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Conserved domains on  [gi|494737763|ref|WP_007473183|]
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nitrate reductase subunit beta [Listeria fleischmannii]

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 ...
 1-488 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: 1020.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763   1 MKIKAQIGMVMNLDKCIGCHTCSVTCKNTWTNRPGAEYMWFNNVETKPGVGYPKRWEDQEEYKGGWTLNKKGKLELKSGS 80
Cdd:COG1140    1 MKVRAQIAMVMNLDKCIGCHTCSVTCKNVWTNREGVEYMWFNNVETKPGIGYPKRWEDQEKWKGGWELDRNGKLRLRAGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763  81 KWSKvaLGKIFYNPDMPELKDYYEPWTYDYENLFSPEQRKNQPVARPKSVISGANMEIEWGPNWEDDLAGAPNTLPKDPN 160
Cdd:COG1140   81 RLKK--LANIFANPDLPEIDDYYEPWTYDYENLINAPEGDDQPVARPRSLITGEPMKIEWGPNWDDDLGGSFEYASKDPN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 161 MKKIESEIRSNFETTFMMYLPRLCEHCLNPACVASCPSGAMYKRDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNK 240
Cdd:COG1140  159 LEGLQEEIYFEFENTFMFYLPRICEHCLNPACVASCPSGAIYKREEDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGK 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 241 AEKCTFCFPRIEAGLPTVCSETCTGRIRYLGVMLYDADRVKEAAETKDEKELYEAQLDLFIDPFDPEMIEQARKDGITED 320
Cdd:COG1140  239 AEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADRVEEAASVPDEQDLYEAQLDVFLDPHDPEVIAAARKDGIPDD 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 321 WITAAQNSPIYKMAKEYKIAFPLHPEYRTMPMVWYVPPLSPIMNYFEGKDSIQNPDMIFPAIEEMRLPVDYLASILTAGN 400
Cdd:COG1140  319 WIEAAQRSPVYKLAKEWKVALPLHPEYRTLPMVWYVPPLSPVVDAVEAGGHDGDADGLFPAIDSLRIPVEYLANLFTAGD 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 401 TTVIKEALHKMAMMRLYMRNVSSGKEFDTARLERVGLTEENLKKMYRLLAIAKYEDRFVIPTSHKEDYIDTYRAQGEAGF 480
Cdd:COG1140  399 EEPVEAALRRLAAMRAYMRAKNVGGEPDEEILAAVGLTEEQAEEMYRLLAIAKYEDRFVIPTAHREQAEDLYELQGGCGF 478


                 ....*...
gi 494737763 481 SDAcSGCS 488
Cdd:COG1140  479 DFG-GGCP 485
 
Name Accession Description Interval E-value
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 1-488 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: 1020.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763   1 MKIKAQIGMVMNLDKCIGCHTCSVTCKNTWTNRPGAEYMWFNNVETKPGVGYPKRWEDQEEYKGGWTLNKKGKLELKSGS 80
Cdd:COG1140    1 MKVRAQIAMVMNLDKCIGCHTCSVTCKNVWTNREGVEYMWFNNVETKPGIGYPKRWEDQEKWKGGWELDRNGKLRLRAGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763  81 KWSKvaLGKIFYNPDMPELKDYYEPWTYDYENLFSPEQRKNQPVARPKSVISGANMEIEWGPNWEDDLAGAPNTLPKDPN 160
Cdd:COG1140   81 RLKK--LANIFANPDLPEIDDYYEPWTYDYENLINAPEGDDQPVARPRSLITGEPMKIEWGPNWDDDLGGSFEYASKDPN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 161 MKKIESEIRSNFETTFMMYLPRLCEHCLNPACVASCPSGAMYKRDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNK 240
Cdd:COG1140  159 LEGLQEEIYFEFENTFMFYLPRICEHCLNPACVASCPSGAIYKREEDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGK 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 241 AEKCTFCFPRIEAGLPTVCSETCTGRIRYLGVMLYDADRVKEAAETKDEKELYEAQLDLFIDPFDPEMIEQARKDGITED 320
Cdd:COG1140  239 AEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADRVEEAASVPDEQDLYEAQLDVFLDPHDPEVIAAARKDGIPDD 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 321 WITAAQNSPIYKMAKEYKIAFPLHPEYRTMPMVWYVPPLSPIMNYFEGKDSIQNPDMIFPAIEEMRLPVDYLASILTAGN 400
Cdd:COG1140  319 WIEAAQRSPVYKLAKEWKVALPLHPEYRTLPMVWYVPPLSPVVDAVEAGGHDGDADGLFPAIDSLRIPVEYLANLFTAGD 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 401 TTVIKEALHKMAMMRLYMRNVSSGKEFDTARLERVGLTEENLKKMYRLLAIAKYEDRFVIPTSHKEDYIDTYRAQGEAGF 480
Cdd:COG1140  399 EEPVEAALRRLAAMRAYMRAKNVGGEPDEEILAAVGLTEEQAEEMYRLLAIAKYEDRFVIPTAHREQAEDLYELQGGCGF 478


                 ....*...
gi 494737763 481 SDAcSGCS 488
Cdd:COG1140  479 DFG-GGCP 485
narH TIGR01660
nitrate reductase, beta subunit; The Nitrate reductase enzyme complex allows bacteria to use ...
 1-488 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: 831.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763    1 MKIKAQIGMVMNLDKCIGCHTCSVTCKNTWTNRPGAEYMWFNNVETKPGVGYPKRWEDQEEYKGGWTLNKKGKLELKSGS 80
Cdd:TIGR01660   1 MKIRSQIGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGIGYPKDWENQDKYKGGWVRKRDGKLEPRIGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763   81 KWSKvaLGKIFYNPDMPELKDYYEPWTYDYENLFSPEQRKNQPVARPKSVISGANME-IEWGPNWEDDLAGAPNTLPKDP 159
Cdd:TIGR01660  81 KWRV--LANIFANPDLPSIDDYYEPFDFDYQHLHTAPEGKHQPTARPRSLITGERMEkIEWGPNWEDDLGGEFAKRRKDK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763  160 NMKKIESEIRSNFETTFMMYLPRLCEHCLNPACVASCPSGAMYKRDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTN 239
Cdd:TIGR01660 159 NFDKIQKDIYGEFENTFMMYLPRLCEHCLNPACVASCPSGAIYKREEDGIVLIDQDKCRGWRMCISGCPYKKIYFNWKTG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763  240 KAEKCTFCFPRIEAGLPTVCSETCTGRIRYLGVMLYDADRVKEAAETKDEKELYEAQLDLFIDPFDPEMIEQARKDGITE 319
Cdd:TIGR01660 239 KSEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADKIEEAASTENEKDLYHRQLDVFLDPNDPEVIAQAKKDGIPL 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763  320 DWITAAQNSPIYKMAKEYKIAFPLHPEYRTMPMVWYVPPLSPIMNYFEGkdSIQNPDMIFPAIEEMRLPVDYLASILTAG 399
Cdd:TIGR01660 319 SVIEAAQQSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQNAAEA--GKVGANGIMPDVESLRIPVRYLANLLTAG 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763  400 NTTVIKEALHKMAMMRLYMRNVSSGKEFDTARLERVGLTEENLKKMYRLLAIAKYEDRFVIPTSHKEDYIDTYRAQGEAG 479
Cdd:TIGR01660 397 DTKPVLLALKRMLAMRHYMRAETVDGVVDTEVLEDVGLTEQQIEEMYRYLAIANYEDRFVIPSSHREIARDAFPERGGCG 476


                  ....*....
gi 494737763  480 FSDAcSGCS 488
Cdd:TIGR01660 477 FSFG-DGCH 484
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: 755.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763   3 IKAQIGMVMNLDKCIGCHTCSVTCKNTWTNRPGAEYMWFNNVETKPGVGYPKRWEDQEEYKGGWTLnKKGKLELKSGSKW 82
Cdd:cd10557    1 IRAQISMVMNLDKCIGCHTCSVTCKNVWTNRKGAEYMWWNNVETKPGIGYPKQWEDQEKYRGGWVL-KGGKLKLKRGGKI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763  83 SKvaLGKIFYNPDMPELKDYYEPWTYDYENLFSPEQRKNQPVARPKSVISGANMEIEWGPNWEDDLAGAPNTLPKDPNMK 162
Cdd:cd10557   80 QK--LANIFYNPKLPEIDDYYEPWTYDYENLFTAPEGDDQPVARPKSLITGEPMDIEWGPNWDDDLAGSPEYAAEDPNLK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 163 KIESEIRSNFETTFMMYLPRLCEHCLNPACVASCPSGAMYKRDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNKAE 242
Cdd:cd10557  158 KLQEEIYLEFENTFMFYLPRICNHCLNPACVAACPSGAIYKREEDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSE 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 243 KCTFCFPRIEAGLPTVCSETCTGRIRYLGVMLYDADRVKEAAETKDEKELYEAQLDLFIDPFDPEMIEQARKDGITEDWI 322
Cdd:cd10557  238 KCIFCYPRLEAGQPTVCSETCVGRIRYLGVLLYDADRILEAAAVVPEKDLVEAQLDIILDPNDPEVIAAAKANGIPDNWI 317

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 494737763 323 TAAQNSPIYKMAKEYKIAFPLHPEYRTMPMVWYVPPLSPIMNYFEG 368
Cdd:cd10557  318 EAAQRSPVYKMVKEWKIALPLHPEYRTLPMVFYVPPLSPVVAAVEA 363
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 175-273 6.17e-52

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


Pssm-ID: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 171.66  E-value: 6.17e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763  175 TFMMYLPRLCEHCLNPACVASCPSGAMYKRDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCFPRIEAG 254
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPVGAIYKDEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAG 80

                          90
                  ....*....|....*....
gi 494737763  255 LPTVCSETCTGRIRYLGVM 273
Cdd:pfam13247  81 LLPACVQTCPTGAMNFGDR 99
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
180-271 1.59e-29

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 116.51  E-value: 1.59e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 180 LPRLCEHCLNPACVASCPSGAMYKRdEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCFPRIEAGLPTVC 259
Cdd:PRK14993  96 LPRLCNHCDNPPCVPVCPVQATFQR-EDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPAC 174

                         90
                 ....*....|..
gi 494737763 260 SETCTGRIRYLG 271
Cdd:PRK14993 175 VESCVGGARIIG 186
 
Name Accession Description Interval E-value
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 1-488 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: 1020.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763   1 MKIKAQIGMVMNLDKCIGCHTCSVTCKNTWTNRPGAEYMWFNNVETKPGVGYPKRWEDQEEYKGGWTLNKKGKLELKSGS 80
Cdd:COG1140    1 MKVRAQIAMVMNLDKCIGCHTCSVTCKNVWTNREGVEYMWFNNVETKPGIGYPKRWEDQEKWKGGWELDRNGKLRLRAGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763  81 KWSKvaLGKIFYNPDMPELKDYYEPWTYDYENLFSPEQRKNQPVARPKSVISGANMEIEWGPNWEDDLAGAPNTLPKDPN 160
Cdd:COG1140   81 RLKK--LANIFANPDLPEIDDYYEPWTYDYENLINAPEGDDQPVARPRSLITGEPMKIEWGPNWDDDLGGSFEYASKDPN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 161 MKKIESEIRSNFETTFMMYLPRLCEHCLNPACVASCPSGAMYKRDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNK 240
Cdd:COG1140  159 LEGLQEEIYFEFENTFMFYLPRICEHCLNPACVASCPSGAIYKREEDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGK 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 241 AEKCTFCFPRIEAGLPTVCSETCTGRIRYLGVMLYDADRVKEAAETKDEKELYEAQLDLFIDPFDPEMIEQARKDGITED 320
Cdd:COG1140  239 AEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADRVEEAASVPDEQDLYEAQLDVFLDPHDPEVIAAARKDGIPDD 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 321 WITAAQNSPIYKMAKEYKIAFPLHPEYRTMPMVWYVPPLSPIMNYFEGKDSIQNPDMIFPAIEEMRLPVDYLASILTAGN 400
Cdd:COG1140  319 WIEAAQRSPVYKLAKEWKVALPLHPEYRTLPMVWYVPPLSPVVDAVEAGGHDGDADGLFPAIDSLRIPVEYLANLFTAGD 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 401 TTVIKEALHKMAMMRLYMRNVSSGKEFDTARLERVGLTEENLKKMYRLLAIAKYEDRFVIPTSHKEDYIDTYRAQGEAGF 480
Cdd:COG1140  399 EEPVEAALRRLAAMRAYMRAKNVGGEPDEEILAAVGLTEEQAEEMYRLLAIAKYEDRFVIPTAHREQAEDLYELQGGCGF 478


                 ....*...
gi 494737763 481 SDAcSGCS 488
Cdd:COG1140  479 DFG-GGCP 485
narH TIGR01660
nitrate reductase, beta subunit; The Nitrate reductase enzyme complex allows bacteria to use ...
 1-488 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: 831.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763    1 MKIKAQIGMVMNLDKCIGCHTCSVTCKNTWTNRPGAEYMWFNNVETKPGVGYPKRWEDQEEYKGGWTLNKKGKLELKSGS 80
Cdd:TIGR01660   1 MKIRSQIGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGIGYPKDWENQDKYKGGWVRKRDGKLEPRIGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763   81 KWSKvaLGKIFYNPDMPELKDYYEPWTYDYENLFSPEQRKNQPVARPKSVISGANME-IEWGPNWEDDLAGAPNTLPKDP 159
Cdd:TIGR01660  81 KWRV--LANIFANPDLPSIDDYYEPFDFDYQHLHTAPEGKHQPTARPRSLITGERMEkIEWGPNWEDDLGGEFAKRRKDK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763  160 NMKKIESEIRSNFETTFMMYLPRLCEHCLNPACVASCPSGAMYKRDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTN 239
Cdd:TIGR01660 159 NFDKIQKDIYGEFENTFMMYLPRLCEHCLNPACVASCPSGAIYKREEDGIVLIDQDKCRGWRMCISGCPYKKIYFNWKTG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763  240 KAEKCTFCFPRIEAGLPTVCSETCTGRIRYLGVMLYDADRVKEAAETKDEKELYEAQLDLFIDPFDPEMIEQARKDGITE 319
Cdd:TIGR01660 239 KSEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADKIEEAASTENEKDLYHRQLDVFLDPNDPEVIAQAKKDGIPL 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763  320 DWITAAQNSPIYKMAKEYKIAFPLHPEYRTMPMVWYVPPLSPIMNYFEGkdSIQNPDMIFPAIEEMRLPVDYLASILTAG 399
Cdd:TIGR01660 319 SVIEAAQQSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQNAAEA--GKVGANGIMPDVESLRIPVRYLANLLTAG 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763  400 NTTVIKEALHKMAMMRLYMRNVSSGKEFDTARLERVGLTEENLKKMYRLLAIAKYEDRFVIPTSHKEDYIDTYRAQGEAG 479
Cdd:TIGR01660 397 DTKPVLLALKRMLAMRHYMRAETVDGVVDTEVLEDVGLTEQQIEEMYRYLAIANYEDRFVIPSSHREIARDAFPERGGCG 476


                  ....*....
gi 494737763  480 FSDAcSGCS 488
Cdd:TIGR01660 477 FSFG-DGCH 484
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: 755.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763   3 IKAQIGMVMNLDKCIGCHTCSVTCKNTWTNRPGAEYMWFNNVETKPGVGYPKRWEDQEEYKGGWTLnKKGKLELKSGSKW 82
Cdd:cd10557    1 IRAQISMVMNLDKCIGCHTCSVTCKNVWTNRKGAEYMWWNNVETKPGIGYPKQWEDQEKYRGGWVL-KGGKLKLKRGGKI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763  83 SKvaLGKIFYNPDMPELKDYYEPWTYDYENLFSPEQRKNQPVARPKSVISGANMEIEWGPNWEDDLAGAPNTLPKDPNMK 162
Cdd:cd10557   80 QK--LANIFYNPKLPEIDDYYEPWTYDYENLFTAPEGDDQPVARPKSLITGEPMDIEWGPNWDDDLAGSPEYAAEDPNLK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 163 KIESEIRSNFETTFMMYLPRLCEHCLNPACVASCPSGAMYKRDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNKAE 242
Cdd:cd10557  158 KLQEEIYLEFENTFMFYLPRICNHCLNPACVAACPSGAIYKREEDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSE 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 243 KCTFCFPRIEAGLPTVCSETCTGRIRYLGVMLYDADRVKEAAETKDEKELYEAQLDLFIDPFDPEMIEQARKDGITEDWI 322
Cdd:cd10557  238 KCIFCYPRLEAGQPTVCSETCVGRIRYLGVLLYDADRILEAAAVVPEKDLVEAQLDIILDPNDPEVIAAAKANGIPDNWI 317

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 494737763 323 TAAQNSPIYKMAKEYKIAFPLHPEYRTMPMVWYVPPLSPIMNYFEG 368
Cdd:cd10557  318 EAAQRSPVYKMVKEWKIALPLHPEYRTLPMVFYVPPLSPVVAAVEA 363
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 3-396 5.98e-120

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


Pssm-ID: 319877 [Multi-domain]  Cd Length: 316  Bit Score: 355.07  E-value: 5.98e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763   3 IKAQIGMVMNLDKCIGCHTCSVTCKNTWTNRPGAEYMWFNNVETKPGVGYPKRWEDqeeyKGGWTlnkKGKLELKSGSkw 82
Cdd:cd10555    1 SKRQLAMVMDLNKCIGCQTCTVACKTLWTNRNGREYMYWNNVETQPGKGYPKNWEK----KGGGF---KDKGELKPGI-- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763  83 skvalgkifynpdMPELKDYYEPWTYDYENLFSpEQRKNQPVARPKSvisganmEIEWGPNWEDDLAGApntlpkdpnmk 162
Cdd:cd10555   72 -------------IPTLEDYGVPWEYNHEEELF-EGKGGRVRPSPKG-------DPTWGPNWDEDQGAG----------- 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 163 kieseirsNFETTFMMYLPRLCEHCLNPACVASCPSGAMYKRDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNKAE 242
Cdd:cd10555  120 --------EYPNSYYFYLPRICNHCTNPACLAACPRKAIYKREEDGIVLVDQDRCRGYRYCVEACPYKKIYFNPVEQKSE 191

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 243 KCTFCFPRIEAGLPTVCSETCTGRIRYLGvmlydadrvkeaaetkdekelyeaqldlFIDpfDPEmieqarkdgitedwi 322
Cdd:cd10555  192 KCIFCYPRIEKGVAPACARQCVGRIRFVG----------------------------YLD--DEE--------------- 226

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494737763 323 taaqnSPIYKMAKEYKIAFPLHPEYRTMPMVWYVPPLSPIMNYFEGKdsiqnpdmifpAIEEMRLPVDYLASIL 396
Cdd:cd10555  227 -----SPVYKLVKKWKVALPLHPEYGTEPNVFYVPPLSPPKLGDDGE-----------PTDEPRIPLEYLESLF 284
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 6-361 5.89e-98

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: 294.49  E-value: 5.89e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763   6 QIGMVMNLDKCIGCHTCSVTCKNTWTNRPGAEYMWFNNVETKPGVGYPKRWEDQEEYKGGWTlnkkgklelksgskwskv 85
Cdd:cd16365    2 QFAAVFNLNKCIGCQTCTVACKNAWTYRKGQEYMWWNNVETKPGGGYPQDWEVKTIDNGGNT------------------ 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763  86 algkifynpdmpelkdyyepwtydyenlfspeqrknqpvarpksvisganmeiewgpnweddlagapntlpkdpnmkkie 165
Cdd:cd16365      --------------------------------------------------------------------------------

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 166 seirsnfetTFMMYLPRLCEHCLNPACVASCPSGAMYKRDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNKAEKCT 245
Cdd:cd16365   64 ---------RFFFYLQRLCNHCTNPACLAACPRGAIYKREEDGIVLIDQKRCRGYRKCVEQCPYKKIYFNGLSRVSEKCI 134

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 246 FCFPRIEAGLPTVCSETCTGRIRYLGVMLYDadrvkeaaetkdekelyeaqldlfidpfdpemieqarkdgitedwitaa 325
Cdd:cd16365  135 ACYPRIEGGDPTRCMSACVGRIRLQGFLDDN------------------------------------------------- 165

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 494737763 326 QNSPIYKMAKEYKIAFPLHPEYRTMPMVWYVPPLSP 361
Cdd:cd16365  166 PKSPVTKLIRHWKVALPLHPEYGTEPNIYYVPPRWA 201
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 4-358 2.94e-74

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: 236.59  E-value: 2.94e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763   4 KAQIGMVMNLDKCIGCHTCSVTCKNTWTNRPGAEYMWFNNVETKPGVGYPKRWeDQeeykggwtlnkkgklelksgskws 83
Cdd:cd10556    9 DKQFAMVFDTNKCIACQTCTMACKSTWTSGKGQEYMWWNNVETKPYGGYPLGW-DV------------------------ 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763  84 kvalgKIFYNPDMPELKDYyepWTYDYENLFSPEQRKNQPVArpksvisganmeieWGPnwEDDLAGAPNTLPKDPNMKK 163
Cdd:cd10556   64 -----RLLDEEGGQTWAEG---GVYEGKTIFEAAAAGEQVLG--------------YRP--EDEDWRYPNIGEDEVNGER 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 164 IESEIRSNFE-TTFMMYLPRLCEHCLNPACVASCPSGAMYKRDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNKAE 242
Cdd:cd10556  120 TPDTGSSLPPhPIWFFYLPRICNHCTYPACLAACPRKAIYKREEDGIVLIDQERCRGYRECVEACPYKKPMYNPTTRVSE 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 243 KCTFCFPRIEAGLPTVCSETCTGRIRYLGvmlydadrvkeaaetkdekelyeaqldlFIDPFDpemieQARkdgitedWI 322
Cdd:cd10556  200 KCIGCYPRIEEGDQTQCVSACIGKIRLQG----------------------------FINTPP-----DAR-------WA 239

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 494737763 323 TAAQNsPIYKMAKEYKIAFPLHPEYRTMPMVWYVPP 358
Cdd:cd10556  240 DDRDN-PIDFLVHIKKVALPLYPQFGTEPNVYYIPP 274
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 175-273 6.17e-52

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


Pssm-ID: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 171.66  E-value: 6.17e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763  175 TFMMYLPRLCEHCLNPACVASCPSGAMYKRDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCFPRIEAG 254
Cdd:pfam13247   1 VDWLFFPEQCRHCLNPPCKASCPVGAIYKDEETGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAG 80

                          90
                  ....*....|....*....
gi 494737763  255 LPTVCSETCTGRIRYLGVM 273
Cdd:pfam13247  81 LLPACVQTCPTGAMNFGDR 99
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 153-356 1.56e-44

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: 155.00  E-value: 1.56e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 153 NTLPKDPNMKKIESEIRSNFETTFMMYLPRLCEHCLNPACVASCPSGAMYKRdEDGIVLVDQEACRGWRYCMTGCPYKKV 232
Cdd:cd10551   22 NNVPPGVFRNRVLEYEVGEYPNVKRTFLPVLCNHCENPPCVKVCPTGATYKR-EDGIVLVDYDKCIGCRYCMAACPYGAR 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 233 YFNW------------KTNKAEKCTFCFPRIEAGLPTVCSETCTGRIRYLGvmlyDADrvkeaaetkdekelyeaqldlf 300
Cdd:cd10551  101 YFNPeephefgevpvrPKGVVEKCTFCYHRLDEGLLPACVEACPTGARIFG----DLD---------------------- 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 494737763 301 iDPfdpemieqarkdgitedwitaaqNSPIYKMAKEYKiAFPLHPEYRTMPMVWYV 356
Cdd:cd10551  155 -DP-----------------------NSEVSKLLAERR-AYVLKPELGTKPKVYYI 185
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 153-294 1.60e-41

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 147.02  E-value: 1.60e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 153 NTLPKDPNMKKIESEIRSNFETTFMMYLPRLCEHCLNPACVASCPSGAMYKRdEDGIVLVDQEACRGWRYCMTGCPYKKV 232
Cdd:COG0437   29 NNLPVGVTWRRVRRYEEGEFPNVEWLFVPVLCNHCDDPPCVKVCPTGATYKR-EDGIVLVDYDKCIGCRYCVAACPYGAP 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494737763 233 YFNWKTNKAEKCTFCFPRIEAGLPTVCSETCTGRIRYLGVMLYDADRVKEAAETKDEKELYE 294
Cdd:COG0437  108 RFNPETGVVEKCTFCADRLDEGLLPACVEACPTGALVFGDLDDPESEVSKRLAELPAYRLLP 169
Nitr_red_bet_C pfam14711
Respiratory nitrate reductase beta C-terminal; This domain occurs near the C-terminus of the ...
 359-439 4.62e-38

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: 134.16  E-value: 4.62e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763  359 LSPIMNYFEGKDSIQNPDMIFPAIEEMRLPVDYLASILTAGNTTVIKEALHKMAMMRLYMRNVSSGKEFDTARLERVGLT 438
Cdd:pfam14711   1 LSPVVDAAEAGGHDEDADGLFPAIDSLRIPVEYLANLLTAGDTEPVRRALRRLAAMRAYMRAKNVGGEPDESILEAVGLT 80


                  .
gi 494737763  439 E 439
Cdd:pfam14711  81 E 81
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 153-271 1.69e-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: 1.69e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 153 NTLPKDPNMKKIEseiRSNFETTFMMYLPRLCEHCLNPACVASCPSGAMYKrDEDGIVLVDQEACRGWRYCMTGCPYKKV 232
Cdd:cd04410   22 HGLRPGPDWSRIK---VIEGGGLERAFLPVSCMHCEDPPCVKACPTGAIYK-DEDGIVLIDEDKCIGCGSCVEACPYGAI 97

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 494737763 233 YFNWKTNKAEKCTFCFPRIEAGLPTVCSETCTGRIRYLG 271
Cdd:cd04410   98 VFDPEPGKAVKCDLCGDRLDEGLEPACVKACPTGALTFG 136
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 153-266 1.64e-34

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


Pssm-ID: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 126.52  E-value: 1.64e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 153 NTLPKDPNMKKIESEIRSNFETTFMMYLPRLCEHCLNPACVASCPSGAMYKRdEDGIVLVDQEACRGWRYCMTGCPYKKV 232
Cdd:cd16371   23 NDLPPGVNWRRVYEYEGGEFPEVFAYFLSMSCNHCENPACVKVCPTGAITKR-EDGIVVVDQDKCIGCGYCVWACPYGAP 101

                         90       100       110
                 ....*....|....*....|....*....|....
gi 494737763 233 YFNWKTNKAEKCTFCFPRIEAGLPTVCSETCTGR 266
Cdd:cd16371  102 QYNPETGKMDKCDMCVDRLDEGEKPACVAACPTR 135
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
180-271 1.59e-29

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 116.51  E-value: 1.59e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 180 LPRLCEHCLNPACVASCPSGAMYKRdEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCFPRIEAGLPTVC 259
Cdd:PRK14993  96 LPRLCNHCDNPPCVPVCPVQATFQR-EDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPAC 174

                         90
                 ....*....|..
gi 494737763 260 SETCTGRIRYLG 271
Cdd:PRK14993 175 VESCVGGARIIG 186
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 179-269 1.30e-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: 1.30e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 179 YLPRLCEHCLNPACVASCPSGAMYKrDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWktNKAE----KCTFCFPRIEAG 254
Cdd:cd10561   64 FVKRQCMHCLDPACVSACPVGALRK-TPEGPVTYDEDKCIGCRYCMVACPFNIPKYEW--DSANpkirKCTMCYDRLKEG 140

                         90
                 ....*....|....*.
gi 494737763 255 LPTVCSETC-TGRIRY 269
Cdd:cd10561  141 KQPACVEACpTGALLF 156
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 177-269 1.36e-27

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: 108.26  E-value: 1.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 177 MMYLPRLCEHCLNPACVASCPSGAMYkRDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCFPRIEAGLP 256
Cdd:cd16366   63 WLFRKDQCMHCTDAGCLAACPTGAII-RTETGTVVVDPETCIGCGYCVNACPFDIPRFDEETGRVAKCTLCYDRISNGLQ 141

                         90
                 ....*....|....
gi 494737763 257 TVCSETC-TGRIRY 269
Cdd:cd16366  142 PACVKTCpTGALTF 155
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 177-264 1.23e-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: 105.14  E-value: 1.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 177 MMYLPRLCEHCLNPACVASCPSGAMYKRDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCFPRIEAGLP 256
Cdd:cd10553   51 LKFVYMSCFHCENPWCVKACPTGAMQKREKDGIVYVDQELCIGCKACIEACPWGIPQWNPATGKVVKCDYCMDRIDQGLK 130


                 ....*...
gi 494737763 257 TVCSETCT 264
Cdd:cd10553  131 PACVTGCT 138
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 182-269 1.07e-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: 103.15  E-value: 1.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 182 RLCEHCLNPACVASCPSGAMYKrDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCFPRIEAGLPTVCSE 261
Cdd:cd10562   68 RQCMHCTDAACVKVCPTGALYK-TENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCFDRIENGMQPACVK 146


                 ....*....
gi 494737763 262 TC-TGRIRY 269
Cdd:cd10562  147 TCpTGALTF 155
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 163-270 4.78e-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: 96.24  E-value: 4.78e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 163 KIESEIRSNFETTFMMYLPRLCEHCLNPACVASCPSGAMYKRDeDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNKAE 242
Cdd:cd10552   43 RILRRERGQYPKVDVAYLPVPCNHCDNAPCIKAAKDGAVYKRD-DGIVIIDPEKAKGQKQLVDACPYGAIYWNEELQVPQ 121

                         90       100       110
                 ....*....|....*....|....*....|
gi 494737763 243 KCTFCFPRIEAGLPTV-CSETC-TGRIRYL 270
Cdd:cd10552  122 KCTFCAHLLDDGWKEPrCVQACpTGALRFG 151
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 184-269 7.24e-22

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: 93.99  E-value: 7.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 184 CEHCLNPACVASCPSGAMYkRDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCFPRIEAGLPTVCSETC 263
Cdd:cd10560   78 CKHCTDAGCLEACPTGAIF-RTEFGTVYIQPDICNGCGYCVAACPFGVIDRNEETGRAHKCTLCYDRLKDGLEPACAKAC 156


                 ....*..
gi 494737763 264 -TGRIRY 269
Cdd:cd10560  157 pTGSIQF 163
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 151-269 4.04e-20

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: 88.60  E-value: 4.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 151 APNTLPKdpnMKKIESEIRSNFETTFMmylPRLCEHCLNPACVASCPS-GAMYKRdEDGIVLVDQEACRGWRYCMTGCPY 229
Cdd:cd10558   43 SPETWTL---MKFREVEDNGKLEWLIR---KDGCMHCADPGCLKACPSpGAIVQY-ANGIVDFQSDKCIGCGYCIKGCPF 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 494737763 230 KKVYFNWKTNKAEKCTFCFPRIEAGLPTVCSETC-TGRIRY 269
Cdd:cd10558  116 DIPRISKDDNKMYKCTLCSDRVSVGLEPACVKTCpTGALHF 156
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
179-269 5.47e-20

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 90.88  E-value: 5.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 179 YLPRLCEHCLNPACVASCPSGAMYKRDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWK--TNKAEKCTFC----FPRIE 252
Cdd:PRK10882 107 YIKKQCMHCVDPNCVSVCPVSALTKDPKTGIVHYDKDVCTGCRYCMVACPFNVPKYDYNnpFGAIHKCELCnqkgVERLD 186

                         90
                 ....*....|....*...
gi 494737763 253 AGLPTVCSETC-TGRIRY 269
Cdd:PRK10882 187 KGGLPGCVEVCpTGAVIF 204
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 179-269 2.10e-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: 81.47  E-value: 2.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 179 YLPRLCEHCLNPACVASCPSGAMYKRDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCfprieAGLPtV 258
Cdd:cd10550   44 DVPVVCRQCEDAPCVEACPVGAISRDEETGAVVVDEDKCIGCGMCVEACPFGAIRVDPETGKAIKCDLC-----GGDP-A 117

                         90
                 ....*....|..
gi 494737763 259 CSETC-TGRIRY 269
Cdd:cd10550  118 CVKVCpTGALEF 129
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 178-269 4.72e-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: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 80.78  E-value: 4.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 178 MYLPRLCEHCLNPACVASCPSGAMYkRDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCFPRIEAGLPT 257
Cdd:cd16374   37 ASVPVRCRHCEDAPCMEVCPTGAIY-RDEDGAVLVDPDKCIGCGMCAMACPFGVPRFDPSLKVAVKCDLCIDRRREGKLP 115

                         90
                 ....*....|...
gi 494737763 258 VCSETC-TGRIRY 269
Cdd:cd16374  116 ACVEACpTGALKF 128
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 179-263 2.96e-17

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


Pssm-ID: 319885 [Multi-domain]  Cd Length: 140  Bit Score: 78.45  E-value: 2.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 179 YLPRLCEHCLNPACVASCPSGAMYKRDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCFPRieaGLPtV 258
Cdd:cd10563   52 SFPLQCRHCDEPPCVKACMSGAMHKDPETGIVIHDEEKCVGCWMCVMVCPYGAIRPDKERKVALKCDLCPDR---ETP-A 127


                 ....*
gi 494737763 259 CSETC 263
Cdd:cd10563  128 CVEAC 132
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 180-270 3.04e-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: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 70.88  E-value: 3.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 180 LPRLCEHCLNPACVASCPSGAMyKRDEDGIVL-VDQEACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFCFPRIEAGLPTV 258
Cdd:cd16369   47 APTVCMHCEDPTCAEVCPADAI-KVTEDGVVQsALKPRCIGCSNCVNACPFGVPKYDEERNLMMKCDMCYDRTSVGKAPM 125

                         90
                 ....*....|...
gi 494737763 259 CSETC-TGRIRYL 270
Cdd:cd16369  126 CASVCpSGALFYG 138
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 179-271 1.11e-13

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


Pssm-ID: 319890 [Multi-domain]  Cd Length: 200  Bit Score: 69.76  E-value: 1.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 179 YLPRLCEHCLNPACVASCPSGAMYKRDEdGIVLVDQEACRGWRYCMTGCP------------YKKVYFNWKTNKAE-KCT 245
Cdd:cd16368   86 FIPRRCMHCDNPPCAKLCPFGAARKTPE-GAVYIDDDLCFGGAKCRDVCPwhipqrqagvgiYLHLAPEYAGGGVMyKCD 164

                         90       100
                 ....*....|....*....|....*.
gi 494737763 246 FCFPRIEAGLPTVCSETCTGRIRYLG 271
Cdd:cd16368  165 LCKDLLAQGKPPACIEACPKGAQYFG 190
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 166-295 1.61e-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: 69.39  E-value: 1.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 166 SEIRSNFETTFMMYLPRLCEHCLNPACVASCPS--GAMYKRDEDGIVLVDQEACRGWRYCMT-GCPYKKVYFNWKTNKAE 242
Cdd:cd10559   53 NEVRNENGKPDWLFFPDQCRHCVTPPCKDAADMvpGAVIQDEATGAVVFTEKTAELDFDDVLsACPYNIPRKNEATGRIV 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 494737763 243 KCTFCFPRIEAGLPTVCSETC-TGRIRY--LGVMLYDA-DRVKEAAETKDEKELYEA 295
Cdd:cd10559  133 KCDMCIDRVSNGLQPACVKACpTGAMNFgdRDEMLAMAsKRLEELKKRYPKANLYDP 189
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
178-269 3.66e-13

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 66.60  E-value: 3.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 178 MYLPRLCEHCLNPACVASCPSGAMYKrdEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNK--AEKCTFCFPRIEAGL 255
Cdd:COG1142   46 VSAPVQCRHCEDAPCAEVCPVGAITR--DDGAVVVDEEKCIGCGLCVLACPFGAITMVGEKSRavAVKCDLCGGREGGPA 123

                         90
                 ....*....|....*
gi 494737763 256 ptvCSETC-TGRIRY 269
Cdd:COG1142  124 ---CVEACpTGALRL 135
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 184-229 1.12e-11

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: 62.66  E-value: 1.12e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 494737763 184 CEHCLNPACVASCPSGAMYKrdEDGIVLVDQEACRGWRYCMTGCPY 229
Cdd:cd10554   56 CRQCEDAPCANVCPVGAISQ--EDGVVQVDEERCIGCKLCVLACPF 99
PRK09898 PRK09898
ferredoxin-like protein;
177-247 2.94e-10

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 59.85  E-value: 2.94e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494737763 177 MMYLPRLCEHCLNPACVASCPSGAMYKRDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFC 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 1.34e-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: 56.13  E-value: 1.34e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494737763 182 RLCEHCLNPACVASCPSGAMYKRdEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNKAEKCTFC 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 2.30e-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: 52.69  E-value: 2.30e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494737763 180 LPRLCEHCLNPACVASCPSGAMyKRDEDGIVLVDqEACRGWRYCMTGCPYKKVyfnwKTNKAEKCTFCF 248
Cdd:cd16367   53 VPTACRHCVDPVCMIGCPTGAI-HRDDGGEVVIS-DACCGCGNCASACPYGAI----QMVRAVKCDLCA 115
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 184-263 1.15e-07

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 54.37  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 184 CEHCLNPACVASCPSGAMYKRDEDgiVLVDQEACRGWRYCMTGCPY-------KKVYFNWKTNKAEKCTFCFPRiEAGlp 256
Cdd:PRK12769  56 CHHCEDAPCARSCPNGAISHVDDS--IQVNQQKCIGCKSCVVACPFgtmqivlTPVAAGKVKATAHKCDLCAGR-ENG-- 130


                 ....*..
gi 494737763 257 TVCSETC 263
Cdd:PRK12769 131 PACVENC 137
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 181-228 9.65e-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: 9.65e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 494737763  181 PRLCEHCLNpaCVASCPSGAM-----YKRDEDGIVLVDQEACRGWRYCMTGCP 228
Cdd:pfam13237   6 PDKCIGCGR--CTAACPAGLTrvgaiVERLEGEAVRIGVWKCIGCGACVEACP 56
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 181-266 9.94e-07

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 51.57  E-value: 9.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 181 PRLCEHCLNPACVASCPSGAMYKRDEDgiVLVDQEACRGWRYCMTGCPYKKVyfNWKTNKAEKCTFCFPRIEAglPTVCS 260
Cdd:PRK12809  53 PVACHHCNNAPCVTACPVNALTFQSDS--VQLDEQKCIGCKRCAIACPFGVV--EMVDTIAQKCDLCNQRSSG--TQACI 126


                 ....*.
gi 494737763 261 ETCTGR 266
Cdd:PRK12809 127 EVCPTQ 132
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
181-238 1.08e-05

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 43.57  E-value: 1.08e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 494737763 181 PRLCEHCLnpACVASCPSGAMYKrdEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKT 238
Cdd:COG2768   10 EEKCIGCG--ACVKVCPVGAISI--EDGKAVIDPEKCIGCGACIEVCPVGAIKIEWEE 63
napG PRK09476
quinol dehydrogenase periplasmic component; Provisional
 184-265 9.46e-05

quinol dehydrogenase periplasmic component; Provisional


Pssm-ID: 236534 [Multi-domain]  Cd Length: 254  Bit Score: 44.23  E-value: 9.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 184 CEHCLNPACVASCPSGAMYKRDED------GI-VLVDQEACRGWR-----YCMTGCP---------YKKvyfNWKTNKAE 242
Cdd:PRK09476  99 CEMCEDIPCVKACPSGALDRELVDiddarmGLaVLVDQENCLNFQglrcdVCYRVCPlidkaitleLER---NERTGKHA 175

                         90       100
                 ....*....|....*....|...
gi 494737763 243 KCtfcfprieagLPTVCSETCTG 265
Cdd:PRK09476 176 FF----------LPTVHSDACTG 188
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 191-269 3.58e-04

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: 40.46  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 191 ACVASCPSGAMYKRDEDGI-------VLVDQEACRGWRYCMTGCPYKKVYFNWKTNK---AEKCTFCfprieaGlptVCS 260
Cdd:cd10549   47 ACVEVCPTGAIELTPEGKEyvpkekeAEIDEEKCIGCGLCVKVCPVDAITLEDELEIvidKEKCIGC------G---ICA 117

                         90
                 ....*....|
gi 494737763 261 ETC-TGRIRY 269
Cdd:cd10549  118 EVCpVNAIKL 127
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 170-265 3.76e-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: 41.09  E-value: 3.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 170 SNFETTFMMYLPRLCEHCLNpACVASCPSGAMYKRDED------GIVLVDQEACRGW------RYCMTGCPYKKVYFnwk 237
Cdd:cd16373   41 EGGRTPYLDPREGPCDLCCD-ACVEVCPTGALRPLDLEeqkvkmGVAVIDKDRCLAWqggtdcGVCVEACPTEAIAI--- 116

                         90       100
                 ....*....|....*....|....*...
gi 494737763 238 tnkaekctfcFPRIEAGLPTVCSETCTG 265
Cdd:cd16373  117 ----------VLEDDVLRPVVDEDKCVG 134
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
181-240 3.78e-04

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 42.92  E-value: 3.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 181 PRLCEHCLnpACVASCPSGAMyKRDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNK 240
Cdd:COG1148  495 PEKCTGCG--RCVEVCPYGAI-SIDEKGVAEVNPALCKGCGTCAAACPSGAISLKGFTDD 551
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 174-228 5.41e-04

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 38.49  E-value: 5.41e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 494737763 174 TTFMMYLPRLCEHClnPACVASCPSGAMYKrdEDGIVLVDQEACRGWRYCMTGCP 228
Cdd:COG2221    7 TWPPKIDEEKCIGC--GLCVAVCPTGAISL--DDGKLVIDEEKCIGCGACIRVCP 57
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 184-230 6.61e-04

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 37.89  E-value: 6.61e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 494737763  184 CEHCLnpACVASCPSGAMYKRDED-----GIVLVDQEACRGWRYCMTGCPYK 230
Cdd:pfam12838   1 CIGCG--ACVAACPVGAITLDEVGekkgtKTVVIDPERCVGCGACVAVCPTG 50
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 157-263 7.28e-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: 39.63  E-value: 7.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494737763 157 KDPNMKKieSEIRSNFETTfmMYLPRLCEHCLNpaCVASCPSGAMYkRDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNW 236
Cdd:cd16372   26 KEEDREK--SCIRITETEG--GYAINVCNQCGE--CIDVCPTGAIT-RDANGVVMINKKLCVGCLMCVGFCPEGAMFKHE 98

                         90       100
                 ....*....|....*....|....*..
gi 494737763 237 KTNKAEKCTFCfprieaGLptvCSETC 263
Cdd:cd16372   99 DYPEPFKCIAC------GI---CVKAC 116
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 181-230 9.68e-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: 37.79  E-value: 9.68e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 494737763 181 PRLCEHCLnpACVASCPSGAMyKRDEDGIVLVDQEACRGWRYCMTGCPYK 230
Cdd:COG1149   10 EEKCIGCG--LCVEVCPEGAI-KLDDGGAPVVDPDLCTGCGACVGVCPTG 56
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 181-233 2.38e-03

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 36.94  E-value: 2.38e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 494737763 181 PRLCEHCLnpACVASCPSGAMYKrdEDGIVLVDQEACRGWRYCMTGCPYKKVY 233
Cdd:COG4231   21 EDKCTGCG--ACVKVCPADAIEE--GDGKAVIDPDLCIGCGSCVQVCPVDAIK 69
PRK00783 PRK00783
DNA-directed RNA polymerase subunit D; Provisional
 179-240 2.54e-03

DNA-directed RNA polymerase subunit D; Provisional


Pssm-ID: 234837 [Multi-domain]  Cd Length: 263  Bit Score: 39.87  E-value: 2.54e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494737763 179 YLPRL-----CEHCLnpACVASCPSGAMyKRDEDGIVLVDQEACRGWRYCMTGCPYKKVYFNWKTNK 240
Cdd:PRK00783 161 YYPRIevsedCDECE--KCVEACPRGVL-ELKEGKLVVTDLLNCSLCKLCERACPGKAIRVSDDENK 224
NapF COG1145
Ferredoxin [Energy production and conversion];
184-230 3.10e-03

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 39.32  E-value: 3.10e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 494737763 184 CEHCLnpACVASCPSGAMYKRDEDGIVLVDQEACRGWRYCMTGCPYK 230
Cdd:COG1145  184 CIGCG--LCVKVCPTGAIRLKDGKPQIVVDPDKCIGCGACVKVCPVG 228
PRK13795 PRK13795
hypothetical protein; Provisional
 192-228 5.03e-03

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 39.59  E-value: 5.03e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 494737763 192 CVASCPSGAMYKRDEDGIVLVDQEACRGWRYCMTGCP 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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