDADRIEEAAStEHETDL 291
Cdd:PRK14993 151 HETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRIATMLH-QHRDAI 206
 
Name Accession Description Interval E-value
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 1-485 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: 1062.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367   1 MKIRSQVGMVLNLDKCIGCHTCSVTCKNVWTGREGMEYAWFNNVETKPGIGYPKNWEDQDEWQGGWIRGIHGKLTPRLGG 80
Cdd:COG1140    1 MKVRAQIAMVMNLDKCIGCHTCSVTCKNVWTNREGVEYMWFNNVETKPGIGYPKRWEDQEKWKGGWELDRNGKLRLRAGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367  81 KMGVLSKIFANPVLPQIDDYYEPFTFDYQDLHRAPEGDHLPTARPRSLIDGKRMdKIEWGPNWEELLGGEFEKRARDRNF 160
Cdd:COG1140   81 RLKKLANIFANPDLPEIDDYYEPWTYDYENLINAPEGDDQPVARPRSLITGEPM-KIEWGPNWDDDLGGSFEYASKDPNL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 161 QKIQKEMYGQFENTFMMYLPRLCEHCLNPSCVATCPSGAIYKREEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKS 240
Cdd:COG1140  160 EGLQEEIYFEFENTFMFYLPRICEHCLNPACVASCPSGAIYKREEDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGKA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 241 EKCIFCYPRIESGQPTVCSETCVGRIRYLGVLLYDADRIEEAASTEHETDLYERQCDVFLNPNDPAVIEEALKQGIPQNV 320
Cdd:COG1140  240 EKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADRVEEAASVPDEQDLYEAQLDVFLDPHDPEVIAAARKDGIPDDW 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 321 IDAAQRSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQSYADAGGLP-QSDGVLPAVESLRIPVQYLANMLSAGDT 399
Cdd:COG1140  320 IEAAQRSPVYKLAKEWKVALPLHPEYRTLPMVWYVPPLSPVVDAVEAGGHDgDADGLFPAIDSLRIPVEYLANLFTAGDE 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 400 GPVLRALKRMMAMRHYKRSQTVEGVTDTRAIEEVGLTEEQVEEMYRYLAIANYEDRFVIPTSHREMARDAFPEKNGCGFT 479
Cdd:COG1140  400 EPVEAALRRLAAMRAYMRAKNVGGEPDEEILAAVGLTEEQAEEMYRLLAIAKYEDRFVIPTAHREQAEDLYELQGGCGFD 479


                 ....*.
gi 505383367 480 FGDGCH 485
Cdd:COG1140  480 FGGGCP 485
narH TIGR01660
nitrate reductase, beta subunit; The Nitrate reductase enzyme complex allows bacteria to use ...
 1-494 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: 1006.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367    1 MKIRSQVGMVLNLDKCIGCHTCSVTCKNVWTGREGMEYAWFNNVETKPGIGYPKNWEDQDEWQGGWIRGIHGKLTPRLGG 80
Cdd:TIGR01660   1 MKIRSQIGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGIGYPKDWENQDKYKGGWVRKRDGKLEPRIGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367   81 KMGVLSKIFANPVLPQIDDYYEPFTFDYQDLHRAPEGDHLPTARPRSLIDGKRMDKIEWGPNWEELLGGEFEKRARDRNF 160
Cdd:TIGR01660  81 KWRVLANIFANPDLPSIDDYYEPFDFDYQHLHTAPEGKHQPTARPRSLITGERMEKIEWGPNWEDDLGGEFAKRRKDKNF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367  161 QKIQKEMYGQFENTFMMYLPRLCEHCLNPSCVATCPSGAIYKREEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKS 240
Cdd:TIGR01660 161 DKIQKDIYGEFENTFMMYLPRLCEHCLNPACVASCPSGAIYKREEDGIVLIDQDKCRGWRMCISGCPYKKIYFNWKTGKS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367  241 EKCIFCYPRIESGQPTVCSETCVGRIRYLGVLLYDADRIEEAASTEHETDLYERQCDVFLNPNDPAVIEEALKQGIPQNV 320
Cdd:TIGR01660 241 EKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADKIEEAASTENEKDLYHRQLDVFLDPNDPEVIAQAKKDGIPLSV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367  321 IDAAQRSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQSYADAGGLpQSDGVLPAVESLRIPVQYLANMLSAGDTG 400
Cdd:TIGR01660 321 IEAAQQSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQNAAEAGKV-GANGIMPDVESLRIPVRYLANLLTAGDTK 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367  401 PVLRALKRMMAMRHYKRSQTVEGVTDTRAIEEVGLTEEQVEEMYRYLAIANYEDRFVIPTSHREMARDAFPEKNGCGFTF 480
Cdd:TIGR01660 400 PVLLALKRMLAMRHYMRAETVDGVVDTEVLEDVGLTEQQIEEMYRYLAIANYEDRFVIPSSHREIARDAFPERGGCGFSF 479

                         490
                  ....*....|....
gi 505383367  481 GDGCHGSDTKfNLF 494
Cdd:TIGR01660 480 GDGCHGSDTK-NLF 492
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 3-367 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: 764.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367   3 IRSQVGMVLNLDKCIGCHTCSVTCKNVWTGREGMEYAWFNNVETKPGIGYPKNWEDQDEWQGGWIRGiHGKLTPRLGGKM 82
Cdd:cd10557    1 IRAQISMVMNLDKCIGCHTCSVTCKNVWTNRKGAEYMWWNNVETKPGIGYPKQWEDQEKYRGGWVLK-GGKLKLKRGGKI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367  83 GVLSKIFANPVLPQIDDYYEPFTFDYQDLHRAPEGDHLPTARPRSLIDGKRMDkIEWGPNWEELLGGEFEKRARDRNFQK 162
Cdd:cd10557   80 QKLANIFYNPKLPEIDDYYEPWTYDYENLFTAPEGDDQPVARPKSLITGEPMD-IEWGPNWDDDLAGSPEYAAEDPNLKK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 163 IQKEMYGQFENTFMMYLPRLCEHCLNPSCVATCPSGAIYKREEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKSEK 242
Cdd:cd10557  159 LQEEIYLEFENTFMFYLPRICNHCLNPACVAACPSGAIYKREEDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSEK 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 243 CIFCYPRIESGQPTVCSETCVGRIRYLGVLLYDADRIEEAASTEHETDLYERQCDVFLNPNDPAVIEEALKQGIPQNVID 322
Cdd:cd10557  239 CIFCYPRLEAGQPTVCSETCVGRIRYLGVLLYDADRILEAAAVVPEKDLVEAQLDIILDPNDPEVIAAAKANGIPDNWIE 318

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 505383367 323 AAQRSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQSYADA 367
Cdd:cd10557  319 AAQRSPVYKMVKEWKIALPLHPEYRTLPMVFYVPPLSPVVAAVEA 363
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 6-418 6.20e-120

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: 354.69  E-value: 6.20e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367   6 QVGMVLNLDKCIGCHTCSVTCKNVWTGREGMEYAWFNNVETKPGIGYPKNWEDQdewqGGWIRGiHGKLTPrlgGKMgvl 85
Cdd:cd10555    4 QLAMVMDLNKCIGCQTCTVACKTLWTNRNGREYMYWNNVETQPGKGYPKNWEKK----GGGFKD-KGELKP---GII--- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367  86 skifanpvlPQIDDYYEPFTFDYQdlHRAPEGdhlptARPRSLIDGKRmdKIEWGPNWEELLGGefekrardrnfqkiqk 165
Cdd:cd10555   73 ---------PTLEDYGVPWEYNHE--EELFEG-----KGGRVRPSPKG--DPTWGPNWDEDQGA---------------- 118

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 166 emyGQFENTFMMYLPRLCEHCLNPSCVATCPSGAIYKREEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKSEKCIF 245
Cdd:cd10555  119 ---GEYPNSYYFYLPRICNHCTNPACLAACPRKAIYKREEDGIVLVDQDRCRGYRYCVEACPYKKIYFNPVEQKSEKCIF 195

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 246 CYPRIESGQPTVCSETCVGRIRYLGVLlydadrieeaastehetdlyerqcdvflnpNDPAvieealkqgipqnvidaaq 325
Cdd:cd10555  196 CYPRIEKGVAPACARQCVGRIRFVGYL------------------------------DDEE------------------- 226

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 326 rSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQsYADAGGLPQSDgvlpaveslRIPVQYLANMLsagdtGP-VLR 404
Cdd:cd10555  227 -SPVYKLVKKWKVALPLHPEYGTEPNVFYVPPLSPPK-LGDDGEPTDEP---------RIPLEYLESLF-----GPrVKQ 290

                        410
                 ....*....|....
gi 505383367 405 ALKRMMAMRHYKRS 418
Cdd:cd10555  291 ALDTLKAEREKKRA 304
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 5-360 6.76e-110

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: 324.92  E-value: 6.76e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367   5 SQVGMVLNLDKCIGCHTCSVTCKNVWTGREGMEYAWFNNVETKPGIGYPKNWEDQDEWQGGWIRgihgkltprlggkmgv 84
Cdd:cd16365    1 KQFAAVFNLNKCIGCQTCTVACKNAWTYRKGQEYMWWNNVETKPGGGYPQDWEVKTIDNGGNTR---------------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367  85 lskifanpvlpqiddyyepftfdyqdlhrapegdhlptarprslidgkrmdkiewgpnweellggefekrardrnfqkiq 164
Cdd:cd16365      --------------------------------------------------------------------------------

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 165 kemygqfentFMMYLPRLCEHCLNPSCVATCPSGAIYKREEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKSEKCI 244
Cdd:cd16365   65 ----------FFFYLQRLCNHCTNPACLAACPRGAIYKREEDGIVLIDQKRCRGYRKCVEQCPYKKIYFNGLSRVSEKCI 134

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 245 FCYPRIESGQPTVCSETCVGRIRYLGVLLYDadrieeaastehetdlyerqcdvflnpndpavieealkqgipqnvidaa 324
Cdd:cd16365  135 ACYPRIEGGDPTRCMSACVGRIRLQGFLDDN------------------------------------------------- 165

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 505383367 325 QRSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSP 360
Cdd:cd16365  166 PKSPVTKLIRHWKVALPLHPEYGTEPNIYYVPPRWA 201
DMSO_red_II_bet TIGR03478
DMSO reductase family type II enzyme, iron-sulfur subunit; This model represents the ...
 6-427 2.08e-108

DMSO reductase family type II enzyme, iron-sulfur subunit; This model represents the iron-sulfur subunit, typically called the beta subunit, of various proteins that also contain a molybdopterin subunit and a heme b subunit. The group includes two distinct but very closely related periplasmic proteins of anaerobic respiration, selenate reductase and chlorate reductase. Other members of this family include dimethyl sulphide dehydrogenase and ethylbenzene dehydrogenase. [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]


Pssm-ID: 132518 [Multi-domain]  Cd Length: 321  Bit Score: 325.59  E-value: 2.08e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367    6 QVGMVLNLDKCIGCHTCSVTCKNVWTGREGMEYAWFNNVETKPGIGYPKNWEDQDewqGGWIRGihgkltprlggkmGVL 85
Cdd:TIGR03478   3 QLAYVIDLNKCIGCQTCTVACKNLWTNRPGREYMYWNNVETYPGKGYPRNWERKG---GGFKRG-------------GKL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367   86 SKifaNPVLPQIDDYYEPFTFDYQDlhRAPEGDHlPTARPRslidgkrmDKIEWGPNWEELLGGefekrardrnfqkiqk 165
Cdd:TIGR03478  67 KQ---PGIIPTLIDYGDPWEFNHEE--VLYEGKD-ETVRPH--------PTPTWGPNWDEDQGA---------------- 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367  166 emyGQFENTFMMYLPRLCEHCLNPSCVATCPSGAIYKREEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKSEKCIF 245
Cdd:TIGR03478 117 ---GEYPNNYYFYLPRICNHCTNPACLAACPTGAIYKREEDGIVLVDQERCKGYRYCVEACPYKKVYFNPQSQKSEKCIG 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367  246 CYPRIESGQPTVCSETCVGRIRYLGVLlydadrieeaastehetdlyerqcdvflnpNDpavieealkqgipqnvidaaQ 325
Cdd:TIGR03478 194 CYPRIEKGIAPACVKQCPGRIRFVGYL------------------------------DD--------------------E 223

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367  326 RSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQSyadagglpQSDGVLpaVESLRIPVQYLANMLSAGdtgpVLRA 405
Cdd:TIGR03478 224 EGPVHKLVKRWKVALPLHPEYGTEPNVFYVPPMGPRGF--------GEDGEI--TDKTRIPLDYLEGLFGPG----VKQA 289

                         410       420
                  ....*....|....*....|..
gi 505383367  406 LKRMMAMRHYKRSQTVEGVTDT 427
Cdd:TIGR03478 290 LATLHTEREKKRKGQGSELMDL 311
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 4-357 4.16e-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: 243.91  E-value: 4.16e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367   4 RSQVGMVLNLDKCIGCHTCSVTCKNVWTGREGMEYAWFNNVETKPGIGYPKNWEdqdewqggwirgihgkltprlggkmg 83
Cdd:cd10556    9 DKQFAMVFDTNKCIACQTCTMACKSTWTSGKGQEYMWWNNVETKPYGGYPLGWD-------------------------- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367  84 vlSKIFANPVLPQIDDY--YEPFT-FDyqdlhRAPEGDHLPTARPRslidgkrmdkiewGPNWEELLGGEFEKrardrNF 160
Cdd:cd10556   63 --VRLLDEEGGQTWAEGgvYEGKTiFE-----AAAAGEQVLGYRPE-------------DEDWRYPNIGEDEV-----NG 117

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 161 QKIQKEMYGQFEN-TFMMYLPRLCEHCLNPSCVATCPSGAIYKREEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGK 239
Cdd:cd10556  118 ERTPDTGSSLPPHpIWFFYLPRICNHCTYPACLAACPRKAIYKREEDGIVLIDQERCRGYRECVEACPYKKPMYNPTTRV 197

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 240 SEKCIFCYPRIESGQPTVCSETCVGRIRYLGvllydadrieeaastehetdlyerqcdvFLNPNDpavieEALKQGIPQN 319
Cdd:cd10556  198 SEKCIGCYPRIEEGDQTQCVSACIGKIRLQG----------------------------FINTPP-----DARWADDRDN 244

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 505383367 320 vidaaqrsPVYKMAMDWKLALPLHPEYRTLPMVWYVPP 357
Cdd:cd10556  245 --------PIDFLVHIKKVALPLYPQFGTEPNVYYIPP 274
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 174-272 1.73e-52

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: 172.82  E-value: 1.73e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367  174 TFMMYLPRLCEHCLNPSCVATCPSGAIYKREEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKSEKCIFCYPRIESG 253
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPVGAIYKDEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAG 80

                          90
                  ....*....|....*....
gi 505383367  254 QPTVCSETCVGRIRYLGVL 272
Cdd:pfam13247  81 LLPACVQTCPTGAMNFGDR 99
Nitr_red_bet_C pfam14711
Respiratory nitrate reductase beta C-terminal; This domain occurs near the C-terminus of the ...
 358-437 1.40e-41

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: 143.41  E-value: 1.40e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367  358 LSPIQSYADAGGLPQS-DGVLPAVESLRIPVQYLANMLSAGDTGPVLRALKRMMAMRHYKRSQTVEGVTDTRAIEEVGLT 436
Cdd:pfam14711   1 LSPVVDAAEAGGHDEDaDGLFPAIDSLRIPVEYLANLLTAGDTEPVRRALRRLAAMRAYMRAKNVGGEPDESILEAVGLT 80


                  .
gi 505383367  437 E 437
Cdd:pfam14711  81 E 81
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 156-355 3.14e-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: 143.44  E-value: 3.14e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 156 RDRNFQKIQKEMYGQFENTFMMYLPRLCEHCLNPSCVATCPSGAIYKReEDGIVLIDQDKCRGWRLCISGCPYKKIYFNW 235
Cdd:cd10551   26 PGVFRNRVLEYEVGEYPNVKRTFLPVLCNHCENPPCVKVCPTGATYKR-EDGIVLVDYDKCIGCRYCMAACPYGARYFNP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 236 KS------------GKSEKCIFCYPRIESGQPTVCSETCVGRIRYLGvllydadrieeaastehetDLyerqcdvflnpN 303
Cdd:cd10551  105 EEphefgevpvrpkGVVEKCTFCYHRLDEGLLPACVEACPTGARIFG-------------------DL-----------D 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 505383367 304 DPAvieealkqgipqnvidaaqrSPVYKMAMDWKlALPLHPEYRTLPMVWYV 355
Cdd:cd10551  155 DPN--------------------SEVSKLLAERR-AYVLKPELGTKPKVYYI 185
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 159-293 4.32e-38

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 137.77  E-value: 4.32e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 159 NFQKIQKEMYGQFENTFMMYLPRLCEHCLNPSCVATCPSGAIYKREeDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSG 238
Cdd:COG0437   36 TWRRVRRYEEGEFPNVEWLFVPVLCNHCDDPPCVKVCPTGATYKRE-DGIVLVDYDKCIGCRYCVAACPYGAPRFNPETG 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 505383367 239 KSEKCIFCYPRIESGQPTVCSETCVGRIRYLGVLLYDADRIEEAASTEHETDLYE 293
Cdd:COG0437  115 VVEKCTFCADRLDEGLLPACVEACPTGALVFGDLDDPESEVSKRLAELPAYRLLP 169
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 170-270 3.65e-37

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: 133.67  E-value: 3.65e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 170 QFENTFMMYLPRLCEHCLNPSCVATCPSGAIYKREeDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKSEKCIFCYPR 249
Cdd:cd04410   37 EGGGLERAFLPVSCMHCEDPPCVKACPTGAIYKDE-DGIVLIDEDKCIGCGSCVEACPYGAIVFDPEPGKAVKCDLCGDR 115

                         90       100
                 ....*....|....*....|.
gi 505383367 250 IESGQPTVCSETCVGRIRYLG 270
Cdd:cd04410  116 LDEGLEPACVKACPTGALTFG 136
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 155-265 1.70e-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: 118.43  E-value: 1.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 155 ARDRNFQKIQKEMYGQFENTFMMYLPRLCEHCLNPSCVATCPSGAIYKREeDGIVLIDQDKCRGWRLCISGCPYKKIYFN 234
Cdd:cd16371   26 PPGVNWRRVYEYEGGEFPEVFAYFLSMSCNHCENPACVKVCPTGAITKRE-DGIVVVDQDKCIGCGYCVWACPYGAPQYN 104

                         90       100       110
                 ....*....|....*....|....*....|.
gi 505383367 235 WKSGKSEKCIFCYPRIESGQPTVCSETCVGR 265
Cdd:cd16371  105 PETGKMDKCDMCVDRLDEGEKPACVAACPTR 135
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
169-291 1.57e-25

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 104.96  E-value: 1.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 169 GQFENTFMMY--------------LPRLCEHCLNPSCVATCPSGAIYKREeDGIVLIDQDKCRGWRLCISGCPYKKIYFN 234
Cdd:PRK14993  72 GAFRTTVNQYqvqregsqevtnvlLPRLCNHCDNPPCVPVCPVQATFQRE-DGIVVVDNKRCVGCAYCVQACPYDARFIN 150

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 505383367 235 WKSGKSEKCIFCYPRIESGQPTVCSETCVGRIRYLGVLLYDADRIEEAAStEHETDL 291
Cdd:PRK14993 151 HETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRIATMLH-QHRDAI 206
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 176-263 1.92e-24

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: 99.40  E-value: 1.92e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 176 MMYLPRLCEHCLNPSCVATCPSGAIYkREEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKSEKCIFCYPRIESGQP 255
Cdd:cd16366   63 WLFRKDQCMHCTDAGCLAACPTGAII-RTETGTVVVDPETCIGCGYCVNACPFDIPRFDEETGRVAKCTLCYDRISNGLQ 141


                 ....*...
gi 505383367 256 TVCSETCV 263
Cdd:cd16366  142 PACVKTCP 149
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 162-288 2.70e-23

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: 97.01  E-value: 2.70e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 162 KIQKEMYGQFENTFMMYLPRLCEHCLNPSCVATCPSGAIYKREeDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKSE 241
Cdd:cd10552   43 RILRRERGQYPKVDVAYLPVPCNHCDNAPCIKAAKDGAVYKRD-DGIVIIDPEKAKGQKQLVDACPYGAIYWNEELQVPQ 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 505383367 242 KCIFCYPRIESGQPTV-CSETC-VGRIRYLgvllyDADRIEEAASTEHE 288
Cdd:cd10552  122 KCTFCAHLLDDGWKEPrCVQACpTGALRFG-----KLEDEEMAAKAAEE 165
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 176-262 3.26e-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: 95.51  E-value: 3.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 176 MMYLPRLCEHCLNPSCVATCPSGAIYKREEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKSEKCIFCYPRIESGQP 255
Cdd:cd10553   51 LKFVYMSCFHCENPWCVKACPTGAMQKREKDGIVYVDQELCIGCKACIEACPWGIPQWNPATGKVVKCDYCMDRIDQGLK 130


                 ....*..
gi 505383367 256 TVCSETC 262
Cdd:cd10553  131 PACVTGC 137
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 181-262 6.48e-23

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: 95.06  E-value: 6.48e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 181 RLCEHCLNPSCVATCPSGAIYKrEEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKSEKCIFCYPRIESGQPTVCSE 260
Cdd:cd10562   68 RQCMHCTDAACVKVCPTGALYK-TENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCFDRIENGMQPACVK 146


                 ..
gi 505383367 261 TC 262
Cdd:cd10562  147 TC 148
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 178-262 8.17e-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: 96.13  E-value: 8.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 178 YLPRLCEHCLNPSCVATCPSGAIYKREEdGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKSE--KCIFCYPRIESGQP 255
Cdd:cd10561   64 FVKRQCMHCLDPACVSACPVGALRKTPE-GPVTYDEDKCIGCRYCMVACPFNIPKYEWDSANPKirKCTMCYDRLKEGKQ 142


                 ....*..
gi 505383367 256 TVCSETC 262
Cdd:cd10561  143 PACVEAC 149
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 178-246 1.94e-20

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


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 87.25  E-value: 1.94e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505383367 178 YLPRLCEHCLNPSCVATCPSGAIYKREEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKSEKCIFC 246
Cdd:cd10550   44 DVPVVCRQCEDAPCVEACPVGAISRDEETGAVVVDEDKCIGCGMCVEACPFGAIRVDPETGKAIKCDLC 112
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 183-262 9.19e-20

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: 88.21  E-value: 9.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 183 CEHCLNPSCVATCPSGAIYKREEDGIVlIDQDKCRGWRLCISGCPYKKIYFNWKSGKSEKCIFCYPRIESGQPTVCSETC 262
Cdd:cd10560   78 CKHCTDAGCLEACPTGAIFRTEFGTVY-IQPDICNGCGYCVAACPFGVIDRNEETGRAHKCTLCYDRLKDGLEPACAKAC 156
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 177-262 2.68e-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: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 84.25  E-value: 2.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 177 MYLPRLCEHCLNPSCVATCPSGAIYkREEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKSEKCIFCYPRIESGQPT 256
Cdd:cd16374   37 ASVPVRCRHCEDAPCMEVCPTGAIY-RDEDGAVLVDPDKCIGCGMCAMACPFGVPRFDPSLKVAVKCDLCIDRRREGKLP 115


                 ....*.
gi 505383367 257 VCSETC 262
Cdd:cd16374  116 ACVEAC 121
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 178-262 8.80e-18

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: 81.70  E-value: 8.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 178 YLPRLCEHCLNPSCVATCPSGAIYKREEdGIVLIDQDKCRGWRLCISGCPYK--------KIYFNWK-----SGKSEKCI 244
Cdd:cd16368   86 FIPRRCMHCDNPPCAKLCPFGAARKTPE-GAVYIDDDLCFGGAKCRDVCPWHipqrqagvGIYLHLApeyagGGVMYKCD 164

                         90
                 ....*....|....*...
gi 505383367 245 FCYPRIESGQPTVCSETC 262
Cdd:cd16368  165 LCKDLLAQGKPPACIEAC 182
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
178-262 1.06e-17

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 83.95  E-value: 1.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 178 YLPRLCEHCLNPSCVATCPSGAIYKREEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKS--GKSEKCIFC----YPRIE 251
Cdd:PRK10882 107 YIKKQCMHCVDPNCVSVCPVSALTKDPKTGIVHYDKDVCTGCRYCMVACPFNVPKYDYNNpfGAIHKCELCnqkgVERLD 186

                         90
                 ....*....|.
gi 505383367 252 SGQPTVCSETC 262
Cdd:PRK10882 187 KGGLPGCVEVC 197
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 178-262 3.08e-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: 78.45  E-value: 3.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 178 YLPRLCEHCLNPSCVATCPSGAIYKREEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKSEKCIFCYPRiesGQPtV 257
Cdd:cd10563   52 SFPLQCRHCDEPPCVKACMSGAMHKDPETGIVIHDEEKCVGCWMCVMVCPYGAIRPDKERKVALKCDLCPDR---ETP-A 127


                 ....*
gi 505383367 258 CSETC 262
Cdd:cd10563  128 CVEAC 132
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 183-262 4.06e-16

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: 77.04  E-value: 4.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 183 CEHCLNPSCVATCPS-GAIYKReEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKSEKCIFCYPRIESGQPTVCSET 261
Cdd:cd10558   70 CMHCADPGCLKACPSpGAIVQY-ANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVGLEPACVKT 148


                 .
gi 505383367 262 C 262
Cdd:cd10558  149 C 149
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
177-262 5.30e-15

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 72.00  E-value: 5.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 177 MYLPRLCEHCLNPSCVATCPSGAIYKreEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKSE--KCIFCYPRIESGQ 254
Cdd:COG1142   46 VSAPVQCRHCEDAPCAEVCPVGAITR--DDGAVVVDEEKCIGCGLCVLACPFGAITMVGEKSRAVavKCDLCGGREGGPA 123


                 ....*...
gi 505383367 255 ptvCSETC 262
Cdd:COG1142  124 ---CVEAC 128
PRK09898 PRK09898
ferredoxin-like protein;
167-246 7.64e-13

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 67.55  E-value: 7.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 167 MYGQFentfmMYLPRLCEHCLNPSCVATCPSGAIYKREEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKSEKCIFC 246
Cdd:PRK09898 112 LYGDL-----NYTADTCRQCKEPQCMNVCPIGAITWQQKEGCITVDHKRCIGCSACTTACPWMMATVNTESKKSSKCVLC 186
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 183-228 3.26e-12

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: 64.20  E-value: 3.26e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 505383367 183 CEHCLNPSCVATCPSGAIYKreEDGIVLIDQDKCRGWRLCISGCPY 228
Cdd:cd10554   56 CRQCEDAPCANVCPVGAISQ--EDGVVQVDEERCIGCKLCVLACPF 99
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 179-262 4.70e-12

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: 64.33  E-value: 4.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 179 LPRLCEHCLNPSCVATCPSGAIyKREEDGIVL-IDQDKCRGWRLCISGCPYKKIYFNWKSGKSEKCIFCYPRIESGQPTV 257
Cdd:cd16369   47 APTVCMHCEDPTCAEVCPADAI-KVTEDGVVQsALKPRCIGCSNCVNACPFGVPKYDEERNLMMKCDMCYDRTSVGKAPM 125


                 ....*
gi 505383367 258 CSETC 262
Cdd:cd16369  126 CASVC 130
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 142-308 8.28e-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: 64.38  E-value: 8.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 142 NWEELLGGEFEKRA-----RDRNFQKIQKEMYGQFEN----TFMMYLPRLCEHCLNPSCVATCPS--GAIYKREEDGIVL 210
Cdd:cd10559   21 QWNQLPAEQTKNTGshqnpPDLSANTYKLVRFNEVRNengkPDWLFFPDQCRHCVTPPCKDAADMvpGAVIQDEATGAVV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 211 IDQdkcRGWRLC----ISGCPYKKIYFNWKSGKSEKCIFCYPRIESGQPTVCSETC-VGRIR---YLGVLLYDADRIEEA 282
Cdd:cd10559  101 FTE---KTAELDfddvLSACPYNIPRKNEATGRIVKCDMCIDRVSNGLQPACVKACpTGAMNfgdRDEMLAMASKRLEEL 177

                        170       180
                 ....*....|....*....|....*.
gi 505383367 283 ASTEHETDLYerqcdvflNPNDPAVI 308
Cdd:cd10559  178 KKRYPKANLY--------DPDDVRVI 195
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 163-246 2.02e-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: 55.74  E-value: 2.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 163 IQKEMYGQFENTFMMylpRLCEHCLNPSCVATCPSGAIYKREEDGIVLiDQDKCRGWRLCISGCPYKKIYFNWKSGKSEK 242
Cdd:cd16370   36 IRVRTRGGLEGGFTV---VVCRACEDPPCAEACPTGALEPRKGGGVVL-DKEKCIGCGNCVKACIVGAIFWDEETNKPII 111


                 ....
gi 505383367 243 CIFC 246
Cdd:cd16370  112 CIHC 115
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 179-246 1.35e-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: 1.35e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505383367 179 LPRLCEHCLNPSCVATCPSGAIyKREEDGIVLIDqDKCRGWRLCISGCPYKKIyfnwKSGKSEKCIFC 246
Cdd:cd16367   53 VPTACRHCVDPVCMIGCPTGAI-HRDDGGEVVIS-DACCGCGNCASACPYGAI----QMVRAVKCDLC 114
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
180-236 2.43e-08

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 50.88  E-value: 2.43e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 505383367 180 PRLCEHCLnpSCVATCPSGAIYkrEEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWK 236
Cdd:COG2768   10 EEKCIGCG--ACVKVCPVGAIS--IEDGKAVIDPEKCIGCGACIEVCPVGAIKIEWE 62
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 191-268 1.22e-07

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 50.47  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 191 CVATCPSGAIYKREEDGI-------VLIDQDKCRGWRLCISGCPYKKIYFNWKSGK---SEKCIFCypriesGqptVCSE 260
Cdd:cd10549   48 CVEVCPTGAIELTPEGKEyvpkekeAEIDEEKCIGCGLCVKVCPVDAITLEDELEIvidKEKCIGC------G---ICAE 118


                 ....*....
gi 505383367 261 TC-VGRIRY 268
Cdd:cd10549  119 VCpVNAIKL 127
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 177-262 4.21e-07

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: 48.87  E-value: 4.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 177 MYLPRLCEHCLNpsCVATCPSGAIYkREEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKSEKCIFCypriesGQpt 256
Cdd:cd16372   43 GYAINVCNQCGE--CIDVCPTGAIT-RDANGVVMINKKLCVGCLMCVGFCPEGAMFKHEDYPEPFKCIAC------GI-- 111


                 ....*.
gi 505383367 257 vCSETC 262
Cdd:cd16372  112 -CVKAC 116
PRK10330 PRK10330
electron transport protein HydN;
182-262 4.79e-07

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 49.89  E-value: 4.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 182 LCEHCLNPSCVATCPSGAIYKreEDGIVLIDQDKCRGWRLCISGCPYKKIY-------------FNWKSGKSE--KCIFC 246
Cdd:PRK10330  57 VCRQCEDAPCANVCPNGAISR--DKGFVHVMQERCIGCKTCVVACPYGAMEvvvrpvirnsgagLNVRAEKAEanKCDLC 134

                         90
                 ....*....|....*.
gi 505383367 247 YPRiESGqpTVCSETC 262
Cdd:PRK10330 135 NHR-EDG--PACMAAC 147
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 180-227 9.71e-07

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: 45.70  E-value: 9.71e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 505383367  180 PRLCEHCLNpsCVATCPS-----GAIYKREEDGIVLIDQDKCRGWRLCISGCP 227
Cdd:pfam13237   6 PDKCIGCGR--CTAACPAgltrvGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 183-262 1.22e-06

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 51.29  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 183 CEHCLNPSCVATCPSGAIyKREEDGIVLIdQDKCRGWRLCISGCPYKKIYF-------NWKSGKSEKCIFCYPRiESGQp 255
Cdd:PRK12769  56 CHHCEDAPCARSCPNGAI-SHVDDSIQVN-QQKCIGCKSCVVACPFGTMQIvltpvaaGKVKATAHKCDLCAGR-ENGP- 131


                 ....*..
gi 505383367 256 tVCSETC 262
Cdd:PRK12769 132 -ACVENC 137
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 180-232 2.48e-06

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 45.42  E-value: 2.48e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 505383367 180 PRLCEHCLnpSCVATCPSGAIYkrEEDGIVLIDQDKCRGWRLCISGCPYKKIY 232
Cdd:COG4231   21 EDKCTGCG--ACVKVCPADAIE--EGDGKAVIDPDLCIGCGSCVQVCPVDAIK 69
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 180-262 3.05e-06

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 50.02  E-value: 3.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 180 PRLCEHCLNPSCVATCPSGAIYKREEDgiVLIDQDKCRGWRLCISGCPYKKIyfNWKSGKSEKCIFCYPRiESGQpTVCS 259
Cdd:PRK12809  53 PVACHHCNNAPCVTACPVNALTFQSDS--VQLDEQKCIGCKRCAIACPFGVV--EMVDTIAQKCDLCNQR-SSGT-QACI 126


                 ...
gi 505383367 260 ETC 262
Cdd:PRK12809 127 EVC 129
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
191-231 3.35e-06

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 48.78  E-value: 3.35e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 505383367 191 CVATCPSGAIykREEDGIVLIDQDKCRGWRLCISGCPYKKI 231
Cdd:PRK07118 221 CVKACPAGAI--TMENNLAVIDQEKCTSCGKCVEKCPTKAI 259
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 180-237 3.65e-06

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 44.72  E-value: 3.65e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 505383367 180 PRLCEHCLnpSCVATCPSGAIyKREEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKS 237
Cdd:COG1149   10 EEKCIGCG--LCVEVCPEGAI-KLDDGGAPVVDPDLCTGCGACVGVCPTGAITLEERE 64
NapF COG1145
Ferredoxin [Energy production and conversion];
183-233 7.02e-06

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 47.41  E-value: 7.02e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 505383367 183 CEHCLNpsCVATCPSGAIYKREEDGIVLIDQDKCRGWRLCISGCPYKKIYF 233
Cdd:COG1145  184 CIGCGL--CVKVCPTGAIRLKDGKPQIVVDPDKCIGCGACVKVCPVGAISL 232
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
181-262 1.39e-05

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 47.33  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 181 RLCEHCLNPSCVATCPSGAIYKReeDGIVLIDQDKCRGWRLCISGCPYKKIYFN--WKSGKSEKCIFCypriesGQptvC 258
Cdd:COG4624   60 CCCRCCVAISCIQVRGIIIIDKR--GPSIIRDKEKCKNCYPCVRACPVKAIKVDdgKAEIDEEKCISC------GQ---C 128


                 ....
gi 505383367 259 SETC 262
Cdd:COG4624  129 VAVC 132
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 178-262 1.44e-05

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: 44.70  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 178 YLPRLCEHCLNpsCVATCPSGAIYKREEDGIVL---IDQDKCRGWRLCISGCP--------YKKIYFNWKSGKS---EKC 243
Cdd:cd10549    3 YDPEKCIGCGI--CVKACPTDAIELGPNGAIARgpeIDEDKCVFCGACVEVCPtgaieltpEGKEYVPKEKEAEideEKC 80

                         90
                 ....*....|....*....
gi 505383367 244 IFCypriesgqpTVCSETC 262
Cdd:cd10549   81 IGC---------GLCVKVC 90
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 182-232 1.97e-05

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 42.35  E-value: 1.97e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 505383367 182 LCEHClnPSCVATCPSGAIykREEDGIVLIDQDKCRGWRLCISGCPYKKIY 232
Cdd:COG2221   16 KCIGC--GLCVAVCPTGAI--SLDDGKLVIDEEKCIGCGACIRVCPTGAIK 62
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 183-229 2.04e-05

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 42.13  E-value: 2.04e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 505383367  183 CEHCLNpsCVATCPSGAIYKREED-----GIVLIDQDKCRGWRLCISGCPYK 229
Cdd:pfam12838   1 CIGCGA--CVAACPVGAITLDEVGekkgtKTVVIDPERCVGCGACVAVCPTG 50
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
191-231 3.26e-05

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 43.01  E-value: 3.26e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 505383367 191 CVATCPSGAIYKREeDGIVLIDQDKCRGWRLCISGCPYKKI 231
Cdd:PRK09623  59 CWKFCPEPAIYIKE-DGYVAIDYDYCKGCGICANECPTKAI 98
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
190-227 3.74e-05

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 45.69  E-value: 3.74e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 505383367 190 SCVATCPSGAIykREEDGIVLIDQDKCRGWRLCISGCP 227
Cdd:PRK07118 146 SCVAACPFDAI--HIENGLPVVDEDKCTGCGACVKACP 181
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 183-264 4.00e-05

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 43.78  E-value: 4.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 183 CEHCLNpSCVATCPSGAI--YKREED----GIVLIDQDKCRGW------RLCISGCPYKKIYFnwksgksekcifcYPRI 250
Cdd:cd16373   55 CDLCCD-ACVEVCPTGALrpLDLEEQkvkmGVAVIDKDRCLAWqggtdcGVCVEACPTEAIAI-------------VLED 120

                         90
                 ....*....|....
gi 505383367 251 ESGQPTVCSETCVG 264
Cdd:cd16373  121 DVLRPVVDEDKCVG 134
PRK13795 PRK13795
hypothetical protein; Provisional
 191-234 6.28e-05

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 45.76  E-value: 6.28e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 505383367 191 CVATCPSGAIYKREEDGIVLIDQDKCRGWRLCISGCPYKKIYFN 234
Cdd:PRK13795 589 CVGACPTGAIRIEEGKRKISVDEEKCIHCGKCTEVCPVVKYKDK 632
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
180-234 1.10e-04

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 44.85  E-value: 1.10e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 505383367 180 PRLCEHCLnpSCVATCPSGAIyKREEDGIVLIDQDKCRGWRLCISGCPYKKIYFN 234
Cdd:COG1148  495 PEKCTGCG--RCVEVCPYGAI-SIDEKGVAEVNPALCKGCGTCAAACPSGAISLK 546
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 183-231 2.45e-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: 40.04  E-value: 2.45e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 505383367 183 CEHCLNpsCVATCPSGAIyKREEDGIVLIDQDKCRGWRLCISGCPYKKI 231
Cdd:COG1144   32 CIGCGL--CWIVCPDGAI-RVDDGKYYGIDYDYCKGCGICAEVCPVKAI 77
napG PRK09476
quinol dehydrogenase periplasmic component; Provisional
 183-264 5.96e-04

quinol dehydrogenase periplasmic component; Provisional


Pssm-ID: 236534 [Multi-domain]  Cd Length: 254  Bit Score: 41.53  E-value: 5.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 183 CEHCLNPSCVATCPSGAIYKREED------GI-VLIDQDKCRGWR-----LCISGCPY--KKIYF----NWKSGKSEKCI 244
Cdd:PRK09476  99 CEMCEDIPCVKACPSGALDRELVDiddarmGLaVLVDQENCLNFQglrcdVCYRVCPLidKAITLelerNERTGKHAFFL 178

                         90       100
                 ....*....|....*....|
gi 505383367 245 fcypriesgqPTVCSETCVG 264
Cdd:PRK09476 179 ----------PTVHSDACTG 188
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 190-227 6.65e-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: 6.65e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 505383367 190 SCVATCPSGAIYKrEEDGIVLIDQDKCRGWRLCISGCP 227
Cdd:COG2878  144 DCIKACPFDAIVG-AAKGMHTVDEDKCTGCGLCVEACP 180
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 191-233 6.75e-04

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 38.19  E-value: 6.75e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 505383367 191 CVATCPSGAIY--KREEDGIVLIDQDKCRGWRLCISGCPYKKIYF 233
Cdd:COG1143   10 CVRVCPVDAITieDGEPGKVYVIDPDKCIGCGLCVEVCPTGAISM 54
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 182-227 7.15e-04

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 42.17  E-value: 7.15e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 505383367 182 LCEHCLNpsCVATCPSGAIYKREEDGIVLIDQDKCRGWRLCISGCP 227
Cdd:PRK12771 511 NCFECDN--CYGACPQDAIIKLGPGRRYHFDYDKCTGCHICADVCP 554
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 182-233 1.01e-03

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 37.77  E-value: 1.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 505383367 182 LCEHCLnpSCVATCPSGAIYKREEDGIVL-IDQDKCRGWRLCISGCPYKKIYF 233
Cdd:COG1146    9 KCIGCG--ACVEVCPVDVLELDEEGKKALvINPEECIGCGACELVCPVGAITV 59
porD PRK09625
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
 143-227 2.62e-03

pyruvate flavodoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 236596 [Multi-domain]  Cd Length: 133  Bit Score: 38.19  E-value: 2.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383367 143 WEELLGG----EFEKRARDRNFQKIQKEMYGQFeNTFM-----------MYLPRLCEHCLNpsCVATCPSGAIYKREEDg 207
Cdd:PRK09625   7 WDEFEMGavlfPFEKNAQSEMEKHNEERHYTEQ-SSFTtsvahwrvekpVHNNEICINCFN--CWVYCPDAAILSRDKK- 82

                         90       100
                 ....*....|....*....|
gi 505383367 208 IVLIDQDKCRGWRLCISGCP 227
Cdd:PRK09625  83 LKGVDYSHCKGCGVCVEVCP 102
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 180-231 4.87e-03

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: 39.38  E-value: 4.87e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 505383367 180 PRLCEHclnpSCVATCP---SG--AIYKREEDGIVLIDQDKCRGWRLCISGCPYKKI 231
Cdd:COG1245   14 PKKCNY----ECIKYCPvnrTGkeAIEIDEDDGKPVISEELCIGCGICVKKCPFDAI 66
porD PRK09624
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
 191-231 7.76e-03

pyruvate ferredoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 170017 [Multi-domain]  Cd Length: 105  Bit Score: 36.16  E-value: 7.76e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 505383367 191 CVATCPSGAIYKREEdGIVLIDQDKCRGWRLCISGCPYKKI 231
Cdd:PRK09624  59 CYIYCPEPAIYLDEE-GYPVFDYDYCKGCGICANECPTKAI 98
 
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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