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Conserved domains on  [gi|2020379483|ref|WP_208690122|]
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MULTISPECIES: FAD-dependent oxidoreductase [Rhodococcus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02852 super family cl30539
ferredoxin-NADP+ reductase
 102-560 9.85e-154

ferredoxin-NADP+ reductase


The actual alignment was detected with superfamily member PLN02852:

Pssm-ID: 357415  Cd Length: 491  Bit Score: 449.92  E-value: 9.85e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 102 KGRPPLRVAIVGSGPSAMYAADELLTQPD-VQVNVFDRLPVPYGLVRAGVAPDHQKTKQVTRLFDKIAAQKGFEFYLNVE 180
Cdd:PLN02852   22 STSEPLHVCVVGSGPAGFYTADKLLKAHDgARVDIIERLPTPFGLVRSGVAPDHPETKNVTNQFSRVATDDRVSFFGNVT 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 181 IGKHISHSELLENHHAVLYAVGASSDRGLGIPGADLPGTASATDFVAWYNGHPDHADDVFDL-SHRRAVIIGNGNVALDV 259
Cdd:PLN02852  102 LGRDVSLSELRDLYHVVVLAYGAESDRRLGIPGEDLPGVLSAREFVWWYNGHPDCVHLPPDLkSSDTAVVLGQGNVALDC 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 260 ARILTADPEKLAGTDISAHALAALRKSRVEEVVIVGRRGIAQSAFTVPEFTGLMALPDIELSVGPDDMVLDSAtEELAKR 339
Cdd:PLN02852  182 ARILLRPTDELASTDIAEHALEALRGSSVRKVYLVGRRGPVQAACTAKELRELLGLKNVRVRIKEADLTLSPE-DEEELK 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 340 GELPHAVEQKLRLLEALKNRDHVDVGNKRITLRYLLTPTSI----TGDDQVSGIAFARNALVDANGTVQIEA--TGDTET 413
Cdd:PLN02852  261 ASRPKRRVYELLSKAAAAGKCAPSGGQRELHFVFFRNPTRFldsgDGNGHVAGVKLERTVLEGAAGSGKQVAvgTGEFED 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 414 IDTGLVLTSIGYRGVPIPGVPFDERASVIPNENGRVLEAPNG-DPATGVYATGWIKRGPSGFIGTNKSCAQETIRMLVDD 492
Cdd:PLN02852  341 LPCGLVLKSIGYKSLPVDGLPFDHKRGVVPNVHGRVLSSASGaDTEPGLYVVGWLKRGPTGIIGTNLTCAEETVASIAED 420

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020379483 493 FNDGRLTN----PVADDSAVDRLVRARQSDVVDREGWHAIDKAELERGAAHDRAREKVldqVEITSILDAAA 560
Cdd:PLN02852  421 LEQGRLRGvaspPKPGRDGLLELLESRGVRVVPFSGWEKIDSAEKEAGRARGKPREKI---TSIEEMLKAAN 489
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 1-71 7.20e-19

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


:

Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 80.91  E-value: 7.20e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2020379483   1 MPHVVTQSCCSDASCVYACPVNCIHPTPDEPdfltaEMLHIDPQACVDCGACVSACPVDAIVPESKLTDPQ 71
Cdd:COG1146     2 MPVIDTDKCIGCGACVEVCPVDVLELDEEGK-----KALVINPEECIGCGACELVCPVGAITVEDDEPEEQ 67
 
Name Accession Description Interval E-value
PLN02852 PLN02852
ferredoxin-NADP+ reductase
 102-560 9.85e-154

ferredoxin-NADP+ reductase


Pssm-ID: 215457  Cd Length: 491  Bit Score: 449.92  E-value: 9.85e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 102 KGRPPLRVAIVGSGPSAMYAADELLTQPD-VQVNVFDRLPVPYGLVRAGVAPDHQKTKQVTRLFDKIAAQKGFEFYLNVE 180
Cdd:PLN02852   22 STSEPLHVCVVGSGPAGFYTADKLLKAHDgARVDIIERLPTPFGLVRSGVAPDHPETKNVTNQFSRVATDDRVSFFGNVT 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 181 IGKHISHSELLENHHAVLYAVGASSDRGLGIPGADLPGTASATDFVAWYNGHPDHADDVFDL-SHRRAVIIGNGNVALDV 259
Cdd:PLN02852  102 LGRDVSLSELRDLYHVVVLAYGAESDRRLGIPGEDLPGVLSAREFVWWYNGHPDCVHLPPDLkSSDTAVVLGQGNVALDC 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 260 ARILTADPEKLAGTDISAHALAALRKSRVEEVVIVGRRGIAQSAFTVPEFTGLMALPDIELSVGPDDMVLDSAtEELAKR 339
Cdd:PLN02852  182 ARILLRPTDELASTDIAEHALEALRGSSVRKVYLVGRRGPVQAACTAKELRELLGLKNVRVRIKEADLTLSPE-DEEELK 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 340 GELPHAVEQKLRLLEALKNRDHVDVGNKRITLRYLLTPTSI----TGDDQVSGIAFARNALVDANGTVQIEA--TGDTET 413
Cdd:PLN02852  261 ASRPKRRVYELLSKAAAAGKCAPSGGQRELHFVFFRNPTRFldsgDGNGHVAGVKLERTVLEGAAGSGKQVAvgTGEFED 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 414 IDTGLVLTSIGYRGVPIPGVPFDERASVIPNENGRVLEAPNG-DPATGVYATGWIKRGPSGFIGTNKSCAQETIRMLVDD 492
Cdd:PLN02852  341 LPCGLVLKSIGYKSLPVDGLPFDHKRGVVPNVHGRVLSSASGaDTEPGLYVVGWLKRGPTGIIGTNLTCAEETVASIAED 420

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020379483 493 FNDGRLTN----PVADDSAVDRLVRARQSDVVDREGWHAIDKAELERGAAHDRAREKVldqVEITSILDAAA 560
Cdd:PLN02852  421 LEQGRLRGvaspPKPGRDGLLELLESRGVRVVPFSGWEKIDSAEKEAGRARGKPREKI---TSIEEMLKAAN 489
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 10-472 1.96e-51

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: 182.26  E-value: 1.96e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483  10 CSDASCVYACPVNCihptpDEPDFLT----------AEMLHID---PQAC--VdCGA-CVSACpVDAIVPESkltdpqrv 73
Cdd:COG0493    27 CGDPPCQTGCPVGN-----DIPEWIRliaegdyeeaLELIHETnpfPEVCgrV-CPApCEGAC-VRGIVDEP-------- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483  74 fLSIN------ADFYKEERPRPLLakvIPAAHVDKgrpplRVAIVGSGPSAMYAADELLTQpDVQVNVFDRLPVPYGLVR 147
Cdd:COG0493    92 -VAIGalerfiADKAFEEGWVKPP---PPAPRTGK-----KVAVVGSGPAGLAAAYQLARA-GHEVTVFEALDKPGGLLR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 148 AGVaPDHQKTKQVTRLFDKIAAQKGFEFYLNVEIGKHISHSELLENHHAVLYAVGASSDRGLGIPGADLPGTASATDFVA 227
Cdd:COG0493   162 YGI-PEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGAGKPRDLGIPGEDLKGVHSAMDFLT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 228 WYNGHpdHADDVFDLSHRRAVIIGNGNVALDVARiltadpeklagtdiSAHALAAlrksrvEEVVIVGRRGIAQSAFTVP 307
Cdd:COG0493   241 AVNLG--EAPDTILAVGKRVVVIGGGNTAMDCAR--------------TALRLGA------ESVTIVYRRTREEMPASKE 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 308 EftglmalpdielsvgpddmvLDSATEElakrGelphaveqklrllealknrdhvdvgnkrITLRYLLTPTSITGDD--Q 385
Cdd:COG0493   299 E--------------------VEEALEE----G----------------------------VEFLFLVAPVEIIGDEngR 326

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 386 VSGIAFARNALV--DANGTVQ-IEATGDTETIDTGLVLTSIGYRGVPI-----PGVPFDERasvipnenGRVlEAPNGDP 457
Cdd:COG0493   327 VTGLECVRMELGepDESGRRRpVPIEGSEFTLPADLVILAIGQTPDPSgleeeLGLELDKR--------GTI-VVDEETY 397

                         490
                  ....*....|....*...
gi 2020379483 458 AT---GVYATGWIKRGPS 472
Cdd:COG0493   398 QTslpGVFAGGDAVRGPS 415
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 1-71 7.20e-19

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 80.91  E-value: 7.20e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2020379483   1 MPHVVTQSCCSDASCVYACPVNCIHPTPDEPdfltaEMLHIDPQACVDCGACVSACPVDAIVPESKLTDPQ 71
Cdd:COG1146     2 MPVIDTDKCIGCGACVEVCPVDVLELDEEGK-----KALVINPEECIGCGACELVCPVGAITVEDDEPEEQ 67
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 8-62 2.66e-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: 64.33  E-value: 2.66e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2020379483   8 SC--CSDASCVYACPVNCIHPTPDEpdfltaeMLHIDPQACVDCGACVSACPVDAIV 62
Cdd:cd04410    49 SCmhCEDPPCVKACPTGAIYKDEDG-------IVLIDEDKCIGCGSCVEACPYGAIV 98
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 15-60 2.25e-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: 53.30  E-value: 2.25e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2020379483  15 CVYACPVNCIHPTPDEPDFLTAEMlHIDPQACVDCGACVSACPVDA 60
Cdd:pfam12838   7 CVAACPVGAITLDEVGEKKGTKTV-VIDPERCVGCGACVAVCPTGA 51
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
8-78 3.04e-07

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 52.24  E-value: 3.04e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020379483   8 SCCSDASCVYACPVNCIHPTPDEPdfltaemlHIDPQACVDCGACVSACP--VDAIVPESkltdpQRVFLSIN 78
Cdd:PRK07118  140 GCLGLGSCVAACPFDAIHIENGLP--------VVDEDKCTGCGACVKACPrnVIELIPKS-----ARVFVACN 199
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 108-465 1.74e-05

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 46.93  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 108 RVAIVGSGPSAMYAADElLTQPDVQVNVFDR-------LPVPYGLVRAGVAPDH----------QKTKQVTRLfdkiaaQ 170
Cdd:pfam07992   2 DVVVIGGGPAGLAAALT-LAQLGGKVTLIEDegtcpygGCVLSKALLGAAEAPEiaslwadlykRKEEVVKKL------N 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 171 KGFEFYLNVE-----------IGKHISHSELLE-NHHAVLYAVGASSdRGLGIPGADLPGTASATDFvawynghpDHADD 238
Cdd:pfam07992  75 NGIEVLLGTEvvsidpgakkvVLEELVDGDGETiTYDRLVIATGARP-RLPPIPGVELNVGFLVRTL--------DSAEA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 239 VF-DLSHRRAVIIGNGNVALDVAriltadpeklagtdISAHALAAlrksrveEVVIVGRRGIAQSAFtvpeftglmalpD 317
Cdd:pfam07992 146 LRlKLLPKRVVVVGGGYIGVELA--------------AALAKLGK-------EVTLIEALDRLLRAF------------D 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 318 IELSvgpddmvlDSATEELAKRGelphaveqklrllealknrdhVDVgnkritlrylLTPTSITGddqvsgiafarnalV 397
Cdd:pfam07992 193 EEIS--------AALEKALEKNG---------------------VEV----------RLGTSVKE--------------I 219

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020379483 398 DANGTVQIEATGDTETIDTGLVLTSIGYRGVPIP----GVPFDERASVIPNENGRVleapngdPATGVYATG 465
Cdd:pfam07992 220 IGDGDGVEVILKDGTEIDADLVVVAIGRRPNTELleaaGLELDERGGIVVDEYLRT-------SVPGIYAAG 284
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 41-62 1.39e-04

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: 42.86  E-value: 1.39e-04
                          10        20
                  ....*....|....*....|..
gi 2020379483  41 IDPQACVDCGACVSACPVDAIV 62
Cdd:TIGR01944 110 IDEDNCIGCTKCIQACPVDAIV 131
 
Name Accession Description Interval E-value
PLN02852 PLN02852
ferredoxin-NADP+ reductase
 102-560 9.85e-154

ferredoxin-NADP+ reductase


Pssm-ID: 215457  Cd Length: 491  Bit Score: 449.92  E-value: 9.85e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 102 KGRPPLRVAIVGSGPSAMYAADELLTQPD-VQVNVFDRLPVPYGLVRAGVAPDHQKTKQVTRLFDKIAAQKGFEFYLNVE 180
Cdd:PLN02852   22 STSEPLHVCVVGSGPAGFYTADKLLKAHDgARVDIIERLPTPFGLVRSGVAPDHPETKNVTNQFSRVATDDRVSFFGNVT 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 181 IGKHISHSELLENHHAVLYAVGASSDRGLGIPGADLPGTASATDFVAWYNGHPDHADDVFDL-SHRRAVIIGNGNVALDV 259
Cdd:PLN02852  102 LGRDVSLSELRDLYHVVVLAYGAESDRRLGIPGEDLPGVLSAREFVWWYNGHPDCVHLPPDLkSSDTAVVLGQGNVALDC 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 260 ARILTADPEKLAGTDISAHALAALRKSRVEEVVIVGRRGIAQSAFTVPEFTGLMALPDIELSVGPDDMVLDSAtEELAKR 339
Cdd:PLN02852  182 ARILLRPTDELASTDIAEHALEALRGSSVRKVYLVGRRGPVQAACTAKELRELLGLKNVRVRIKEADLTLSPE-DEEELK 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 340 GELPHAVEQKLRLLEALKNRDHVDVGNKRITLRYLLTPTSI----TGDDQVSGIAFARNALVDANGTVQIEA--TGDTET 413
Cdd:PLN02852  261 ASRPKRRVYELLSKAAAAGKCAPSGGQRELHFVFFRNPTRFldsgDGNGHVAGVKLERTVLEGAAGSGKQVAvgTGEFED 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 414 IDTGLVLTSIGYRGVPIPGVPFDERASVIPNENGRVLEAPNG-DPATGVYATGWIKRGPSGFIGTNKSCAQETIRMLVDD 492
Cdd:PLN02852  341 LPCGLVLKSIGYKSLPVDGLPFDHKRGVVPNVHGRVLSSASGaDTEPGLYVVGWLKRGPTGIIGTNLTCAEETVASIAED 420

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020379483 493 FNDGRLTN----PVADDSAVDRLVRARQSDVVDREGWHAIDKAELERGAAHDRAREKVldqVEITSILDAAA 560
Cdd:PLN02852  421 LEQGRLRGvaspPKPGRDGLLELLESRGVRVVPFSGWEKIDSAEKEAGRARGKPREKI---TSIEEMLKAAN 489
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 10-472 1.96e-51

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: 182.26  E-value: 1.96e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483  10 CSDASCVYACPVNCihptpDEPDFLT----------AEMLHID---PQAC--VdCGA-CVSACpVDAIVPESkltdpqrv 73
Cdd:COG0493    27 CGDPPCQTGCPVGN-----DIPEWIRliaegdyeeaLELIHETnpfPEVCgrV-CPApCEGAC-VRGIVDEP-------- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483  74 fLSIN------ADFYKEERPRPLLakvIPAAHVDKgrpplRVAIVGSGPSAMYAADELLTQpDVQVNVFDRLPVPYGLVR 147
Cdd:COG0493    92 -VAIGalerfiADKAFEEGWVKPP---PPAPRTGK-----KVAVVGSGPAGLAAAYQLARA-GHEVTVFEALDKPGGLLR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 148 AGVaPDHQKTKQVTRLFDKIAAQKGFEFYLNVEIGKHISHSELLENHHAVLYAVGASSDRGLGIPGADLPGTASATDFVA 227
Cdd:COG0493   162 YGI-PEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGAGKPRDLGIPGEDLKGVHSAMDFLT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 228 WYNGHpdHADDVFDLSHRRAVIIGNGNVALDVARiltadpeklagtdiSAHALAAlrksrvEEVVIVGRRGIAQSAFTVP 307
Cdd:COG0493   241 AVNLG--EAPDTILAVGKRVVVIGGGNTAMDCAR--------------TALRLGA------ESVTIVYRRTREEMPASKE 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 308 EftglmalpdielsvgpddmvLDSATEElakrGelphaveqklrllealknrdhvdvgnkrITLRYLLTPTSITGDD--Q 385
Cdd:COG0493   299 E--------------------VEEALEE----G----------------------------VEFLFLVAPVEIIGDEngR 326

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 386 VSGIAFARNALV--DANGTVQ-IEATGDTETIDTGLVLTSIGYRGVPI-----PGVPFDERasvipnenGRVlEAPNGDP 457
Cdd:COG0493   327 VTGLECVRMELGepDESGRRRpVPIEGSEFTLPADLVILAIGQTPDPSgleeeLGLELDKR--------GTI-VVDEETY 397

                         490
                  ....*....|....*...
gi 2020379483 458 AT---GVYATGWIKRGPS 472
Cdd:COG0493   398 QTslpGVFAGGDAVRGPS 415
PTZ00188 PTZ00188
adrenodoxin reductase; Provisional
 106-556 1.67e-43

adrenodoxin reductase; Provisional


Pssm-ID: 240308  Cd Length: 506  Bit Score: 162.36  E-value: 1.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 106 PLRVAIVGSGPSAMYAADELLTQPDVQVNVFDRLPVPYGLVRAGVAPDHQKTKQVTRLFDKIAAQKGFEFYLNVEIGKHI 185
Cdd:PTZ00188   39 PFKVGIIGAGPSALYCCKHLLKHERVKVDIFEKLPNPYGLIRYGVAPDHIHVKNTYKTFDPVFLSPNYRFFGNVHVGVDL 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 186 SHSELLENHHAVLYAVGAS---------SDRGLGIPGADLP----GTASATDFVAWYNGHPD----HADDVFDLSHRR-- 246
Cdd:PTZ00188  119 KMEELRNHYNCVIFCCGASevsipigqqDEDKAVSGGETNPrkqnGIFHARDLIYFYNNMYNdvrcKAVDNYLNSFENft 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 247 -AVIIGNGNVALDVARILTADPEKLAGTDISAHALAALRKSRVEEVVIVGRRGIAQSAFTVPEFTGLMALPDIELSVGPD 325
Cdd:PTZ00188  199 tSIIIGNGNVSLDIARILIKSPDDLSKTDISSDYLKVIKRHNIKHIYIVGRRGFWQSSFTNAELRELISLENTKVILSKK 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 326 DMVL------DSATEELAKRgelPHAVEQKLrlleaLKNRDHVDvGNKRITLRYLLTPTSITGD-DQVSGIAFA-RNALV 397
Cdd:PTZ00188  279 NYDLcchlksDEENTNMKKR---QHEIFQKM-----VKNYEEVE-KNKEFYKTYKIIEFIFYFEiRQIRPIDGAmKNVEL 349

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 398 DANGTVQIEATGDTE--TIDTGLVLTSIGYRGvpipgvpfDERASVIPNENGRVLEAPNGDPATGVYATGWIKRGPSGFI 475
Cdd:PTZ00188  350 ELNKNVPMSFSSFKEnkVLVTPLVIFATGFKK--------SNFAENLYNQSVQMFKEDIGQHKFAIFKAGWFDKGPKGNI 421

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 476 GTNKSCAQETIRMLVDDFNdgrlTNPVADDSAVDRLVRARQSDVVDREGWHAIDKAELERGAAHDRAREKVLDQVEITSI 555
Cdd:PTZ00188  422 ASQILNSKNSTHLVLNFLQ----KVDIFFDNDISSLLKEKQIPYVSFDDWTYLHQLEKQMGAQQNKIAQKFSQTGEVLRI 497


                  .
gi 2020379483 556 L 556
Cdd:PTZ00188  498 L 498
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 108-470 1.47e-35

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 138.77  E-value: 1.47e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 108 RVAIVGSGPSAMYAADELlTQPDVQVNVFDRLPVPYGLVRAGVA----PDHQKTKQVTRLfdkiaAQKGFEFYLNVEIGK 183
Cdd:PRK11749  142 KVAVIGAGPAGLTAAHRL-ARKGYDVTIFEARDKAGGLLRYGIPefrlPKDIVDREVERL-----LKLGVEIRTNTEVGR 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 184 HISHSELLENHHAVLYAVGASSDRGLGIPGADLPGTASATDFVAwyngHPDHADDVFDLSH-RRAVIIGNGNVALDVARI 262
Cdd:PRK11749  216 DITLDELRAGYDAVFIGTGAGLPRFLGIPGENLGGVYSAVDFLT----RVNQAVADYDLPVgKRVVVIGGGNTAMDAART 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 263 ltadpeklagtdisahalaALRKSrVEEVVIVGRRGIAqsaftvpeftglmalpdielsvgpdDMvldSATEElakrgEL 342
Cdd:PRK11749  292 -------------------AKRLG-AESVTIVYRRGRE-------------------------EM---PASEE-----EV 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 343 PHAVEQKlrllealknrdhvdvgnkrITLRYLLTPTSITGDDQ-VSGIAFARNALV--DANGTVQIEATGDTETIDTGLV 419
Cdd:PRK11749  319 EHAKEEG-------------------VEFEWLAAPVEILGDEGrVTGVEFVRMELGepDASGRRRVPIEGSEFTLPADLV 379

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2020379483 420 LTSIGYRgvPIPGVPFDERASVIPNENGRVLEAPNGdpAT---GVYATGWIKRG 470
Cdd:PRK11749  380 IKAIGQT--PNPLILSTTPGLELNRWGTIIADDETG--RTslpGVFAGGDIVTG 429
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 44-472 1.37e-28

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 119.11  E-value: 1.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483  44 QA--CVDCGA--CVSACPVDAIVPE-SKLTDPQRVF-----------------------------LSINAD--------- 80
Cdd:PRK12810   42 QAarCMDCGIpfCHWGCPVHNYIPEwNDLVYRGRWEeaaerlhqtnnfpeftgrvcpapcegactLNINFGpvtiknier 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483  81 -----FYKEERPRPLlakvIPAAHVDKgrpplRVAIVGSGPSAMYAADELlTQPDVQVNVFDRLPVPYGLVRAGVaPDHQ 155
Cdd:PRK12810  122 yiidkAFEEGWVKPD----PPVKRTGK-----KVAVVGSGPAGLAAADQL-ARAGHKVTVFERADRIGGLLRYGI-PDFK 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 156 KTKQV--TRLfdKIAAQKGFEFYLNVEIGKHISHSELLENHHAVLYAVGASSDRGLGIPGADLPGTASATDFVAWYNGH- 232
Cdd:PRK12810  191 LEKEVidRRI--ELMEAEGIEFRTNVEVGKDITAEELLAEYDAVFLGTGAYKPRDLGIPGRDLDGVHFAMDFLIQNTRRv 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 233 -PDHADDVFDLSHRRAVIIGNGNVALDVARiltadpeklagtdiSAHALAAlrksrvEEVVivgRRGIA-QSAFTVPEFT 310
Cdd:PRK12810  269 lGDETEPFISAKGKHVVVIGGGDTGMDCVG--------------TAIRQGA------KSVT---QRDIMpMPPSRRNKNN 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 311 GLMALPDIelsvgpddMVLDSATEELAKRgelphaveqklrllealknrdhvdvgnkritlRYLLTPTSITGDD-QVSGI 389
Cdd:PRK12810  326 PWPYWPMK--------LEVSNAHEEGVER--------------------------------EFNVQTKEFEGENgKVTGV 365

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 390 AFARNALVDANGTvqiEATGDTETIDTGLVLTSIGYRGVPIP-----GVPFDERasvipnenGRVlEAPNGDPAT---GV 461
Cdd:PRK12810  366 KVVRTELGEGDFE---PVEGSEFVLPADLVLLAMGFTGPEAGllaqfGVELDER--------GRV-AAPDNAYQTsnpKV 433

                         490
                  ....*....|.
gi 2020379483 462 YATGWIKRGPS 472
Cdd:PRK12810  434 FAAGDMRRGQS 444
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
 102-477 1.75e-28

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 116.63  E-value: 1.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 102 KGRPPLRVAIVGSGPSAMYAADELLTQpDVQVNVFDRLPVPYGLVRAGVaPDHQKTKQVTRLFDKIAAQKGFEFYLNVEI 181
Cdd:PRK12770   14 PPPTGKKVAIIGAGPAGLAAAGYLACL-GYEVHVYDKLPEPGGLMLFGI-PEFRIPIERVREGVKELEEAGVVFHTRTKV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 182 ---------------GKHISHSELLENHHAVLYAVGASSDRGLGIPGADLPGTASATDFV----AWYNGHPDHaDDVFDL 242
Cdd:PRK12770   92 ccgeplheeegdefvERIVSLEELVKKYDAVLIATGTWKSRKLGIPGEDLPGVYSALEYLfrirAAKLGYLPW-EKVPPV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 243 SHRRAVIIGNGNVALDVAriltadpeklagtdISAHALAAlrksrvEEVVIVGRRGIAQSAFTVPEFtglmalpdielsv 322
Cdd:PRK12770  171 EGKKVVVVGAGLTAVDAA--------------LEAVLLGA------EKVYLAYRRTINEAPAGKYEI------------- 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 323 gpddmvldsatEELAKRGelphaveqklrllealknrdhvdvgnkrITLRYLLTPTSITGDDQVSGIAFARNALVDANGT 402
Cdd:PRK12770  218 -----------ERLIARG----------------------------VEFLELVTPVRIIGEGRVEGVELAKMRLGEPDES 258

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 403 VQ---IEATGDTETIDTGLVLTSIGYrgVPIP-------GVPFDERASVIPNENGRVLEApngdpatGVYATGWIKRGPS 472
Cdd:PRK12770  259 GRprpVPIPGSEFVLEADTVVFAIGE--IPTPpfakeclGIELNRKGEIVVDEKHMTSRE-------GVFAAGDVVTGPS 329


                  ....*
gi 2020379483 473 gFIGT 477
Cdd:PRK12770  330 -KIGK 333
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 9-261 1.01e-21

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 99.33  E-value: 1.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483   9 CCSDASCVYACPV-NCIhptpdePDFL----------TAEMLHIDPQACVDCGacvSACPVDAIVPESKLTDPQRVFLSI 77
Cdd:PRK12809  213 CAEKANCNWHCPLhNAI------PDYIrlvqegkiieAAELCHQTSSLPEICG---RVCPQDRLCEGACTLKDHSGAVSI 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483  78 -NADFYKEERP-----RPLLAKVIPAAHvdkgrpplRVAIVGSGPSAMYAADeLLTQPDVQVNVFDRLPVPYGLVRAGVA 151
Cdd:PRK12809  284 gNLERYITDTAlamgwRPDVSKVVPRSE--------KVAVIGAGPAGLGCAD-ILARAGVQVDVFDRHPEIGGMLTFGIP 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 152 PdHQKTKQVTRLFDKIAAQKGFEFYLNVEIGKHISHSELLENHHAVLYAVGASSDRGLGIPGADLPGTASATDFVAWYN- 230
Cdd:PRK12809  355 P-FKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVFIGVGTYGMMRADLPHEDAPGVIQALPFLTAHTr 433

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2020379483 231 ---GHPDHAD-DVFDLSHRRAVIIGNGNVALDVAR 261
Cdd:PRK12809  434 qlmGLPESEEyPLTDVEGKRVVVLGGGDTTMDCLR 468
PRK12831 PRK12831
putative oxidoreductase; Provisional
 102-483 3.01e-20

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 93.93  E-value: 3.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 102 KGRPPLRVAIVGSGPSAMYAADELLTQpDVQVNVFDRLPVPYGLVRAGVaPDHQ--KTKQVTRLFDKIAAQkGFEFYLNV 179
Cdd:PRK12831  136 EEKKGKKVAVIGSGPAGLTCAGDLAKM-GYDVTIFEALHEPGGVLVYGI-PEFRlpKETVVKKEIENIKKL-GVKIETNV 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 180 EIGKHISHSELLENHH--AVLYAVGASSDRGLGIPGADLPGTASATDFVAWYNGHPDHADDvFD---LSHRRAVIIGNGN 254
Cdd:PRK12831  213 VVGKTVTIDELLEEEGfdAVFIGSGAGLPKFMGIPGENLNGVFSANEFLTRVNLMKAYKPE-YDtpiKVGKKVAVVGGGN 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 255 VALDVARiltadpeklagtdiSAHALAAlrksrveEVVIVGRRGiaqsaftvpeftglmalpdielsvgpddmvldsaTE 334
Cdd:PRK12831  292 VAMDAAR--------------TALRLGA-------EVHIVYRRS----------------------------------EE 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 335 EL-AKRGELPHAVEQKlrllealknrdhvdvgnkrITLRYLLTPTSITGDDQ--VSGIAFARNAL--VDANGTVQ-IEAT 408
Cdd:PRK12831  317 ELpARVEEVHHAKEEG-------------------VIFDLLTNPVEILGDENgwVKGMKCIKMELgePDASGRRRpVEIE 377

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 409 GDTETIDTGLVLTSIGYRGVPI-----PGVPFDERASVIPNENGRVLEAPngdpatGVYATGWIKRGPSGFI---GTNKS 480
Cdd:PRK12831  378 GSEFVLEVDTVIMSLGTSPNPLissttKGLKINKRGCIVADEETGLTSKE------GVFAGGDAVTGAATVIlamGAGKK 451


                  ...
gi 2020379483 481 CAQ 483
Cdd:PRK12831  452 AAK 454
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 96-297 7.02e-20

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 93.40  E-value: 7.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483  96 PAAHVDKGRpplRVAIVGSGPSAMYAAdELLTQPDVQVNVFDRLPVPYGLVRAGVaPDHQKTKQVtrLFDKIAA--QKGF 173
Cdd:PRK12771  130 PAPAPDTGK---RVAVIGGGPAGLSAA-YHLRRMGHAVTIFEAGPKLGGMMRYGI-PAYRLPREV--LDAEIQRilDLGV 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 174 EFYLNVEIGKHISHSELLENHHAVLYAVGASSDRGLGIPGADLPGTASATDFVAWYN-GHPDHaddvfdlSHRRAVIIGN 252
Cdd:PRK12771  203 EVRLGVRVGEDITLEQLEGEFDAVFVAIGAQLGKRLPIPGEDAAGVLDAVDFLRAVGeGEPPF-------LGKRVVVIGG 275

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2020379483 253 GNVALDVARiltadpeklagtdiSAHALAAlrksrvEEVVIVGRR 297
Cdd:PRK12771  276 GNTAMDAAR--------------TARRLGA------EEVTIVYRR 300
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 1-71 7.20e-19

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 80.91  E-value: 7.20e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2020379483   1 MPHVVTQSCCSDASCVYACPVNCIHPTPDEPdfltaEMLHIDPQACVDCGACVSACPVDAIVPESKLTDPQ 71
Cdd:COG1146     2 MPVIDTDKCIGCGACVEVCPVDVLELDEEGK-----KALVINPEECIGCGACELVCPVGAITVEDDEPEEQ 67
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 108-301 2.01e-17

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 85.94  E-value: 2.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 108 RVAIVGSGPSAMYAADELLTQPDvQVNVFDRLPVPYGLVRAGVA----PDHQKTKQVTRLfdkiaAQKGFEFYLNVEIGK 183
Cdd:PRK12814  195 KVAIIGAGPAGLTAAYYLLRKGH-DVTIFDANEQAGGMMRYGIPrfrlPESVIDADIAPL-----RAMGAEFRFNTVFGR 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 184 HISHSELLENHHAVLYAVGASSDRGLGIPGADLPGTASATDFVAwynghpDHADDVFDLSHRRAVIIGNGNVALDVARil 263
Cdd:PRK12814  269 DITLEELQKEFDAVLLAVGAQKASKMGIPGEELPGVISGIDFLR------NVALGTALHPGKKVVVIGGGNTAIDAAR-- 340

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2020379483 264 tadpeklagtdiSAHALAAlrksrvEEVVIVGRRGIAQ 301
Cdd:PRK12814  341 ------------TALRLGA------ESVTILYRRTREE 360
PRK13984 PRK13984
putative oxidoreductase; Provisional
 108-261 8.36e-16

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 80.58  E-value: 8.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 108 RVAIVGSGPSAMYAADELLTQpDVQVNVFDRLPVPYGLVRAGVA----PDHQKTKQVtrlfDKIAAQkGFEFYLNVEIGK 183
Cdd:PRK13984  285 KVAIVGSGPAGLSAAYFLATM-GYEVTVYESLSKPGGVMRYGIPsyrlPDEALDKDI----AFIEAL-GVKIHLNTRVGK 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 184 HISHSELLENHHAVLYAVGASSDRGLGIPGADLPGTASA-------TDFVAWYNGHPDHAddvfdlshRRAVIIGNGNVA 256
Cdd:PRK13984  359 DIPLEELREKHDAVFLSTGFTLGRSTRIPGTDHPDVIQAlpllreiRDYLRGEGPKPKIP--------RSLVVIGGGNVA 430


                  ....*
gi 2020379483 257 LDVAR 261
Cdd:PRK13984  431 MDIAR 435
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 88-261 1.45e-15

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 79.79  E-value: 1.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483  88 RPLLAKVIPaahVDKgrpplRVAIVGSGPSAMYAADeLLTQPDVQVNVFDRLPVPYGLVRAGVaPDHQKTKQVTRLFDKI 167
Cdd:PRK12769  317 RPDLSQVTK---SDK-----RVAIIGAGPAGLACAD-VLARNGVAVTVYDRHPEIGGLLTFGI-PAFKLDKSLLARRREI 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 168 AAQKGFEFYLNVEIGKHISHSELLENHHAVLYAVGASSDRGLGIPGADLPGTASATDFVAWYNGH----PDHADDVF-DL 242
Cdd:PRK12769  387 FSAMGIEFELNCEVGKDISLESLLEDYDAVFVGVGTYRSMKAGLPNEDAPGVYDALPFLIANTKQvmglEELPEEPFiNT 466

                         170
                  ....*....|....*....
gi 2020379483 243 SHRRAVIIGNGNVALDVAR 261
Cdd:PRK12769  467 AGLNVVVLGGGDTAMDCVR 485
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 34-483 6.01e-15

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 78.25  E-value: 6.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483  34 LTAEMLHIDPQACVDCG--ACVSACPVDAIVPESKLTDPQRVFLSiNADFYKEERPRP-LLAKVIP--------AAHVDK 102
Cdd:PRK12778  319 LTKEQAMTEAKRCLDCKnpGCVEGCPVGIDIPRFIKNIERGNFLE-AAKILKETSALPaVCGRVCPqekqceskCIHGKM 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 103 GRPPL------------------------------RVAIVGSGPSAMYAADELLTQpDVQVNVFDRLPVPYGLVRAGVaP 152
Cdd:PRK12778  398 GEEAVaigylerfvadyeresgnisvpevaekngkKVAVIGSGPAGLSFAGDLAKR-GYDVTVFEALHEIGGVLKYGI-P 475

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 153 DHQKTKQVTRLFDKIAAQKGFEFYLNVEIGKHISHSELL-ENHHAVLYAVGASSDRGLGIPGADLPGTASATDFVAWYN- 230
Cdd:PRK12778  476 EFRLPKKIVDVEIENLKKLGVKFETDVIVGKTITIEELEeEGFKGIFIASGAGLPNFMNIPGENSNGVMSSNEYLTRVNl 555

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 231 ---GHPDHADDVfdLSHRRAVIIGNGNVALDVARiltadpeklagtdiSAHALAAlrksrvEEVVIVGRRgiaqsaftvp 307
Cdd:PRK12778  556 mdaASPDSDTPI--KFGKKVAVVGGGNTAMDSAR--------------TAKRLGA------ERVTIVYRR---------- 603

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 308 eftglmalpdielsvgpddmvldSATEELAKRGELPHAVEQKLRLLealknrdhvdvgnkritlrYLLTPTSITGDDQ-- 385
Cdd:PRK12778  604 -----------------------SEEEMPARLEEVKHAKEEGIEFL-------------------TLHNPIEYLADEKgw 641

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 386 VSGIAFARNAL--VDANGTVQ-IEATGDTETIDTGLVLTSIGYRGVP-----IPGVPFDERASVIPNENGRVLEApngdp 457
Cdd:PRK12778  642 VKQVVLQKMELgePDASGRRRpVAIPGSTFTVDVDLVIVSVGVSPNPlvpssIPGLELNRKGTIVVDEEMQSSIP----- 716

                         490       500
                  ....*....|....*....|....*....
gi 2020379483 458 atGVYATGWIKRGPSGFI---GTNKSCAQ 483
Cdd:PRK12778  717 --GIYAGGDIVRGGATVIlamGDGKRAAA 743
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 9-62 4.98e-14

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: 67.08  E-value: 4.98e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2020379483   9 CCSDASCVYACPVNCIHPTPDEPDFltaeMLHIDPQACVDCGACVSACPVDAIV 62
Cdd:COG1143     4 CIGCGLCVRVCPVDAITIEDGEPGK----VYVIDPDKCIGCGLCVEVCPTGAIS 53
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
1-69 1.33e-13

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 65.91  E-value: 1.33e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020379483   1 MPHVVTQSCCSDASCVYACPVNCIHptpdepdfLTAEMLHIDPQACVDCGACVSACPVDAIVPESKLTD 69
Cdd:COG2768     5 KPYVDEEKCIGCGACVKVCPVGAIS--------IEDGKAVIDPEKCIGCGACIEVCPVGAIKIEWEEDE 65
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 1-64 3.96e-13

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 64.68  E-value: 3.96e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020379483   1 MPHVV-TQSCCSDASCVYACPVNCIHPTPDepdfltaeMLHIDPQACVDCGACVSACPVDAIVPE 64
Cdd:COG4231    15 MRYVIdEDKCTGCGACVKVCPADAIEEGDG--------KAVIDPDLCIGCGSCVQVCPVDAIKLE 71
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 8-62 2.66e-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: 64.33  E-value: 2.66e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2020379483   8 SC--CSDASCVYACPVNCIHPTPDEpdfltaeMLHIDPQACVDCGACVSACPVDAIV 62
Cdd:cd04410    49 SCmhCEDPPCVKACPTGAIYKDEDG-------IVLIDEDKCIGCGSCVEACPYGAIV 98
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 15-80 3.44e-12

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: 63.57  E-value: 3.44e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020379483  15 CVYACPVNCIHPTPDEPdflTAEMLHIDPQACVDCGACVSACPVDAI--VPESKLTDPQRVFLSINAD 80
Cdd:cd10549    14 CVKACPTDAIELGPNGA---IARGPEIDEDKCVFCGACVEVCPTGAIelTPEGKEYVPKEKEAEIDEE 78
PRK12779 PRK12779
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ...
 89-523 9.91e-12

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


Pssm-ID: 183740 [Multi-domain]  Cd Length: 944  Bit Score: 67.93  E-value: 9.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483  89 PLLAKVIPAAHVDKgrPPlrVAIVGSGPSAMYAAdELLTQPDVQVNVFDRLPVPYGLVRAGVAPDHQKTKQVTRLFDKIA 168
Cdd:PRK12779  293 RFAGRISPWAAAVK--PP--IAVVGSGPSGLINA-YLLAVEGFPVTVFEAFHDLGGVLRYGIPEFRLPNQLIDDVVEKIK 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 169 AQKGfEFYLNVEIGKHISHSEL-LENHHAVLYAVGASSDRGLGIPGADLPGTASATDFVAWYN----GHPDHADDVFDLS 243
Cdd:PRK12779  368 LLGG-RFVKNFVVGKTATLEDLkAAGFWKIFVGTGAGLPTFMNVPGEHLLGVMSANEFLTRVNlmrgLDDDYETPLPEVK 446

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 244 HRRAVIIGNGNVALDVARilTAdpEKLAGTdisahalaalrksrveeVVIVGRRGIAQsaftvpeftglmaLPdielsvg 323
Cdd:PRK12779  447 GKEVFVIGGGNTAMDAAR--TA--KRLGGN-----------------VTIVYRRTKSE-------------MP------- 485

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 324 pddmvldsateelAKRGELPHAVEQKlrllealknrdhvdvgnkrITLRYLLTPTSITGDDQ---VSGIAFARNAL--VD 398
Cdd:PRK12779  486 -------------ARVEELHHALEEG-------------------INLAVLRAPREFIGDDHthfVTHALLDVNELgePD 533

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 399 ANGTVQIEATGDTETIDTGLVLTSIGYRGVPIPGvpfDERASVIPNENGrVLEAPNGDPAT---GVYATGWIKRGPSGFI 475
Cdd:PRK12779  534 KSGRRSPKPTGEIERVPVDLVIMALGNTANPIMK---DAEPGLKTNKWG-TIEVEKGSQRTsikGVYSGGDAARGGSTAI 609

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2020379483 476 ---GTNKSCAQETIRMLvdDFNDGRLTNPVADDSAVDRLVRARQSDVVDRE 523
Cdd:PRK12779  610 raaGDGQAAAKEIVGEI--PFTPAEIKDRVERAARYTELGQIPQTIVGKVQ 658
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 4-66 1.56e-11

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: 60.45  E-value: 1.56e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020379483   4 VVTQSCCSD-ASCVYACPVNCIHPTPDEpdfltaeMLHIDPQACVDCGACVSACPVDAI--VPESK 66
Cdd:COG1144    26 VVDEDKCIGcGLCWIVCPDGAIRVDDGK-------YYGIDYDYCKGCGICAEVCPVKAIemVPEEK 84
NapF COG1145
Ferredoxin [Energy production and conversion];
4-69 2.35e-11

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 63.97  E-value: 2.35e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020379483   4 VVTQSCCSDASCVYACPVNCIHPTPDEPdfltaeMLHIDPQACVDCGACVSACPVDAIVPESKLTD 69
Cdd:COG1145   179 IDAEKCIGCGLCVKVCPTGAIRLKDGKP------QIVVDPDKCIGCGACVKVCPVGAISLEPKEIE 238
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 15-68 1.19e-10

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: 59.33  E-value: 1.19e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2020379483  15 CVYACPVNCIHPTPDEPDFLTAEM-LHIDPQACVDCGACVSACPVDAIVPESKLT 68
Cdd:cd10549    48 CVEVCPTGAIELTPEGKEYVPKEKeAEIDEEKCIGCGLCVKVCPVDAITLEDELE 102
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 1-66 2.58e-10

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 56.27  E-value: 2.58e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020379483   1 MPHVVTQSCCSDASCVYACPVNCIHPTPDEPdfltaemLHIDPQACVDCGACVSACPVDAIVPESK 66
Cdd:COG1149     5 IPVIDEEKCIGCGLCVEVCPEGAIKLDDGGA-------PVVDPDLCTGCGACVGVCPTGAITLEER 63
PRK12775 PRK12775
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ...
 98-262 3.21e-10

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


Pssm-ID: 183738 [Multi-domain]  Cd Length: 1006  Bit Score: 63.04  E-value: 3.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483   98 AHVDKGRPPL------RVAIVGSGPSAMYAADElLTQPDVQVNVFDRLPVPYGLVRAGVAPDHQKTKQVTRLFDKIAAQk 171
Cdd:PRK12775   416 ARAKPVKPPRfskklgKVAICGSGPAGLAAAAD-LVKYGVDVTVYEALHVVGGVLQYGIPSFRLPRDIIDREVQRLVDI- 493

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483  172 GFEFYLNVEIGKHISHSELLEN--HHAVLYAVGASSDRGLGIPGADLPGTASATDFVAWYNghpDHADDVFDLSH----- 244
Cdd:PRK12775   494 GVKIETNKVIGKTFTVPQLMNDkgFDAVFLGVGAGAPTFLGIPGEFAGQVYSANEFLTRVN---LMGGDKFPFLDtpisl 570

                          170
                   ....*....|....*....
gi 2020379483  245 -RRAVIIGNGNVALDVARI 262
Cdd:PRK12775   571 gKSVVVIGAGNTAMDCLRV 589
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
10-66 8.57e-10

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 56.97  E-value: 8.57e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2020379483  10 CSDASCVYACPVNCIHPTPDEPdfltaemlHIDPQACVDCGACVSACPVDAIVPESK 66
Cdd:COG1142    55 CEDAPCAEVCPVGAITRDDGAV--------VVDEEKCIGCGLCVLACPFGAITMVGE 103
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 15-65 1.49e-09

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 54.29  E-value: 1.49e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2020379483  15 CVYACPVNCIHPTPDEpdfltaemLHIDPQACVDCGACVSACPVDAIVPES 65
Cdd:COG2221    23 CVAVCPTGAISLDDGK--------LVIDEEKCIGCGACIRVCPTGAIKGEK 65
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 15-60 2.25e-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: 53.30  E-value: 2.25e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2020379483  15 CVYACPVNCIHPTPDEPDFLTAEMlHIDPQACVDCGACVSACPVDA 60
Cdd:pfam12838   7 CVAACPVGAITLDEVGEKKGTKTV-VIDPERCVGCGACVAVCPTGA 51
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 5-61 6.81e-09

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 55.72  E-value: 6.81e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2020379483   5 VTQSC--CSDASCVYACPVNCIHPTPDEpdfltaeMLHIDPQACVDCGACVSACPVDAI 61
Cdd:COG0437    56 VPVLCnhCDDPPCVKVCPTGATYKREDG-------IVLVDYDKCIGCRYCVAACPYGAP 107
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 14-66 1.10e-08

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: 56.16  E-value: 1.10e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2020379483  14 SCVYACPVNCIHPTPDepdfltaeMLH-IDPQACVDCGACVSACPVDAI--VPESK 66
Cdd:COG2878   144 DCIKACPFDAIVGAAK--------GMHtVDEDKCTGCGLCVEACPVDCIemVPVSP 191
Fer4_9 pfam13187
4Fe-4S dicluster domain;
9-61 1.16e-08

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 51.40  E-value: 1.16e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2020379483   9 CCSDASCVYACPVNCIhpTPDEPDFLTAemLHIDPQACVDCGACVSACPVDAI 61
Cdd:pfam13187   2 CTGCGACVAACPAGAI--VPDLVGQTIR--GDIAGLACIGCGACVDACPRGAI 50
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 1-66 1.44e-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: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 53.35  E-value: 1.44e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020379483   1 MPHVVTQscCSDASCVYACPVNCIHPtpDEPDFltaeMLHIDPQACVDCGACVSACPVDAIV--PESK 66
Cdd:cd10550    45 VPVVCRQ--CEDAPCVEACPVGAISR--DEETG----AVVVDEDKCIGCGMCVEACPFGAIRvdPETG 104
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 9-62 2.93e-08

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: 52.40  E-value: 2.93e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2020379483   9 CCSDASCVYACPVNCIHptpdepdfLTAEMLH-IDPQACVDCGACVSACPVDAIV 62
Cdd:cd10549    80 CIGCGLCVKVCPVDAIT--------LEDELEIvIDKEKCIGCGICAEVCPVNAIK 126
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 15-66 4.67e-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: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 52.64  E-value: 4.67e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2020379483  15 CVYACPVNCIHPTPDEPDFLTAEMLHIDP--QACV-DCGACVSACPVDAIVPESK 66
Cdd:cd16373    22 CVEACPTGVIQPAGLEDGLEGGRTPYLDPreGPCDlCCDACVEVCPTGALRPLDL 76
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 7-61 5.15e-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: 52.69  E-value: 5.15e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2020379483   7 QSC--CSDASCVYACPVNCIHPTpdepdflTAEMLHIDPQACVDCGACVSACPVDAI 61
Cdd:cd10562    68 RQCmhCTDAACVKVCPTGALYKT-------ENGAVVVDEDKCIGCGYCVAACPFDVP 117
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 10-61 1.04e-07

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: 51.63  E-value: 1.04e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2020379483  10 CSDASCVYACPVNCIHPTPDEpdfltaeMLHIDPQACVDCGACVSACPVDAI 61
Cdd:cd16366    73 CTDAGCLAACPTGAIIRTETG-------TVVVDPETCIGCGYCVNACPFDIP 117
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
8-78 3.04e-07

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 52.24  E-value: 3.04e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020379483   8 SCCSDASCVYACPVNCIHPTPDEPdfltaemlHIDPQACVDCGACVSACP--VDAIVPESkltdpQRVFLSIN 78
Cdd:PRK07118  140 GCLGLGSCVAACPFDAIHIENGLP--------VVDEDKCTGCGACVKACPrnVIELIPKS-----ARVFVACN 199
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 8-66 6.25e-07

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


Pssm-ID: 319885 [Multi-domain]  Cd Length: 140  Bit Score: 48.79  E-value: 6.25e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2020379483   8 SC--CSDASCVYACPVNCIHPTPdepdfLTAEMLHiDPQACVDCGACVSACPVDAIVPESK 66
Cdd:cd10563    56 QCrhCDEPPCVKACMSGAMHKDP-----ETGIVIH-DEEKCVGCWMCVMVCPYGAIRPDKE 110
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 5-61 7.52e-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: 7.52e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2020379483   5 VTQSC--CSDASCVYACPVNCIHPTPDEPDFltaemlhIDPqACVDCGACVSACPVDAI 61
Cdd:cd16367    53 VPTACrhCVDPVCMIGCPTGAIHRDDGGEVV-------ISD-ACCGCGNCASACPYGAI 103
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
3-77 7.58e-07

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 51.95  E-value: 7.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483   3 HVVTQSCCSDA-SCVYACPVNCIHPTpdepdfltAEMLHIDPQACVDCGACVSACPVDAIVPES-------KLTDPQRVF 74
Cdd:COG4624    86 IIRDKEKCKNCyPCVRACPVKAIKVD--------DGKAEIDEEKCISCGQCVAVCPFGAITEKSdiekvkkALKDPEKVV 157


                  ...
gi 2020379483  75 LSI 77
Cdd:COG4624   158 AQV 160
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 14-61 1.20e-06

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: 48.01  E-value: 1.20e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2020379483  14 SCVYACPVNCIH--PTPDEPdfltaEMLHIDPQACVDCGACVSACPVDAI 61
Cdd:cd10564    90 SCQDACPTQAIRfrPRLGGI-----ALPELDADACTGCGACVSVCPVGAI 134
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 41-61 1.30e-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: 44.93  E-value: 1.30e-06
                          10        20
                  ....*....|....*....|.
gi 2020379483  41 IDPQACVDCGACVSACPVDAI 61
Cdd:pfam00037   3 IDEEKCIGCGACVEVCPVGAI 23
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
46-90 1.37e-06

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 45.94  E-value: 1.37e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2020379483  46 CVDCGACVSACPVDAIVPESKLTDPQRVfLSINADFYKEERPRPL 90
Cdd:pfam13484   1 CGSCGKCIDACPTGAIVGPEGVLDARRC-ISYLTIEKKGLIPDEL 44
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
15-105 2.44e-06

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 47.57  E-value: 2.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483  15 CVYACPVNCI----HPTPD---EPDFLTaemlhIDPQACVDCGACVSACPVDAIV--PESKLTDPQRVFLsinadFYKEE 85
Cdd:PRK05888   66 CAAICPADAItieaAEREDgrrRTTRYD-----INFGRCIFCGFCEEACPTDAIVetPDFELATETREEL-----IYDKE 135

                          90       100
                  ....*....|....*....|
gi 2020379483  86 RPRPLLAKVIPAAHVDKGRP 105
Cdd:PRK05888  136 KLLANGDRVEREIAPGKAAD 155
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 1-57 2.88e-06

4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 44.55  E-value: 2.88e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2020379483   1 MPHVVTQSCCSDASCVYACPVNCIHPTPDEPDFLtAEMLHIDPQACVDCGACVSACP 57
Cdd:pfam13237   1 KVVIDPDKCIGCGRCTAACPAGLTRVGAIVERLE-GEAVRIGVWKCIGCGACVEACP 56
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 41-66 3.47e-06

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 44.66  E-value: 3.47e-06
                          10        20
                  ....*....|....*....|....*.
gi 2020379483  41 IDPQACVDCGACVSACPVDAIVPESK 66
Cdd:COG2221    12 IDEEKCIGCGLCVAVCPTGAISLDDG 37
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 35-66 4.12e-06

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 44.65  E-value: 4.12e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2020379483  35 TAEMLHIDPQACVDCGACVSACPVDAIVPESK 66
Cdd:COG4231    13 TAMRYVIDEDKCTGCGACVKVCPADAIEEGDG 44
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 10-61 6.89e-06

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: 46.76  E-value: 6.89e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2020379483  10 CSDASCVYACPVNCIHPTPDEpdfltaeMLHIDPQACVDCGACVSACPVDAI 61
Cdd:cd10551    56 CENPPCVKVCPTGATYKREDG-------IVLVDYDKCIGCRYCMAACPYGAR 100
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 10-57 1.03e-05

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: 47.00  E-value: 1.03e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2020379483  10 CSDASCVYACPVNCIHPTPdepdFLTaemLHIDPQACVDCGACVSACP 57
Cdd:cd10560    81 CTDAGCLEACPTGAIFRTE----FGT---VYIQPDICNGCGYCVAACP 121
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 2-57 1.21e-05

the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 (Hyd-2), an enzyme that catalyzes the reversible oxidation of H2 to protons and electrons. Hyd-2 is membrane-associated and forms an unusual heterotetrameric [NiFe]-hydrogenase in that it lacks the typical cytochrome b membrane anchor subunit that transfers electrons to the quinone pool. The electron transfer subunit of Hyd-2 (HybA) which is predicted to contain four iron-sulfur clusters, is essential for electron transfer from Hyd-2 to menaquinone/demethylmenaquinone (MQ/DMQ) to couple hydrogen oxidation to fumarate reduction.


Pssm-ID: 319883 [Multi-domain]  Cd Length: 196  Bit Score: 46.44  E-value: 1.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2020379483   2 PHVVTQSC--CSDASCVYACPVNCIHPTPDEPdfltaemLHIDPQACVDCGACVSACP 57
Cdd:cd10561    62 FVFVKRQCmhCLDPACVSACPVGALRKTPEGP-------VTYDEDKCIGCRYCMVACP 112
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 108-465 1.74e-05

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 46.93  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 108 RVAIVGSGPSAMYAADElLTQPDVQVNVFDR-------LPVPYGLVRAGVAPDH----------QKTKQVTRLfdkiaaQ 170
Cdd:pfam07992   2 DVVVIGGGPAGLAAALT-LAQLGGKVTLIEDegtcpygGCVLSKALLGAAEAPEiaslwadlykRKEEVVKKL------N 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 171 KGFEFYLNVE-----------IGKHISHSELLE-NHHAVLYAVGASSdRGLGIPGADLPGTASATDFvawynghpDHADD 238
Cdd:pfam07992  75 NGIEVLLGTEvvsidpgakkvVLEELVDGDGETiTYDRLVIATGARP-RLPPIPGVELNVGFLVRTL--------DSAEA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 239 VF-DLSHRRAVIIGNGNVALDVAriltadpeklagtdISAHALAAlrksrveEVVIVGRRGIAQSAFtvpeftglmalpD 317
Cdd:pfam07992 146 LRlKLLPKRVVVVGGGYIGVELA--------------AALAKLGK-------EVTLIEALDRLLRAF------------D 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483 318 IELSvgpddmvlDSATEELAKRGelphaveqklrllealknrdhVDVgnkritlrylLTPTSITGddqvsgiafarnalV 397
Cdd:pfam07992 193 EEIS--------AALEKALEKNG---------------------VEV----------RLGTSVKE--------------I 219

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020379483 398 DANGTVQIEATGDTETIDTGLVLTSIGYRGVPIP----GVPFDERASVIPNENGRVleapngdPATGVYATG 465
Cdd:pfam07992 220 IGDGDGVEVILKDGTEIDADLVVVAIGRRPNTELleaaGLELDERGGIVVDEYLRT-------SVPGIYAAG 284
PRK09898 PRK09898
ferredoxin-like protein;
6-66 2.12e-05

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 45.60  E-value: 2.12e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020379483   6 TQSC--CSDASCVYACPVNCIHPTPDEPDFLtaemlhIDPQACVDCGACVSACP--VDAIVPESK 66
Cdd:PRK09898  120 ADTCrqCKEPQCMNVCPIGAITWQQKEGCIT------VDHKRCIGCSACTTACPwmMATVNTESK 178
Fer4_6 pfam12837
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 40-61 2.32e-05

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: 41.06  E-value: 2.32e-05
                          10        20
                  ....*....|....*....|..
gi 2020379483  40 HIDPQACVDCGACVSACPVDAI 61
Cdd:pfam12837   3 EVDPDKCIGCGRCVVVCPYGAI 24
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
15-63 5.11e-05

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 45.31  E-value: 5.11e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2020379483  15 CVYACPVNCIHPTpdepDFLtaemLHIDPQACVDCGACVSACPVDAIVP 63
Cdd:PRK07118  221 CVKACPAGAITME----NNL----AVIDQEKCTSCGKCVEKCPTKAIRI 261
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 41-61 5.68e-05

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 43.15  E-value: 5.68e-05
                          10        20
                  ....*....|....*....|.
gi 2020379483  41 IDPQACVDCGACVSACPVDAI 61
Cdd:cd10549     3 YDPEKCIGCGICVKACPTDAI 23
FixX COG2440
Ferredoxin-like protein FixX [Energy production and conversion];
10-64 6.56e-05

Ferredoxin-like protein FixX [Energy production and conversion];


Pssm-ID: 441981 [Multi-domain]  Cd Length: 87  Bit Score: 41.73  E-value: 6.56e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483  10 CSDASCVYACPVNC--IHPTPDepdfltaemLHIDPQACVDCGACVSACPVDAI---VPE 64
Cdd:COG2440    27 CLAKPCTRYCPAGVyeIVGDGR---------LQINYENCLECGTCRIKCPTQNItwvYPE 77
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 15-62 6.56e-05

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 43.40  E-value: 6.56e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2020379483  15 CVYACPVNCIHPTPDEPDFLTaemlHIDPQACVDCGACVSACPVD---AIV 62
Cdd:cd16373   105 CVEACPTEAIAIVLEDDVLRP----VVDEDKCVGCGLCEYVCPVEppkAIV 151
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 10-61 6.81e-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: 43.03  E-value: 6.81e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2020379483  10 CSDASCVYACPVNCIHPTPDEPdfltaemLHIDPQACVDCGACVSACPVDAI 61
Cdd:cd16370    56 CEDPPCAEACPTGALEPRKGGG-------VVLDKEKCIGCGNCVKACIVGAI 100
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 9-61 7.54e-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: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 42.71  E-value: 7.54e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2020379483   9 CCSDASCVYACPVNCIHPTPDepdfltaemlHIDPQACVDCGACVSACPVDAI 61
Cdd:cd16372    79 CVGCLMCVGFCPEGAMFKHED----------YPEPFKCIACGICVKACPTGAL 121
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
9-61 8.19e-05

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 45.40  E-value: 8.19e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2020379483   9 CCSDASCVYACPVNCIHPTPDEPDFltaEMLHIDPQACVDCGACVSACPVDAI 61
Cdd:COG4624    59 CCCCRCCVAISCIQVRGIIIIDKRG---PSIIRDKEKCKNCYPCVRACPVKAI 108
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
5-63 9.13e-05

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 44.66  E-value: 9.13e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2020379483   5 VTQSC--CSDASCVYACPVNCIHPTPdepdflTAEMLHIDPQACVDCGACVSACPVDaiVP 63
Cdd:PRK10882  108 IKKQCmhCVDPNCVSVCPVSALTKDP------KTGIVHYDKDVCTGCRYCMVACPFN--VP 160
Fer4_2 pfam12797
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 37-58 9.74e-05

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: 39.31  E-value: 9.74e-05
                          10        20
                  ....*....|....*....|..
gi 2020379483  37 EMLHIDPQACVDCGACVSACPV 58
Cdd:pfam12797   1 WKPLIDADKCIGCGACVSACPA 22
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 41-62 1.39e-04

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: 42.86  E-value: 1.39e-04
                          10        20
                  ....*....|....*....|..
gi 2020379483  41 IDPQACVDCGACVSACPVDAIV 62
Cdd:TIGR01944 110 IDEDNCIGCTKCIQACPVDAIV 131
PRK13795 PRK13795
hypothetical protein; Provisional
 15-58 1.54e-04

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 44.60  E-value: 1.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2020379483  15 CVYACPVNCIhpTPDEPdfltAEMLHIDPQACVDCGACVSACPV 58
Cdd:PRK13795  589 CVGACPTGAI--RIEEG----KRKISVDEEKCIHCGKCTEVCPV 626
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 2-71 1.62e-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: 42.24  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483   2 PHVV--TQSC--CSDAsCVYACPVNCIHPTPDEPDFL---TAEmlhIDPQACV------DCGACVSACPVD--AIVPESK 66
Cdd:cd16373    46 PYLDprEGPCdlCCDA-CVEVCPTGALRPLDLEEQKVkmgVAV---IDKDRCLawqggtDCGVCVEACPTEaiAIVLEDD 121


                  ....*
gi 2020379483  67 LTDPQ 71
Cdd:cd16373   122 VLRPV 126
PRK10194 PRK10194
ferredoxin-type protein NapF;
40-64 1.89e-04

ferredoxin-type protein NapF;


Pssm-ID: 182296 [Multi-domain]  Cd Length: 163  Bit Score: 42.32  E-value: 1.89e-04
                          10        20
                  ....*....|....*....|....*
gi 2020379483  40 HIDPQACVDCGACVSACPVDAIVPE 64
Cdd:PRK10194  134 QLNSQLCNGCGACAASCPVSAITAE 158
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
2-61 2.03e-04

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 44.08  E-value: 2.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483   2 PHVVTQSCCSDASCVYACPVNCIhptpDEPDFLTAEmlhIDPQACVDCGACVSACPVDAI 61
Cdd:COG1148   491 AEVDPEKCTGCGRCVEVCPYGAI----SIDEKGVAE---VNPALCKGCGTCAAACPSGAI 543
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
15-57 2.35e-04

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 39.40  E-value: 2.35e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2020379483  15 CVYACPVNCIHPTPDEPD------FLTAEM--LHIDPQACVD------CGACVSACP 57
Cdd:pfam13484   7 CIDACPTGAIVGPEGVLDarrcisYLTIEKkgLIPDELRCLLgnrcygCDICQDVCP 63
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 43-66 2.70e-04

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 39.34  E-value: 2.70e-04
                          10        20
                  ....*....|....*....|....
gi 2020379483  43 PQACVDCGACVSACPVDAIVPESK 66
Cdd:COG1143     1 EDKCIGCGLCVRVCPVDAITIEDG 24
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 4-57 2.83e-04

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: 41.58  E-value: 2.83e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2020379483   4 VVTQSC--CSDASCVYACPVNCIhpTPDEPDFLtaemLHIDPQACVDCGACVSACP 57
Cdd:cd10553    53 FVYMSCfhCENPWCVKACPTGAM--QKREKDGI----VYVDQELCIGCKACIEACP 102
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
10-61 2.89e-04

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 42.74  E-value: 2.89e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2020379483  10 CSD-ASCVYACPVNCIhptPDEPDFLTAEmlhidpqaCVDCGACVSACPVDAI 61
Cdd:COG0348   212 CIDcGLCVKVCPMGID---IRKGEINQSE--------CINCGRCIDACPKDAI 253
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
15-70 3.25e-04

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 42.74  E-value: 3.25e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2020379483  15 CVYACPVNCIHPTPDEPDFLTaemLHIDPQACVDCGACVSACPVDAIVPESKLTDP 70
Cdd:COG0348   184 CRYLCPYGAFQGLLSDLSTLR---VRYDRGDCIDCGLCVKVCPMGIDIRKGEINQS 236
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 46-80 3.42e-04

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 38.66  E-value: 3.42e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2020379483  46 CVDCGACVSACPVDAIVPESKLTDPQRVFLSINAD 80
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKKGTKTVVIDPE 35
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 10-60 5.48e-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: 5.48e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2020379483  10 CSDASCVYACPVNCIHPTPDepdflTAEMLhIDPQACVDCGACVSACPVDA 60
Cdd:pfam13247  13 CLNPPCKASCPVGAIYKDEE-----TGAVL-LDEKTCRGWRECVSACPYNI 57
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 29-63 7.82e-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: 40.32  E-value: 7.82e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2020379483  29 DEPDFLtaemlhidpQACVDCGACVSACPVDAIVP 63
Cdd:cd16373     8 DEEEFL---------ALCIRCGLCVEACPTGVIQP 33
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 38-61 8.28e-04

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: 37.62  E-value: 8.28e-04
                          10        20
                  ....*....|....*....|....
gi 2020379483  38 MLHIDPQACVDCGACVSACPVDAI 61
Cdd:pfam13237   1 KVVIDPDKCIGCGRCTAACPAGLT 24
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 6-66 8.97e-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: 39.92  E-value: 8.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020379483   6 TQSC--CSDasCVYACPVNCIHPTPD---EPDFLTAEmlhidpqaCVDCGACVSACPVDAIVPESK 66
Cdd:cd10564    12 LDLCtrCGD--CVEACPEGIIVRGDGgfpELDFSRGE--------CTFCGACAEACPEGALDPARE 67
PRK06273 PRK06273
ferredoxin; Provisional
 2-83 1.11e-03

ferredoxin; Provisional


Pssm-ID: 235764 [Multi-domain]  Cd Length: 165  Bit Score: 40.08  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020379483   2 PHVVTQSCCSDASCVYACPVNCIHPTPDEP-----DFLTAEMLHIDPQACVDCGACVSACPVDAIVPESKLTDPQRVFLS 76
Cdd:PRK06273   44 KKVFEELCIGCGGCANVCPTKAIEMIPVEPvkiteGYVKTKIPKIDYEKCVYCLYCHDFCPVFALFNEISPIHPRDVGED 123


                  ....*..
gi 2020379483  77 INADFYK 83
Cdd:PRK06273  124 IEVDVSK 130
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 42-62 1.71e-03

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: 40.36  E-value: 1.71e-03
                          10        20
                  ....*....|....*....|.
gi 2020379483  42 DPQACVDCGACVSACPVDAIV 62
Cdd:COG2878   135 CEYGCIGCGDCIKACPFDAIV 155
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 10-72 1.81e-03

N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This family includes the beta subunit of pyrogallol-phloroglucinol transhydroxylase (TH), a cytoplasmic molybdenum (Mo) enzyme from anaerobic microorganisms like Pelobacter acidigallici and Desulfitobacterium hafniense which catalyzes the conversion of pyrogallol to phloroglucinol, an important building block of plant polymers. TH belongs to the DMSO reductase (DMSOR) family; it is a heterodimer consisting of a large alpha catalytic subunit and a small beta FeS subunit. The beta subunit has two domains with the N-terminal domain containing three [4Fe-4S] centers and a seven-stranded, mainly antiparallel beta-barrel domain. In the anaerobic bacterium Pelobacter acidigallici, gallic acid, pyrogallol, phloroglucinol, or phloroglucinol carboxylic acid are fermented to three molecules of acetate (plus CO2), and TH is the key enzyme in the fermentation pathway, which converts pyrogallol to phloroglucinol in the absence of O2.


Pssm-ID: 319874 [Multi-domain]  Cd Length: 186  Bit Score: 39.62  E-value: 1.81e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020379483  10 CSDASCVYACPVNCIHPTPDEpdfltaeMLHIDPQACVDCGACVSACPVDAIVPESKLTDPQR 72
Cdd:cd10552    67 CDNAPCIKAAKDGAVYKRDDG-------IVIIDPEKAKGQKQLVDACPYGAIYWNEELQVPQK 122
Fer4_21 pfam14697
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 9-59 2.00e-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: 434137 [Multi-domain]  Cd Length: 59  Bit Score: 36.88  E-value: 2.00e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2020379483   9 CCSDASCVYACPVN---CIHPTPDEpdfltaeMLHIDPQACVDCGACVSACPVD 59
Cdd:pfam14697   8 CIGCGKCYIACPDTshqAIVGDGKR-------HHTVIEDECTGCNLCVSVCPVD 54
PRK06991 PRK06991
electron transport complex subunit RsxB;
41-66 2.05e-03

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 40.16  E-value: 2.05e-03
                          10        20
                  ....*....|....*....|....*.
gi 2020379483  41 IDPQACVDCGACVSACPVDAIVPESK 66
Cdd:PRK06991   82 IDEQLCIGCTLCMQACPVDAIVGAPK 107
Fer4_9 pfam13187
4Fe-4S dicluster domain;
45-63 2.57e-03

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 35.99  E-value: 2.57e-03
                          10
                  ....*....|....*....
gi 2020379483  45 ACVDCGACVSACPVDAIVP 63
Cdd:pfam13187   1 KCTGCGACVAACPAGAIVP 19
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 15-61 3.13e-03

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 40.54  E-value: 3.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2020379483  15 CVYACPVN-----CIHpTPDEPDFLtaemlHIDPQACVDCGACVSACPVDAI 61
Cdd:COG1245    21 CIKYCPVNrtgkeAIE-IDEDDGKP-----VISEELCIGCGICVKKCPFDAI 66
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 15-59 3.73e-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: 433017 [Multi-domain]  Cd Length: 64  Bit Score: 36.13  E-value: 3.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2020379483  15 CVYACPV------NCIHPTPDEPDFLTAEMLHIDPQA-----CVDCGACVSACPVD 59
Cdd:pfam13183   8 CLAACPVylvtggRFPGDPRGGAAALLGRLEALEGLAeglwlCTLCGACTEVCPVG 63
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
 42-73 4.14e-03

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 38.47  E-value: 4.14e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2020379483  42 DPQACVDCGACVSACPVDAIVPESKLTDPQRV 73
Cdd:PRK12387   36 NPQQCIGCAACVNACPSNALTVETDLATGELA 67
PRK05113 PRK05113
electron transport complex protein RnfB; Provisional
 41-62 5.08e-03

electron transport complex protein RnfB; Provisional


Pssm-ID: 235347 [Multi-domain]  Cd Length: 191  Bit Score: 38.39  E-value: 5.08e-03
                          10        20
                  ....*....|....*....|..
gi 2020379483  41 IDPQACVDCGACVSACPVDAIV 62
Cdd:PRK05113  111 IDEDNCIGCTKCIQACPVDAIV 132
YdhS COG4529
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
105-144 7.22e-03

Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];


Pssm-ID: 443597 [Multi-domain]  Cd Length: 466  Bit Score: 39.17  E-value: 7.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2020379483 105 PPLRVAIVGSGPSAMYAADELLTQ--PDVQVNVFDRLP-----VPYG 144
Cdd:COG4529     4 ARKRIAIIGGGASGTALAIHLLRRapEPLRITLFEPRPelgrgVAYS 50
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
2-64 7.66e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 38.38  E-value: 7.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2020379483   2 PHVVTQSCCSDASCVYACPVNCIHPTPDEPDFLTAEMLHIDPQA--------CVDCGACVSACPVDAIVPE 64
Cdd:PRK07118  163 PVVDEDKCTGCGACVKACPRNVIELIPKSARVFVACNSKDKGKAvkkvcevgCIGCGKCVKACPAGAITME 233
Fer4_3 pfam12798
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 46-60 7.74e-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: 463712  Cd Length: 15  Bit Score: 34.14  E-value: 7.74e-03
                          10
                  ....*....|....*
gi 2020379483  46 CVDCGACVSACPVDA 60
Cdd:pfam12798   1 CTGCGACVEVCPVGA 15
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
111-154 9.52e-03

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 34.81  E-value: 9.52e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2020379483 111 IVGSGPSAMYAAdELLTQPDVQVNVFDRLPVPYGLVRAGVAPDH 154
Cdd:pfam13450   1 IVGAGLAGLVAA-ALLAKRGFRVLVLEKRDRLGGNAYSYRVPGY 43
 
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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