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Conserved domains on  [gi|504524127|ref|WP_014711229|]
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FAD-dependent oxidoreductase [Mycobacterium sp. MOTT36Y]

Protein Classification

ferredoxin family protein( domain architecture ID 12802250)

ferredoxin-like protein that may be a iron-sulfur cluster-containing protein which mediates electron transfer

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02852 super family cl30539
ferredoxin-NADP+ reductase
99-532 1.12e-134

ferredoxin-NADP+ reductase


The actual alignment was detected with superfamily member PLN02852:

Pssm-ID: 357415  Cd Length: 491  Bit Score: 399.84  E-value: 1.12e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127  99 PAVERGSLRVAIVGAGPAACYAAAELT-RVAGVEVNMFDRLATPFGLVRTGVAPDHQHTKAVVKLFDPAFASPRFECHFN 177
Cdd:PLN02852  20 SSSTSEPLHVCVVGSGPAGFYTADKLLkAHDGARVDIIERLPTPFGLVRSGVAPDHPETKNVTNQFSRVATDDRVSFFGN 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 178 VEVGETITHEDLLAHHHAVIYAVGAPKGRDLGIPGEKLPGSYAAADFVGWYNGHPDHPDTTFDL-SAERAVIIGNGNVAL 256
Cdd:PLN02852 100 VTLGRDVSLSELRDLYHVVVLAYGAESDRRLGIPGEDLPGVLSAREFVWWYNGHPDCVHLPPDLkSSDTAVVLGQGNVAL 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 257 DVARILLMAPEDLAKTDIAQHALDKLSDSAIDEVVILARRGLREAAFSVGEFLALGHLPGVDVIVDSDELDAHDDDDVE- 335
Cdd:PLN02852 180 DCARILLRPTDELASTDIAEHALEALRGSSVRKVYLVGRRGPVQAACTAKELRELLGLKNVRVRIKEADLTLSPEDEEEl 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 336 --TRMKLEIAREFTQRPTQPQ------NKRIVFRFMVSPVE----------VGG--------EEHAESLRVVHVG-GESE 388
Cdd:PLN02852 260 kaSRPKRRVYELLSKAAAAGKcapsggQRELHFVFFRNPTRfldsgdgnghVAGvklertvlEGAAGSGKQVAVGtGEFE 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 389 VIESRLILRSIGQRGVPIDGVPFDDANGVVSNEHGRVLREDG--QHVPGVYVTGWIKRGPRGVIGTNRSCAEQTVQKLWE 466
Cdd:PLN02852 340 DLPCGLVLKSIGYKSLPVDGLPFDHKRGVVPNVHGRVLSSASgaDTEPGLYVVGWLKRGPTGIIGTNLTCAEETVASIAE 419
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 467 DYDSGLL----DREVADRDAMADLLAERGAEPVDWQGWRAIDAAERERGRETSRPRVKFVDIAELLSAAN 532
Cdd:PLN02852 420 DLEQGRLrgvaSPPKPGRDGLLELLESRGVRVVPFSGWEKIDSAEKEAGRARGKPREKITSIEEMLKAAN 489
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
1-61 3.38e-16

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


:

Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 73.20  E-value: 3.38e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504524127   1 MTYVITQSCCKDASCVPVCPVDCIRPVGatgeiTGTEMLYIDPVTCIDCGACVDACPIDAI 61
Cdd:COG1146    2 MPVIDTDKCIGCGACVEVCPVDVLELDE-----EGKKALVINPEECIGCGACELVCPVGAI 57
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
46-84 1.13e-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: 37.12  E-value: 1.13e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 504524127   46 CIDCGACVDACPIDAIYYEEELPPELERFKDINSSYFEH 84
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKKGTKTVVIDPERCVG 39
 
Name Accession Description Interval E-value
PLN02852 PLN02852
ferredoxin-NADP+ reductase
99-532 1.12e-134

ferredoxin-NADP+ reductase


Pssm-ID: 215457  Cd Length: 491  Bit Score: 399.84  E-value: 1.12e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127  99 PAVERGSLRVAIVGAGPAACYAAAELT-RVAGVEVNMFDRLATPFGLVRTGVAPDHQHTKAVVKLFDPAFASPRFECHFN 177
Cdd:PLN02852  20 SSSTSEPLHVCVVGSGPAGFYTADKLLkAHDGARVDIIERLPTPFGLVRSGVAPDHPETKNVTNQFSRVATDDRVSFFGN 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 178 VEVGETITHEDLLAHHHAVIYAVGAPKGRDLGIPGEKLPGSYAAADFVGWYNGHPDHPDTTFDL-SAERAVIIGNGNVAL 256
Cdd:PLN02852 100 VTLGRDVSLSELRDLYHVVVLAYGAESDRRLGIPGEDLPGVLSAREFVWWYNGHPDCVHLPPDLkSSDTAVVLGQGNVAL 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 257 DVARILLMAPEDLAKTDIAQHALDKLSDSAIDEVVILARRGLREAAFSVGEFLALGHLPGVDVIVDSDELDAHDDDDVE- 335
Cdd:PLN02852 180 DCARILLRPTDELASTDIAEHALEALRGSSVRKVYLVGRRGPVQAACTAKELRELLGLKNVRVRIKEADLTLSPEDEEEl 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 336 --TRMKLEIAREFTQRPTQPQ------NKRIVFRFMVSPVE----------VGG--------EEHAESLRVVHVG-GESE 388
Cdd:PLN02852 260 kaSRPKRRVYELLSKAAAAGKcapsggQRELHFVFFRNPTRfldsgdgnghVAGvklertvlEGAAGSGKQVAVGtGEFE 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 389 VIESRLILRSIGQRGVPIDGVPFDDANGVVSNEHGRVLREDG--QHVPGVYVTGWIKRGPRGVIGTNRSCAEQTVQKLWE 466
Cdd:PLN02852 340 DLPCGLVLKSIGYKSLPVDGLPFDHKRGVVPNVHGRVLSSASgaDTEPGLYVVGWLKRGPTGIIGTNLTCAEETVASIAE 419
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 467 DYDSGLL----DREVADRDAMADLLAERGAEPVDWQGWRAIDAAERERGRETSRPRVKFVDIAELLSAAN 532
Cdd:PLN02852 420 DLEQGRLrgvaSPPKPGRDGLLELLESRGVRVVPFSGWEKIDSAEKEAGRARGKPREKITSIEEMLKAAN 489
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
123-450 2.83e-38

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 145.66  E-value: 2.83e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 123 ELTRvAGVEVNMFDRLATPFGLVRTGVaPDHQHTKAVVKLFDPAFASPRFECHFNVEVGETITHEDLLAHHHAVIYAVGA 202
Cdd:COG0493  139 QLAR-AGHEVTVFEALDKPGGLLRYGI-PEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGA 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 203 PKGRDLGIPGEKLPGSYAAADFVGWYNGHPDHPdtTFDLSAERAVIIGNGNVALDVARillmapedlaktdiaqhaldkl 282
Cdd:COG0493  217 GKPRDLGIPGEDLKGVHSAMDFLTAVNLGEAPD--TILAVGKRVVVIGGGNTAMDCAR---------------------- 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 283 sdSAI----DEVVILARRGLREAAFSVGEflalghlpgvdvivdsdeldahddddvetrmkLEIAREftqrptqpqnKRI 358
Cdd:COG0493  273 --TALrlgaESVTIVYRRTREEMPASKEE--------------------------------VEEALE----------EGV 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 359 VFRFMVSPVEVGGEE--HAESLRVVH----------------VGGESEVIESRLILRSIGQRGVPIdgvPFDDANGVVSN 420
Cdd:COG0493  309 EFLFLVAPVEIIGDEngRVTGLECVRmelgepdesgrrrpvpIEGSEFTLPADLVILAIGQTPDPS---GLEEELGLELD 385
                        330       340       350
                 ....*....|....*....|....*....|...
gi 504524127 421 EHGRVLREDGQH---VPGVYVTGWIKRGPRGVI 450
Cdd:COG0493  386 KRGTIVVDEETYqtsLPGVFAGGDAVRGPSLVV 418
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
1-61 3.38e-16

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 73.20  E-value: 3.38e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504524127   1 MTYVITQSCCKDASCVPVCPVDCIRPVGatgeiTGTEMLYIDPVTCIDCGACVDACPIDAI 61
Cdd:COG1146    2 MPVIDTDKCIGCGACVEVCPVDVLELDE-----EGKKALVINPEECIGCGACELVCPVGAI 57
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
3-61 5.89e-12

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: 63.18  E-value: 5.89e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504524127   3 YVITQSC--CKDASCVPVCPVDCIRPvGATGEItgtemlYIDPVTCIDCGACVDACPIDAI 61
Cdd:cd04410   44 AFLPVSCmhCEDPPCVKACPTGAIYK-DEDGIV------LIDEDKCIGCGSCVEACPYGAI 97
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
10-60 7.59e-09

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: 51.76  E-value: 7.59e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 504524127   10 CKDasCVPVCPVDCIRPVGAtGEITGTEMLYIDPVTCIDCGACVDACPIDA 60
Cdd:pfam12838   4 CGA--CVAACPVGAITLDEV-GEKKGTKTVVIDPERCVGCGACVAVCPTGA 51
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
15-61 7.48e-07

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 49.11  E-value: 7.48e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 504524127  15 CVPVCPVDCIRPVGATGEiTGTEML--Y-IDPVTCIDCGACVDACPIDAI 61
Cdd:PRK05888  66 CAAICPADAITIEAAERE-DGRRRTtrYdINFGRCIFCGFCEEACPTDAI 114
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
46-84 1.13e-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: 37.12  E-value: 1.13e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 504524127   46 CIDCGACVDACPIDAIYYEEELPPELERFKDINSSYFEH 84
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKKGTKTVVIDPERCVG 39
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
26-61 2.75e-03

electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 38.63  E-value: 2.75e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 504524127   26 PVGATGEITGTEML-YIDPVTCIDCGACVDACPIDAI 61
Cdd:TIGR01944  94 PLDADAGTIQPPMVaLIDEDNCIGCTKCIQACPVDAI 130
 
Name Accession Description Interval E-value
PLN02852 PLN02852
ferredoxin-NADP+ reductase
99-532 1.12e-134

ferredoxin-NADP+ reductase


Pssm-ID: 215457  Cd Length: 491  Bit Score: 399.84  E-value: 1.12e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127  99 PAVERGSLRVAIVGAGPAACYAAAELT-RVAGVEVNMFDRLATPFGLVRTGVAPDHQHTKAVVKLFDPAFASPRFECHFN 177
Cdd:PLN02852  20 SSSTSEPLHVCVVGSGPAGFYTADKLLkAHDGARVDIIERLPTPFGLVRSGVAPDHPETKNVTNQFSRVATDDRVSFFGN 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 178 VEVGETITHEDLLAHHHAVIYAVGAPKGRDLGIPGEKLPGSYAAADFVGWYNGHPDHPDTTFDL-SAERAVIIGNGNVAL 256
Cdd:PLN02852 100 VTLGRDVSLSELRDLYHVVVLAYGAESDRRLGIPGEDLPGVLSAREFVWWYNGHPDCVHLPPDLkSSDTAVVLGQGNVAL 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 257 DVARILLMAPEDLAKTDIAQHALDKLSDSAIDEVVILARRGLREAAFSVGEFLALGHLPGVDVIVDSDELDAHDDDDVE- 335
Cdd:PLN02852 180 DCARILLRPTDELASTDIAEHALEALRGSSVRKVYLVGRRGPVQAACTAKELRELLGLKNVRVRIKEADLTLSPEDEEEl 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 336 --TRMKLEIAREFTQRPTQPQ------NKRIVFRFMVSPVE----------VGG--------EEHAESLRVVHVG-GESE 388
Cdd:PLN02852 260 kaSRPKRRVYELLSKAAAAGKcapsggQRELHFVFFRNPTRfldsgdgnghVAGvklertvlEGAAGSGKQVAVGtGEFE 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 389 VIESRLILRSIGQRGVPIDGVPFDDANGVVSNEHGRVLREDG--QHVPGVYVTGWIKRGPRGVIGTNRSCAEQTVQKLWE 466
Cdd:PLN02852 340 DLPCGLVLKSIGYKSLPVDGLPFDHKRGVVPNVHGRVLSSASgaDTEPGLYVVGWLKRGPTGIIGTNLTCAEETVASIAE 419
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 467 DYDSGLL----DREVADRDAMADLLAERGAEPVDWQGWRAIDAAERERGRETSRPRVKFVDIAELLSAAN 532
Cdd:PLN02852 420 DLEQGRLrgvaSPPKPGRDGLLELLESRGVRVVPFSGWEKIDSAEKEAGRARGKPREKITSIEEMLKAAN 489
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
123-450 2.83e-38

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 145.66  E-value: 2.83e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 123 ELTRvAGVEVNMFDRLATPFGLVRTGVaPDHQHTKAVVKLFDPAFASPRFECHFNVEVGETITHEDLLAHHHAVIYAVGA 202
Cdd:COG0493  139 QLAR-AGHEVTVFEALDKPGGLLRYGI-PEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGA 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 203 PKGRDLGIPGEKLPGSYAAADFVGWYNGHPDHPdtTFDLSAERAVIIGNGNVALDVARillmapedlaktdiaqhaldkl 282
Cdd:COG0493  217 GKPRDLGIPGEDLKGVHSAMDFLTAVNLGEAPD--TILAVGKRVVVIGGGNTAMDCAR---------------------- 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 283 sdSAI----DEVVILARRGLREAAFSVGEflalghlpgvdvivdsdeldahddddvetrmkLEIAREftqrptqpqnKRI 358
Cdd:COG0493  273 --TALrlgaESVTIVYRRTREEMPASKEE--------------------------------VEEALE----------EGV 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 359 VFRFMVSPVEVGGEE--HAESLRVVH----------------VGGESEVIESRLILRSIGQRGVPIdgvPFDDANGVVSN 420
Cdd:COG0493  309 EFLFLVAPVEIIGDEngRVTGLECVRmelgepdesgrrrpvpIEGSEFTLPADLVILAIGQTPDPS---GLEEELGLELD 385
                        330       340       350
                 ....*....|....*....|....*....|...
gi 504524127 421 EHGRVLREDGQH---VPGVYVTGWIKRGPRGVI 450
Cdd:COG0493  386 KRGTIVVDEETYqtsLPGVFAGGDAVRGPSLVV 418
PTZ00188 PTZ00188
adrenodoxin reductase; Provisional
102-528 2.62e-35

adrenodoxin reductase; Provisional


Pssm-ID: 240308  Cd Length: 506  Bit Score: 138.48  E-value: 2.62e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 102 ERGSLRVAIVGAGPAACYAAAELTRVAGVEVNMFDRLATPFGLVRTGVAPDHQHTKAVVKLFDPAFASPRFECHFNVEVG 181
Cdd:PTZ00188  36 EAKPFKVGIIGAGPSALYCCKHLLKHERVKVDIFEKLPNPYGLIRYGVAPDHIHVKNTYKTFDPVFLSPNYRFFGNVHVG 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 182 ETITHEDLLAHHHAVIYAVGA-----PKGR----DLGIPGEKLP----GSYAAADFVGWYNGHPDH-----PDT---TFD 240
Cdd:PTZ00188 116 VDLKMEELRNHYNCVIFCCGAsevsiPIGQqdedKAVSGGETNPrkqnGIFHARDLIYFYNNMYNDvrckaVDNylnSFE 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 241 lSAERAVIIGNGNVALDVARILLMAPEDLAKTDIAQHALDKLSDSAIDEVVILARRGLREAAFSVGEFLALGHLPGVDVI 320
Cdd:PTZ00188 196 -NFTTSIIIGNGNVSLDIARILIKSPDDLSKTDISSDYLKVIKRHNIKHIYIVGRRGFWQSSFTNAELRELISLENTKVI 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 321 VDSDELD---AHDDDDVETRMK-------LEIAREFTQRPTQPQ----NKRIVFRFM------------VSPVEVGGEEH 374
Cdd:PTZ00188 275 LSKKNYDlccHLKSDEENTNMKkrqheifQKMVKNYEEVEKNKEfyktYKIIEFIFYfeirqirpidgaMKNVELELNKN 354
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 375 AESLRVVHVggESEVIESRLILRSIGqrgvpidgvpFDDANGVVS--NEHGRVLRED-GQHVPGVYVTGWIKRGPRGVIG 451
Cdd:PTZ00188 355 VPMSFSSFK--ENKVLVTPLVIFATG----------FKKSNFAENlyNQSVQMFKEDiGQHKFAIFKAGWFDKGPKGNIA 422
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 452 T---NRSCAEQTVQKLWEDYDSglldreVADRDaMADLLAERGAEPVDWQGWRAIDAAERERGRETSRPRVKFVDIAELL 528
Cdd:PTZ00188 423 SqilNSKNSTHLVLNFLQKVDI------FFDND-ISSLLKEKQIPYVSFDDWTYLHQLEKQMGAQQNKIAQKFSQTGEVL 495
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
10-450 4.26e-21

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 96.02  E-value: 4.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127  10 CKDASCVPVCPV-----DCIRPVgATGEITGT-EMLY---IDPVTC-------IDC-GACVdacpidaiyyeeelppele 72
Cdd:PRK11749  45 CKDAPCVKACPVsidipEFIRLI-AEGNLKGAaETILetnPLPAVCgrvcpqeRLCeGACV------------------- 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127  73 rfkdINSSyfeHHPLAMDS-QRAGTDH----------PAVERGSlRVAIVGAGPAACYAAAELTRvAGVEVNMFDRLATP 141
Cdd:PRK11749 105 ----RGKK---GEPVAIGRlERYITDWametgwvlfkRAPKTGK-KVAVIGAGPAGLTAAHRLAR-KGYDVTIFEARDKA 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 142 FGLVRTGVapdhqhtkavvklfdPAFASPR----------------FEChfNVEVGETITHEDLLAHHHAVIYAVGAPKG 205
Cdd:PRK11749 176 GGLLRYGI---------------PEFRLPKdivdreverllklgveIRT--NTEVGRDITLDELRAGYDAVFIGTGAGLP 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 206 RDLGIPGEKLPGSYAAADFVgwynGHPDHPDTTFDLSA-ERAVIIGNGNVALDVAR--ILLMApedlaktdiaqhaldkl 282
Cdd:PRK11749 239 RFLGIPGENLGGVYSAVDFL----TRVNQAVADYDLPVgKRVVVIGGGNTAMDAARtaKRLGA----------------- 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 283 sdsaiDEVVILARRGlREaafsvgeflalgHLPGvdvivdsdeldahddddveTRMKLEIAREftqrptqpqnKRIVFRF 362
Cdd:PRK11749 298 -----ESVTIVYRRG-RE------------EMPA-------------------SEEEVEHAKE----------EGVEFEW 330
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 363 MVSPVEVGGEEHAES----------------LRVVHVGGESEVIESRLILRSIGQRgvPIDGVPFDDANGVVSNEHGRVL 426
Cdd:PRK11749 331 LAAPVEILGDEGRVTgvefvrmelgepdasgRRRVPIEGSEFTLPADLVIKAIGQT--PNPLILSTTPGLELNRWGTIIA 408
                        490       500
                 ....*....|....*....|....*.
gi 504524127 427 -REDGQ-HVPGVYVTGWIKRGPRGVI 450
Cdd:PRK11749 409 dDETGRtSLPGVFAGGDIVTGAATVV 434
gltD PRK12810
glutamate synthase subunit beta; Reviewed
99-458 1.59e-19

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 91.38  E-value: 1.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127  99 PAVERGSLRVAIVGAGPAACYAAAELTRvAGVEVNMFDRLATPFGLVRTGVaPDHQHTKAVV----KLFDPA---Faspr 171
Cdd:PRK12810 137 PPVKRTGKKVAVVGSGPAGLAAADQLAR-AGHKVTVFERADRIGGLLRYGI-PDFKLEKEVIdrriELMEAEgieF---- 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 172 fecHFNVEVGETITHEDLLAHHHAVIYAVGAPKGRDLGIPGEKLPGSYAAADFVGWYNGH--PDHPDTTFDLSAERAVII 249
Cdd:PRK12810 211 ---RTNVEVGKDITAEELLAEYDAVFLGTGAYKPRDLGIPGRDLDGVHFAMDFLIQNTRRvlGDETEPFISAKGKHVVVI 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 250 GNGNVALDVARillmapedlakTDIAQHALdklsdsaidEVVilaRRGLREAafsvgeflalghlPGvdvivdsdeldah 329
Cdd:PRK12810 288 GGGDTGMDCVG-----------TAIRQGAK---------SVT---QRDIMPM-------------PP------------- 318
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 330 ddddvETRMKLeiarefTQRPTQPQNKRI--------VFRFMVSPVE-VGGEEHAESLRVVHVG----------GESEVI 390
Cdd:PRK12810 319 -----SRRNKN------NPWPYWPMKLEVsnaheegvEREFNVQTKEfEGENGKVTGVKVVRTElgegdfepveGSEFVL 387
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504524127 391 ESRLILRSIGQRGvPIDGVPfdDANGVVSNEHGRVLREDGQH---VPGVYVTGWIKRGPRGV---IGTNRSCAE 458
Cdd:PRK12810 388 PADLVLLAMGFTG-PEAGLL--AQFGVELDERGRVAAPDNAYqtsNPKVFAAGDMRRGQSLVvwaIAEGRQAAR 458
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
1-61 3.38e-16

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 73.20  E-value: 3.38e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504524127   1 MTYVITQSCCKDASCVPVCPVDCIRPVGatgeiTGTEMLYIDPVTCIDCGACVDACPIDAI 61
Cdd:COG1146    2 MPVIDTDKCIGCGACVEVCPVDVLELDE-----EGKKALVINPEECIGCGACELVCPVGAI 57
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
129-452 9.70e-14

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 72.71  E-value: 9.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 129 GVEVNMFDRLATPFGL--------------VRTGV-------APDHQHTKAVvklfdpaFASPRFECHFNVEVGETITHE 187
Cdd:PRK12770  41 GYEVHVYDKLPEPGGLmlfgipefripierVREGVkeleeagVVFHTRTKVC-------CGEPLHEEEGDEFVERIVSLE 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 188 DLLAHHHAVIYAVGAPKGRDLGIPGEKLPGSYAAADFVGWYN----GHPDHpDTTFDLSAERAVIIGNGNVALDVArill 263
Cdd:PRK12770 114 ELVKKYDAVLIATGTWKSRKLGIPGEDLPGVYSALEYLFRIRaaklGYLPW-EKVPPVEGKKVVVVGAGLTAVDAA---- 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 264 mapeDLAKTDIAqhaldklsdsaiDEVVILARRGLREAAFSvgeflalghlpgvdvivdsdeldahddddvetrmKLEIA 343
Cdd:PRK12770 189 ----LEAVLLGA------------EKVYLAYRRTINEAPAG----------------------------------KYEIE 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 344 ReftqrptqPQNKRIVFRFMVSPVEVGGEEHAESLRVVH----------------VGGESEVIESRLILRSIGQRGVPid 407
Cdd:PRK12770 219 R--------LIARGVEFLELVTPVRIIGEGRVEGVELAKmrlgepdesgrprpvpIPGSEFVLEADTVVFAIGEIPTP-- 288
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 504524127 408 gvPF-DDANGVVSNEHGRVlREDGQH---VPGVYVTGWIKRGPRgVIGT 452
Cdd:PRK12770 289 --PFaKECLGIELNRKGEI-VVDEKHmtsREGVFAAGDVVTGPS-KIGK 333
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
1-61 9.90e-14

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 66.22  E-value: 9.90e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504524127   1 MTYVI-TQSC--CKDasCVPVCPVDCIRPvgatgeitGTEMLYIDPVTCIDCGACVDACPIDAI 61
Cdd:COG4231   15 MRYVIdEDKCtgCGA--CVKVCPADAIEE--------GDGKAVIDPDLCIGCGSCVQVCPVDAI 68
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
173-450 8.80e-13

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 70.67  E-value: 8.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 173 ECHFNVEVGETITHEDLLAHHHAVIYAVGAPKGRDLGIPGEKLPGSYAAADFVGWYN-GHPDHpdttfdlSAERAVIIGN 251
Cdd:PRK12771 203 EVRLGVRVGEDITLEQLEGEFDAVFVAIGAQLGKRLPIPGEDAAGVLDAVDFLRAVGeGEPPF-------LGKRVVVIGG 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 252 GNVALDVARillmapedLAKTDIAqhaldklsdsaiDEVVILARRGLRE---AAFSVGEFLAlghlPGVDVIvdsdelda 328
Cdd:PRK12771 276 GNTAMDAAR--------TARRLGA------------EEVTIVYRRTREDmpaHDEEIEEALR----EGVEIN-------- 323
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 329 hddddvETRMKLEIAREftqrptqpQNKRIVFRfmVSPVEVGgeEHAESLRVVHVGGESEVIESRLILRSIGQRgvpIDG 408
Cdd:PRK12771 324 ------WLRTPVEIEGD--------ENGATGLR--VITVEKM--ELDEDGRPSPVTGEEETLEADLVVLAIGQD---IDS 382
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 504524127 409 VPFDDANGvVSNEHGRVLREDGQHV---PGVYVTGWIKRGPRGVI 450
Cdd:PRK12771 383 AGLESVPG-VEVGRGVVQVDPNFMMtgrPGVFAGGDMVPGPRTVT 426
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
3-61 5.89e-12

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: 63.18  E-value: 5.89e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504524127   3 YVITQSC--CKDASCVPVCPVDCIRPvGATGEItgtemlYIDPVTCIDCGACVDACPIDAI 61
Cdd:cd04410   44 AFLPVSCmhCEDPPCVKACPTGAIYK-DEDGIV------LIDEDKCIGCGSCVEACPYGAI 97
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
15-61 8.55e-12

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 60.53  E-value: 8.55e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 504524127  15 CVPVCPVDCIRPVgatgEITGTEMLYIDPVTCIDCGACVDACPIDAI 61
Cdd:COG1143   10 CVRVCPVDAITIE----DGEPGKVYVIDPDKCIGCGLCVEVCPTGAI 52
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
1-61 2.59e-11

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 59.36  E-value: 2.59e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504524127   1 MTYVITQSCCKDASCVPVCPVDCIRPvgatgeitGTEMLYIDPVTCIDCGACVDACPIDAI 61
Cdd:COG2768    5 KPYVDEEKCIGCGACVKVCPVGAISI--------EDGKAVIDPEKCIGCGACIEVCPVGAI 57
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
107-260 1.74e-10

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 63.51  E-value: 1.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 107 RVAIVGAGPAACYAAAELTRvAGVEVNMFDRLATPFGLVRTGVAPdHQHTKAVVKLFDPAFASPRFECHFNVEVGETITH 186
Cdd:PRK12809 312 KVAVIGAGPAGLGCADILAR-AGVQVDVFDRHPEIGGMLTFGIPP-FKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITF 389
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 187 EDLLAHHHAVIYAVGAPKGRDLGIPGEKLPGSYAAADFVGWYN----GHP---DHPDTtfDLSAERAVIIGNGNVALDVA 259
Cdd:PRK12809 390 SDLTSEYDAVFIGVGTYGMMRADLPHEDAPGVIQALPFLTAHTrqlmGLPeseEYPLT--DVEGKRVVVLGGGDTTMDCL 467

                 .
gi 504524127 260 R 260
Cdd:PRK12809 468 R 468
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
10-61 2.73e-10

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


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 58.36  E-value: 2.73e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504524127  10 CKDASCVPVCPVDCIRPVGATGEITgtemlyIDPVTCIDCGACVDACPIDAI 61
Cdd:cd10550   52 CEDAPCVEACPVGAISRDEETGAVV------VDEDKCIGCGMCVEACPFGAI 97
PRK13984 PRK13984
putative oxidoreductase; Provisional
97-260 1.27e-09

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 60.94  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127  97 DHPAVERGSlRVAIVGAGPAACYAAAELTRVaGVEVNMFDRLATPFGLVRTGVA----PDHQHTKavvklfDPAF-ASPR 171
Cdd:PRK13984 276 DDEPEKKNK-KVAIVGSGPAGLSAAYFLATM-GYEVTVYESLSKPGGVMRYGIPsyrlPDEALDK------DIAFiEALG 347
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 172 FECHFNVEVGETITHEDLLAHHHAVIYAVGAPKGRDLGIPGEKLPGSYAAADFV----GWYNGHPDHPDTtfdlsAERAV 247
Cdd:PRK13984 348 VKIHLNTRVGKDIPLEELREKHDAVFLSTGFTLGRSTRIPGTDHPDVIQALPLLreirDYLRGEGPKPKI-----PRSLV 422
                        170
                 ....*....|...
gi 504524127 248 IIGNGNVALDVAR 260
Cdd:PRK13984 423 VIGGGNVAMDIAR 435
NapF COG1145
Ferredoxin [Energy production and conversion];
4-61 2.33e-09

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 58.20  E-value: 2.33e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504524127   4 VITQSCCKDASCVPVCPVDCIRPVGatgeitGTEMLYIDPVTCIDCGACVDACPIDAI 61
Cdd:COG1145  179 IDAEKCIGCGLCVKVCPTGAIRLKD------GKPQIVVDPDKCIGCGACVKVCPVGAI 230
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
3-61 3.05e-09

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: 55.10  E-value: 3.05e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127   3 YVITQSCC-KDASCVPVCPVDCIrpvgatgEITGTEMLYIDPVTCIDCGACVDACPIDAI 61
Cdd:cd10549   73 AEIDEEKCiGCGLCVKVCPVDAI-------TLEDELEIVIDKEKCIGCGICAEVCPVNAI 125
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
107-263 3.25e-09

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 59.36  E-value: 3.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 107 RVAIVGAGPAACYAAAELTRVaGVEVNMFDRLATPFGLVRTGVaPDHQHTKAVVklfDPAFASPR---FECHFNVEVGET 183
Cdd:PRK12814 195 KVAIIGAGPAGLTAAYYLLRK-GHDVTIFDANEQAGGMMRYGI-PRFRLPESVI---DADIAPLRamgAEFRFNTVFGRD 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 184 ITHEDLLAHHHAVIYAVGAPKGRDLGIPGEKLPGSYAAADFVGWYN-GHPDHPdttfdlsAERAVIIGNGNVALDVARIL 262
Cdd:PRK12814 270 ITLEELQKEFDAVLLAVGAQKASKMGIPGEELPGVISGIDFLRNVAlGTALHP-------GKKVVVIGGGNTAIDAARTA 342

                 .
gi 504524127 263 L 263
Cdd:PRK12814 343 L 343
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
4-61 3.28e-09

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 53.13  E-value: 3.28e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504524127   4 VITQSCCKD-ASCVPVCPVDCIRPVGATgeitgtemLYIDPVTCIDCGACVDACPIDAI 61
Cdd:COG2221   11 KIDEEKCIGcGLCVAVCPTGAISLDDGK--------LVIDEEKCIGCGACIRVCPTGAI 61
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
15-61 3.71e-09

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: 55.10  E-value: 3.71e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 504524127  15 CVPVCPVDCIRPVGATGEITGTEmlyIDPVTCIDCGACVDACPIDAI 61
Cdd:cd10549   14 CVKACPTDAIELGPNGAIARGPE---IDEDKCVFCGACVEVCPTGAI 57
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
4-61 5.51e-09

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 52.42  E-value: 5.51e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504524127   4 VITQSCCKDASCVPVCPVDCIRpvgatgeITGTEMLYIDPVTCIDCGACVDACPIDAI 61
Cdd:COG1149    8 IDEEKCIGCGLCVEVCPEGAIK-------LDDGGAPVVDPDLCTGCGACVGVCPTGAI 58
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
15-61 6.62e-09

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: 54.33  E-value: 6.62e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 504524127  15 CVPVCPVDCIRPVGATGEITGTEM-LYIDPVTCIDCGACVDACPIDAI 61
Cdd:cd10549   48 CVEVCPTGAIELTPEGKEYVPKEKeAEIDEEKCIGCGLCVKVCPVDAI 95
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
1-61 7.29e-09

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


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 52.75  E-value: 7.29e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504524127   1 MTYVITQSCCKD-ASCVPVCPVDCIRPvgatgeiTGTEMLYIDPVTCIDCGACVDACPIDAI 61
Cdd:COG1144   23 ERPVVDEDKCIGcGLCWIVCPDGAIRV-------DDGKYYGIDYDYCKGCGICAEVCPVKAI 77
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
10-60 7.59e-09

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: 51.76  E-value: 7.59e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 504524127   10 CKDasCVPVCPVDCIRPVGAtGEITGTEMLYIDPVTCIDCGACVDACPIDA 60
Cdd:pfam12838   4 CGA--CVAACPVGAITLDEV-GEKKGTKTVVIDPERCVGCGACVAVCPTGA 51
Fer4_9 pfam13187
4Fe-4S dicluster domain;
9-61 1.31e-08

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 51.02  E-value: 1.31e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 504524127    9 CCKDASCVPVCPVDCIRPVGATGEItgteMLYIDPVTCIDCGACVDACPIDAI 61
Cdd:pfam13187   2 CTGCGACVAACPAGAIVPDLVGQTI----RGDIAGLACIGCGACVDACPRGAI 50
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
3-61 2.02e-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: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 52.95  E-value: 2.02e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504524127   3 YVITQSC--CKDASCVPVCPVDCI--RPVGATgeitgtemlYIDPVTCIDCGACVDACPIDAI 61
Cdd:cd16371   48 YFLSMSCnhCENPACVKVCPTGAItkREDGIV---------VVDQDKCIGCGYCVWACPYGAP 101
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
10-61 2.98e-08

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: 53.17  E-value: 2.98e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504524127  10 CKDASCVPVCPvdcirpvgaTGEITGTE--MLYIDPVTCIDCGACVDACPIDAI 61
Cdd:cd16366   73 CTDAGCLAACP---------TGAIIRTEtgTVVVDPETCIGCGYCVNACPFDIP 117
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
8-61 3.39e-08

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 53.41  E-value: 3.39e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504524127   8 SC--CKDASCVPVCPVDCIRpVGATGEItgtemlYIDPVTCIDCGACVDACPIDAI 61
Cdd:COG0437   59 LCnhCDDPPCVKVCPTGATY-KREDGIV------LVDYDKCIGCRYCVAACPYGAP 107
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
102-260 4.99e-08

bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 55.90  E-value: 4.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 102 ERGSLRVAIVGAGPAACYAAAELTRvAGVEVNMFDRLATPFGLVRTGVaPDHQHTKAVVKLFDPAFASPRFECHFNVEVG 181
Cdd:PRK12778 428 EKNGKKVAVIGSGPAGLSFAGDLAK-RGYDVTVFEALHEIGGVLKYGI-PEFRLPKKIVDVEIENLKKLGVKFETDVIVG 505
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 182 ETITHEDLLAHHHAVIY-AVGAPKGRDLGIPGEKLPGSYAAADF---VGWYNGHPDHPDTTFDLsAERAVIIGNGNVALD 257
Cdd:PRK12778 506 KTITIEELEEEGFKGIFiASGAGLPNFMNIPGENSNGVMSSNEYltrVNLMDAASPDSDTPIKF-GKKVAVVGGGNTAMD 584

                 ...
gi 504524127 258 VAR 260
Cdd:PRK12778 585 SAR 587
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
7-61 6.04e-08

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: 52.31  E-value: 6.04e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504524127   7 QSC--CKDASCVPVCPVDCIrpvgatgEITGTEMLYIDPVTCIDCGACVDACPIDAI 61
Cdd:cd10562   68 RQCmhCTDAACVKVCPTGAL-------YKTENGAVVVDEDKCIGCGYCVAACPFDVP 117
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
10-61 9.76e-08

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 51.20  E-value: 9.76e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504524127  10 CKDASCVPVCPVDCIRPvgatgeitGTEMLYIDPVTCIDCGACVDACPIDAI 61
Cdd:COG1142   55 CEDAPCAEVCPVGAITR--------DDGAVVVDEEKCIGCGLCVLACPFGAI 98
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
1-57 1.49e-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: 48.40  E-value: 1.49e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 504524127    1 MTYVITQSCCKDASCVPVCPVdCIRPVGATGEITGTEMLYIDPVTCIDCGACVDACP 57
Cdd:pfam13237   1 KVVIDPDKCIGCGRCTAACPA-GLTRVGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
PRK12831 PRK12831
putative oxidoreductase; Provisional
177-263 1.50e-07

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 53.87  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 177 NVEVGETITHEDLLAHHH--AVIYAVGAPKGRDLGIPGEKLPGSYAAADFVGWYN---GHPDHPDTTFdLSAERAVIIGN 251
Cdd:PRK12831 211 NVVVGKTVTIDELLEEEGfdAVFIGSGAGLPKFMGIPGENLNGVFSANEFLTRVNlmkAYKPEYDTPI-KVGKKVAVVGG 289
                         90
                 ....*....|..
gi 504524127 252 GNVALDVARILL 263
Cdd:PRK12831 290 GNVAMDAARTAL 301
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
2-57 2.54e-07

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: 50.05  E-value: 2.54e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504524127   2 TYVITQSC--CKDASCVPVCPvdcirpvgaTGEITGTE---MLYIDPVTCIDCGACVDACP 57
Cdd:cd10553   51 LKFVYMSCfhCENPWCVKACP---------TGAMQKREkdgIVYVDQELCIGCKACIEACP 102
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
107-260 3.08e-07

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 53.21  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 107 RVAIVGAGPAACYAAAELTRvAGVEVNMFDRLATPFGLVRTGVaPDHQHTKAVVKLFDPAFASPRFECHFNVEVGETITH 186
Cdd:PRK12769 329 RVAIIGAGPAGLACADVLAR-NGVAVTVYDRHPEIGGLLTFGI-PAFKLDKSLLARRREIFSAMGIEFELNCEVGKDISL 406
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 187 EDLLAHHHAVIYAVGAPKGRDLGIPGEKLPGSYAAADF-------VGWYNGHPDHPdtTFDLSAERAVIIGNGNVALDVA 259
Cdd:PRK12769 407 ESLLEDYDAVFVGVGTYRSMKAGLPNEDAPGVYDALPFliantkqVMGLEELPEEP--FINTAGLNVVVLGGGDTAMDCV 484

                 .
gi 504524127 260 R 260
Cdd:PRK12769 485 R 485
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
1-61 3.11e-07

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: 50.61  E-value: 3.11e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504524127   1 MTYVITQsC--CKDASCVPVCPVdcirpvGATgeitgtemlY--------IDPVTCIDCGACVDACPIDAI 61
Cdd:cd10551   46 RTFLPVL-CnhCENPPCVKVCPT------GAT---------YkredgivlVDYDKCIGCRYCMAACPYGAR 100
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
5-61 5.91e-07

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


Pssm-ID: 319889 [Multi-domain]  Cd Length: 138  Bit Score: 48.84  E-value: 5.91e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504524127   5 ITQSC--CKDASCVPVCPVDCIRpVGATGEITgtemlyIDPvTCIDCGACVDACPIDAI 61
Cdd:cd16367   53 VPTACrhCVDPVCMIGCPTGAIH-RDDGGEVV------ISD-ACCGCGNCASACPYGAI 103
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
10-61 6.96e-07

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 50.83  E-value: 6.96e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504524127  10 CKDasCVPVCPVDC-IRpvgaTGEITGTEmlyidpvtCIDCGACVDACPIDAI 61
Cdd:COG0348  215 CGL--CVKVCPMGIdIR----KGEINQSE--------CINCGRCIDACPKDAI 253
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
15-61 7.48e-07

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 49.11  E-value: 7.48e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 504524127  15 CVPVCPVDCIRPVGATGEiTGTEML--Y-IDPVTCIDCGACVDACPIDAI 61
Cdd:PRK05888  66 CAAICPADAITIEAAERE-DGRRRTtrYdINFGRCIFCGFCEEACPTDAI 114
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
4-61 1.35e-06

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 50.79  E-value: 1.35e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504524127   4 VITQSCCKDA-SCVPVCPVDCIRPVGATgeitgtemLYIDPVTCIDCGACVDACPIDAI 61
Cdd:COG4624   87 IRDKEKCKNCyPCVRACPVKAIKVDDGK--------AEIDEEKCISCGQCVAVCPFGAI 137
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
10-61 1.74e-06

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: 47.64  E-value: 1.74e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504524127  10 CKDASCVPVCPVDCIRPVGatGEITgtemlyIDPVTCIDCGACVDACPIDAI 61
Cdd:cd10554   59 CEDAPCANVCPVGAISQED--GVVQ------VDEERCIGCKLCVLACPFGAI 102
PRK12775 PRK12775
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ...
107-261 1.92e-06

putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional


Pssm-ID: 183738 [Multi-domain]  Cd Length: 1006  Bit Score: 50.71  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127  107 RVAIVGAGPAACYAAAELTRVaGVEVNMFDRLATPFGLVRTGVA----PDHQHTKAVVKLFDPAFaspRFEChfNVEVGE 182
Cdd:PRK12775  432 KVAICGSGPAGLAAAADLVKY-GVDVTVYEALHVVGGVLQYGIPsfrlPRDIIDREVQRLVDIGV---KIET--NKVIGK 505
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127  183 TITHEDLLAH--HHAVIYAVGAPKGRDLGIPGEKLPGSYAAADFVGWYN--GHPDHP--DTTFDLsAERAVIIGNGNVAL 256
Cdd:PRK12775  506 TFTVPQLMNDkgFDAVFLGVGAGAPTFLGIPGEFAGQVYSANEFLTRVNlmGGDKFPflDTPISL-GKSVVVIGAGNTAM 584

                  ....*
gi 504524127  257 DVARI 261
Cdd:PRK12775  585 DCLRV 589
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
9-61 1.96e-06

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 47.64  E-value: 1.96e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504524127   9 CCKDasCVPVCPVDCIRPVgaTGEITGTEM--LYIDPVTCI------DCGACVDACPIDAI 61
Cdd:cd16373   58 CCDA--CVEVCPTGALRPL--DLEEQKVKMgvAVIDKDRCLawqggtDCGVCVEACPTEAI 114
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
10-57 6.81e-06

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: 47.38  E-value: 6.81e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 504524127  10 CKDASCVPVCPvdcirpvgaTGEITGTEM--LYIDPVTCIDCGACVDACP 57
Cdd:cd10560   81 CTDAGCLEACP---------TGAIFRTEFgtVYIQPDICNGCGYCVAACP 121
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
39-61 8.82e-06

4Fe-4S binding 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.


Pssm-ID: 459642 [Multi-domain]  Cd Length: 24  Bit Score: 42.24  E-value: 8.82e-06
                          10        20
                  ....*....|....*....|...
gi 504524127   39 LYIDPVTCIDCGACVDACPIDAI 61
Cdd:pfam00037   1 VVIDEEKCIGCGACVEVCPVGAI 23
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
14-61 1.82e-05

Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 46.53  E-value: 1.82e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 504524127  14 SCVPVCPVDCIRpVGATGeitgteMLYIDPVTCIDCGACVDACPIDAI 61
Cdd:COG2878  144 DCIKACPFDAIV-GAAKG------MHTVDEDKCTGCGLCVEACPVDCI 184
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
10-61 2.48e-05

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


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 44.19  E-value: 2.48e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504524127  10 CKDASCVPVCPVDCIRPVGATGEItgtemlyIDPVTCIDCGACVDACPIDAI 61
Cdd:cd16370   56 CEDPPCAEACPTGALEPRKGGGVV-------LDKEKCIGCGNCVKACIVGAI 100
PRK12779 PRK12779
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ...
177-260 3.05e-05

putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional


Pssm-ID: 183740 [Multi-domain]  Cd Length: 944  Bit Score: 46.75  E-value: 3.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 177 NVEVGETITHEDLLAHHHAVIY-AVGAPKGRDLGIPGEKLPGSYAAADFVGWYN---GHPDHPDTTF-DLSAERAVIIGN 251
Cdd:PRK12779 376 NFVVGKTATLEDLKAAGFWKIFvGTGAGLPTFMNVPGEHLLGVMSANEFLTRVNlmrGLDDDYETPLpEVKGKEVFVIGG 455

                 ....*....
gi 504524127 252 GNVALDVAR 260
Cdd:PRK12779 456 GNTAMDAAR 464
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
9-61 3.15e-05

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 46.56  E-value: 3.15e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504524127   9 CCKDASCVPVCPVDCIRPVGATGEITGTEMLYIDPVTCIDCGACVDACPIDAI 61
Cdd:COG4624   56 LCCCCCCRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCYPCVRACPVKAI 108
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
33-61 3.83e-05

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 41.58  E-value: 3.83e-05
                         10        20
                 ....*....|....*....|....*....
gi 504524127  33 ITGTEMLYIDPVTCIDCGACVDACPIDAI 61
Cdd:COG2221    4 IIGTWPPKIDEEKCIGCGLCVAVCPTGAI 32
PRK09898 PRK09898
ferredoxin-like protein;
6-61 6.68e-05

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 44.06  E-value: 6.68e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504524127   6 TQSC--CKDASCVPVCPVDCIRPVGATGEITGTE----------------MLYIDPVT-----CIDCGACVDACPIDAI 61
Cdd:PRK09898 120 ADTCrqCKEPQCMNVCPIGAITWQQKEGCITVDHkrcigcsacttacpwmMATVNTESkksskCVLCGECANACPTGAL 198
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
5-59 1.07e-04

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 44.27  E-value: 1.07e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504524127   5 ITQSC--CKDASCVPVCPVDCIRPVGATGEITgtemlYiDPVTCIDCGACVDACPID 59
Cdd:PRK10882 108 IKKQCmhCVDPNCVSVCPVSALTKDPKTGIVH-----Y-DKDVCTGCRYCMVACPFN 158
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
39-61 1.22e-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: 42.00  E-value: 1.22e-04
                         10        20
                 ....*....|....*....|...
gi 504524127  39 LYIDPVTCIDCGACVDACPIDAI 61
Cdd:cd10549    1 LKYDPEKCIGCGICVKACPTDAI 23
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
15-61 1.87e-04

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 43.38  E-value: 1.87e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 504524127  15 CVPVCPVDCIRPVGAtgeitgteMLYIDPVTCIDCGACVDACPIDAI 61
Cdd:PRK07118 221 CVKACPAGAITMENN--------LAVIDQEKCTSCGKCVEKCPTKAI 259
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
14-61 2.00e-04

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


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 41.17  E-value: 2.00e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 504524127  14 SCVPVCPVDCIRPVGAtgeitgtemlYIDPVTCIDCGACVDACPIDAI 61
Cdd:cd16372   84 MCVGFCPEGAMFKHED----------YPEPFKCIACGICVKACPTGAL 121
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
194-440 2.40e-04

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 43.18  E-value: 2.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 194 HAVIYAVGApKGRDLGIPGEKLPG----SYAA----ADFVGwynghpdhpdttfdlsaERAVIIGNGNVALDVARILlma 265
Cdd:COG0492  102 KAVIIATGA-GPRKLGLPGEEEFEgrgvSYCAtcdgFFFRG-----------------KDVVVVGGGDSALEEALYL--- 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 266 pedlakTDIAqhaldklsdsaiDEVVILARRG-LREAAFSVGEflaLGHLPGVDVIVDSDeldahddddvetrmkleiar 344
Cdd:COG0492  161 ------TKFA------------SKVTLIHRRDeLRASKILVER---LRANPKIEVLWNTE-------------------- 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127 345 eftqrptqpqnkrivfrfmvsPVEVGGEEHAESLRVVHV-GGESEVIESRLILRSIGQrgVPIDGvPFDDAnGVVSNEHG 423
Cdd:COG0492  200 ---------------------VTEIEGDGRVEGVTLKNVkTGEEKELEVDGVFVAIGL--KPNTE-LLKGL-GLELDEDG 254
                        250
                 ....*....|....*....
gi 504524127 424 RVLREDGQH--VPGVYVTG 440
Cdd:COG0492  255 YIVVDEDMEtsVPGVFAAG 273
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
34-61 2.71e-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: 39.33  E-value: 2.71e-04
                         10        20
                 ....*....|....*....|....*...
gi 504524127  34 TGTEMLYIDPVTCIDCGACVDACPIDAI 61
Cdd:COG1149    1 VKRKIPVIDEEKCIGCGLCVEVCPEGAI 28
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
4-61 3.04e-04

NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. 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 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: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 41.08  E-value: 3.04e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504524127   4 VITQSC----------CKDAscvpvCPVDCIRpvgATGEITGTEMLYIDPVTCIDCGACVDACPIDAI 61
Cdd:cd10564   75 EIGDSClalqgvecrsCQDA-----CPTQAIR---FRPRLGGIALPELDADACTGCGACVSVCPVGAI 134
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
15-61 3.11e-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: 41.47  E-value: 3.11e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 504524127  15 CVPVCPVDCIRPVGATGEITGTEMLYIDPVT--CI-DCGACVDACPIDAI 61
Cdd:cd16373   22 CVEACPTGVIQPAGLEDGLEGGRTPYLDPREgpCDlCCDACVEVCPTGAL 71
PRK13795 PRK13795
hypothetical protein; Provisional
15-58 3.15e-04

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 43.44  E-value: 3.15e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 504524127  15 CVPVCPVDCIRPVGATGEItgtemlYIDPVTCIDCGACVDACPI 58
Cdd:PRK13795 589 CVGACPTGAIRIEEGKRKI------SVDEEKCIHCGKCTEVCPV 626
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
10-57 3.71e-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: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 41.60  E-value: 3.71e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 504524127  10 CKDASCVPVCPVDCIRpVGATGEItgtemLYIDPVTCIDCGACVDACP 57
Cdd:cd16369   54 CEDPTCAEVCPADAIK-VTEDGVV-----QSALKPRCIGCSNCVNACP 95
PRK12844 PRK12844
3-ketosteroid-delta-1-dehydrogenase; Reviewed
405-440 3.96e-04

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 183787 [Multi-domain]  Cd Length: 557  Bit Score: 43.20  E-value: 3.96e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 504524127 405 PIDGVPF----------DDANGVVSNEHGRVLREDGQHVPGVYVTG 440
Cdd:PRK12844 469 PLDKPPFyavrmvpgdvGTSGGLLTDEHARVLREDGSVIPGLYATG 514
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
46-61 4.24e-04

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 38.63  E-value: 4.24e-04
                          10
                  ....*....|....*.
gi 504524127   46 CIDCGACVDACPIDAI 61
Cdd:pfam13484   1 CGSCGKCIDACPTGAI 16
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
10-60 4.31e-04

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 42.17  E-value: 4.31e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504524127  10 CKDASCVPVCPVDCI--RPVGatgeitgteMLYIDPVTCIDCGACVDACPIDA 60
Cdd:PRK14993 103 CDNPPCVPVCPVQATfqREDG---------IVVVDNKRCVGCAYCVQACPYDA 146
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
10-60 4.90e-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: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 39.54  E-value: 4.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 504524127   10 CKDASCVPVCPVDCIRPVGATGEITgtemlyIDPVTCIDCGACVDACPIDA 60
Cdd:pfam13247  13 CLNPPCKASCPVGAIYKDEETGAVL------LDEKTCRGWRECVSACPYNI 57
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
15-57 6.10e-04

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 38.24  E-value: 6.10e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 504524127   15 CVPVCPVDCIRPVGATGE--------ITGTEMLYIDPVTCID------CGACVDACP 57
Cdd:pfam13484   7 CIDACPTGAIVGPEGVLDarrcisylTIEKKGLIPDELRCLLgnrcygCDICQDVCP 63
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
3-61 7.89e-04

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 40.03  E-value: 7.89e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504524127   3 YVITQSC--CKdaSCVPVCPVDCIRPVGATGEITgtemlyidPVTCIDCG------ACVDACPIDAI 61
Cdd:COG1142   77 VVDEEKCigCG--LCVLACPFGAITMVGEKSRAV--------AVKCDLCGgreggpACVEACPTGAL 133
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
46-84 1.13e-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: 37.12  E-value: 1.13e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 504524127   46 CIDCGACVDACPIDAIYYEEELPPELERFKDINSSYFEH 84
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKKGTKTVVIDPERCVG 39
PRK06273 PRK06273
ferredoxin; Provisional
4-58 1.39e-03

ferredoxin; Provisional


Pssm-ID: 235764 [Multi-domain]  Cd Length: 165  Bit Score: 39.69  E-value: 1.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127   4 VITQSCCKDASCVPVCPVDCI-----RPVGATGEITGTEMLYIDPVTCIDCGACVDACPI 58
Cdd:PRK06273  46 VFEELCIGCGGCANVCPTKAIemipvEPVKITEGYVKTKIPKIDYEKCVYCLYCHDFCPV 105
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
46-61 2.07e-03

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 36.65  E-value: 2.07e-03
                         10
                 ....*....|....*.
gi 504524127  46 CIDCGACVDACPIDAI 61
Cdd:COG1143    4 CIGCGLCVRVCPVDAI 19
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
4-61 2.33e-03

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 40.61  E-value: 2.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504524127   4 VITQSC--CKdaSCVPVCPVDCIrpvgatgEITGTEMLYIDPVTCIDCGACVDACPIDAI 61
Cdd:COG1148  493 VDPEKCtgCG--RCVEVCPYGAI-------SIDEKGVAEVNPALCKGCGTCAAACPSGAI 543
PRK12835 PRK12835
3-ketosteroid-delta-1-dehydrogenase; Reviewed
393-440 2.44e-03

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 237221 [Multi-domain]  Cd Length: 584  Bit Score: 40.56  E-value: 2.44e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 504524127 393 RLILRSIGQRGvpidgvpfddanGVVSNEHGRVLREDGQHVPGVYVTG 440
Cdd:PRK12835 499 RIELGDLGTSG------------GLRTDEHARVLREDDSVIPGLYAVG 534
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
26-61 2.75e-03

electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 38.63  E-value: 2.75e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 504524127   26 PVGATGEITGTEML-YIDPVTCIDCGACVDACPIDAI 61
Cdd:TIGR01944  94 PLDADAGTIQPPMVaLIDEDNCIGCTKCIQACPVDAI 130
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
3-61 3.02e-03

electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 38.63  E-value: 3.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 504524127    3 YVITQSCCKDASCVPVCPVDCIrpVGATgeitgTEMLYIDPVTCIDCGACVDACPIDAI 61
Cdd:TIGR01944 109 LIDEDNCIGCTKCIQACPVDAI--VGAA-----KAMHTVIADECTGCDLCVEPCPTDCI 160
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
15-61 3.56e-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: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 37.70  E-value: 3.56e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 504524127  15 CVPVCPVDCIrpvgaTGEITGTEMlyIDPVTCIDCGACVDACPIDAI 61
Cdd:cd16372   55 CIDVCPTGAI-----TRDANGVVM--INKKLCVGCLMCVGFCPEGAM 94
Fer4_6 pfam12837
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
41-61 3.75e-03

4Fe-4S binding domain; This 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.


Pssm-ID: 432822 [Multi-domain]  Cd Length: 24  Bit Score: 34.90  E-value: 3.75e-03
                          10        20
                  ....*....|....*....|.
gi 504524127   41 IDPVTCIDCGACVDACPIDAI 61
Cdd:pfam12837   4 VDPDKCIGCGRCVVVCPYGAI 24
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
10-59 4.53e-03

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: 38.52  E-value: 4.53e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504524127  10 CKDASCVPVCPvdcirpvgATGEITGTEMLYIDPVT--CIDCGACVDACPID 59
Cdd:cd10558   73 CADPGCLKACP--------SPGAIVQYANGIVDFQSdkCIGCGYCIKGCPFD 116
Fer4_2 pfam12797
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
37-57 5.13e-03

4Fe-4S binding domain; This 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.


Pssm-ID: 463711 [Multi-domain]  Cd Length: 22  Bit Score: 34.68  E-value: 5.13e-03
                          10        20
                  ....*....|....*....|.
gi 504524127   37 EMLYIDPVTCIDCGACVDACP 57
Cdd:pfam12797   1 WKPLIDADKCIGCGACVSACP 21
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
8-57 5.34e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 38.76  E-value: 5.34e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 504524127   8 SCCKDASCVPVCPVDCIRPVGATGEItgtemlyiDPVTCIDCGACVDACP 57
Cdd:PRK07118 140 GCLGLGSCVAACPFDAIHIENGLPVV--------DEDKCTGCGACVKACP 181
Fer4_13 pfam13370
4Fe-4S single cluster domain of Ferredoxin I; Fer4_13 is a ferredoxin I from sulfate-reducing ...
41-57 5.84e-03

4Fe-4S single cluster domain of Ferredoxin I; Fer4_13 is a ferredoxin I from sulfate-reducing bacteria. Chemical sequence analysis suggests that this characteriztic [4Fe-4S] cluster sulfur environment is widely distributed among ferredoxins.


Pssm-ID: 433153 [Multi-domain]  Cd Length: 58  Bit Score: 35.36  E-value: 5.84e-03
                          10
                  ....*....|....*..
gi 504524127   41 IDPVTCIDCGACVDACP 57
Cdd:pfam13370   1 VDEDTCIDCGTCRELAP 17
PRK06991 PRK06991
electron transport complex subunit RsxB;
1-35 8.17e-03

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 38.24  E-value: 8.17e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 504524127   1 MTYVITQSCCKDASCVPVCPVDCIRPVGATGEITG 35
Cdd:PRK06991 109 MHTVLADLCTGCDLCVPPCPVDCIDMVPVTGERTG 143
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
3-32 9.19e-03

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 35.40  E-value: 9.19e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 504524127   3 YVITQS-CCKDASCVPVCPVDCIRPVGATGE 32
Cdd:COG4231   46 AVIDPDlCIGCGSCVQVCPVDAIKLEKRVPE 76
PRK05113 PRK05113
electron transport complex protein RnfB; Provisional
40-61 9.72e-03

electron transport complex protein RnfB; Provisional


Pssm-ID: 235347 [Multi-domain]  Cd Length: 191  Bit Score: 37.62  E-value: 9.72e-03
                         10        20
                 ....*....|....*....|..
gi 504524127  40 YIDPVTCIDCGACVDACPIDAI 61
Cdd:PRK05113 110 FIDEDNCIGCTKCIQACPVDAI 131
 
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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