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Conserved domains on  [gi|1837895546|gb|QJQ05116|]
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nitrate reductase subunit beta [Undibacterium piscinae]

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 ...
 1-484 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: 1078.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546   1 MRIRAQVGMVLNLDKCIGCHTCSVTCKNVWTSRDGVEYAWFNNVETKPGIGYPKEWENQQKWRGGWHRNEAGKLEPKQGG 80
Cdd:COG1140     1 MKVRAQIAMVMNLDKCIGCHTCSVTCKNVWTNREGVEYMWFNNVETKPGIGYPKRWEDQEKWKGGWELDRNGKLRLRAGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546  81 KLRILSNLFANPNLPSIDDYYEPFTFDYEHLQNAPLMQTPPTARPVSVITGKKMeKIVWGPNWEDDLGGEFSSRSRDQLF 160
Cdd:COG1140    81 RLKKLANIFANPDLPEIDDYYEPWTYDYENLINAPEGDDQPVARPRSLITGEPM-KIEWGPNWDDDLGGSFEYASKDPNL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 161 EGIQKEMYSTFESTFMMYLPRLCEHCLNPACVASCPSGSIYKREDDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKA 240
Cdd:COG1140   160 EGLQEEIYFEFENTFMFYLPRICEHCLNPACVASCPSGAIYKREEDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGKA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 241 EKCTFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADKIESAASVPDVQDLYEAQLDCFLDPHDPAVIAEARKHGIPDSW 320
Cdd:COG1140   240 EKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADRVEEAASVPDEQDLYEAQLDVFLDPHDPEVIAAARKDGIPDDW 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 321 ITSAQKSPVYKMAVEWKIAFPLHPEYRTLPMVWYVPPLSPIQKAAEAGH--MGMNGIIPDVKSLRIPVRYLANLLTAGKE 398
Cdd:COG1140   320 IEAAQRSPVYKLAKEWKVALPLHPEYRTLPMVWYVPPLSPVVDAVEAGGhdGDADGLFPAIDSLRIPVEYLANLFTAGDE 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 399 EPVLKALERMLAMRAYKRAEVVHGQEDKAVLAQVGLTAAQVEDMYQTMAIANYEDRFVIPSSHKEMVEDSFNEKGSCGFT 478
Cdd:COG1140   400 EPVEAALRRLAAMRAYMRAKNVGGEPDEEILAAVGLTEEQAEEMYRLLAIAKYEDRFVIPTAHREQAEDLYELQGGCGFD 479


                  ....*.
gi 1837895546 479 FGNGCS 484
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 ...
 1-484 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: 1078.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546   1 MRIRAQVGMVLNLDKCIGCHTCSVTCKNVWTSRDGVEYAWFNNVETKPGIGYPKEWENQQKWRGGWHRNEAGKLEPKQGG 80
Cdd:COG1140     1 MKVRAQIAMVMNLDKCIGCHTCSVTCKNVWTNREGVEYMWFNNVETKPGIGYPKRWEDQEKWKGGWELDRNGKLRLRAGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546  81 KLRILSNLFANPNLPSIDDYYEPFTFDYEHLQNAPLMQTPPTARPVSVITGKKMeKIVWGPNWEDDLGGEFSSRSRDQLF 160
Cdd:COG1140    81 RLKKLANIFANPDLPEIDDYYEPWTYDYENLINAPEGDDQPVARPRSLITGEPM-KIEWGPNWDDDLGGSFEYASKDPNL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 161 EGIQKEMYSTFESTFMMYLPRLCEHCLNPACVASCPSGSIYKREDDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKA 240
Cdd:COG1140   160 EGLQEEIYFEFENTFMFYLPRICEHCLNPACVASCPSGAIYKREEDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGKA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 241 EKCTFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADKIESAASVPDVQDLYEAQLDCFLDPHDPAVIAEARKHGIPDSW 320
Cdd:COG1140   240 EKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADRVEEAASVPDEQDLYEAQLDVFLDPHDPEVIAAARKDGIPDDW 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 321 ITSAQKSPVYKMAVEWKIAFPLHPEYRTLPMVWYVPPLSPIQKAAEAGH--MGMNGIIPDVKSLRIPVRYLANLLTAGKE 398
Cdd:COG1140   320 IEAAQRSPVYKLAKEWKVALPLHPEYRTLPMVWYVPPLSPVVDAVEAGGhdGDADGLFPAIDSLRIPVEYLANLFTAGDE 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 399 EPVLKALERMLAMRAYKRAEVVHGQEDKAVLAQVGLTAAQVEDMYQTMAIANYEDRFVIPSSHKEMVEDSFNEKGSCGFT 478
Cdd:COG1140   400 EPVEAALRRLAAMRAYMRAKNVGGEPDEEILAAVGLTEEQAEEMYRLLAIAKYEDRFVIPTAHREQAEDLYELQGGCGFD 479


                  ....*.
gi 1837895546 479 FGNGCS 484
Cdd:COG1140   480 FGGGCP 485
narH TIGR01660
nitrate reductase, beta subunit; The Nitrate reductase enzyme complex allows bacteria to use ...
 1-493 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: 964.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546   1 MRIRAQVGMVLNLDKCIGCHTCSVTCKNVWTSRDGVEYAWFNNVETKPGIGYPKEWENQQKWRGGWHRNEAGKLEPKQGG 80
Cdd:TIGR01660   1 MKIRSQIGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGIGYPKDWENQDKYKGGWVRKRDGKLEPRIGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546  81 KLRILSNLFANPNLPSIDDYYEPFTFDYEHLQNAPLMQTPPTARPVSVITGKKMEKIVWGPNWEDDLGGEFSSRSRDQLF 160
Cdd:TIGR01660  81 KWRVLANIFANPDLPSIDDYYEPFDFDYQHLHTAPEGKHQPTARPRSLITGERMEKIEWGPNWEDDLGGEFAKRRKDKNF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 161 EGIQKEMYSTFESTFMMYLPRLCEHCLNPACVASCPSGSIYKREDDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKA 240
Cdd:TIGR01660 161 DKIQKDIYGEFENTFMMYLPRLCEHCLNPACVASCPSGAIYKREEDGIVLIDQDKCRGWRMCISGCPYKKIYFNWKTGKS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 241 EKCTFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADKIESAASVPDVQDLYEAQLDCFLDPHDPAVIAEARKHGIPDSW 320
Cdd:TIGR01660 241 EKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADKIEEAASTENEKDLYHRQLDVFLDPNDPEVIAQAKKDGIPLSV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 321 ITSAQKSPVYKMAVEWKIAFPLHPEYRTLPMVWYVPPLSPIQKAAEAGHMGMNGIIPDVKSLRIPVRYLANLLTAGKEEP 400
Cdd:TIGR01660 321 IEAAQQSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQNAAEAGKVGANGIMPDVESLRIPVRYLANLLTAGDTKP 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 401 VLKALERMLAMRAYKRAEVVHGQEDKAVLAQVGLTAAQVEDMYQTMAIANYEDRFVIPSSHKEMVEDSFNEKGSCGFTFG 480
Cdd:TIGR01660 401 VLLALKRMLAMRHYMRAETVDGVVDTEVLEDVGLTEQQIEEMYRYLAIANYEDRFVIPSSHREIARDAFPERGGCGFSFG 480

                         490
                  ....*....|...
gi 1837895546 481 NGCSGGtSDGALF 493
Cdd:TIGR01660 481 DGCHGS-DTKNLF 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: 758.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546   3 IRAQVGMVLNLDKCIGCHTCSVTCKNVWTSRDGVEYAWFNNVETKPGIGYPKEWENQQKWRGGWHRNEaGKLEPKQGGKL 82
Cdd:cd10557     1 IRAQISMVMNLDKCIGCHTCSVTCKNVWTNRKGAEYMWWNNVETKPGIGYPKQWEDQEKYRGGWVLKG-GKLKLKRGGKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546  83 RILSNLFANPNLPSIDDYYEPFTFDYEHLQNAPLMQTPPTARPVSVITGKKMEkIVWGPNWEDDLGGEFSSRSRDQLFEG 162
Cdd:cd10557    80 QKLANIFYNPKLPEIDDYYEPWTYDYENLFTAPEGDDQPVARPKSLITGEPMD-IEWGPNWDDDLAGSPEYAAEDPNLKK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 163 IQKEMYSTFESTFMMYLPRLCEHCLNPACVASCPSGSIYKREDDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKAEK 242
Cdd:cd10557   159 LQEEIYLEFENTFMFYLPRICNHCLNPACVAACPSGAIYKREEDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSEK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 243 CTFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADKIESAASVPDVQDLYEAQLDCFLDPHDPAVIAEARKHGIPDSWIT 322
Cdd:cd10557   239 CIFCYPRLEAGQPTVCSETCVGRIRYLGVLLYDADRILEAAAVVPEKDLVEAQLDIILDPNDPEVIAAAKANGIPDNWIE 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1837895546 323 SAQKSPVYKMAVEWKIAFPLHPEYRTLPMVWYVPPLSPIQKAAEA 367
Cdd:cd10557   319 AAQRSPVYKMVKEWKIALPLHPEYRTLPMVFYVPPLSPVVAAVEA 363
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 174-272 5.33e-54

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: 177.06  E-value: 5.33e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 174 TFMMYLPRLCEHCLNPACVASCPSGSIYKREDDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKAEKCTFCYPRIEAG 253
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPVGAIYKDEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAG 80

                          90
                  ....*....|....*....
gi 1837895546 254 QPTVCSETCVGRIRYLGVL 272
Cdd:pfam13247  81 LLPACVQTCPTGAMNFGDR 99
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
172-272 1.46e-26

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 108.04  E-value: 1.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 172 ESTFMMYLPRLCEHCLNPACVASCPSGSIYKREDdGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKAEKCTFCYPRIE 251
Cdd:PRK14993   89 QEVTNVLLPRLCNHCDNPPCVPVCPVQATFQRED-GIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLE 167

                          90       100
                  ....*....|....*....|.
gi 1837895546 252 AGQPTVCSETCVGRIRYLGVL 272
Cdd:PRK14993  168 AGLLPACVESCVGGARIIGDI 188
 
Name Accession Description Interval E-value
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 1-484 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: 1078.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546   1 MRIRAQVGMVLNLDKCIGCHTCSVTCKNVWTSRDGVEYAWFNNVETKPGIGYPKEWENQQKWRGGWHRNEAGKLEPKQGG 80
Cdd:COG1140     1 MKVRAQIAMVMNLDKCIGCHTCSVTCKNVWTNREGVEYMWFNNVETKPGIGYPKRWEDQEKWKGGWELDRNGKLRLRAGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546  81 KLRILSNLFANPNLPSIDDYYEPFTFDYEHLQNAPLMQTPPTARPVSVITGKKMeKIVWGPNWEDDLGGEFSSRSRDQLF 160
Cdd:COG1140    81 RLKKLANIFANPDLPEIDDYYEPWTYDYENLINAPEGDDQPVARPRSLITGEPM-KIEWGPNWDDDLGGSFEYASKDPNL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 161 EGIQKEMYSTFESTFMMYLPRLCEHCLNPACVASCPSGSIYKREDDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKA 240
Cdd:COG1140   160 EGLQEEIYFEFENTFMFYLPRICEHCLNPACVASCPSGAIYKREEDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGKA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 241 EKCTFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADKIESAASVPDVQDLYEAQLDCFLDPHDPAVIAEARKHGIPDSW 320
Cdd:COG1140   240 EKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADRVEEAASVPDEQDLYEAQLDVFLDPHDPEVIAAARKDGIPDDW 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 321 ITSAQKSPVYKMAVEWKIAFPLHPEYRTLPMVWYVPPLSPIQKAAEAGH--MGMNGIIPDVKSLRIPVRYLANLLTAGKE 398
Cdd:COG1140   320 IEAAQRSPVYKLAKEWKVALPLHPEYRTLPMVWYVPPLSPVVDAVEAGGhdGDADGLFPAIDSLRIPVEYLANLFTAGDE 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 399 EPVLKALERMLAMRAYKRAEVVHGQEDKAVLAQVGLTAAQVEDMYQTMAIANYEDRFVIPSSHKEMVEDSFNEKGSCGFT 478
Cdd:COG1140   400 EPVEAALRRLAAMRAYMRAKNVGGEPDEEILAAVGLTEEQAEEMYRLLAIAKYEDRFVIPTAHREQAEDLYELQGGCGFD 479


                  ....*.
gi 1837895546 479 FGNGCS 484
Cdd:COG1140   480 FGGGCP 485
narH TIGR01660
nitrate reductase, beta subunit; The Nitrate reductase enzyme complex allows bacteria to use ...
 1-493 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: 964.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546   1 MRIRAQVGMVLNLDKCIGCHTCSVTCKNVWTSRDGVEYAWFNNVETKPGIGYPKEWENQQKWRGGWHRNEAGKLEPKQGG 80
Cdd:TIGR01660   1 MKIRSQIGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGIGYPKDWENQDKYKGGWVRKRDGKLEPRIGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546  81 KLRILSNLFANPNLPSIDDYYEPFTFDYEHLQNAPLMQTPPTARPVSVITGKKMEKIVWGPNWEDDLGGEFSSRSRDQLF 160
Cdd:TIGR01660  81 KWRVLANIFANPDLPSIDDYYEPFDFDYQHLHTAPEGKHQPTARPRSLITGERMEKIEWGPNWEDDLGGEFAKRRKDKNF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 161 EGIQKEMYSTFESTFMMYLPRLCEHCLNPACVASCPSGSIYKREDDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKA 240
Cdd:TIGR01660 161 DKIQKDIYGEFENTFMMYLPRLCEHCLNPACVASCPSGAIYKREEDGIVLIDQDKCRGWRMCISGCPYKKIYFNWKTGKS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 241 EKCTFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADKIESAASVPDVQDLYEAQLDCFLDPHDPAVIAEARKHGIPDSW 320
Cdd:TIGR01660 241 EKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADKIEEAASTENEKDLYHRQLDVFLDPNDPEVIAQAKKDGIPLSV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 321 ITSAQKSPVYKMAVEWKIAFPLHPEYRTLPMVWYVPPLSPIQKAAEAGHMGMNGIIPDVKSLRIPVRYLANLLTAGKEEP 400
Cdd:TIGR01660 321 IEAAQQSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQNAAEAGKVGANGIMPDVESLRIPVRYLANLLTAGDTKP 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 401 VLKALERMLAMRAYKRAEVVHGQEDKAVLAQVGLTAAQVEDMYQTMAIANYEDRFVIPSSHKEMVEDSFNEKGSCGFTFG 480
Cdd:TIGR01660 401 VLLALKRMLAMRHYMRAETVDGVVDTEVLEDVGLTEQQIEEMYRYLAIANYEDRFVIPSSHREIARDAFPERGGCGFSFG 480

                         490
                  ....*....|...
gi 1837895546 481 NGCSGGtSDGALF 493
Cdd:TIGR01660 481 DGCHGS-DTKNLF 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: 758.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546   3 IRAQVGMVLNLDKCIGCHTCSVTCKNVWTSRDGVEYAWFNNVETKPGIGYPKEWENQQKWRGGWHRNEaGKLEPKQGGKL 82
Cdd:cd10557     1 IRAQISMVMNLDKCIGCHTCSVTCKNVWTNRKGAEYMWWNNVETKPGIGYPKQWEDQEKYRGGWVLKG-GKLKLKRGGKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546  83 RILSNLFANPNLPSIDDYYEPFTFDYEHLQNAPLMQTPPTARPVSVITGKKMEkIVWGPNWEDDLGGEFSSRSRDQLFEG 162
Cdd:cd10557    80 QKLANIFYNPKLPEIDDYYEPWTYDYENLFTAPEGDDQPVARPKSLITGEPMD-IEWGPNWDDDLAGSPEYAAEDPNLKK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 163 IQKEMYSTFESTFMMYLPRLCEHCLNPACVASCPSGSIYKREDDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKAEK 242
Cdd:cd10557   159 LQEEIYLEFENTFMFYLPRICNHCLNPACVAACPSGAIYKREEDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSEK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 243 CTFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADKIESAASVPDVQDLYEAQLDCFLDPHDPAVIAEARKHGIPDSWIT 322
Cdd:cd10557   239 CIFCYPRLEAGQPTVCSETCVGRIRYLGVLLYDADRILEAAAVVPEKDLVEAQLDIILDPNDPEVIAAAKANGIPDNWIE 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1837895546 323 SAQKSPVYKMAVEWKIAFPLHPEYRTLPMVWYVPPLSPIQKAAEA 367
Cdd:cd10557   319 AAQRSPVYKMVKEWKIALPLHPEYRTLPMVFYVPPLSPVVAAVEA 363
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 6-417 7.50e-118

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: 349.68  E-value: 7.50e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546   6 QVGMVLNLDKCIGCHTCSVTCKNVWTSRDGVEYAWFNNVETKPGIGYPKEWENQqkwrGGWHRNEAgklEPKQGGklril 85
Cdd:cd10555     4 QLAMVMDLNKCIGCQTCTVACKTLWTNRNGREYMYWNNVETQPGKGYPKNWEKK----GGGFKDKG---ELKPGI----- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546  86 snlfanpnLPSIDDYYEPFTFDYEHLQnapLMQTPPTARPVSvitgkkMEKIVWGPNWEDDLGGefssrsrdqlfegiqk 165
Cdd:cd10555    72 --------IPTLEDYGVPWEYNHEEEL---FEGKGGRVRPSP------KGDPTWGPNWDEDQGA---------------- 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 166 emySTFESTFMMYLPRLCEHCLNPACVASCPSGSIYKREDDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKAEKCTF 245
Cdd:cd10555   119 ---GEYPNSYYFYLPRICNHCTNPACLAACPRKAIYKREEDGIVLVDQDRCRGYRYCVEACPYKKIYFNPVEQKSEKCIF 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 246 CYPRIEAGQPTVCSETCVGRIRYLGvllydadkiesaasvpdvqdlyeaqldcFLDphDPAviaearkhgipdswitsaq 325
Cdd:cd10555   196 CYPRIEKGVAPACARQCVGRIRFVG----------------------------YLD--DEE------------------- 226

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 326 kSPVYKMAVEWKIAFPLHPEYRTLPMVWYVPPLSPIQKAAEAGHMGMNgiipdvkslRIPVRYLANLLtaGKEepVLKAL 405
Cdd:cd10555   227 -SPVYKLVKKWKVALPLHPEYGTEPNVFYVPPLSPPKLGDDGEPTDEP---------RIPLEYLESLF--GPR--VKQAL 292

                         410
                  ....*....|..
gi 1837895546 406 ERMLAMRAYKRA 417
Cdd:cd10555   293 DTLKAEREKKRA 304
DMSO_red_II_bet TIGR03478
DMSO reductase family type II enzyme, iron-sulfur subunit; This model represents the ...
 6-417 1.35e-107

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: 323.66  E-value: 1.35e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546   6 QVGMVLNLDKCIGCHTCSVTCKNVWTSRDGVEYAWFNNVETKPGIGYPKEWENQQkwrGGWhrneagklepKQGGKLRIl 85
Cdd:TIGR03478   3 QLAYVIDLNKCIGCQTCTVACKNLWTNRPGREYMYWNNVETYPGKGYPRNWERKG---GGF----------KRGGKLKQ- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546  86 snlfaNPNLPSIDDYYEPFTFDYEHLqnapLMQ-TPPTARPvsvitgkkMEKIVWGPNWEDDLGGefssrsrdqlfegiq 164
Cdd:TIGR03478  69 -----PGIIPTLIDYGDPWEFNHEEV----LYEgKDETVRP--------HPTPTWGPNWDEDQGA--------------- 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 165 kemySTFESTFMMYLPRLCEHCLNPACVASCPSGSIYKREDDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKAEKCT 244
Cdd:TIGR03478 117 ----GEYPNNYYFYLPRICNHCTNPACLAACPTGAIYKREEDGIVLVDQERCKGYRYCVEACPYKKVYFNPQSQKSEKCI 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 245 FCYPRIEAGQPTVCSETCVGRIRYLGvllydadkiesaasvpdvqdlyeaqldcFLDPhdpaviaearkhgipdswitsa 324
Cdd:TIGR03478 193 GCYPRIEKGIAPACVKQCPGRIRFVG----------------------------YLDD---------------------- 222

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 325 QKSPVYKMAVEWKIAFPLHPEYRTLPMVWYVPPLSPiqkaaeaGHMGMNGIIPDVKslRIPVRYLANLLtaGKEepVLKA 404
Cdd:TIGR03478 223 EEGPVHKLVKRWKVALPLHPEYGTEPNVFYVPPMGP-------RGFGEDGEITDKT--RIPLDYLEGLF--GPG--VKQA 289

                         410
                  ....*....|...
gi 1837895546 405 LERMLAMRAYKRA 417
Cdd:TIGR03478 290 LATLHTEREKKRK 302
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 6-360 1.61e-107

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: 318.76  E-value: 1.61e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546   6 QVGMVLNLDKCIGCHTCSVTCKNVWTSRDGVEYAWFNNVETKPGIGYPKEWENQQKWRGGWHRneagklepkqggklril 85
Cdd:cd16365     2 QFAAVFNLNKCIGCQTCTVACKNAWTYRKGQEYMWWNNVETKPGGGYPQDWEVKTIDNGGNTR----------------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546  86 snlfanpnlpsiddyyepftfdyehlqnaplmqtpptarpvsvitgkkmekivwgpnweddlggefssrsrdqlfegiqk 165
Cdd:cd16365       --------------------------------------------------------------------------------

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 166 emystfestFMMYLPRLCEHCLNPACVASCPSGSIYKREDDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKAEKCTF 245
Cdd:cd16365    65 ---------FFFYLQRLCNHCTNPACLAACPRGAIYKREEDGIVLIDQKRCRGYRKCVEQCPYKKIYFNGLSRVSEKCIA 135

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 246 CYPRIEAGQPTVCSETCVGRIRYLGVLLYDadkiesaasvpdvqdlyeaqldcfldphdpaviaearkhgipdswitsaQ 325
Cdd:cd16365   136 CYPRIEGGDPTRCMSACVGRIRLQGFLDDN-------------------------------------------------P 166

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1837895546 326 KSPVYKMAVEWKIAFPLHPEYRTLPMVWYVPPLSP 360
Cdd:cd16365   167 KSPVTKLIRHWKVALPLHPEYGTEPNIYYVPPRWA 201
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 1-357 2.17e-75

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: 239.67  E-value: 2.17e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546   1 MRIRAQVGMVLNLDKCIGCHTCSVTCKNVWTSRDGVEYAWFNNVETKPGIGYPKEWEnqqkwrggwhrneagklepkqgg 80
Cdd:cd10556     6 SRPDKQFAMVFDTNKCIACQTCTMACKSTWTSGKGQEYMWWNNVETKPYGGYPLGWD----------------------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546  81 kLRILSNLFANPNLPsiDDYYEPFTFdyehlqnaplmqtPPTARPVSVITGKKMEKIVWG-PN-WEDDLGGEFSSRSRDQ 158
Cdd:cd10556    63 -VRLLDEEGGQTWAE--GGVYEGKTI-------------FEAAAAGEQVLGYRPEDEDWRyPNiGEDEVNGERTPDTGSS 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 159 LFEgiqkemystfESTFMMYLPRLCEHCLNPACVASCPSGSIYKREDDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSG 238
Cdd:cd10556   127 LPP----------HPIWFFYLPRICNHCTYPACLAACPRKAIYKREEDGIVLIDQERCRGYRECVEACPYKKPMYNPTTR 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 239 KAEKCTFCYPRIEAGQPTVCSETCVGRIRYLGvllydadkiesaasvpdvqdlyeaqldcFLDPHDPAVIAEARKHgipd 318
Cdd:cd10556   197 VSEKCIGCYPRIEEGDQTQCVSACIGKIRLQG----------------------------FINTPPDARWADDRDN---- 244

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1837895546 319 switsaqksPVYKMAVEWKIAFPLHPEYRTLPMVWYVPP 357
Cdd:cd10556   245 ---------PIDFLVHIKKVALPLYPQFGTEPNVYYIPP 274
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 174-272 5.33e-54

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: 177.06  E-value: 5.33e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 174 TFMMYLPRLCEHCLNPACVASCPSGSIYKREDDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKAEKCTFCYPRIEAG 253
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPVGAIYKDEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAG 80

                          90
                  ....*....|....*....
gi 1837895546 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 ...
 358-436 9.06e-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: 141.48  E-value: 9.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 358 LSPIQKAAEAGHMGM--NGIIPDVKSLRIPVRYLANLLTAGKEEPVLKALERMLAMRAYKRAEVVHGQEDKAVLAQVGLT 435
Cdd:pfam14711   1 LSPVVDAAEAGGHDEdaDGLFPAIDSLRIPVEYLANLLTAGDTEPVRRALRRLAAMRAYMRAKNVGGEPDESILEAVGLT 80


                  .
gi 1837895546 436 A 436
Cdd:pfam14711  81 E 81
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 170-355 1.84e-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: 144.21  E-value: 1.84e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 170 TFESTFMMYLPRLCEHCLNPACVASCPSGSIYKREdDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSS------------ 237
Cdd:cd10551    40 EYPNVKRTFLPVLCNHCENPPCVKVCPTGATYKRE-DGIVLVDYDKCIGCRYCMAACPYGARYFNPEEphefgevpvrpk 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 238 GKAEKCTFCYPRIEAGQPTVCSETCVGRIRYLGvllydadkiesaasvpdvqdlyeaqldcflDPHDPaviaearkhgip 317
Cdd:cd10551   119 GVVEKCTFCYHRLDEGLLPACVEACPTGARIFG------------------------------DLDDP------------ 156

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1837895546 318 dswitsaqKSPVYKMAVEWKiAFPLHPEYRTLPMVWYV 355
Cdd:cd10551   157 --------NSEVSKLLAERR-AYVLKPELGTKPKVYYI 185
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 170-284 1.31e-38

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 139.31  E-value: 1.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 170 TFESTFMMYLPRLCEHCLNPACVASCPSGSIYKREDdGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKAEKCTFCYPR 249
Cdd:COG0437    47 EFPNVEWLFVPVLCNHCDDPPCVKVCPTGATYKRED-GIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADR 125

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1837895546 250 IEAGQPTVCSETCVGRIRYLGvllyDADKIESAAS 284
Cdd:COG0437   126 LDEGLLPACVEACPTGALVFG----DLDDPESEVS 156
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 171-270 1.75e-36

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: 131.74  E-value: 1.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 171 FESTFMMYLPRLCEHCLNPACVASCPSGSIYKREDdGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKAEKCTFCYPRI 250
Cdd:cd04410    38 GGGLERAFLPVSCMHCEDPPCVKACPTGAIYKDED-GIVLIDEDKCIGCGSCVEACPYGAIVFDPEPGKAVKCDLCGDRL 116

                          90       100
                  ....*....|....*....|
gi 1837895546 251 EAGQPTVCSETCVGRIRYLG 270
Cdd:cd04410   117 DEGLEPACVKACPTGALTFG 136
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 170-265 1.23e-32

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: 121.52  E-value: 1.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 170 TFESTFMMYLPRLCEHCLNPACVASCPSGSIYKREDdGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKAEKCTFCYPR 249
Cdd:cd16371    41 EFPEVFAYFLSMSCNHCENPACVKVCPTGAITKRED-GIVVVDQDKCIGCGYCVWACPYGAPQYNPETGKMDKCDMCVDR 119

                          90
                  ....*....|....*.
gi 1837895546 250 IEAGQPTVCSETCVGR 265
Cdd:cd16371   120 LDEGEKPACVAACPTR 135
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
172-272 1.46e-26

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 108.04  E-value: 1.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 172 ESTFMMYLPRLCEHCLNPACVASCPSGSIYKREDdGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKAEKCTFCYPRIE 251
Cdd:PRK14993   89 QEVTNVLLPRLCNHCDNPPCVPVCPVQATFQRED-GIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLE 167

                          90       100
                  ....*....|....*....|.
gi 1837895546 252 AGQPTVCSETCVGRIRYLGVL 272
Cdd:PRK14993  168 AGLLPACVESCVGGARIIGDI 188
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 176-263 2.39e-25

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: 101.71  E-value: 2.39e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 176 MMYLPRLCEHCLNPACVASCPSGSIYKREDdGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKAEKCTFCYPRIEAGQP 255
Cdd:cd16366    63 WLFRKDQCMHCTDAGCLAACPTGAIIRTET-GTVVVDPETCIGCGYCVNACPFDIPRFDEETGRVAKCTLCYDRISNGLQ 141


                  ....*...
gi 1837895546 256 TVCSETCV 263
Cdd:cd16366   142 PACVKTCP 149
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 178-262 2.09e-24

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: 100.36  E-value: 2.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 178 YLPRLCEHCLNPACVASCPSGSIYKREdDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSS--GKAEKCTFCYPRIEAGQP 255
Cdd:cd10561    64 FVKRQCMHCLDPACVSACPVGALRKTP-EGPVTYDEDKCIGCRYCMVACPFNIPKYEWDSanPKIRKCTMCYDRLKEGKQ 142


                  ....*..
gi 1837895546 256 TVCSETC 262
Cdd:cd10561   143 PACVEAC 149
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 181-262 3.03e-24

uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes the beta-subunit of formate dehydrogenases that are as yet uncharacterized. Members of the DMSO reductase family include formate dehydrogenase N and O (FDH-N, FDH-O) and tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N, a major component of nitrate respiration of Escherichia coli, is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. It forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.


Pssm-ID: 319884 [Multi-domain]  Cd Length: 161  Bit Score: 98.91  E-value: 3.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 181 RLCEHCLNPACVASCPSGSIYKrEDDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKAEKCTFCYPRIEAGQPTVCSE 260
Cdd:cd10562    68 RQCMHCTDAACVKVCPTGALYK-TENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCFDRIENGMQPACVK 146


                  ..
gi 1837895546 261 TC 262
Cdd:cd10562   147 TC 148
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 176-262 4.89e-24

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: 97.82  E-value: 4.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 176 MMYLPRLCEHCLNPACVASCPSGSIYKREDDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKAEKCTFCYPRIEAGQP 255
Cdd:cd10553    51 LKFVYMSCFHCENPWCVKACPTGAMQKREKDGIVYVDQELCIGCKACIEACPWGIPQWNPATGKVVKCDYCMDRIDQGLK 130


                  ....*..
gi 1837895546 256 TVCSETC 262
Cdd:cd10553   131 PACVTGC 137
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 178-285 7.15e-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: 95.86  E-value: 7.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 178 YLPRLCEHCLNPACVASCPSGSIYKReDDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKAEKCTFCYPRIEAGQPTV 257
Cdd:cd10552    59 YLPVPCNHCDNAPCIKAAKDGAVYKR-DDGIVIIDPEKAKGQKQLVDACPYGAIYWNEELQVPQKCTFCAHLLDDGWKEP 137

                          90       100       110
                  ....*....|....*....|....*....|
gi 1837895546 258 -CSETC-VGRIRYLgvllyDADKIESAASV 285
Cdd:cd10552   138 rCVQACpTGALRFG-----KLEDEEMAAKA 162
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 183-262 5.74e-21

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: 91.68  E-value: 5.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 183 CEHCLNPACVASCPSGSIYKREDDGIVlVDQDKCRGWRMCISGCPYKKIYYNWSSGKAEKCTFCYPRIEAGQPTVCSETC 262
Cdd:cd10560    78 CKHCTDAGCLEACPTGAIFRTEFGTVY-IQPDICNGCGYCVAACPFGVIDRNEETGRAHKCTLCYDRLKDGLEPACAKAC 156
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 178-246 1.37e-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: 87.63  E-value: 1.37e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1837895546 178 YLPRLCEHCLNPACVASCPSGSIYKREDDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKAEKCTFC 246
Cdd:cd10550    44 DVPVVCRQCEDAPCVEACPVGAISRDEETGAVVVDEDKCIGCGMCVEACPFGAIRVDPETGKAIKCDLC 112
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 177-262 2.95e-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: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 86.95  E-value: 2.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 177 MYLPRLCEHCLNPACVASCPSGSIYkREDDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKAEKCTFCYPRIEAGQPT 256
Cdd:cd16374    37 ASVPVRCRHCEDAPCMEVCPTGAIY-RDEDGAVLVDPDKCIGCGMCAMACPFGVPRFDPSLKVAVKCDLCIDRRREGKLP 115


                  ....*.
gi 1837895546 257 VCSETC 262
Cdd:cd16374   116 ACVEAC 121
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 178-262 4.16e-18

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: 80.76  E-value: 4.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 178 YLPRLCEHCLNPACVASCPSGSIYKREDDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKAEKCTFCYPRieaGQPtV 257
Cdd:cd10563    52 SFPLQCRHCDEPPCVKACMSGAMHKDPETGIVIHDEEKCVGCWMCVMVCPYGAIRPDKERKVALKCDLCPDR---ETP-A 127


                  ....*
gi 1837895546 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 6.18e-18

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: 82.44  E-value: 6.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 183 CEHCLNPACVASCPS-GSIYKREdDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKAEKCTFCYPRIEAGQPTVCSET 261
Cdd:cd10558    70 CMHCADPGCLKACPSpGAIVQYA-NGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVGLEPACVKT 148


                  .
gi 1837895546 262 C 262
Cdd:cd10558   149 C 149
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
178-262 1.67e-16

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 80.48  E-value: 1.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 178 YLPRLCEHCLNPACVASCPSGSIYKREDDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSS--GKAEKCTFC----YPRIE 251
Cdd:PRK10882  107 YIKKQCMHCVDPNCVSVCPVSALTKDPKTGIVHYDKDVCTGCRYCMVACPFNVPKYDYNNpfGAIHKCELCnqkgVERLD 186

                          90
                  ....*....|.
gi 1837895546 252 AGQPTVCSETC 262
Cdd:PRK10882  187 KGGLPGCVEVC 197
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 178-262 3.15e-16

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


Pssm-ID: 319890 [Multi-domain]  Cd Length: 200  Bit Score: 77.08  E-value: 3.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 178 YLPRLCEHCLNPACVASCPSGSIYKREdDGIVLVDQDKCRGWRMCISGCPYK--------KIYYNWS-----SGKAEKCT 244
Cdd:cd16368    86 FIPRRCMHCDNPPCAKLCPFGAARKTP-EGAVYIDDDLCFGGAKCRDVCPWHipqrqagvGIYLHLApeyagGGVMYKCD 164

                          90
                  ....*....|....*...
gi 1837895546 245 FCYPRIEAGQPTVCSETC 262
Cdd:cd16368   165 LCKDLLAQGKPPACIEAC 182
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
177-262 4.23e-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: 4.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 177 MYLPRLCEHCLNPACVASCPSGSIYKreDDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGK--AEKCTFCYPRIEAGQ 254
Cdd:COG1142    46 VSAPVQCRHCEDAPCAEVCPVGAITR--DDGAVVVDEEKCIGCGLCVLACPFGAITMVGEKSRavAVKCDLCGGREGGPA 123


                  ....*...
gi 1837895546 255 ptvCSETC 262
Cdd:COG1142   124 ---CVEAC 128
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 183-262 1.15e-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: 65.36  E-value: 1.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 183 CEHCLNPACVASCPSGSIYKreDDGIVLVDQDKCRGWRMCISGCPYKKIY--------YNWSSG---KAEKCTFCYPRie 251
Cdd:cd10554    56 CRQCEDAPCANVCPVGAISQ--EDGVVQVDEERCIGCKLCVLACPFGAIEmapttvpgVDWERGpraVAVKCDLCAGR-- 131

                          90
                  ....*....|.
gi 1837895546 252 AGQPtVCSETC 262
Cdd:cd10554   132 EGGP-ACVEAC 141
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 179-262 4.69e-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: 4.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 179 LPRLCEHCLNPACVASCPSGSIyKREDDGIVL-VDQDKCRGWRMCISGCPYKKIYYNWSSGKAEKCTFCYPRIEAGQPTV 257
Cdd:cd16369    47 APTVCMHCEDPTCAEVCPADAI-KVTEDGVVQsALKPRCIGCSNCVNACPFGVPKYDEERNLMMKCDMCYDRTSVGKAPM 125


                  ....*
gi 1837895546 258 CSETC 262
Cdd:cd16369   126 CASVC 130
PRK09898 PRK09898
ferredoxin-like protein;
142-246 5.78e-11

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 62.16  E-value: 5.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 142 NWEDDLGGEFSSR---SRDQLF--EGIQKE--MYSTFestfmMYLPRLCEHCLNPACVASCPSGSIYKREDDGIVLVDQD 214
Cdd:PRK09898   80 NFNDGSVGTFFSRikiHRNYFFgdNGVGSGggLYGDL-----NYTADTCRQCKEPQCMNVCPIGAITWQQKEGCITVDHK 154

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1837895546 215 KCRGWRMCISGCPYKKIYYNWSSGKAEKCTFC 246
Cdd:PRK09898  155 RCIGCSACTTACPWMMATVNTESKKSSKCVLC 186
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 179-246 4.63e-10

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: 57.70  E-value: 4.63e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1837895546 179 LPRLCEHCLNPACVASCPSGSIyKREDDGIVLVDqDKCRGWRMCISGCPYKKIyynwSSGKAEKCTFC 246
Cdd:cd16367    53 VPTACRHCVDPVCMIGCPTGAI-HRDDGGEVVIS-DACCGCGNCASACPYGAI----QMVRAVKCDLC 114
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 176-308 5.00e-10

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: 58.98  E-value: 5.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 176 MMYLPRLCEHCLNPACVASCPS--GSIYKREDDGIVLVDQ---DKCRgwRMCISGCPYKKIYYNWSSGKAEKCTFCYPRI 250
Cdd:cd10559    64 WLFFPDQCRHCVTPPCKDAADMvpGAVIQDEATGAVVFTEktaELDF--DDVLSACPYNIPRKNEATGRIVKCDMCIDRV 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1837895546 251 EAGQPTVCSETC-VGRIRYlGvllyDADKIESAAS--VPDVQDLY-EAQLdcfLDPHDPAVI 308
Cdd:cd10559   142 SNGLQPACVKACpTGAMNF-G----DRDEMLAMASkrLEELKKRYpKANL---YDPDDVRVI 195
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 181-246 4.55e-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: 54.59  E-value: 4.55e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1837895546 181 RLCEHCLNPACVASCPSGSIYKREDDGIVLvDQDKCRGWRMCISGCPYKKIYYNWSSGKAEKCTFC 246
Cdd:cd16370    51 VVCRACEDPPCAEACPTGALEPRKGGGVVL-DKEKCIGCGNCVKACIVGAIFWDEETNKPIICIHC 115
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 183-262 8.22e-08

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 54.75  E-value: 8.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 183 CEHCLNPACVASCPSGSIYKREDDgiVLVDQDKCRGWRMCISGCPYKKI-------YYNWSSGKAEKCTFCYPRiEAGQp 255
Cdd:PRK12769   56 CHHCEDAPCARSCPNGAISHVDDS--IQVNQQKCIGCKSCVVACPFGTMqivltpvAAGKVKATAHKCDLCAGR-ENGP- 131


                  ....*..
gi 1837895546 256 tVCSETC 262
Cdd:PRK12769  132 -ACVENC 137
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 180-262 2.97e-07

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 53.11  E-value: 2.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 180 PRLCEHCLNPACVASCPSGSIYKREDDgiVLVDQDKCRGWRMCISGCPYKKIyyNWSSGKAEKCTFCYPRIEAGQptVCS 259
Cdd:PRK12809   53 PVACHHCNNAPCVTACPVNALTFQSDS--VQLDEQKCIGCKRCAIACPFGVV--EMVDTIAQKCDLCNQRSSGTQ--ACI 126


                  ...
gi 1837895546 260 ETC 262
Cdd:PRK12809  127 EVC 129
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 180-227 9.58e-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: 9.58e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1837895546 180 PRLCEHCLNpaCVASCPSGS-----IYKREDDGIVLVDQDKCRGWRMCISGCP 227
Cdd:pfam13237   6 PDKCIGCGR--CTAACPAGLtrvgaIVERLEGEAVRIGVWKCIGCGACVEACP 56
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
180-235 1.02e-06

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 46.26  E-value: 1.02e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1837895546 180 PRLCEHCLnpACVASCPSGSIYkrEDDGIVLVDQDKCRGWRMCISGCPYKKIYYNW 235
Cdd:COG2768    10 EEKCIGCG--ACVKVCPVGAIS--IEDGKAVIDPEKCIGCGACIEVCPVGAIKIEW 61
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 180-233 3.41e-06

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 45.03  E-value: 3.41e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1837895546 180 PRLCEHCLnpACVASCPSGSIYkrEDDGIVLVDQDKCRGWRMCISGCPYKKIYY 233
Cdd:COG4231    21 EDKCTGCG--ACVKVCPADAIE--EGDGKAVIDPDLCIGCGSCVQVCPVDAIKL 70
NapF COG1145
Ferredoxin [Energy production and conversion];
183-233 7.28e-06

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 47.41  E-value: 7.28e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1837895546 183 CEHCLnpACVASCPSGSIYKREDDGIVLVDQDKCRGWRMCISGCPYKKIYY 233
Cdd:COG1145   184 CIGCG--LCVKVCPTGAIRLKDGKPQIVVDPDKCIGCGACVKVCPVGAISL 232
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 190-268 1.96e-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: 44.31  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 190 ACVASCPSGSIYKREDDGI-------VLVDQDKCRGWRMCISGCPYKKIYYNWSSGK---AEKCTFCyprieaGqptVCS 259
Cdd:cd10549    47 ACVEVCPTGAIELTPEGKEyvpkekeAEIDEEKCIGCGLCVKVCPVDAITLEDELEIvidKEKCIGC------G---ICA 117

                          90
                  ....*....|
gi 1837895546 260 ETC-VGRIRY 268
Cdd:cd10549   118 EVCpVNAIKL 127
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 182-233 2.96e-05

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 41.96  E-value: 2.96e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1837895546 182 LCEHClnPACVASCPSGSIykREDDGIVLVDQDKCRGWRMCISGCPYKKIYY 233
Cdd:COG2221    16 KCIGC--GLCVAVCPTGAI--SLDDGKLVIDEEKCIGCGACIRVCPTGAIKG 63
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 180-231 1.23e-04

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 40.10  E-value: 1.23e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1837895546 180 PRLCEHCLnpACVASCPSGSIyKREDDGIVLVDQDKCRGWRMCISGCPYKKI 231
Cdd:COG1149    10 EEKCIGCG--LCVEVCPEGAI-KLDDGGAPVVDPDLCTGCGACVGVCPTGAI 58
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 177-262 1.26e-04

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


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 41.94  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 177 MYLPRLCEHCLNpaCVASCPSGSIYkREDDGIVLVDQDKCRGWRMCISGCPYKKIYYNWSSGKAEKCTFCyprieaGQpt 256
Cdd:cd16372    43 GYAINVCNQCGE--CIDVCPTGAIT-RDANGVVMINKKLCVGCLMCVGFCPEGAMFKHEDYPEPFKCIAC------GI-- 111


                  ....*.
gi 1837895546 257 vCSETC 262
Cdd:cd16372   112 -CVKAC 116
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 183-229 1.67e-04

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 39.43  E-value: 1.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1837895546 183 CEHCLnpACVASCPSGSIYKREDD-----GIVLVDQDKCRGWRMCISGCPYK 229
Cdd:pfam12838   1 CIGCG--ACVAACPVGAITLDEVGekkgtKTVVIDPERCVGCGACVAVCPTG 50
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
191-231 2.95e-04

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 40.31  E-value: 2.95e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1837895546 191 CVASCPSGSIYKREDdGIVLVDQDKCRGWRMCISGCPYKKI 231
Cdd:PRK09623   59 CWKFCPEPAIYIKED-GYVAIDYDYCKGCGICANECPTKAI 98
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
181-262 3.97e-04

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 42.71  E-value: 3.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 181 RLCEHCLNPACVASCPSGSIYKRedDGIVLVDQDKCRGWRMCISGCPYKKIYYNwsSGKA----EKCTFCyprieaGQpt 256
Cdd:COG4624    60 CCCRCCVAISCIQVRGIIIIDKR--GPSIIRDKEKCKNCYPCVRACPVKAIKVD--DGKAeideEKCISC------GQ-- 127


                  ....*.
gi 1837895546 257 vCSETC 262
Cdd:COG4624   128 -CVAVC 132
PRK13795 PRK13795
hypothetical protein; Provisional
 191-232 5.20e-04

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 42.67  E-value: 5.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1837895546 191 CVASCPSGSIYKREDDGIVLVDQDKCRGWRMCISGCPYKKIY 232
Cdd:PRK13795  589 CVGACPTGAIRIEEGKRKISVDEEKCIHCGKCTEVCPVVKYK 630
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
191-231 5.42e-04

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 41.84  E-value: 5.42e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1837895546 191 CVASCPSGSIykREDDGIVLVDQDKCRGWRMCISGCPYKKI 231
Cdd:PRK07118  221 CVKACPAGAI--TMENNLAVIDQEKCTSCGKCVEKCPTKAI 259
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 183-231 6.32e-04

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 38.88  E-value: 6.32e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1837895546 183 CEHCLNpaCVASCPSGSIyKREDDGIVLVDQDKCRGWRMCISGCPYKKI 231
Cdd:COG1144    32 CIGCGL--CWIVCPDGAI-RVDDGKYYGIDYDYCKGCGICAEVCPVKAI 77
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 183-264 7.88e-04

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 39.93  E-value: 7.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1837895546 183 CEHCLNpACVASCPSGSIYKREDD------GIVLVDQDKCRGW------RMCISGCPYKkiyynwssGKAEKctfcyPRI 250
Cdd:cd16373    55 CDLCCD-ACVEVCPTGALRPLDLEeqkvkmGVAVIDKDRCLAWqggtdcGVCVEACPTE--------AIAIV-----LED 120

                          90
                  ....*....|....
gi 1837895546 251 EAGQPTVCSETCVG 264
Cdd:cd16373   121 DVLRPVVDEDKCVG 134
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 178-232 2.75e-03

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: 38.15  E-value: 2.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1837895546 178 YLPRLCEHCLnpACVASCPSGSIYKREDDGIVL---VDQDKCRGWRMCISGCPYKKIY 232
Cdd:cd10549     3 YDPEKCIGCG--ICVKACPTDAIELGPNGAIARgpeIDEDKCVFCGACVEVCPTGAIE 58
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 182-233 2.83e-03

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 36.23  E-value: 2.83e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1837895546 182 LCEHCLnpACVASCPSGSIYKREDDGIVLV-DQDKCRGWRMCISGCPYKKIYY 233
Cdd:COG1146     9 KCIGCG--ACVEVCPVDVLELDEEGKKALViNPEECIGCGACELVCPVGAITV 59
porD PRK09625
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
 178-227 2.96e-03

pyruvate flavodoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 236596 [Multi-domain]  Cd Length: 133  Bit Score: 38.19  E-value: 2.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1837895546 178 YLPRLCEHCLNpaCVASCPSGSIYKReDDGIVLVDQDKCRGWRMCISGCP 227
Cdd:PRK09625   56 HNNEICINCFN--CWVYCPDAAILSR-DKKLKGVDYSHCKGCGVCVEVCP 102
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 182-227 3.50e-03

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 39.86  E-value: 3.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1837895546 182 LCEHCLNpaCVASCPSGSIYKREDDGIVLVDQDKCRGWRMCISGCP 227
Cdd:PRK12771  511 NCFECDN--CYGACPQDAIIKLGPGRRYHFDYDKCTGCHICADVCP 554
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
191-227 3.78e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 39.15  E-value: 3.78e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1837895546 191 CVASCPSGSIykREDDGIVLVDQDKCRGWRMCISGCP 227
Cdd:PRK07118  147 CVAACPFDAI--HIENGLPVVDEDKCTGCGACVKACP 181
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 181-234 3.92e-03

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: 37.38  E-value: 3.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1837895546 181 RLCEHCLnpACVASCPSGSIyKREDDGIVLVDQDKCRGWRMCISGCPYKKIYYN 234
Cdd:cd10549    78 EKCIGCG--LCVKVCPVDAI-TLEDELEIVIDKEKCIGCGICAEVCPVNAIKLV 128
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 183-232 7.96e-03

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: 35.11  E-value: 7.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1837895546 183 CEHCLnpACVASCPSGSIY--KREDDGIVLVDQDKCRGWRMCISGCPYKKIY 232
Cdd:COG1143     4 CIGCG--LCVRVCPVDAITieDGEPGKVYVIDPDKCIGCGLCVEVCPTGAIS 53
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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