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Conserved domains on  [gi|1450693874|dbj|GBU73475|]
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nitrate reductase subunit beta [Staphylococcus aureus]

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: 1027.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874   1 MKIKAQVAMVLNLDKCIGCHTCSVTCKNTWTNRPGAEYMWFNNVETKPGVGYPKRWEDQEHYKGGWVLNRKGKLELKSGS 80
Cdd:COG1140     1 MKVRAQIAMVMNLDKCIGCHTCSVTCKNVWTNREGVEYMWFNNVETKPGIGYPKRWEDQEKWKGGWELDRNGKLRLRAGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874  81 RISKiaLGKIFYNPDMPLIKDYYEPWNYNYEHLTTAKSGNHSPVARAYSEITGDNIEIEWGPNWEDDLAGGHVTGPKDPN 160
Cdd:COG1140    81 RLKK--LANIFANPDLPEIDDYYEPWTYDYENLINAPEGDDQPVARPRSLITGEPMKIEWGPNWDDDLGGSFEYASKDPN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 161 IKKIEEDIKFQFDETFMMYLPRLCEHCLNPSCVASCPSGAMYKRDEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNK 240
Cdd:COG1140   159 LEGLQEEIYFEFENTFMFYLPRICEHCLNPACVASCPSGAIYKREEDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 241 AEKCTFCFPRIEAGMPTVCSETCTGRMRYLGVLLYDADRVHEAASAVDEKDLYEKQLDIFLNPFDEEVIAQAEKDGISYD 320
Cdd:COG1140   239 AEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADRVEEAASVPDEQDLYEAQLDVFLDPHDPEVIAAARKDGIPDD 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 321 WIEAAQNSPIYKLAIEYKLAFPLHPEFRTMPMVWYCPPLSPIMSYFEGKNTNQNPDAIFPAIEEMRLPIEYLANIFTAGD 400
Cdd:COG1140   319 WIEAAQRSPVYKLAKEWKVALPLHPEYRTLPMVWYVPPLSPVVDAVEAGGHDGDADGLFPAIDSLRIPVEYLANLFTAGD 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 401 TKPVKEALQRMAMMRSYMRSQVTQQPFDTSRLERLGLTERQTKDMYRLLGLAKYEDRFVIPTSHKETYLDTYHAQGSTGY 480
Cdd:COG1140   399 EEPVEAALRRLAAMRAYMRAKNVGGEPDEEILAAVGLTEEQAEEMYRLLAIAKYEDRFVIPTAHREQAEDLYELQGGCGF 478


                  ....
gi 1450693874 481 NYGG 484
Cdd:COG1140   479 DFGG 482
 
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: 1027.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874   1 MKIKAQVAMVLNLDKCIGCHTCSVTCKNTWTNRPGAEYMWFNNVETKPGVGYPKRWEDQEHYKGGWVLNRKGKLELKSGS 80
Cdd:COG1140     1 MKVRAQIAMVMNLDKCIGCHTCSVTCKNVWTNREGVEYMWFNNVETKPGIGYPKRWEDQEKWKGGWELDRNGKLRLRAGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874  81 RISKiaLGKIFYNPDMPLIKDYYEPWNYNYEHLTTAKSGNHSPVARAYSEITGDNIEIEWGPNWEDDLAGGHVTGPKDPN 160
Cdd:COG1140    81 RLKK--LANIFANPDLPEIDDYYEPWTYDYENLINAPEGDDQPVARPRSLITGEPMKIEWGPNWDDDLGGSFEYASKDPN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 161 IKKIEEDIKFQFDETFMMYLPRLCEHCLNPSCVASCPSGAMYKRDEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNK 240
Cdd:COG1140   159 LEGLQEEIYFEFENTFMFYLPRICEHCLNPACVASCPSGAIYKREEDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 241 AEKCTFCFPRIEAGMPTVCSETCTGRMRYLGVLLYDADRVHEAASAVDEKDLYEKQLDIFLNPFDEEVIAQAEKDGISYD 320
Cdd:COG1140   239 AEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADRVEEAASVPDEQDLYEAQLDVFLDPHDPEVIAAARKDGIPDD 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 321 WIEAAQNSPIYKLAIEYKLAFPLHPEFRTMPMVWYCPPLSPIMSYFEGKNTNQNPDAIFPAIEEMRLPIEYLANIFTAGD 400
Cdd:COG1140   319 WIEAAQRSPVYKLAKEWKVALPLHPEYRTLPMVWYVPPLSPVVDAVEAGGHDGDADGLFPAIDSLRIPVEYLANLFTAGD 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 401 TKPVKEALQRMAMMRSYMRSQVTQQPFDTSRLERLGLTERQTKDMYRLLGLAKYEDRFVIPTSHKETYLDTYHAQGSTGY 480
Cdd:COG1140   399 EEPVEAALRRLAAMRAYMRAKNVGGEPDEEILAAVGLTEEQAEEMYRLLAIAKYEDRFVIPTAHREQAEDLYELQGGCGF 478


                  ....
gi 1450693874 481 NYGG 484
Cdd:COG1140   479 DFGG 482
narH TIGR01660
nitrate reductase, beta subunit; The Nitrate reductase enzyme complex allows bacteria to use ...
 1-494 0e+00

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


Pssm-ID: 211677 [Multi-domain]  Cd Length: 492  Bit Score: 834.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874   1 MKIKAQVAMVLNLDKCIGCHTCSVTCKNTWTNRPGAEYMWFNNVETKPGVGYPKRWEDQEHYKGGWVLNRKGKLELKSGS 80
Cdd:TIGR01660   1 MKIRSQIGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGIGYPKDWENQDKYKGGWVRKRDGKLEPRIGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874  81 RISKiaLGKIFYNPDMPLIKDYYEPWNYNYEHLTTAKSGNHSPVARAYSEITGDNIE-IEWGPNWEDDLAGGHVTGPKDP 159
Cdd:TIGR01660  81 KWRV--LANIFANPDLPSIDDYYEPFDFDYQHLHTAPEGKHQPTARPRSLITGERMEkIEWGPNWEDDLGGEFAKRRKDK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 160 NIKKIEEDIKFQFDETFMMYLPRLCEHCLNPSCVASCPSGAMYKRDEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTN 239
Cdd:TIGR01660 159 NFDKIQKDIYGEFENTFMMYLPRLCEHCLNPACVASCPSGAIYKREEDGIVLIDQDKCRGWRMCISGCPYKKIYFNWKTG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 240 KAEKCTFCFPRIEAGMPTVCSETCTGRMRYLGVLLYDADRVHEAASAVDEKDLYEKQLDIFLNPFDEEVIAQAEKDGISY 319
Cdd:TIGR01660 239 KSEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADKIEEAASTENEKDLYHRQLDVFLDPNDPEVIAQAKKDGIPL 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 320 DWIEAAQNSPIYKLAIEYKLAFPLHPEFRTMPMVWYCPPLSPIMSYFEGknTNQNPDAIFPAIEEMRLPIEYLANIFTAG 399
Cdd:TIGR01660 319 SVIEAAQQSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQNAAEA--GKVGANGIMPDVESLRIPVRYLANLLTAG 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 400 DTKPVKEALQRMAMMRSYMRSQVTQQPFDTSRLERLGLTERQTKDMYRLLGLAKYEDRFVIPTSHKETYLDTYHAQGSTG 479
Cdd:TIGR01660 397 DTKPVLLALKRMLAMRHYMRAETVDGVVDTEVLEDVGLTEQQIEEMYRYLAIANYEDRFVIPSSHREIARDAFPERGGCG 476

                         490
                  ....*....|....*
gi 1450693874 480 YNYGGEHFGDNCEGC 494
Cdd:TIGR01660 477 FSFGDGCHGSDTKNL 491
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 3-368 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: 739.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874   3 IKAQVAMVLNLDKCIGCHTCSVTCKNTWTNRPGAEYMWFNNVETKPGVGYPKRWEDQEHYKGGWVLnRKGKLELKSGSRI 82
Cdd:cd10557     1 IRAQISMVMNLDKCIGCHTCSVTCKNVWTNRKGAEYMWWNNVETKPGIGYPKQWEDQEKYRGGWVL-KGGKLKLKRGGKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874  83 SKiaLGKIFYNPDMPLIKDYYEPWNYNYEHLTTAKSGNHSPVARAYSEITGDNIEIEWGPNWEDDLAGGHVTGPKDPNIK 162
Cdd:cd10557    80 QK--LANIFYNPKLPEIDDYYEPWTYDYENLFTAPEGDDQPVARPKSLITGEPMDIEWGPNWDDDLAGSPEYAAEDPNLK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 163 KIEEDIKFQFDETFMMYLPRLCEHCLNPSCVASCPSGAMYKRDEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNKAE 242
Cdd:cd10557   158 KLQEEIYLEFENTFMFYLPRICNHCLNPACVAACPSGAIYKREEDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSE 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 243 KCTFCFPRIEAGMPTVCSETCTGRMRYLGVLLYDADRVHEAASAVDEKDLYEKQLDIFLNPFDEEVIAQAEKDGISYDWI 322
Cdd:cd10557   238 KCIFCYPRLEAGQPTVCSETCVGRIRYLGVLLYDADRILEAAAVVPEKDLVEAQLDIILDPNDPEVIAAAKANGIPDNWI 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1450693874 323 EAAQNSPIYKLAIEYKLAFPLHPEFRTMPMVWYCPPLSPIMSYFEG 368
Cdd:cd10557   318 EAAQRSPVYKMVKEWKIALPLHPEYRTLPMVFYVPPLSPVVAAVEA 363
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 175-273 1.58e-51

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: 170.51  E-value: 1.58e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 175 TFMMYLPRLCEHCLNPSCVASCPSGAMYKRDEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCFPRIEAG 254
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPVGAIYKDEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAG 80

                          90
                  ....*....|....*....
gi 1450693874 255 MPTVCSETCTGRMRYLGVL 273
Cdd:pfam13247  81 LLPACVQTCPTGAMNFGDR 99
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
180-289 1.55e-28

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 113.43  E-value: 1.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 180 LPRLCEHCLNPSCVASCPSGAMYKRdEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCFPRIEAGMPTVC 259
Cdd:PRK14993   96 LPRLCNHCDNPPCVPVCPVQATFQR-EDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPAC 174

                          90       100       110
                  ....*....|....*....|....*....|
gi 1450693874 260 SETCTGRMRYLGVLlydADRVHEAASAVDE 289
Cdd:PRK14993  175 VESCVGGARIIGDI---KDPHSRIATMLHQ 201
 
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: 1027.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874   1 MKIKAQVAMVLNLDKCIGCHTCSVTCKNTWTNRPGAEYMWFNNVETKPGVGYPKRWEDQEHYKGGWVLNRKGKLELKSGS 80
Cdd:COG1140     1 MKVRAQIAMVMNLDKCIGCHTCSVTCKNVWTNREGVEYMWFNNVETKPGIGYPKRWEDQEKWKGGWELDRNGKLRLRAGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874  81 RISKiaLGKIFYNPDMPLIKDYYEPWNYNYEHLTTAKSGNHSPVARAYSEITGDNIEIEWGPNWEDDLAGGHVTGPKDPN 160
Cdd:COG1140    81 RLKK--LANIFANPDLPEIDDYYEPWTYDYENLINAPEGDDQPVARPRSLITGEPMKIEWGPNWDDDLGGSFEYASKDPN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 161 IKKIEEDIKFQFDETFMMYLPRLCEHCLNPSCVASCPSGAMYKRDEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNK 240
Cdd:COG1140   159 LEGLQEEIYFEFENTFMFYLPRICEHCLNPACVASCPSGAIYKREEDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 241 AEKCTFCFPRIEAGMPTVCSETCTGRMRYLGVLLYDADRVHEAASAVDEKDLYEKQLDIFLNPFDEEVIAQAEKDGISYD 320
Cdd:COG1140   239 AEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADRVEEAASVPDEQDLYEAQLDVFLDPHDPEVIAAARKDGIPDD 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 321 WIEAAQNSPIYKLAIEYKLAFPLHPEFRTMPMVWYCPPLSPIMSYFEGKNTNQNPDAIFPAIEEMRLPIEYLANIFTAGD 400
Cdd:COG1140   319 WIEAAQRSPVYKLAKEWKVALPLHPEYRTLPMVWYVPPLSPVVDAVEAGGHDGDADGLFPAIDSLRIPVEYLANLFTAGD 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 401 TKPVKEALQRMAMMRSYMRSQVTQQPFDTSRLERLGLTERQTKDMYRLLGLAKYEDRFVIPTSHKETYLDTYHAQGSTGY 480
Cdd:COG1140   399 EEPVEAALRRLAAMRAYMRAKNVGGEPDEEILAAVGLTEEQAEEMYRLLAIAKYEDRFVIPTAHREQAEDLYELQGGCGF 478


                  ....
gi 1450693874 481 NYGG 484
Cdd:COG1140   479 DFGG 482
narH TIGR01660
nitrate reductase, beta subunit; The Nitrate reductase enzyme complex allows bacteria to use ...
 1-494 0e+00

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


Pssm-ID: 211677 [Multi-domain]  Cd Length: 492  Bit Score: 834.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874   1 MKIKAQVAMVLNLDKCIGCHTCSVTCKNTWTNRPGAEYMWFNNVETKPGVGYPKRWEDQEHYKGGWVLNRKGKLELKSGS 80
Cdd:TIGR01660   1 MKIRSQIGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGIGYPKDWENQDKYKGGWVRKRDGKLEPRIGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874  81 RISKiaLGKIFYNPDMPLIKDYYEPWNYNYEHLTTAKSGNHSPVARAYSEITGDNIE-IEWGPNWEDDLAGGHVTGPKDP 159
Cdd:TIGR01660  81 KWRV--LANIFANPDLPSIDDYYEPFDFDYQHLHTAPEGKHQPTARPRSLITGERMEkIEWGPNWEDDLGGEFAKRRKDK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 160 NIKKIEEDIKFQFDETFMMYLPRLCEHCLNPSCVASCPSGAMYKRDEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTN 239
Cdd:TIGR01660 159 NFDKIQKDIYGEFENTFMMYLPRLCEHCLNPACVASCPSGAIYKREEDGIVLIDQDKCRGWRMCISGCPYKKIYFNWKTG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 240 KAEKCTFCFPRIEAGMPTVCSETCTGRMRYLGVLLYDADRVHEAASAVDEKDLYEKQLDIFLNPFDEEVIAQAEKDGISY 319
Cdd:TIGR01660 239 KSEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADKIEEAASTENEKDLYHRQLDVFLDPNDPEVIAQAKKDGIPL 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 320 DWIEAAQNSPIYKLAIEYKLAFPLHPEFRTMPMVWYCPPLSPIMSYFEGknTNQNPDAIFPAIEEMRLPIEYLANIFTAG 399
Cdd:TIGR01660 319 SVIEAAQQSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQNAAEA--GKVGANGIMPDVESLRIPVRYLANLLTAG 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 400 DTKPVKEALQRMAMMRSYMRSQVTQQPFDTSRLERLGLTERQTKDMYRLLGLAKYEDRFVIPTSHKETYLDTYHAQGSTG 479
Cdd:TIGR01660 397 DTKPVLLALKRMLAMRHYMRAETVDGVVDTEVLEDVGLTEQQIEEMYRYLAIANYEDRFVIPSSHREIARDAFPERGGCG 476

                         490
                  ....*....|....*
gi 1450693874 480 YNYGGEHFGDNCEGC 494
Cdd:TIGR01660 477 FSFGDGCHGSDTKNL 491
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 3-368 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: 739.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874   3 IKAQVAMVLNLDKCIGCHTCSVTCKNTWTNRPGAEYMWFNNVETKPGVGYPKRWEDQEHYKGGWVLnRKGKLELKSGSRI 82
Cdd:cd10557     1 IRAQISMVMNLDKCIGCHTCSVTCKNVWTNRKGAEYMWWNNVETKPGIGYPKQWEDQEKYRGGWVL-KGGKLKLKRGGKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874  83 SKiaLGKIFYNPDMPLIKDYYEPWNYNYEHLTTAKSGNHSPVARAYSEITGDNIEIEWGPNWEDDLAGGHVTGPKDPNIK 162
Cdd:cd10557    80 QK--LANIFYNPKLPEIDDYYEPWTYDYENLFTAPEGDDQPVARPKSLITGEPMDIEWGPNWDDDLAGSPEYAAEDPNLK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 163 KIEEDIKFQFDETFMMYLPRLCEHCLNPSCVASCPSGAMYKRDEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNKAE 242
Cdd:cd10557   158 KLQEEIYLEFENTFMFYLPRICNHCLNPACVAACPSGAIYKREEDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSE 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 243 KCTFCFPRIEAGMPTVCSETCTGRMRYLGVLLYDADRVHEAASAVDEKDLYEKQLDIFLNPFDEEVIAQAEKDGISYDWI 322
Cdd:cd10557   238 KCIFCYPRLEAGQPTVCSETCVGRIRYLGVLLYDADRILEAAAVVPEKDLVEAQLDIILDPNDPEVIAAAKANGIPDNWI 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1450693874 323 EAAQNSPIYKLAIEYKLAFPLHPEFRTMPMVWYCPPLSPIMSYFEG 368
Cdd:cd10557   318 EAAQRSPVYKMVKEWKIALPLHPEYRTLPMVFYVPPLSPVVAAVEA 363
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 3-420 4.32e-119

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: 352.76  E-value: 4.32e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874   3 IKAQVAMVLNLDKCIGCHTCSVTCKNTWTNRPGAEYMWFNNVETKPGVGYPKRWEDqehyKGGWVlnrKGKLELKSGSri 82
Cdd:cd10555     1 SKRQLAMVMDLNKCIGCQTCTVACKTLWTNRNGREYMYWNNVETQPGKGYPKNWEK----KGGGF---KDKGELKPGI-- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874  83 skialgkifynpdMPLIKDYYEPWNYNYEHLT-TAKSGNHSPVarayseitgDNIEIEWGPNWEDDLAGGHVtgpkdPNi 161
Cdd:cd10555    72 -------------IPTLEDYGVPWEYNHEEELfEGKGGRVRPS---------PKGDPTWGPNWDEDQGAGEY-----PN- 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 162 kkieedikfqfdeTFMMYLPRLCEHCLNPSCVASCPSGAMYKRDEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNKA 241
Cdd:cd10555   124 -------------SYYFYLPRICNHCTNPACLAACPRKAIYKREEDGIVLVDQDRCRGYRYCVEACPYKKIYFNPVEQKS 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 242 EKCTFCFPRIEAGMPTVCSETCTGRMRYLGVLlydadrvheaasavdekdlyekqldiflnpfDEEviaqaekdgisydw 321
Cdd:cd10555   191 EKCIFCYPRIEKGVAPACARQCVGRIRFVGYL-------------------------------DDE-------------- 225

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 322 ieaaqNSPIYKLAIEYKLAFPLHPEFRTMPMVWYCPPLSPIMSYFEGKNTNqnpdaifpaieEMRLPIEYLANIFtaGDT 401
Cdd:cd10555   226 -----ESPVYKLVKKWKVALPLHPEYGTEPNVFYVPPLSPPKLGDDGEPTD-----------EPRIPLEYLESLF--GPR 287

                         410
                  ....*....|....*....
gi 1450693874 402 kpVKEALQRMAMMRSYMRS 420
Cdd:cd10555   288 --VKQALDTLKAEREKKRA 304
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 6-361 5.28e-96

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: 289.48  E-value: 5.28e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874   6 QVAMVLNLDKCIGCHTCSVTCKNTWTNRPGAEYMWFNNVETKPGVGYPKRWEDQEHYKGGWVlnrkgklelksgsriski 85
Cdd:cd16365     2 QFAAVFNLNKCIGCQTCTVACKNAWTYRKGQEYMWWNNVETKPGGGYPQDWEVKTIDNGGNT------------------ 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874  86 algkifynpdmplikdyyepwnynyehlttaksgnhspvarayseitgdnieiewgpnweddlagghvtgpkdpnikkie 165
Cdd:cd16365       --------------------------------------------------------------------------------

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 166 edikfqfdeTFMMYLPRLCEHCLNPSCVASCPSGAMYKRDEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNKAEKCT 245
Cdd:cd16365    64 ---------RFFFYLQRLCNHCTNPACLAACPRGAIYKREEDGIVLIDQKRCRGYRKCVEQCPYKKIYFNGLSRVSEKCI 134

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 246 FCFPRIEAGMPTVCSETCTGRMRYLGVLLYDadrvheaasavdekdlyekqldiflnpfdeeviaqaekdgisydwieaa 325
Cdd:cd16365   135 ACYPRIEGGDPTRCMSACVGRIRLQGFLDDN------------------------------------------------- 165

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1450693874 326 QNSPIYKLAIEYKLAFPLHPEFRTMPMVWYCPPLSP 361
Cdd:cd16365   166 PKSPVTKLIRHWKVALPLHPEYGTEPNIYYVPPRWA 201
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 4-358 2.08e-69

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: 224.26  E-value: 2.08e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874   4 KAQVAMVLNLDKCIGCHTCSVTCKNTWTNRPGAEYMWFNNVETKPGVGYPKRWeDQE--HYKGGWVLNRKGKLELKS--- 78
Cdd:cd10556     9 DKQFAMVFDTNKCIACQTCTMACKSTWTSGKGQEYMWWNNVETKPYGGYPLGW-DVRllDEEGGQTWAEGGVYEGKTife 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874  79 GSRISKIALGkifYNPDMplikdyyEPWNYnyehlttaksgnhspvarayseitgDNIeiewgpnWEDDlagghVTGPKD 158
Cdd:cd10556    88 AAAAGEQVLG---YRPED-------EDWRY-------------------------PNI-------GEDE-----VNGERT 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 159 PNIKKIEEDikfqfDETFMMYLPRLCEHCLNPSCVASCPSGAMYKRDEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKT 238
Cdd:cd10556   121 PDTGSSLPP-----HPIWFFYLPRICNHCTYPACLAACPRKAIYKREEDGIVLIDQERCRGYRECVEACPYKKPMYNPTT 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 239 NKAEKCTFCFPRIEAGMPTVCSETCTGRMRYLGvllydadrvheaasavdekdlyekqldiFLNPFDEEviaqaekdgis 318
Cdd:cd10556   196 RVSEKCIGCYPRIEEGDQTQCVSACIGKIRLQG----------------------------FINTPPDA----------- 236

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1450693874 319 yDWIEAAQNsPIYKLAIEYKLAFPLHPEFRTMPMVWYCPP 358
Cdd:cd10556   237 -RWADDRDN-PIDFLVHIKKVALPLYPQFGTEPNVYYIPP 274
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 175-273 1.58e-51

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: 170.51  E-value: 1.58e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 175 TFMMYLPRLCEHCLNPSCVASCPSGAMYKRDEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCFPRIEAG 254
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPVGAIYKDEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAG 80

                          90
                  ....*....|....*....
gi 1450693874 255 MPTVCSETCTGRMRYLGVL 273
Cdd:pfam13247  81 LLPACVQTCPTGAMNFGDR 99
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 163-355 6.54e-43

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: 150.76  E-value: 6.54e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 163 KIEEDIKFQFDETFMMYLPRLCEHCLNPSCVASCPSGAMYKRdEDGIVLVDQDACRGWRYCMTGCPYKKVYFNW------ 236
Cdd:cd10551    32 RVLEYEVGEYPNVKRTFLPVLCNHCENPPCVKVCPTGATYKR-EDGIVLVDYDKCIGCRYCMAACPYGARYFNPeephef 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 237 ------KTNKAEKCTFCFPRIEAGMPTVCSETCTGRMRYLGvllydadrvheaasavdekDLyekqldifLNPfdeevia 310
Cdd:cd10551   111 gevpvrPKGVVEKCTFCYHRLDEGLLPACVEACPTGARIFG-------------------DL--------DDP------- 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1450693874 311 qaekdgisydwieaaqNSPIYKLAIEYKlAFPLHPEFRTMPMVWY 355
Cdd:cd10551   157 ----------------NSEVSKLLAERR-AYVLKPELGTKPKVYY 184
Nitr_red_bet_C pfam14711
Respiratory nitrate reductase beta C-terminal; This domain occurs near the C-terminus of the ...
 359-439 1.04e-39

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: 138.40  E-value: 1.04e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 359 LSPIMSYFEGKNTNQNPDAIFPAIEEMRLPIEYLANIFTAGDTKPVKEALQRMAMMRSYMRSQVTQQPFDTSRLERLGLT 438
Cdd:pfam14711   1 LSPVVDAAEAGGHDEDADGLFPAIDSLRIPVEYLANLLTAGDTEPVRRALRRLAAMRAYMRAKNVGGEPDESILEAVGLT 80


                  .
gi 1450693874 439 E 439
Cdd:pfam14711  81 E 81
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 155-294 2.20e-39

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 141.24  E-value: 2.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 155 GPKDPNIKKIEEDIKFQFDETFMMYLPRLCEHCLNPSCVASCPSGAMYKRdEDGIVLVDQDACRGWRYCMTGCPYKKVYF 234
Cdd:COG0437    31 LPVGVTWRRVRRYEEGEFPNVEWLFVPVLCNHCDDPPCVKVCPTGATYKR-EDGIVLVDYDKCIGCRYCVAACPYGAPRF 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 235 NWKTNKAEKCTFCFPRIEAGMPTVCSETCTGRMRYLGVLLYDADRVHEAASAVDEKDLYE 294
Cdd:COG0437   110 NPETGVVEKCTFCADRLDEGLLPACVEACPTGALVFGDLDDPESEVSKRLAELPAYRLLP 169
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 149-271 3.78e-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: 130.97  E-value: 3.78e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 149 AGGHVTGPKDPNIKKIEEDikfqfdETFMMYLPRLCEHCLNPSCVASCPSGAMYKrDEDGIVLVDQDACRGWRYCMTGCP 228
Cdd:cd04410    21 EHGLRPGPDWSRIKVIEGG------GLERAFLPVSCMHCEDPPCVKACPTGAIYK-DEDGIVLIDEDKCIGCGSCVEACP 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1450693874 229 YKKVYFNWKTNKAEKCTFCFPRIEAGMPTVCSETCTGRMRYLG 271
Cdd:cd04410    94 YGAIVFDPEPGKAVKCDLCGDRLDEGLEPACVKACPTGALTFG 136
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 156-266 1.97e-31

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


Pssm-ID: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 118.05  E-value: 1.97e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 156 PKDPNIKKIEEDIKFQFDETFMMYLPRLCEHCLNPSCVASCPSGAMYKRdEDGIVLVDQDACRGWRYCMTGCPYKKVYFN 235
Cdd:cd16371    26 PPGVNWRRVYEYEGGEFPEVFAYFLSMSCNHCENPACVKVCPTGAITKR-EDGIVVVDQDKCIGCGYCVWACPYGAPQYN 104

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1450693874 236 WKTNKAEKCTFCFPRIEAGMPTVCSETCTGR 266
Cdd:cd16371   105 PETGKMDKCDMCVDRLDEGEKPACVAACPTR 135
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
180-289 1.55e-28

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 113.43  E-value: 1.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 180 LPRLCEHCLNPSCVASCPSGAMYKRdEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCFPRIEAGMPTVC 259
Cdd:PRK14993   96 LPRLCNHCDNPPCVPVCPVQATFQR-EDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPAC 174

                          90       100       110
                  ....*....|....*....|....*....|
gi 1450693874 260 SETCTGRMRYLGVLlydADRVHEAASAVDE 289
Cdd:PRK14993  175 VESCVGGARIIGDI---KDPHSRIATMLHQ 201
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 147-269 7.47e-28

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: 109.03  E-value: 7.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 147 DLAGGHvTGPKDPNIK-----KIEEDIKFQFDETFMMyLPRLCEHCLNPSCVASCPSGAMYkRDEDGIVLVDQDACRGWR 221
Cdd:cd16366    30 EFTGSY-QNPPDLTAHtwtlvRFYEVEKPGGDLSWLF-RKDQCMHCTDAGCLAACPTGAII-RTETGTVVVDPETCIGCG 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1450693874 222 YCMTGCPYKKVYFNWKTNKAEKCTFCFPRIEAGMPTVCSETC-TGRMRY 269
Cdd:cd16366   107 YCVNACPFDIPRFDEETGRVAKCTLCYDRISNGLQPACVKTCpTGALTF 155
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 179-263 1.14e-27

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: 109.61  E-value: 1.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 179 YLPRLCEHCLNPSCVASCPSGAMYKrDEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWktNKAE----KCTFCFPRIEAG 254
Cdd:cd10561    64 FVKRQCMHCLDPACVSACPVGALRK-TPEGPVTYDEDKCIGCRYCMVACPFNIPKYEW--DSANpkirKCTMCYDRLKEG 140


                  ....*....
gi 1450693874 255 MPTVCSETC 263
Cdd:cd10561   141 KQPACVEAC 149
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 177-264 7.94e-26

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: 102.83  E-value: 7.94e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 177 MMYLPRLCEHCLNPSCVASCPSGAMYKRDEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCFPRIEAGMP 256
Cdd:cd10553    51 LKFVYMSCFHCENPWCVKACPTGAMQKREKDGIVYVDQELCIGCKACIEACPWGIPQWNPATGKVVKCDYCMDRIDQGLK 130


                  ....*...
gi 1450693874 257 TVCSETCT 264
Cdd:cd10553   131 PACVTGCT 138
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 182-264 4.14e-25

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: 101.23  E-value: 4.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 182 RLCEHCLNPSCVASCPSGAMYKrDEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCFPRIEAGMPTVCSE 261
Cdd:cd10562    68 RQCMHCTDAACVKVCPTGALYK-TENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCFDRIENGMQPACVK 146


                  ...
gi 1450693874 262 TCT 264
Cdd:cd10562   147 TCP 149
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 179-270 1.75e-22

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: 94.70  E-value: 1.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 179 YLPRLCEHCLNPSCVASCPSGAMYKRDeDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCFPRIEAGMPTV 258
Cdd:cd10552    59 YLPVPCNHCDNAPCIKAAKDGAVYKRD-DGIVIIDPEKAKGQKQLVDACPYGAIYWNEELQVPQKCTFCAHLLDDGWKEP 137

                          90
                  ....*....|....
gi 1450693874 259 -CSETC-TGRMRYL 270
Cdd:cd10552   138 rCVQACpTGALRFG 151
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 184-264 3.61e-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: 92.06  E-value: 3.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 184 CEHCLNPSCVASCPSGAMYkRDEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCFPRIEAGMPTVCSETC 263
Cdd:cd10560    78 CKHCTDAGCLEACPTGAIF-RTEFGTVYIQPDICNGCGYCVAACPFGVIDRNEETGRAHKCTLCYDRLKDGLEPACAKAC 156


                  .
gi 1450693874 264 T 264
Cdd:cd10560   157 P 157
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
179-265 1.89e-20

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 92.42  E-value: 1.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 179 YLPRLCEHCLNPSCVASCPSGAMYKRDEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWK--TNKAEKCTFC----FPRIE 252
Cdd:PRK10882  107 YIKKQCMHCVDPNCVSVCPVSALTKDPKTGIVHYDKDVCTGCRYCMVACPFNVPKYDYNnpFGAIHKCELCnqkgVERLD 186

                          90
                  ....*....|....
gi 1450693874 253 AGMPTVCSETC-TG 265
Cdd:PRK10882  187 KGGLPGCVEVCpTG 200
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 184-269 1.96e-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: 83.98  E-value: 1.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 184 CEHCLNPSCVASCPS-GAMYKRdEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCFPRIEAGMPTVCSET 262
Cdd:cd10558    70 CMHCADPGCLKACPSpGAIVQY-ANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVGLEPACVKT 148


                  ....*...
gi 1450693874 263 C-TGRMRY 269
Cdd:cd10558   149 CpTGALHF 156
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 179-247 9.43e-18

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


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 79.54  E-value: 9.43e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1450693874 179 YLPRLCEHCLNPSCVASCPSGAMYKRDEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFC 247
Cdd:cd10550    44 DVPVVCRQCEDAPCVEACPVGAISRDEETGAVVVDEDKCIGCGMCVEACPFGAIRVDPETGKAIKCDLC 112
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 178-269 1.10e-17

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: 79.63  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 178 MYLPRLCEHCLNPSCVASCPSGAMYkRDEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCFPRIEAGMPT 257
Cdd:cd16374    37 ASVPVRCRHCEDAPCMEVCPTGAIY-RDEDGAVLVDPDKCIGCGMCAMACPFGVPRFDPSLKVAVKCDLCIDRRREGKLP 115

                          90
                  ....*....|...
gi 1450693874 258 VCSETC-TGRMRY 269
Cdd:cd16374   116 ACVEACpTGALKF 128
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 179-263 9.24e-17

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


Pssm-ID: 319885 [Multi-domain]  Cd Length: 140  Bit Score: 76.91  E-value: 9.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 179 YLPRLCEHCLNPSCVASCPSGAMYKRDEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCFPRieaGMPtV 258
Cdd:cd10563    52 SFPLQCRHCDEPPCVKACMSGAMHKDPETGIVIHDEEKCVGCWMCVMVCPYGAIRPDKERKVALKCDLCPDR---ETP-A 127


                  ....*
gi 1450693874 259 CSETC 263
Cdd:cd10563   128 CVEAC 132
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 179-271 5.36e-14

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: 70.91  E-value: 5.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 179 YLPRLCEHCLNPSCVASCPSGAMYKRDEdGIVLVDQDACRGWRYCMTGCP------------YKKVYFNWKTNKAE-KCT 245
Cdd:cd16368    86 FIPRRCMHCDNPPCAKLCPFGAARKTPE-GAVYIDDDLCFGGAKCRDVCPwhipqrqagvgiYLHLAPEYAGGGVMyKCD 164

                          90       100
                  ....*....|....*....|....*.
gi 1450693874 246 FCFPRIEAGMPTVCSETCTGRMRYLG 271
Cdd:cd16368   165 LCKDLLAQGKPPACIEACPKGAQYFG 190
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 177-293 7.36e-13

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: 67.46  E-value: 7.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 177 MMYLPRLCEHCLNPSCVASCPS--GAMYKRDEDGIVLVDQDACRGWRYCMT-GCPYKKVYFNWKTNKAEKCTFCFPRIEA 253
Cdd:cd10559    64 WLFFPDQCRHCVTPPCKDAADMvpGAVIQDEATGAVVFTEKTAELDFDDVLsACPYNIPRKNEATGRIVKCDMCIDRVSN 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1450693874 254 GMPTVCSETC-TGRMR---YLGVLLYDADRVHEAASAVDEKDLY 293
Cdd:cd10559   144 GLQPACVKACpTGAMNfgdRDEMLAMASKRLEELKKRYPKANLY 187
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 180-270 2.11e-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: 65.49  E-value: 2.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 180 LPRLCEHCLNPSCVASCPSGAMyKRDEDGIVL-VDQDACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCFPRIEAGMPTV 258
Cdd:cd16369    47 APTVCMHCEDPTCAEVCPADAI-KVTEDGVVQsALKPRCIGCSNCVNACPFGVPKYDEERNLMMKCDMCYDRTSVGKAPM 125

                          90
                  ....*....|...
gi 1450693874 259 CSETC-TGRMRYL 270
Cdd:cd16369   126 CASVCpSGALFYG 138
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
178-263 2.67e-12

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 64.29  E-value: 2.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 178 MYLPRLCEHCLNPSCVASCPSGAMYKrdEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNK--AEKCTFCFPRieAGM 255
Cdd:COG1142    46 VSAPVQCRHCEDAPCAEVCPVGAITR--DDGAVVVDEEKCIGCGLCVLACPFGAITMVGEKSRavAVKCDLCGGR--EGG 121


                  ....*...
gi 1450693874 256 PtVCSETC 263
Cdd:COG1142   122 P-ACVEAC 128
PRK09898 PRK09898
ferredoxin-like protein;
177-247 3.70e-10

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 59.85  E-value: 3.70e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1450693874 177 MMYLPRLCEHCLNPSCVASCPSGAMYKRDEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFC 247
Cdd:PRK09898  116 LNYTADTCRQCKEPQCMNVCPIGAITWQQKEGCITVDHKRCIGCSACTTACPWMMATVNTESKKSSKCVLC 186
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 182-247 3.73e-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: 54.97  E-value: 3.73e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1450693874 182 RLCEHCLNPSCVASCPSGAMYKRdEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFC 247
Cdd:cd16370    51 VVCRACEDPPCAEACPTGALEPR-KGGGVVLDKEKCIGCGNCVKACIVGAIFWDEETNKPIICIHC 115
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 180-248 3.90e-08

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


Pssm-ID: 319889 [Multi-domain]  Cd Length: 138  Bit Score: 52.31  E-value: 3.90e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1450693874 180 LPRLCEHCLNPSCVASCPSGAMyKRDEDGIVLVDqDACRGWRYCMTGCPYKKVyfnwKTNKAEKCTFCF 248
Cdd:cd16367    53 VPTACRHCVDPVCMIGCPTGAI-HRDDGGEVVIS-DACCGCGNCASACPYGAI----QMVRAVKCDLCA 115
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 184-263 4.51e-07

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 52.44  E-value: 4.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 184 CEHCLNPSCVASCPSGAMYKRDEDgiVLVDQDACRGWRYCMTGCPY-------KKVYFNWKTNKAEKCTFCFPRiEAGmp 256
Cdd:PRK12769   56 CHHCEDAPCARSCPNGAISHVDDS--IQVNQQKCIGCKSCVVACPFgtmqivlTPVAAGKVKATAHKCDLCAGR-ENG-- 130


                  ....*..
gi 1450693874 257 TVCSETC 263
Cdd:PRK12769  131 PACVENC 137
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 181-266 1.69e-06

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 50.79  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 181 PRLCEHCLNPSCVASCPSGAMYKRDEDgiVLVDQDACRGWRYCMTGCPYKKVyfNWKTNKAEKCTFCFPRIEAgmPTVCS 260
Cdd:PRK12809   53 PVACHHCNNAPCVTACPVNALTFQSDS--VQLDEQKCIGCKRCAIACPFGVV--EMVDTIAQKCDLCNQRSSG--TQACI 126


                  ....*.
gi 1450693874 261 ETCTGR 266
Cdd:PRK12809  127 EVCPTQ 132
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 181-228 1.72e-06

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: 45.32  E-value: 1.72e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1450693874 181 PRLCEHCLNpsCVASCPSGAM-----YKRDEDGIVLVDQDACRGWRYCMTGCP 228
Cdd:pfam13237   6 PDKCIGCGR--CTAACPAGLTrvgaiVERLEGEAVRIGVWKCIGCGACVEACP 56
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 178-263 4.48e-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: 40.40  E-value: 4.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 178 MYLPRLCEHCLNpsCVASCPSGAMYkRDEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCfprieagmpT 257
Cdd:cd16372    43 GYAINVCNQCGE--CIDVCPTGAIT-RDANGVVMINKKLCVGCLMCVGFCPEGAMFKHEDYPEPFKCIAC---------G 110


                  ....*.
gi 1450693874 258 VCSETC 263
Cdd:cd16372   111 ICVKAC 116
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 181-230 1.04e-03

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 37.79  E-value: 1.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1450693874 181 PRLCEHCLnpSCVASCPSGAMyKRDEDGIVLVDQDACRGWRYCMTGCPYK 230
Cdd:COG1149    10 EEKCIGCG--LCVEVCPEGAI-KLDDGGAPVVDPDLCTGCGACVGVCPTG 56
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
181-240 1.75e-03

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 41.00  E-value: 1.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 181 PRLCEHCLnpSCVASCPSGAMyKRDEDGIVLVDQDACRGWRYCMTGCPYKKVYFNWKTNK 240
Cdd:COG1148   495 PEKCTGCG--RCVEVCPYGAI-SIDEKGVAEVNPALCKGCGTCAAACPSGAISLKGFTDD 551
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 183-228 1.90e-03

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 36.95  E-value: 1.90e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1450693874 183 LCEHClnPSCVASCPSGAMYKrdEDGIVLVDQDACRGWRYCMTGCP 228
Cdd:COG2221    16 KCIGC--GLCVAVCPTGAISL--DDGKLVIDEEKCIGCGACIRVCP 57
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 184-230 1.93e-03

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 36.35  E-value: 1.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1450693874 184 CEHCLNpsCVASCPSGAMYKRDED-----GIVLVDQDACRGWRYCMTGCPYK 230
Cdd:pfam12838   1 CIGCGA--CVAACPVGAITLDEVGekkgtKTVVIDPERCVGCGACVAVCPTG 50
napG PRK09476
quinol dehydrogenase periplasmic component; Provisional
 184-265 1.98e-03

quinol dehydrogenase periplasmic component; Provisional


Pssm-ID: 236534 [Multi-domain]  Cd Length: 254  Bit Score: 39.99  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 184 CEHCLNPSCVASCPSGAMYKRDED------GI-VLVDQDACRGWR-----YCMTGCP---------YKKvyfNWKTNKAE 242
Cdd:PRK09476   99 CEMCEDIPCVKACPSGALDRELVDiddarmGLaVLVDQENCLNFQglrcdVCYRVCPlidkaitleLER---NERTGKHA 175

                          90       100
                  ....*....|....*....|...
gi 1450693874 243 KCtfcfprieagMPTVCSETCTG 265
Cdd:PRK09476  176 FF----------LPTVHSDACTG 188
NapF COG1145
Ferredoxin [Energy production and conversion];
184-230 2.02e-03

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 40.09  E-value: 2.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1450693874 184 CEHCLNpsCVASCPSGAMYKRDEDGIVLVDQDACRGWRYCMTGCPYK 230
Cdd:COG1145   184 CIGCGL--CVKVCPTGAIRLKDGKPQIVVDPDKCIGCGACVKVCPVG 228
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
192-232 2.91e-03

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 37.62  E-value: 2.91e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1450693874 192 CVASCPSGAMYKRdEDGIVLVDQDACRGWRYCMTGCPYKKV 232
Cdd:PRK09623   59 CWKFCPEPAIYIK-EDGYVAIDYDYCKGCGICANECPTKAI 98
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 181-233 2.94e-03

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 36.56  E-value: 2.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1450693874 181 PRLCEHCLnpSCVASCPSGAMYKrdEDGIVLVDQDACRGWRYCMTGCPYKKVY 233
Cdd:COG4231    21 EDKCTGCG--ACVKVCPADAIEE--GDGKAVIDPDLCIGCGSCVQVCPVDAIK 69
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 184-265 4.96e-03

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 37.62  E-value: 4.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1450693874 184 CEHCLNpSCVASCPSGAMYKRDED------GIVLVDQDACRGW------RYCMTGCPYKKVYFnwktnkaekctfcFPRI 251
Cdd:cd16373    55 CDLCCD-ACVEVCPTGALRPLDLEeqkvkmGVAVIDKDRCLAWqggtdcGVCVEACPTEAIAI-------------VLED 120

                          90
                  ....*....|....
gi 1450693874 252 EAGMPTVCSETCTG 265
Cdd:cd16373   121 DVLRPVVDEDKCVG 134
PRK13795 PRK13795
hypothetical protein; Provisional
 192-228 6.32e-03

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 39.21  E-value: 6.32e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1450693874 192 CVASCPSGAMYKRDEDGIVLVDQDACRGWRYCMTGCP 228
Cdd:PRK13795  589 CVGACPTGAIRIEEGKRKISVDEEKCIHCGKCTEVCP 625
 
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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