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Conserved domains on  [gi|1867174023|ref|WP_178371909|]
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FAD-dependent oxidoreductase [Desulfacinum infernum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
463-1016 0e+00

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


:

Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 757.86  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  463 RVGVFVCHcGVNIAGVVDVEAVADYAETLPGVAYVERNLFTCAQDTQDKMKQIIEEHNLNRIVVAACSPRTHEALFQETL 542
Cdd:COG1148      3 RIGVFVCH-GINIGGVVDVPAVAEYAKTLPGVVYAEDNLYLCSQDGQELIKDDIKEHGLNRVVVAACSPRTHEPLFRETL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  543 KQAGLNKYLFEMANIRNQGSWVHMNEPEAATEKAKDLVRMAVAKVALQQPLGEMQLGVTKSALVVGGGIAGMTAALTLAD 622
Cdd:COG1148     82 REAGLNPYLFEMANIREQCSWVHMDEPEAATEKAKDLVRMAVAKAKLLEPLEPIKVPVNKRALVIGGGIAGMTAALELAE 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  623 QGYPVTLVERKDVLGGHGRKLYSTWDGQ-PVAPFLDELIKRVEAHPEITVLTKARITDVQGFVGNFHTVLDVDG-QRREV 700
Cdd:COG1148    162 QGYEVYLVEKEPELGGRAAQLHKTFPGLdCPQCILEPLIAEVEANPNITVYTGAEVEEVSGYVGNFTVTIKKGPrEEIEI 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  701 DHGVAVIAVGAHSLKP---DEYGYGKSDRIFLNLDLDQAIGE----RDERIVTARSAVFIQCVGSREPD--RPYCSRVCC 771
Cdd:COG1148    242 EVGAIVLATGFKPYDPtklGEYGYGKYPNVITNLELERLLAAgkilRPSDGKEPKSVAFIQCVGSRDEEngLPYCSRVCC 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  772 SHSIENALRLKKLNPDMDVYVLYRDIRTFGLRENLYKEARARGVLFIRFDLENkpvVQVASDGTLKVTVKDHVLQRPVVL 851
Cdd:COG1148    322 MYALKQALYLKEKNPDADVYIFYRDIRTYGKYEEFYRRAREDGVRFIRGRVAE---IEEDEGGKLVVTVEDTLLGEPVEI 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  852 TPDILTLAGAIVMREsEADELAKMFKVPVNAEGFFLEAHAKLRPVDFATDGVFVAGLAHYPKPTEECIAQAKAAASRAAT 931
Cdd:COG1148    399 EADLVVLATGMVPSE-DNEELAKLLKLPLDQDGFFLEAHPKLRPVETATDGIFLAGAAHGPKDIPESIAQATAAAARAIQ 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  932 VLAKDSITAGGVVAVVNKDLCCGCQGCVQCCPFGAIDYLErEGKCEVNQALCKGCGTCAATCPSEAITLLGFSHLQLYAQ 1011
Cdd:COG1148    478 LLSKGELGVEPSVAEVDPEKCTGCGRCVEVCPYGAISIDE-KGVAEVNPALCKGCGTCAAACPSGAISLKGFTDDQILAQ 556


                   ....*
gi 1867174023 1012 IDEAL 1016
Cdd:COG1148    557 IDALL 561
hetero_SS_HdrA2 super family cl48997
CoB-CoM heterodisulfide reductase HdrA2; HdrA2 represents a distinct subclass of the HdrA ...
 15-424 3.97e-154

CoB-CoM heterodisulfide reductase HdrA2; HdrA2 represents a distinct subclass of the HdrA family, which is the A subunit of the CoB-CoM heterodisulfide reductase. HdrA2 from Methanosarcina acetivorans. A distinctive feature is a MvhD-like C-terminal domain, where MvhD is the signature delta subunit of the F420-non-reducing type of hydrogenase, Mvh.


The actual alignment was detected with superfamily member NF040770:

Pssm-ID: 468729 [Multi-domain]  Cd Length: 777  Bit Score: 475.66  E-value: 3.97e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023   15 SVLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIGGAMSMLDKTFPTDDCAMUILSPKLVEVGRHLNIQIHTLSEVKDIT 94
Cdd:NF040770   141 DVLVIGGGVAGIEAALDLADAGYKVYLVEKEPTIGGKMALLNEVFPTNDCSICVLAPKMTEVGNHPNIELLTLSEVTEIS 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023   95 GEAGSFQAKIFQRARYIDMDKCIACGT-CAEKCPRKVTDEYNAGLGKRKAAYVKFPQAVPLKYVIDKDHCIyfekgKCRA 173
Cdd:NF040770   221 GSVGNFTVKVLKKPRYVDEDKCKGCIDdCSSVCPVEIPNEFDYGLGKRKAIYMPFPQAVPQVAYIDMEYCV-----GCGL 295

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  174 CEKFCPTQAVNFDDQDREFTLEVGSVILAPGFEPFDPGVYDTYSYS-HPNVITSMEFERILSSSGPFEGHLVRPSDHQEP 252
Cdd:NF040770   296 CVLACPADAIDFEQKEEEFEFEVGAIIVATGYDVFDASRKEEYGYGrYPNVITNLELERLLNASGPTGGRVVRPSDGKVP 375

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  253 KKIAWLQCVGSRDiHHCDNGYCSGVCCMYAIKEAAIAKEHAgADLNTAIFFMDMRTPGKDFDKYYERAKaEKGVRFIRSR 332
Cdd:NF040770   376 KSVAFIQCVGSRD-EKVGNPYCSRVCCMNSIKNAQLIKERY-PDTEITIHYIDIRAFGEMYEEYYTRAQ-EMGVDFIRGK 452

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  333 VHSIEPLPgTDDLAIQY-VTEDGRITEEVFNLVVLSVGLQISKDTLELAEKLGVEIG-DGRFAATSP-FQPVQTSRTGIY 409
Cdd:NF040770   453 VAEIIEDE-DGNLILRYeDTLEGEVREEEYDLVVLSVGMEPNKDAEVIQRMLNLSRRpDGFFMVAHPkMRPVDTHTKGVF 531

                          410
                   ....*....|....*
gi 1867174023  410 VCGVFQSPKDIPLSV 424
Cdd:NF040770   532 LAGCASGPKDIQDSI 546
 
Name Accession Description Interval E-value
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
463-1016 0e+00

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 757.86  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  463 RVGVFVCHcGVNIAGVVDVEAVADYAETLPGVAYVERNLFTCAQDTQDKMKQIIEEHNLNRIVVAACSPRTHEALFQETL 542
Cdd:COG1148      3 RIGVFVCH-GINIGGVVDVPAVAEYAKTLPGVVYAEDNLYLCSQDGQELIKDDIKEHGLNRVVVAACSPRTHEPLFRETL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  543 KQAGLNKYLFEMANIRNQGSWVHMNEPEAATEKAKDLVRMAVAKVALQQPLGEMQLGVTKSALVVGGGIAGMTAALTLAD 622
Cdd:COG1148     82 REAGLNPYLFEMANIREQCSWVHMDEPEAATEKAKDLVRMAVAKAKLLEPLEPIKVPVNKRALVIGGGIAGMTAALELAE 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  623 QGYPVTLVERKDVLGGHGRKLYSTWDGQ-PVAPFLDELIKRVEAHPEITVLTKARITDVQGFVGNFHTVLDVDG-QRREV 700
Cdd:COG1148    162 QGYEVYLVEKEPELGGRAAQLHKTFPGLdCPQCILEPLIAEVEANPNITVYTGAEVEEVSGYVGNFTVTIKKGPrEEIEI 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  701 DHGVAVIAVGAHSLKP---DEYGYGKSDRIFLNLDLDQAIGE----RDERIVTARSAVFIQCVGSREPD--RPYCSRVCC 771
Cdd:COG1148    242 EVGAIVLATGFKPYDPtklGEYGYGKYPNVITNLELERLLAAgkilRPSDGKEPKSVAFIQCVGSRDEEngLPYCSRVCC 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  772 SHSIENALRLKKLNPDMDVYVLYRDIRTFGLRENLYKEARARGVLFIRFDLENkpvVQVASDGTLKVTVKDHVLQRPVVL 851
Cdd:COG1148    322 MYALKQALYLKEKNPDADVYIFYRDIRTYGKYEEFYRRAREDGVRFIRGRVAE---IEEDEGGKLVVTVEDTLLGEPVEI 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  852 TPDILTLAGAIVMREsEADELAKMFKVPVNAEGFFLEAHAKLRPVDFATDGVFVAGLAHYPKPTEECIAQAKAAASRAAT 931
Cdd:COG1148    399 EADLVVLATGMVPSE-DNEELAKLLKLPLDQDGFFLEAHPKLRPVETATDGIFLAGAAHGPKDIPESIAQATAAAARAIQ 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  932 VLAKDSITAGGVVAVVNKDLCCGCQGCVQCCPFGAIDYLErEGKCEVNQALCKGCGTCAATCPSEAITLLGFSHLQLYAQ 1011
Cdd:COG1148    478 LLSKGELGVEPSVAEVDPEKCTGCGRCVEVCPYGAISIDE-KGVAEVNPALCKGCGTCAAACPSGAISLKGFTDDQILAQ 556


                   ....*
gi 1867174023 1012 IDEAL 1016
Cdd:COG1148    557 IDALL 561
hetero_SS_HdrA2 NF040770
CoB-CoM heterodisulfide reductase HdrA2; HdrA2 represents a distinct subclass of the HdrA ...
 463-1016 4.99e-158

CoB-CoM heterodisulfide reductase HdrA2; HdrA2 represents a distinct subclass of the HdrA family, which is the A subunit of the CoB-CoM heterodisulfide reductase. HdrA2 from Methanosarcina acetivorans. A distinctive feature is a MvhD-like C-terminal domain, where MvhD is the signature delta subunit of the F420-non-reducing type of hydrogenase, Mvh.


Pssm-ID: 468729 [Multi-domain]  Cd Length: 777  Bit Score: 485.67  E-value: 4.99e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  463 RVGVFVCHCGVNIAGVVDVEAVADYAETLPGVAYVERNLFTCAQDTQDKMKQIIEEHNLNRIVVAACSPRTHEALFQETL 542
Cdd:NF040770     1 RIGVYVCHCGLNIAGVVDVEAVAEYAKTLEDVVLARDIQFMCSDSGQEQIKKDIKEHKLDRVVVAACSPRLHEPTFRRVL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  543 KQAGLNKYLFEMANIRNQGSWVHMNEPEAATEKAKDLVRMAVAKVALQQPLGEMQLGVTKSALVVGGGIAGMTAALTLAD 622
Cdd:NF040770    81 EKAGLNPYLLEMANIREQCSWVHMDDPQMATQKAKDLVRMGVARARLLEPLEEKTIPVNRDVLVIGGGVAGIEAALDLAD 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  623 QGYPVTLVERKDVLGGHG---RKLYSTWDGQ--PVAPFLDElikrVEAHPEITVLTKARITDVQGFVGNFH-TVLD---- 692
Cdd:NF040770   161 AGYKVYLVEKEPTIGGKMallNEVFPTNDCSicVLAPKMTE----VGNHPNIELLTLSEVTEISGSVGNFTvKVLKkpry 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  693 VD---------------------------GQRR---------------------------------------------EV 700
Cdd:NF040770   237 VDedkckgciddcssvcpveipnefdyglGKRKaiympfpqavpqvayidmeycvgcglcvlacpadaidfeqkeeefEF 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  701 DHGVAVIAVGAHSLKP---DEYGYGKSDRIFLNLDLDQ---AIGERDERIV------TARSAVFIQCVGSRE--PDRPYC 766
Cdd:NF040770   317 EVGAIIVATGYDVFDAsrkEEYGYGRYPNVITNLELERllnASGPTGGRVVrpsdgkVPKSVAFIQCVGSRDekVGNPYC 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  767 SRVCCSHSIENALRLKKLNPDMDVYVLYRDIRTFG-LRENLYKEARARGVLFIRfdleNKPV-VQVASDGTLKVTVKDHV 844
Cdd:NF040770   397 SRVCCMNSIKNAQLIKERYPDTEITIHYIDIRAFGeMYEEYYTRAQEMGVDFIR----GKVAeIIEDEDGNLILRYEDTL 472

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  845 LQRPVVLTPDILTLagAIVMRESE-ADELAKMFKVPVNAEGFFLEAHAKLRPVDFATDGVFVAGLAHYPKPTEECIAQAK 923
Cdd:NF040770   473 EGEVREEEYDLVVL--SVGMEPNKdAEVIQRMLNLSRRPDGFFMVAHPKMRPVDTHTKGVFLAGCASGPKDIQDSIAQAS 550

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  924 AAASRAATVLAKDSITAGGVVAVVNKDLCCGCQGCVQCCPFGAIdYLEReGKCEVNQALCKGCGTCAATCPSEAITLLGF 1003
Cdd:NF040770   551 AAAARAMILLSKGELEVDPITAHVDEEKCIGCGICEDVCPFNAI-TVDN-GKAVVDEAACAGCGTCSAACPADAIDMRHF 628

                          650
                   ....*....|...
gi 1867174023 1004 SHLQLYAQIDEAL 1016
Cdd:NF040770   629 TDEQILAQIDAAT 641
hetero_SS_HdrA2 NF040770
CoB-CoM heterodisulfide reductase HdrA2; HdrA2 represents a distinct subclass of the HdrA ...
 15-424 3.97e-154

CoB-CoM heterodisulfide reductase HdrA2; HdrA2 represents a distinct subclass of the HdrA family, which is the A subunit of the CoB-CoM heterodisulfide reductase. HdrA2 from Methanosarcina acetivorans. A distinctive feature is a MvhD-like C-terminal domain, where MvhD is the signature delta subunit of the F420-non-reducing type of hydrogenase, Mvh.


Pssm-ID: 468729 [Multi-domain]  Cd Length: 777  Bit Score: 475.66  E-value: 3.97e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023   15 SVLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIGGAMSMLDKTFPTDDCAMUILSPKLVEVGRHLNIQIHTLSEVKDIT 94
Cdd:NF040770   141 DVLVIGGGVAGIEAALDLADAGYKVYLVEKEPTIGGKMALLNEVFPTNDCSICVLAPKMTEVGNHPNIELLTLSEVTEIS 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023   95 GEAGSFQAKIFQRARYIDMDKCIACGT-CAEKCPRKVTDEYNAGLGKRKAAYVKFPQAVPLKYVIDKDHCIyfekgKCRA 173
Cdd:NF040770   221 GSVGNFTVKVLKKPRYVDEDKCKGCIDdCSSVCPVEIPNEFDYGLGKRKAIYMPFPQAVPQVAYIDMEYCV-----GCGL 295

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  174 CEKFCPTQAVNFDDQDREFTLEVGSVILAPGFEPFDPGVYDTYSYS-HPNVITSMEFERILSSSGPFEGHLVRPSDHQEP 252
Cdd:NF040770   296 CVLACPADAIDFEQKEEEFEFEVGAIIVATGYDVFDASRKEEYGYGrYPNVITNLELERLLNASGPTGGRVVRPSDGKVP 375

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  253 KKIAWLQCVGSRDiHHCDNGYCSGVCCMYAIKEAAIAKEHAgADLNTAIFFMDMRTPGKDFDKYYERAKaEKGVRFIRSR 332
Cdd:NF040770   376 KSVAFIQCVGSRD-EKVGNPYCSRVCCMNSIKNAQLIKERY-PDTEITIHYIDIRAFGEMYEEYYTRAQ-EMGVDFIRGK 452

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  333 VHSIEPLPgTDDLAIQY-VTEDGRITEEVFNLVVLSVGLQISKDTLELAEKLGVEIG-DGRFAATSP-FQPVQTSRTGIY 409
Cdd:NF040770   453 VAEIIEDE-DGNLILRYeDTLEGEVREEEYDLVVLSVGMEPNKDAEVIQRMLNLSRRpDGFFMVAHPkMRPVDTHTKGVF 531

                          410
                   ....*....|....*
gi 1867174023  410 VCGVFQSPKDIPLSV 424
Cdd:NF040770   532 LAGCASGPKDIQDSI 546
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
15-424 2.88e-120

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 379.59  E-value: 2.88e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023   15 SVLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIGGAMSMLDKTFPTDDCAMUILSPKLVEVGRHLNIQIHTLSEVKDIT 94
Cdd:COG1148    142 RALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQLHKTFPGLDCPQCILEPLIAEVEANPNITVYTGAEVEEVS 221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023   95 GEAGSFQAKIFQRARyidmdkciacgtcaekcprkvtdeynaglgkrkaayvkfpqavplkyvidkdhciyfekgkcrac 174
Cdd:COG1148    222 GYVGNFTVTIKKGPR----------------------------------------------------------------- 236

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  175 ekfcptqavnfddqdREFTLEVGSVILAPGFEPFDPGVYDTYSY-SHPNVITSMEFERILSssgpfEGHLVRPSDHQEPK 253
Cdd:COG1148    237 ---------------EEIEIEVGAIVLATGFKPYDPTKLGEYGYgKYPNVITNLELERLLA-----AGKILRPSDGKEPK 296

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  254 KIAWLQCVGSRDIHHcDNGYCSGVCCMYAIKEAAIAKEHAGaDLNTAIFFMDMRTPGKdFDKYYERAKaEKGVRFIRSRV 333
Cdd:COG1148    297 SVAFIQCVGSRDEEN-GLPYCSRVCCMYALKQALYLKEKNP-DADVYIFYRDIRTYGK-YEEFYRRAR-EDGVRFIRGRV 372

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  334 HSIEPLPGtDDLAIQYV-TEDGRITEEVFNLVVLSVGLQISKDTLELAEKLGVEIGDGRFAATSPF--QPVQTSRTGIYV 410
Cdd:COG1148    373 AEIEEDEG-GKLVVTVEdTLLGEPVEIEADLVVLATGMVPSEDNEELAKLLKLPLDQDGFFLEAHPklRPVETATDGIFL 451

                          410
                   ....*....|....
gi 1867174023  411 CGVFQSPKDIPLSV 424
Cdd:COG1148    452 AGAAHGPKDIPESI 465
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 15-412 8.12e-15

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: 76.20  E-value: 8.12e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023   15 SVLVVGGGIAGVQAALDLADTGYFVHLIEktsaiggamsmLDKTFPTDDCamuILSPKLVEVGRHLNIQIHTLSEVKDIT 94
Cdd:pfam07992    2 DVVVIGGGPAGLAAALTLAQLGGKVTLIE-----------DEGTCPYGGC---VLSKALLGAAEAPEIASLWADLYKRKE 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023   95 GEAGSFQAKIFQRARyidmdkciacgtcaekcpRKVTDeynaglgkrkaayvkfpqavplkyvIDKDHCIYFEKGKcrac 174
Cdd:pfam07992   68 EVVKKLNNGIEVLLG------------------TEVVS-------------------------IDPGAKKVVLEEL---- 100

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  175 ekfcptqavnfdDQDREFTLEVGSVILAPGFEPFDPGV--YDTYSYSHPNVITSMEferilsssgpfeghlvRPSDHQEP 252
Cdd:pfam07992  101 ------------VDGDGETITYDRLVIATGARPRLPPIpgVELNVGFLVRTLDSAE----------------ALRLKLLP 152

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  253 KKIAwlqCVGSrdihhcdnGYCSgvcCMYAIKEAAIAKE----HAGADLntaiffmdMRTPGKDFDKYYERAKAEKGVRF 328
Cdd:pfam07992  153 KRVV---VVGG--------GYIG---VELAAALAKLGKEvtliEALDRL--------LRAFDEEISAALEKALEKNGVEV 210

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  329 I-RSRVHSIEPlpgtDDLAIQYVTEDGRitEEVFNLVVLSVGLQISkdtLELAEKLGVEIGDGRFAATSPFQpvQTSRTG 407
Cdd:pfam07992  211 RlGTSVKEIIG----DGDGVEVILKDGT--EIDADLVVVAIGRRPN---TELLEAAGLELDERGGIVVDEYL--RTSVPG 279


                   ....*
gi 1867174023  408 IYVCG 412
Cdd:pfam07992  280 IYAAG 284
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 605-745 1.37e-10

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: 63.49  E-value: 1.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  605 LVVGGGIAGMTAALTLADQGYPVTLVERKDVLGGHGRKLYSTWDGQP----VAPFLDELIKRVEAH-----PEITVLTKA 675
Cdd:pfam07992    4 VVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCPYGGCVLSKALLGAAeapeIASLWADLYKRKEEVvkklnNGIEVLLGT 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1867174023  676 RITDVqgFVGN--FHTVLDVDGQRREVDHGVAVIAVGAHSLKPD----EYGYGKSDRIflnLDLDQAI--GERDERIV 745
Cdd:pfam07992   84 EVVSI--DPGAkkVVLEELVDGDGETITYDRLVIATGARPRLPPipgvELNVGFLVRT---LDSAEALrlKLLPKRVV 156
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 111-187 2.96e-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: 58.95  E-value: 2.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  111 IDMDKCIACGTCAEKCPR---KVTDEYNAGLGKRKaayvkfpqavplKYVIDKDHCIYfekgkCRACEKFCPTQAVNFDD 187
Cdd:cd10549     37 IDEDKCVFCGACVEVCPTgaiELTPEGKEYVPKEK------------EAEIDEEKCIG-----CGLCVKVCPVDAITLED 99
PRK07233 PRK07233
hypothetical protein; Provisional
 606-648 1.68e-07

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 54.89  E-value: 1.68e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1867174023  606 VVGGGIAGMTAALTLADQGYPVTLVERKDVLGGhgrkLYSTWD 648
Cdd:PRK07233     4 IVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG----LAASFE 42
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 100-183 9.50e-07

NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes "I" subunits from the closely related F420H2 dehydrogenase and formate hydrogenlyase complexes. [Energy metabolism, Electron transport]


Pssm-ID: 273902 [Multi-domain]  Cd Length: 122  Bit Score: 48.57  E-value: 9.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  100 FQAKIFQRARYIDMDKCIACGTCAEKCP----RKVTDEYNAglGKRKaayvkfpqavPLKYVIDKDHCIYfekgkCRACE 175
Cdd:TIGR01971   29 FRGRIVLTRDPNGEEKCIGCTLCAAVCPadaiRVVPAEGED--GKRR----------LKFYEINFGRCIF-----CGLCE 91


                   ....*...
gi 1867174023  176 KFCPTQAV 183
Cdd:TIGR01971   92 EACPTDAI 99
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 963-1000 1.82e-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: 45.08  E-value: 1.82e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1867174023  963 PFGAIDyLEREGKCEVNQALCKGCGTCAATCPSEAITL 1000
Cdd:cd10549     91 PVDAIT-LEDELEIVIDKEKCIGCGICAEVCPVNAIKL 127
PRK07233 PRK07233
hypothetical protein; Provisional
 16-56 4.72e-05

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 47.19  E-value: 4.72e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1867174023   16 VLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIGGAMSMLD 56
Cdd:PRK07233     2 IAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAASFE 42
glycerol3P_GlpB TIGR03378
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ...
 605-667 6.57e-03

glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are the B subunit, product of the glpB gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase. [Energy metabolism, Anaerobic]


Pssm-ID: 213807  Cd Length: 419  Bit Score: 40.00  E-value: 6.57e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1867174023  605 LVVGGGIAGMTAALTLADQGYPVTLVERK-----------DVLGghgrklySTWDGQPV-APF--LDELIKRVEAHP 667
Cdd:TIGR03378    4 IIIGGGLAGLSCALRLAEAGKKCAIIAAGqsalhfssgslDLLS-------RLPDGQAVeQPMdaLEALAQQAPEHP 73
 
Name Accession Description Interval E-value
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
463-1016 0e+00

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 757.86  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  463 RVGVFVCHcGVNIAGVVDVEAVADYAETLPGVAYVERNLFTCAQDTQDKMKQIIEEHNLNRIVVAACSPRTHEALFQETL 542
Cdd:COG1148      3 RIGVFVCH-GINIGGVVDVPAVAEYAKTLPGVVYAEDNLYLCSQDGQELIKDDIKEHGLNRVVVAACSPRTHEPLFRETL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  543 KQAGLNKYLFEMANIRNQGSWVHMNEPEAATEKAKDLVRMAVAKVALQQPLGEMQLGVTKSALVVGGGIAGMTAALTLAD 622
Cdd:COG1148     82 REAGLNPYLFEMANIREQCSWVHMDEPEAATEKAKDLVRMAVAKAKLLEPLEPIKVPVNKRALVIGGGIAGMTAALELAE 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  623 QGYPVTLVERKDVLGGHGRKLYSTWDGQ-PVAPFLDELIKRVEAHPEITVLTKARITDVQGFVGNFHTVLDVDG-QRREV 700
Cdd:COG1148    162 QGYEVYLVEKEPELGGRAAQLHKTFPGLdCPQCILEPLIAEVEANPNITVYTGAEVEEVSGYVGNFTVTIKKGPrEEIEI 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  701 DHGVAVIAVGAHSLKP---DEYGYGKSDRIFLNLDLDQAIGE----RDERIVTARSAVFIQCVGSREPD--RPYCSRVCC 771
Cdd:COG1148    242 EVGAIVLATGFKPYDPtklGEYGYGKYPNVITNLELERLLAAgkilRPSDGKEPKSVAFIQCVGSRDEEngLPYCSRVCC 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  772 SHSIENALRLKKLNPDMDVYVLYRDIRTFGLRENLYKEARARGVLFIRFDLENkpvVQVASDGTLKVTVKDHVLQRPVVL 851
Cdd:COG1148    322 MYALKQALYLKEKNPDADVYIFYRDIRTYGKYEEFYRRAREDGVRFIRGRVAE---IEEDEGGKLVVTVEDTLLGEPVEI 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  852 TPDILTLAGAIVMREsEADELAKMFKVPVNAEGFFLEAHAKLRPVDFATDGVFVAGLAHYPKPTEECIAQAKAAASRAAT 931
Cdd:COG1148    399 EADLVVLATGMVPSE-DNEELAKLLKLPLDQDGFFLEAHPKLRPVETATDGIFLAGAAHGPKDIPESIAQATAAAARAIQ 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  932 VLAKDSITAGGVVAVVNKDLCCGCQGCVQCCPFGAIDYLErEGKCEVNQALCKGCGTCAATCPSEAITLLGFSHLQLYAQ 1011
Cdd:COG1148    478 LLSKGELGVEPSVAEVDPEKCTGCGRCVEVCPYGAISIDE-KGVAEVNPALCKGCGTCAAACPSGAISLKGFTDDQILAQ 556


                   ....*
gi 1867174023 1012 IDEAL 1016
Cdd:COG1148    557 IDALL 561
hetero_SS_HdrA2 NF040770
CoB-CoM heterodisulfide reductase HdrA2; HdrA2 represents a distinct subclass of the HdrA ...
 463-1016 4.99e-158

CoB-CoM heterodisulfide reductase HdrA2; HdrA2 represents a distinct subclass of the HdrA family, which is the A subunit of the CoB-CoM heterodisulfide reductase. HdrA2 from Methanosarcina acetivorans. A distinctive feature is a MvhD-like C-terminal domain, where MvhD is the signature delta subunit of the F420-non-reducing type of hydrogenase, Mvh.


Pssm-ID: 468729 [Multi-domain]  Cd Length: 777  Bit Score: 485.67  E-value: 4.99e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  463 RVGVFVCHCGVNIAGVVDVEAVADYAETLPGVAYVERNLFTCAQDTQDKMKQIIEEHNLNRIVVAACSPRTHEALFQETL 542
Cdd:NF040770     1 RIGVYVCHCGLNIAGVVDVEAVAEYAKTLEDVVLARDIQFMCSDSGQEQIKKDIKEHKLDRVVVAACSPRLHEPTFRRVL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  543 KQAGLNKYLFEMANIRNQGSWVHMNEPEAATEKAKDLVRMAVAKVALQQPLGEMQLGVTKSALVVGGGIAGMTAALTLAD 622
Cdd:NF040770    81 EKAGLNPYLLEMANIREQCSWVHMDDPQMATQKAKDLVRMGVARARLLEPLEEKTIPVNRDVLVIGGGVAGIEAALDLAD 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  623 QGYPVTLVERKDVLGGHG---RKLYSTWDGQ--PVAPFLDElikrVEAHPEITVLTKARITDVQGFVGNFH-TVLD---- 692
Cdd:NF040770   161 AGYKVYLVEKEPTIGGKMallNEVFPTNDCSicVLAPKMTE----VGNHPNIELLTLSEVTEISGSVGNFTvKVLKkpry 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  693 VD---------------------------GQRR---------------------------------------------EV 700
Cdd:NF040770   237 VDedkckgciddcssvcpveipnefdyglGKRKaiympfpqavpqvayidmeycvgcglcvlacpadaidfeqkeeefEF 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  701 DHGVAVIAVGAHSLKP---DEYGYGKSDRIFLNLDLDQ---AIGERDERIV------TARSAVFIQCVGSRE--PDRPYC 766
Cdd:NF040770   317 EVGAIIVATGYDVFDAsrkEEYGYGRYPNVITNLELERllnASGPTGGRVVrpsdgkVPKSVAFIQCVGSRDekVGNPYC 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  767 SRVCCSHSIENALRLKKLNPDMDVYVLYRDIRTFG-LRENLYKEARARGVLFIRfdleNKPV-VQVASDGTLKVTVKDHV 844
Cdd:NF040770   397 SRVCCMNSIKNAQLIKERYPDTEITIHYIDIRAFGeMYEEYYTRAQEMGVDFIR----GKVAeIIEDEDGNLILRYEDTL 472

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  845 LQRPVVLTPDILTLagAIVMRESE-ADELAKMFKVPVNAEGFFLEAHAKLRPVDFATDGVFVAGLAHYPKPTEECIAQAK 923
Cdd:NF040770   473 EGEVREEEYDLVVL--SVGMEPNKdAEVIQRMLNLSRRPDGFFMVAHPKMRPVDTHTKGVFLAGCASGPKDIQDSIAQAS 550

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  924 AAASRAATVLAKDSITAGGVVAVVNKDLCCGCQGCVQCCPFGAIdYLEReGKCEVNQALCKGCGTCAATCPSEAITLLGF 1003
Cdd:NF040770   551 AAAARAMILLSKGELEVDPITAHVDEEKCIGCGICEDVCPFNAI-TVDN-GKAVVDEAACAGCGTCSAACPADAIDMRHF 628

                          650
                   ....*....|...
gi 1867174023 1004 SHLQLYAQIDEAL 1016
Cdd:NF040770   629 TDEQILAQIDAAT 641
hetero_SS_HdrA2 NF040770
CoB-CoM heterodisulfide reductase HdrA2; HdrA2 represents a distinct subclass of the HdrA ...
 15-424 3.97e-154

CoB-CoM heterodisulfide reductase HdrA2; HdrA2 represents a distinct subclass of the HdrA family, which is the A subunit of the CoB-CoM heterodisulfide reductase. HdrA2 from Methanosarcina acetivorans. A distinctive feature is a MvhD-like C-terminal domain, where MvhD is the signature delta subunit of the F420-non-reducing type of hydrogenase, Mvh.


Pssm-ID: 468729 [Multi-domain]  Cd Length: 777  Bit Score: 475.66  E-value: 3.97e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023   15 SVLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIGGAMSMLDKTFPTDDCAMUILSPKLVEVGRHLNIQIHTLSEVKDIT 94
Cdd:NF040770   141 DVLVIGGGVAGIEAALDLADAGYKVYLVEKEPTIGGKMALLNEVFPTNDCSICVLAPKMTEVGNHPNIELLTLSEVTEIS 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023   95 GEAGSFQAKIFQRARYIDMDKCIACGT-CAEKCPRKVTDEYNAGLGKRKAAYVKFPQAVPLKYVIDKDHCIyfekgKCRA 173
Cdd:NF040770   221 GSVGNFTVKVLKKPRYVDEDKCKGCIDdCSSVCPVEIPNEFDYGLGKRKAIYMPFPQAVPQVAYIDMEYCV-----GCGL 295

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  174 CEKFCPTQAVNFDDQDREFTLEVGSVILAPGFEPFDPGVYDTYSYS-HPNVITSMEFERILSSSGPFEGHLVRPSDHQEP 252
Cdd:NF040770   296 CVLACPADAIDFEQKEEEFEFEVGAIIVATGYDVFDASRKEEYGYGrYPNVITNLELERLLNASGPTGGRVVRPSDGKVP 375

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  253 KKIAWLQCVGSRDiHHCDNGYCSGVCCMYAIKEAAIAKEHAgADLNTAIFFMDMRTPGKDFDKYYERAKaEKGVRFIRSR 332
Cdd:NF040770   376 KSVAFIQCVGSRD-EKVGNPYCSRVCCMNSIKNAQLIKERY-PDTEITIHYIDIRAFGEMYEEYYTRAQ-EMGVDFIRGK 452

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  333 VHSIEPLPgTDDLAIQY-VTEDGRITEEVFNLVVLSVGLQISKDTLELAEKLGVEIG-DGRFAATSP-FQPVQTSRTGIY 409
Cdd:NF040770   453 VAEIIEDE-DGNLILRYeDTLEGEVREEEYDLVVLSVGMEPNKDAEVIQRMLNLSRRpDGFFMVAHPkMRPVDTHTKGVF 531

                          410
                   ....*....|....*
gi 1867174023  410 VCGVFQSPKDIPLSV 424
Cdd:NF040770   532 LAGCASGPKDIQDSI 546
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
15-424 2.88e-120

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 379.59  E-value: 2.88e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023   15 SVLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIGGAMSMLDKTFPTDDCAMUILSPKLVEVGRHLNIQIHTLSEVKDIT 94
Cdd:COG1148    142 RALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQLHKTFPGLDCPQCILEPLIAEVEANPNITVYTGAEVEEVS 221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023   95 GEAGSFQAKIFQRARyidmdkciacgtcaekcprkvtdeynaglgkrkaayvkfpqavplkyvidkdhciyfekgkcrac 174
Cdd:COG1148    222 GYVGNFTVTIKKGPR----------------------------------------------------------------- 236

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  175 ekfcptqavnfddqdREFTLEVGSVILAPGFEPFDPGVYDTYSY-SHPNVITSMEFERILSssgpfEGHLVRPSDHQEPK 253
Cdd:COG1148    237 ---------------EEIEIEVGAIVLATGFKPYDPTKLGEYGYgKYPNVITNLELERLLA-----AGKILRPSDGKEPK 296

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  254 KIAWLQCVGSRDIHHcDNGYCSGVCCMYAIKEAAIAKEHAGaDLNTAIFFMDMRTPGKdFDKYYERAKaEKGVRFIRSRV 333
Cdd:COG1148    297 SVAFIQCVGSRDEEN-GLPYCSRVCCMYALKQALYLKEKNP-DADVYIFYRDIRTYGK-YEEFYRRAR-EDGVRFIRGRV 372

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  334 HSIEPLPGtDDLAIQYV-TEDGRITEEVFNLVVLSVGLQISKDTLELAEKLGVEIGDGRFAATSPF--QPVQTSRTGIYV 410
Cdd:COG1148    373 AEIEEDEG-GKLVVTVEdTLLGEPVEIEADLVVLATGMVPSEDNEELAKLLKLPLDQDGFFLEAHPklRPVETATDGIFL 451

                          410
                   ....*....|....
gi 1867174023  411 CGVFQSPKDIPLSV 424
Cdd:COG1148    452 AGAAHGPKDIPESI 465
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 15-412 8.12e-15

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: 76.20  E-value: 8.12e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023   15 SVLVVGGGIAGVQAALDLADTGYFVHLIEktsaiggamsmLDKTFPTDDCamuILSPKLVEVGRHLNIQIHTLSEVKDIT 94
Cdd:pfam07992    2 DVVVIGGGPAGLAAALTLAQLGGKVTLIE-----------DEGTCPYGGC---VLSKALLGAAEAPEIASLWADLYKRKE 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023   95 GEAGSFQAKIFQRARyidmdkciacgtcaekcpRKVTDeynaglgkrkaayvkfpqavplkyvIDKDHCIYFEKGKcrac 174
Cdd:pfam07992   68 EVVKKLNNGIEVLLG------------------TEVVS-------------------------IDPGAKKVVLEEL---- 100

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  175 ekfcptqavnfdDQDREFTLEVGSVILAPGFEPFDPGV--YDTYSYSHPNVITSMEferilsssgpfeghlvRPSDHQEP 252
Cdd:pfam07992  101 ------------VDGDGETITYDRLVIATGARPRLPPIpgVELNVGFLVRTLDSAE----------------ALRLKLLP 152

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  253 KKIAwlqCVGSrdihhcdnGYCSgvcCMYAIKEAAIAKE----HAGADLntaiffmdMRTPGKDFDKYYERAKAEKGVRF 328
Cdd:pfam07992  153 KRVV---VVGG--------GYIG---VELAAALAKLGKEvtliEALDRL--------LRAFDEEISAALEKALEKNGVEV 210

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  329 I-RSRVHSIEPlpgtDDLAIQYVTEDGRitEEVFNLVVLSVGLQISkdtLELAEKLGVEIGDGRFAATSPFQpvQTSRTG 407
Cdd:pfam07992  211 RlGTSVKEIIG----DGDGVEVILKDGT--EIDADLVVVAIGRRPN---TELLEAAGLELDERGGIVVDEYL--RTSVPG 279


                   ....*
gi 1867174023  408 IYVCG 412
Cdd:pfam07992  280 IYAAG 284
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 605-745 1.37e-10

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: 63.49  E-value: 1.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  605 LVVGGGIAGMTAALTLADQGYPVTLVERKDVLGGHGRKLYSTWDGQP----VAPFLDELIKRVEAH-----PEITVLTKA 675
Cdd:pfam07992    4 VVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCPYGGCVLSKALLGAAeapeIASLWADLYKRKEEVvkklnNGIEVLLGT 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1867174023  676 RITDVqgFVGN--FHTVLDVDGQRREVDHGVAVIAVGAHSLKPD----EYGYGKSDRIflnLDLDQAI--GERDERIV 745
Cdd:pfam07992   84 EVVSI--DPGAkkVVLEELVDGDGETITYDRLVIATGARPRLPPipgvELNVGFLVRT---LDSAEALrlKLLPKRVV 156
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 110-191 2.52e-10

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 57.03  E-value: 2.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  110 YIDMDKCIACGTCAEKCPRKVTDEYNAGlgkRKAayvkfpqavplkYVIDKDHCIYfekgkCRACEKFCPTQAVNFDDQD 189
Cdd:COG1146      4 VIDTDKCIGCGACVEVCPVDVLELDEEG---KKA------------LVINPEECIG-----CGACELVCPVGAITVEDDE 63


                   ..
gi 1867174023  190 RE 191
Cdd:COG1146     64 PE 65
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 111-187 2.96e-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: 58.95  E-value: 2.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  111 IDMDKCIACGTCAEKCPR---KVTDEYNAGLGKRKaayvkfpqavplKYVIDKDHCIYfekgkCRACEKFCPTQAVNFDD 187
Cdd:cd10549     37 IDEDKCVFCGACVEVCPTgaiELTPEGKEYVPKEK------------EAEIDEEKCIG-----CGLCVKVCPVDAITLED 99
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 601-659 9.04e-10

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 62.17  E-value: 9.04e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  601 TKSALVVGGGIAGMTAALTLADQGYPVTLVERKDVLGGHGRKL---------YSTW--DGQPVAPFLDEL 659
Cdd:COG1233      3 MYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTFerpgfrfdvGPSVltMPGVLERLFREL 72
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 601-638 2.40e-09

Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];


Pssm-ID: 442577 [Multi-domain]  Cd Length: 445  Bit Score: 60.64  E-value: 2.40e-09
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1867174023  601 TKSALVVGGGIAGMTAALTLADQGYPVTLVERKDVLGG 638
Cdd:COG3349      3 PPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
110-195 4.36e-09

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 53.97  E-value: 4.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  110 YIDMDKCIACGTCAEKCPRKVTDEYNAglgkrkaayvkfpqavplKYVIDKDHCIyfekgKCRACEKFCPTQAVNFDDQD 189
Cdd:COG2768      7 YVDEEKCIGCGACVKVCPVGAISIEDG------------------KAVIDPEKCI-----GCGACIEVCPVGAIKIEWEE 63


                   ....*.
gi 1867174023  190 REFTLE 195
Cdd:COG2768     64 DEEFQE 69
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 114-189 1.53e-08

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: 52.06  E-value: 1.53e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1867174023  114 DKCIACGTCAEKCPRKVTDEYNAGLGKRkaayvkfpqavplkYVIDKDHCIYfekgkCRACEKFCPTQAVNFDDQD 189
Cdd:COG1143      2 DKCIGCGLCVRVCPVDAITIEDGEPGKV--------------YVIDPDKCIG-----CGLCVEVCPTGAISMTPFE 58
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 601-641 1.92e-08

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 57.26  E-value: 1.92e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1867174023  601 TKSALVVGGGIAGMTAALTLADQGYPVTLVERKDVLGGHGR 641
Cdd:COG0654      3 RTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGR 43
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
606-659 2.08e-08

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 51.76  E-value: 2.08e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1867174023  606 VVGGGIAGMTAALTLADQGYPVTLVERKDVLGGH-------GRKL------YSTWDGQPVAPFLDEL 659
Cdd:pfam13450    1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNaysyrvpGYVFdygahiFHGSDEPNVRDLLDEL 67
GlpB COG3075
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
605-667 2.44e-08

Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 442309  Cd Length: 415  Bit Score: 57.50  E-value: 2.44e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1867174023  605 LVVGGGIAGMTAALTLADQGYPVTLVERK-----------DVLGGHGrklystwDGQPVA-PF--LDELIKRVEAHP 667
Cdd:COG3075      6 VVIGGGLAGLTAAIRAAEAGLRVAIVSAGqsalhfssgslDLLGYLP-------DGEPVAdPFdaLADLPEQAPEHP 75
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 111-187 3.02e-08

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 51.27  E-value: 3.02e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1867174023  111 IDMDKCIACGTCAEKCPrkvtdeYNA-GLGKRKaayvkfpqavplKYVIDKDHCIyfekgKCRACEKFCPTQAVNFDD 187
Cdd:COG1149      8 IDEEKCIGCGLCVEVCP------EGAiKLDDGG------------APVVDPDLCT-----GCGACVGVCPTGAITLEE 62
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 110-183 4.25e-08

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 51.20  E-value: 4.25e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1867174023  110 YIDMDKCIACGTCAEKCPRKVTDEynaglGKRKAayvkfpqavplkyVIDKDHCIyfekgKCRACEKFCPTQAV 183
Cdd:COG4231     18 VIDEDKCTGCGACVKVCPADAIEE-----GDGKA-------------VIDPDLCI-----GCGSCVQVCPVDAI 68
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 602-638 5.18e-08

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 56.38  E-value: 5.18e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1867174023  602 KSALVVGGGIAGMTAALTLADQGYPVTLVERKDVLGG 638
Cdd:COG1232      2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGG 38
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 111-201 5.88e-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: 5.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  111 IDMDKCIACGTCAEKCPrkvtdeYNA-GLGKRKaayvkfpqAVPLKYVIDKDHCIYfekgkCRACEKFCPTQAVNFDDQD 189
Cdd:cd10549      3 YDPEKCIGCGICVKACP------TDAiELGPNG--------AIARGPEIDEDKCVF-----CGACVEVCPTGAIELTPEG 63

                           90
                   ....*....|..
gi 1867174023  190 REFTLEVGSVIL 201
Cdd:cd10549     64 KEYVPKEKEAEI 75
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 605-639 7.85e-08

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 55.99  E-value: 7.85e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1867174023  605 LVVGGGIAGMTAALTLADQGYPVTLVERKDVLGGH 639
Cdd:COG1053      7 VVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGH 41
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
601-702 8.36e-08

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 55.70  E-value: 8.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  601 TKSALVVGGGIAGMTAALTLADQGYPVTLVERKDVLGGHGRKLYSTWDGQPV---APFLDelikrvEAHPEITVL-TKAR 676
Cdd:COG1231      7 GKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGLYAelgAMRIP------PSHTNLLALaRELG 80

                           90       100
                   ....*....|....*....|....*.
gi 1867174023  677 ITDVQGFVGNFHTVLDVDGQRREVDH 702
Cdd:COG1231     81 LPLEPFPNENGNALLYLGGKRVRAGE 106
PRK07233 PRK07233
hypothetical protein; Provisional
 606-648 1.68e-07

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 54.89  E-value: 1.68e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1867174023  606 VVGGGIAGMTAALTLADQGYPVTLVERKDVLGGhgrkLYSTWD 648
Cdd:PRK07233     4 IVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG----LAASFE 42
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 604-639 2.09e-07

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 54.60  E-value: 2.09e-07
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1867174023  604 ALVVGGGIAGMTAALTLADQGYPVTLVERKDVLGGH 639
Cdd:pfam00890    2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGA 37
PRK07208 PRK07208
hypothetical protein; Provisional
 602-638 3.24e-07

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 54.12  E-value: 3.24e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1867174023  602 KSALVVGGGIAGMTAALTLADQGYPVTLVERKDVLGG 638
Cdd:PRK07208     5 KSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGG 41
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
605-667 3.59e-07

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 53.70  E-value: 3.59e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1867174023  605 LVVGGGIAGMTAALTLADQGYPVTLVERK-----------DVLGGHGrklystwDGQPVAPF---LDELIKRVEAHP 667
Cdd:PRK05329     6 LVIGGGLAGLTAALAAAEAGKRVALVAKGqgalhfssgsiDLLGYLP-------DGQPVSDPfeaLAALAEQAPEHP 75
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 963-1000 3.78e-07

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 48.19  E-value: 3.78e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1867174023  963 PFGAIdYLEREGKCEVNQALCKGCGTCAATCPSEAITL 1000
Cdd:COG1149     24 PEGAI-KLDDGGAPVVDPDLCTGCGACVGVCPTGAITL 60
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 104-192 8.97e-07

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 47.35  E-value: 8.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  104 IFQRARYIDMDKCIACGTCAEKCPRKVTDEYNAglgkrkaayvkfpqavplKYVIDKDHCIYfekgkCRACEKFCPTQAV 183
Cdd:COG2221      5 IGTWPPKIDEEKCIGCGLCVAVCPTGAISLDDG------------------KLVIDEEKCIG-----CGACIRVCPTGAI 61


                   ....*....
gi 1867174023  184 NFdDQDREF 192
Cdd:COG2221     62 KG-EKPKKF 69
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 100-183 9.50e-07

NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes "I" subunits from the closely related F420H2 dehydrogenase and formate hydrogenlyase complexes. [Energy metabolism, Electron transport]


Pssm-ID: 273902 [Multi-domain]  Cd Length: 122  Bit Score: 48.57  E-value: 9.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  100 FQAKIFQRARYIDMDKCIACGTCAEKCP----RKVTDEYNAglGKRKaayvkfpqavPLKYVIDKDHCIYfekgkCRACE 175
Cdd:TIGR01971   29 FRGRIVLTRDPNGEEKCIGCTLCAAVCPadaiRVVPAEGED--GKRR----------LKFYEINFGRCIF-----CGLCE 91


                   ....*...
gi 1867174023  176 KFCPTQAV 183
Cdd:TIGR01971   92 EACPTDAI 99
PRK08163 PRK08163
3-hydroxybenzoate 6-monooxygenase;
601-715 1.04e-06

3-hydroxybenzoate 6-monooxygenase;


Pssm-ID: 181262 [Multi-domain]  Cd Length: 396  Bit Score: 52.35  E-value: 1.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  601 TKSALVVGGGIAGMTAALTLADQGYPVTLVERKDVLG--GHGRKL----YSTWD----GQPV---APFLDELI------- 660
Cdd:PRK08163     4 VTPVLIVGGGIGGLAAALALARQGIKVKLLEQAAEIGeiGAGIQLgpnaFSALDalgvGEAArqrAVFTDHLTmmdavda 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  661 ---------------------------------KRVEAHPEITVLTKARITDVQGfVGNFHTVLDVDGQRRevdHGVAVI 707
Cdd:PRK08163    84 eevvriptgqafrarfgnpyavihradihlsllEAVLDHPLVEFRTSTHVVGIEQ-DGDGVTVFDQQGNRW---TGDALI 159


                   ....*...
gi 1867174023  708 avGAHSLK 715
Cdd:PRK08163   160 --GCDGVK 165
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
606-653 1.19e-06

Predicted flavin-containing amine oxidase [General function prediction only];


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 52.04  E-value: 1.19e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1867174023  606 VVGGGIAGMTAALTLADQgYPVTLVERKDVLGGHGRKLYSTWDGQPVA 653
Cdd:COG2907      8 VIGSGISGLTAAWLLSRR-HDVTLFEANDRLGGHTHTVDVDLDGRTVP 54
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 605-717 2.95e-06

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 50.86  E-value: 2.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  605 LVVGGGIAGMTAALTLADQGYPVTLVErKDVLGG--------------HGRKLYST--------WDGQPVAPFLDELIKR 662
Cdd:COG1249      7 VVIGAGPGGYVAAIRAAQLGLKVALVE-KGRLGGtclnvgcipskallHAAEVAHEarhaaefgISAGAPSVDWAALMAR 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1867174023  663 VEAHPE------ITVLTKARITDVQG---FVGNfHTVlDVDGQRR-EVDHgvAVIAVGAHSLKPD 717
Cdd:COG1249     86 KDKVVDrlrggvEELLKKNGVDVIRGrarFVDP-HTV-EVTGGETlTADH--IVIATGSRPRVPP 146
NapF COG1145
Ferredoxin [Energy production and conversion];
111-191 3.01e-06

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 49.72  E-value: 3.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  111 IDMDKCIACGTCAEKCPRKVtdeynAGLGKRKAAyvkfpqavplkYVIDKDHCIyfekgKCRACEKFCPTQAVNFDDQDR 190
Cdd:COG1145    179 IDAEKCIGCGLCVKVCPTGA-----IRLKDGKPQ-----------IVVDPDKCI-----GCGACVKVCPVGAISLEPKEI 237


                   .
gi 1867174023  191 E 191
Cdd:COG1145    238 E 238
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
605-638 3.37e-06

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 50.29  E-value: 3.37e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1867174023  605 LVVGGGIAGMTAALTLADQGYPVTLVERKDVLGG 638
Cdd:COG0665      6 VVIGGGIAGLSTAYHLARRGLDVTVLERGRPGSG 39
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 605-639 3.62e-06

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 50.09  E-value: 3.62e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1867174023  605 LVVGGGIAGMTAALTLADQGYPVTLVERKDVLGGH 639
Cdd:pfam01266    3 VVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSG 37
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 963-1000 4.16e-06

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: 45.81  E-value: 4.16e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1867174023  963 PFGAIDyLEREGKCEVNQALCKGCGTCAATCPSEAITL 1000
Cdd:COG1144     43 PDGAIR-VDDGKYYGIDYDYCKGCGICAEVCPVKAIEM 79
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
602-710 5.00e-06

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 50.14  E-value: 5.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  602 KSALVVGGGIAGMTAALTLADQGYPVTLVERKDVLgghgrklystWDGQpvapfLDELI-KRVEAHPE---ITVLTKARI 677
Cdd:COG1251    143 KRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRL----------LPRQ-----LDEEAgALLQRLLEalgVEVRLGTGV 207

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1867174023  678 TDVQGfVGNFHTVLDVDGQRREVDhgVAVIAVG 710
Cdd:COG1251    208 TEIEG-DDRVTGVRLADGEELPAD--LVVVAIG 237
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
605-730 7.08e-06

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 49.14  E-value: 7.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  605 LVVGGGIAGMTAALTLADQGYPVTLVERKDVLGGHGrKLYSTWdgqpVAPFLDELIKRVEAHPEITVLTKARITDVQgFV 684
Cdd:pfam13738  159 VVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRD-SDPSYS----LSPDTLNRLEELVKNGKIKAHFNAEVKEIT-EV 232

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1867174023  685 GNFHTVLDVDGQRREVDHGVaVIAVGAHS----LKPDEYGYGKSDRIFLN 730
Cdd:pfam13738  233 DVSYKVHTEDGRKVTSNDDP-ILATGYHPdlsfLKKGLFELDEDGRPVLT 281
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 963-1000 8.23e-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: 8.23e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1867174023  963 PFGAIDylEREGKCEVNQALCKGCGTCAATCPSEAITL 1000
Cdd:COG4231     35 PADAIE--EGDGKAVIDPDLCIGCGSCVQVCPVDAIKL 70
PRK06847 PRK06847
hypothetical protein; Provisional
 602-634 9.58e-06

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 49.10  E-value: 9.58e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1867174023  602 KSALVVGGGIAGMTAALTLADQGYPVTLVERKD 634
Cdd:PRK06847     5 KKVLIVGGGIGGLSAAIALRRAGIAVDLVEIDP 37
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
963-1000 1.07e-05

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 44.34  E-value: 1.07e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1867174023  963 PFGAIDylEREGKCEVNQALCKGCGTCAATCPSEAITL 1000
Cdd:COG2768     24 PVGAIS--IEDGKAVIDPEKCIGCGACIEVCPVGAIKI 59
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 110-189 1.17e-05

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 46.86  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  110 YIDMDKCIACGTCAEKCPrkvtdeYNAglgkrkaayvkfPQAVPLKYVIDK-DHCI-YFEKGKCRACEKFCPTQAVNFDD 187
Cdd:COG0437     86 LVDYDKCIGCRYCVAACP------YGA------------PRFNPETGVVEKcTFCAdRLDEGLLPACVEACPTGALVFGD 147


                   ..
gi 1867174023  188 QD 189
Cdd:COG0437    148 LD 149
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 563-638 1.39e-05

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: 48.59  E-value: 1.39e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1867174023  563 WVHMNEPEAATEKakdlvrmavaKVAlqqplgemqlgvtksalVVGGGIAGMTAALTLADQGYPVTLVERKDVLGG 638
Cdd:COG0493    110 WVKPPPPAPRTGK----------KVA-----------------VVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG 158
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 602-710 1.62e-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: 48.08  E-value: 1.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  602 KSALVVGGGIAGMTAALTLADQGYPVTLVERKDVLGGhgrklystwdgqpvaPFLDELIKRVEAHPE---ITVLTKARIT 678
Cdd:pfam07992  153 KRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLR---------------AFDEEISAALEKALEkngVEVRLGTSVK 217

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1867174023  679 DVQGfVGNFHTVLDVDGQRREVDHgvAVIAVG 710
Cdd:pfam07992  218 EIIG-DGDGVEVILKDGTEIDADL--VVVAIG 246
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 963-1000 1.82e-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: 45.08  E-value: 1.82e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1867174023  963 PFGAIDyLEREGKCEVNQALCKGCGTCAATCPSEAITL 1000
Cdd:cd10549     91 PVDAIT-LEDELEIVIDKEKCIGCGICAEVCPVNAIKL 127
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 605-638 1.85e-05

FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 48.37  E-value: 1.85e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1867174023  605 LVVGGGIAGMTAALTLADQGYPVTLVERKDVLGG 638
Cdd:pfam12831    3 VVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGG 36
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 111-185 2.19e-05

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: 45.07  E-value: 2.19e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1867174023  111 IDMDKCIACGTCAEKCPRKVtdeynaglgkrkaayvkfPQAVPLKYVIDK-DHCI-YFEKGKCRACEKFCPTQAVNF 185
Cdd:cd04410     77 IDEDKCIGCGSCVEACPYGA------------------IVFDPEPGKAVKcDLCGdRLDEGLEPACVKACPTGALTF 135
PLN02268 PLN02268
probable polyamine oxidase
 603-652 2.45e-05

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 48.15  E-value: 2.45e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1867174023  603 SALVVGGGIAGMTAALTLADQGYPVTLVERKDVLGGHGRKLYSTwdGQPV 652
Cdd:PLN02268     2 SVIVIGGGIAGIAAARALHDASFKVTLLESRDRIGGRVHTDYSF--GFPV 49
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 611-842 2.56e-05

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 47.87  E-value: 2.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  611 IAGMTAALTLADQGYPVTLVERKDVLGGHGRKLYS------------TWDGQPVAPFLDEL-IKRVEAHPEitvltkari 677
Cdd:pfam01593    1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVRDdgflielgamwfHGAQPPLLALLKELgLEDRLVLPD--------- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  678 tdvqgfVGNFHTVLDVDGQR-----REVDHGVAVIAvgahslkpdeygygksdRIFLNLDLDQAIGERDERIVTARSAVF 752
Cdd:pfam01593   72 ------PAPFYTVLFAGGRRypgdfRRVPAGWEGLL-----------------EFGRLLSIPEKLRLGLAALASDALDEF 128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  753 IQCVGSREP------DRPYCSRVCCSHSIENALRlKKLNPDMDVY-----------VLYRDIRTFGLRENLYK------- 808
Cdd:pfam01593  129 DLDDFSLAEsllflgRRGPGDVEVWDRLIDPELF-AALPFASGAFagdpselsaglALPLLWALLGEGGSLLLprgglga 207

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1867174023  809 -----EARARGVlFIRFdleNKPVVQVA-SDGTLKVTVKD 842
Cdd:pfam01593  208 lpdalAAQLLGG-DVRL---NTRVRSIDrEGDGVTVTLTD 243
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 16-56 3.11e-05

Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];


Pssm-ID: 442577 [Multi-domain]  Cd Length: 445  Bit Score: 47.54  E-value: 3.11e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1867174023   16 VLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIGG-AMSMLD 56
Cdd:COG3349      6 VVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGGrARSFPD 47
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
601-633 3.17e-05

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 47.59  E-value: 3.17e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1867174023  601 TKSALVVGGGIAGMTAALTLADQGYPVTLVERK 633
Cdd:PRK07494     7 HTDIAVIGGGPAGLAAAIALARAGASVALVAPE 39
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 111-182 3.28e-05

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: 43.12  E-value: 3.28e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1867174023  111 IDMDKCIACGTCAEKCPRKVTDEYNAGlgkrkaayvkfpqavplKYVIDKDHCiyfeKGkCRACEKFCPTQA 182
Cdd:COG1144     27 VDEDKCIGCGLCWIVCPDGAIRVDDGK-----------------YYGIDYDYC----KG-CGICAEVCPVKA 76
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
602-721 4.09e-05

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 46.65  E-value: 4.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  602 KSALVVGGGIAGMTAALTLADQGYPVTLVERKDVLGGHgrklystwdgqpvapflDELIKRVEAHPEITVLTKARITDVQ 681
Cdd:COG0492    142 KDVVVVGGGDSALEEALYLTKFASKVTLIHRRDELRAS-----------------KILVERLRANPKIEVLWNTEVTEIE 204

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1867174023  682 G--FVGNFhTVLDVD-GQRREVDHGVAVIAVGAHS---------LKPDEYGY 721
Cdd:COG0492    205 GdgRVEGV-TLKNVKtGEEKELEVDGVFVAIGLKPntellkglgLELDEDGY 255
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
605-917 4.29e-05

NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 47.05  E-value: 4.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  605 LVVGGGIAGMTAALTLADQ---GYPVTLVERKD----------VLGGHgrklYSTWDgqpVAPFLDELIKRveahpeitv 671
Cdd:COG1252      5 VIVGGGFAGLEAARRLRKKlggDAEVTLIDPNPyhlfqpllpeVAAGT----LSPDD---IAIPLRELLRR--------- 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  672 ltkARITDVQGfvgnfhTVLDVDGQRREV--DHG------VAVIAVGAHSLKP-----DEYGYG-KS--------DRIFL 729
Cdd:COG1252     69 ---AGVRFIQG------EVTGIDPEARTVtlADGrtlsydYLVIATGSVTNFFgipglAEHALPlKTledalalrERLLA 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  730 NldLDQAIGERDERIVTArSAVF--IQCVGSrepdrpycsrvcCSHSIENALRLKKLNPD-MDVYVLYRDIRTFG----- 801
Cdd:COG1252    140 A--FERAERRRLLTIVVV-GGGPtgVELAGE------------LAELLRKLLRYPGIDPDkVRITLVEAGPRILPglgek 204

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  802 LRENLYKEARARGVLFIrfdlENKPVVQVASDGtlkVTVKDHvlqrpVVLTPDILTLAGAIvmresEADELAKMFKVPVN 881
Cdd:COG1252    205 LSEAAEKELEKRGVEVH----TGTRVTEVDADG---VTLEDG-----EEIPADTVIWAAGV-----KAPPLLADLGLPTD 267

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1867174023  882 AEGfFLEAHAKLRPVDFatDGVFVAG-LAHYPKPTEE 917
Cdd:COG1252    268 RRG-RVLVDPTLQVPGH--PNVFAIGdCAAVPDPDGK 301
PRK07233 PRK07233
hypothetical protein; Provisional
 16-56 4.72e-05

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 47.19  E-value: 4.72e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1867174023   16 VLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIGGAMSMLD 56
Cdd:PRK07233     2 IAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAASFE 42
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 16-53 5.24e-05

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 46.62  E-value: 5.24e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1867174023   16 VLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIGGAMS 53
Cdd:pfam01266    2 VVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSGAS 39
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 604-648 5.55e-05

Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];


Pssm-ID: 441675 [Multi-domain]  Cd Length: 414  Bit Score: 46.78  E-value: 5.55e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1867174023  604 ALVVGGGIAGMTAALTLADQGYPVTLVERKDVLGGhgrklysTWD 648
Cdd:COG2072      9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGG-------TWR 46
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 602-638 5.98e-05

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 46.71  E-value: 5.98e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1867174023  602 KSALVVGGGIAGMTAALTLADQGYPVTLVERKDVLGG 638
Cdd:PRK11749   141 KKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG 177
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
18-53 9.82e-05

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 41.36  E-value: 9.82e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1867174023   18 VVGGGIAGVQAALDLADTGYFVHLIEKTSAIGGAMS 53
Cdd:pfam13450    1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAY 36
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 963-1000 1.00e-04

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 43.15  E-value: 1.00e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1867174023  963 PFGAID-------YLEREGKCEVNQALCKGCGTCAATCPSEAITL 1000
Cdd:cd10549     53 PTGAIEltpegkeYVPKEKEAEIDEEKCIGCGLCVKVCPVDAITL 97
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 963-999 1.09e-04

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 41.19  E-value: 1.09e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1867174023  963 PFGAIDYleREGKCEVNQALCKGCGTCAATCPSEAIT 999
Cdd:COG2221     28 PTGAISL--DDGKLVIDEEKCIGCGACIRVCPTGAIK 62
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 15-98 1.11e-04

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: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 41.42  E-value: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023   15 SVLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIggaMSMLDKTFptddcamuilSPKLVEVGRHLNIQIHTLSEVKDIT 94
Cdd:pfam00070    1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRL---LPGFDPEI----------AKILQEKLEKNGIEFLLNTTVEAIE 67


                   ....
gi 1867174023   95 GEAG 98
Cdd:pfam00070   68 GNGD 71
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 110-187 1.13e-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: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 43.03  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  110 YIDMDKCIACGTCAEKCPRKVtdeynaglgkrkaayvkfPQAVPLKYVIDK-DHCI-YFEKGKCRACEKFCPTQAVNFDD 187
Cdd:cd16374     69 LVDPDKCIGCGMCAMACPFGV------------------PRFDPSLKVAVKcDLCIdRRREGKLPACVEACPTGALKFGD 130
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
 114-198 1.22e-04

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 43.87  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  114 DKCIACGTCAEKCPRK-VTDEYNAGLGKrkaayvkfpqavpLKYVIDKDHCIYfekgkCRACEKFCPTQAVNFDDqdrEF 192
Cdd:PRK12387    38 QQCIGCAACVNACPSNaLTVETDLATGE-------------LAWEFNLGRCIF-----CGRCEEVCPTAAIKLSQ---EF 96


                   ....*.
gi 1867174023  193 TLEVGS 198
Cdd:PRK12387    97 ELAVWK 102
YhiN COG2081
Predicted flavoprotein YhiN [General function prediction only];
605-643 1.25e-04

Predicted flavoprotein YhiN [General function prediction only];


Pssm-ID: 441684 [Multi-domain]  Cd Length: 402  Bit Score: 45.43  E-value: 1.25e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1867174023  605 LVVGGGIAGMTAALTLADQGYPVTLVERKDVLgghGRKL 643
Cdd:COG2081      1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKV---GRKI 36
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 14-119 1.29e-04

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: 45.00  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023   14 GSVLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIggaMSMLDKtfptddcamuILSPKLVEVGRHLNIQIHTLSEVKDI 93
Cdd:pfam07992  153 KRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRL---LRAFDE----------EISAALEKALEKNGVEVRLGTSVKEI 219

                           90       100
                   ....*....|....*....|....*.
gi 1867174023   94 TGEAGSFQAkIFQRARYIDMDKCIAC 119
Cdd:pfam07992  220 IGDGDGVEV-ILKDGTEIDADLVVVA 244
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 110-191 1.56e-04

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: 42.76  E-value: 1.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  110 YIDMDKCIACGTCAEKCprKVTDEYNAGLGKRKAAYVKFPQAVPLKY-----------------------------VIDK 160
Cdd:cd04410      2 VVDLDRCIGCGTCEVAC--KQEHGLRPGPDWSRIKVIEGGGLERAFLpvscmhcedppcvkacptgaiykdedgivLIDE 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1867174023  161 DHCIyfekgKCRACEKFCPTQAVNFDDQDRE 191
Cdd:cd04410     80 DKCI-----GCGSCVEACPYGAIVFDPEPGK 105
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 602-710 1.63e-04

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 44.80  E-value: 1.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  602 KSALVVGGGIAGMTAALTLADQGYPVTLVERKDVLGGHGRKLYSTWdgqpvapfldeLIKRVEAHPeITVLTKARITDVQ 681
Cdd:COG0446    125 KRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVLDPEMAAL-----------LEEELREHG-VELRLGETVVAID 192

                           90       100
                   ....*....|....*....|....*....
gi 1867174023  682 GfvGNFHTVLDVDGQRREVDhgVAVIAVG 710
Cdd:COG0446    193 G--DDKVAVTLTDGEEIPAD--LVVVAPG 217
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 16-50 1.68e-04

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 45.21  E-value: 1.68e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1867174023   16 VLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIGG 50
Cdd:COG1232      4 VAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGG 38
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
110-151 1.92e-04

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 44.54  E-value: 1.92e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1867174023  110 YIDMDKCIACGTCAEKCPRKVTDEYNAGLGKRKAAYVKFPQA 151
Cdd:PRK07118   238 VIDQEKCTSCGKCVEKCPTKAIRILNKPPKVKEPKKAAAEAA 279
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 16-53 1.97e-04

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 45.23  E-value: 1.97e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1867174023   16 VLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIGGAMS 53
Cdd:COG1233      6 VVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRAR 43
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 110-189 2.05e-04

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: 43.06  E-value: 2.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  110 YIDMDKCIACGTCAEKCPRKVTdEYNAGLGKrkaayvkfpqavplkyvIDK-DHCIY-FEKGKCRACEKFCPTQAVNFDD 187
Cdd:cd10562     96 VVDEDKCIGCGYCVAACPFDVP-RYDETTNK-----------------ITKcTLCFDrIENGMQPACVKTCPTGALTFGD 157


                   ..
gi 1867174023  188 QD 189
Cdd:cd10562    158 RD 159
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 16-51 2.11e-04

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 44.97  E-value: 2.11e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1867174023   16 VLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIGGA 51
Cdd:pfam00890    2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGA 37
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 977-1000 2.40e-04

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 40.42  E-value: 2.40e-04
                           10        20
                   ....*....|....*....|....
gi 1867174023  977 EVNQALCKGCGTCAATCPSEAITL 1000
Cdd:COG2221     11 KIDEEKCIGCGLCVAVCPTGAISL 34
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 602-713 2.53e-04

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 44.87  E-value: 2.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  602 KSALVVGGGIAGMTAALTLADQGYPVTLVERKDVLGGHGRklYstwdGQPVAPF----LDELIKRVEAHPeITVLTKARI 677
Cdd:PRK12771   138 KRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMR--Y----GIPAYRLprevLDAEIQRILDLG-VEVRLGVRV 210

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1867174023  678 TDvqgfvgnfhtvlDVDGQRREVDHGVAVIAVGAHS 713
Cdd:PRK12771   211 GE------------DITLEQLEGEFDAVFVAIGAQL 234
Fer4_9 pfam13187
4Fe-4S dicluster domain;
115-183 2.58e-04

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 39.84  E-value: 2.58e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1867174023  115 KCIACGTCAEKCPRKVTDEYNAGLGkrkaayvkfpqavpLKYVIDKDHCIyfekgKCRACEKFCPTQAV 183
Cdd:pfam13187    1 KCTGCGACVAACPAGAIVPDLVGQT--------------IRGDIAGLACI-----GCGACVDACPRGAI 50
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
604-638 2.88e-04

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 44.78  E-value: 2.88e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1867174023  604 ALVVGGGIAGMTAALTLADQGYPVTLVER--KDVLGG 638
Cdd:COG3573      8 VIVVGAGLAGLVAAAELADAGRRVLLLDQepEANLGG 44
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 108-185 2.94e-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: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 41.79  E-value: 2.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  108 ARYIDMDKCIACGTCAEKCPrkvtdeYNAglgkrkaayvkfpqavpLKYVIDKDHCIyfekgKC------RACEKFCPTQ 181
Cdd:cd10550     74 AVVVDEDKCIGCGMCVEACP------FGA-----------------IRVDPETGKAI-----KCdlcggdPACVKVCPTG 125


                   ....
gi 1867174023  182 AVNF 185
Cdd:cd10550    126 ALEF 129
PRK07843 PRK07843
3-oxosteroid 1-dehydrogenase;
606-638 3.31e-04

3-oxosteroid 1-dehydrogenase;


Pssm-ID: 236111 [Multi-domain]  Cd Length: 557  Bit Score: 44.64  E-value: 3.31e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1867174023  606 VVGGGIAGMTAALTLADQGYPVTLVERKDVLGG 638
Cdd:PRK07843    12 VVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGG 44
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
963-1000 3.32e-04

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 41.09  E-value: 3.32e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1867174023  963 PFGAIdYLEREGKCEVNQALCKGCGTCAATCPSEAITL 1000
Cdd:PRK09623    64 PEPAI-YIKEDGYVAIDYDYCKGCGICANECPTKAITM 100
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 963-1003 3.48e-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: 39.73  E-value: 3.48e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1867174023  963 PFGAI--DYLEREGKCEVNQALCKGCGTCAATCPSEAITLLGF 1003
Cdd:COG1143     15 PVDAItiEDGEPGKVYVIDPDKCIGCGLCVEVCPTGAISMTPF 57
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 977-1000 3.52e-04

NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 41.85  E-value: 3.52e-04
                           10        20
                   ....*....|....*....|....
gi 1867174023  977 EVNQALCKGCGTCAATCPSEAITL 1000
Cdd:cd10564    113 ELDADACTGCGACVSVCPVGAITL 136
NadB COG0029
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the ...
 605-630 4.02e-04

Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439800 [Multi-domain]  Cd Length: 521  Bit Score: 44.33  E-value: 4.02e-04
                           10        20
                   ....*....|....*....|....*.
gi 1867174023  605 LVVGGGIAGMTAALTLADQGyPVTLV 630
Cdd:COG0029      8 LVIGSGIAGLSAALKLAERG-RVTLL 32
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 111-189 4.11e-04

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: 42.52  E-value: 4.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  111 IDMDKCIACGTCAEKCPrkvtdeYNAglgkR----KAAYVKFPQAVPLKYVIDK-DHCI-YFEKGKCRACEKFCPTQAVN 184
Cdd:cd10551     80 VDYDKCIGCRYCMAACP------YGA----RyfnpEEPHEFGEVPVRPKGVVEKcTFCYhRLDEGLLPACVEACPTGARI 149


                   ....*
gi 1867174023  185 FDDQD 189
Cdd:cd10551    150 FGDLD 154
PRK06273 PRK06273
ferredoxin; Provisional
 111-183 4.29e-04

ferredoxin; Provisional


Pssm-ID: 235764 [Multi-domain]  Cd Length: 165  Bit Score: 42.00  E-value: 4.29e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1867174023  111 IDMDKCIACGTCAEKCPRKVTDEYNAGLGKRKAAYVKfpQAVPlkyVIDKDHCIYfekgkCRACEKFCPTQAV 183
Cdd:PRK06273    46 VFEELCIGCGGCANVCPTKAIEMIPVEPVKITEGYVK--TKIP---KIDYEKCVY-----CLYCHDFCPVFAL 108
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 601-634 4.39e-04

bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;


Pssm-ID: 234978 [Multi-domain]  Cd Length: 662  Bit Score: 44.07  E-value: 4.39e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1867174023  601 TKSALVVGGGIAGMTAALTLADQGYPVTLVERKD 634
Cdd:PRK01747   260 ARDAAIIGGGIAGAALALALARRGWQVTLYEADE 293
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 16-53 4.58e-04

FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 43.75  E-value: 4.58e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1867174023   16 VLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIGGAMS 53
Cdd:pfam12831    2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGMLT 39
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 110-179 4.72e-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: 39.16  E-value: 4.72e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  110 YIDMDKCIACGTCAEKCPrkvtdEYNAGLGKRKAAYVKFPQAVPLkyvidkDHCIyfekgKCRACEKFCP 179
Cdd:pfam13237    3 VIDPDKCIGCGRCTAACP-----AGLTRVGAIVERLEGEAVRIGV------WKCI-----GCGACVEACP 56
PRK12839 PRK12839
FAD-dependent oxidoreductase;
600-649 4.98e-04

FAD-dependent oxidoreductase;


Pssm-ID: 237223 [Multi-domain]  Cd Length: 572  Bit Score: 44.05  E-value: 4.98e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1867174023  600 VTKSALVVGGGIAGMTAALTLADQGYPVTLVERKDVLGGHgrklySTWDG 649
Cdd:PRK12839     7 HTYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGGA-----TAWSG 51
PRK08163 PRK08163
3-hydroxybenzoate 6-monooxygenase;
15-51 5.11e-04

3-hydroxybenzoate 6-monooxygenase;


Pssm-ID: 181262 [Multi-domain]  Cd Length: 396  Bit Score: 43.49  E-value: 5.11e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1867174023   15 SVLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIG--GA 51
Cdd:PRK08163     6 PVLIVGGGIGGLAAALALARQGIKVKLLEQAAEIGeiGA 44
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 16-53 5.15e-04

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 43.67  E-value: 5.15e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1867174023   16 VLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIGG--AMS 53
Cdd:COG1053      6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGhtAAA 45
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 110-127 5.40e-04

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: 38.00  E-value: 5.40e-04
                           10
                   ....*....|....*...
gi 1867174023  110 YIDMDKCIACGTCAEKCP 127
Cdd:pfam00037    2 VIDEEKCIGCGACVEVCP 19
ndhI CHL00014
NADH dehydrogenase subunit I
 79-180 5.60e-04

NADH dehydrogenase subunit I


Pssm-ID: 214334 [Multi-domain]  Cd Length: 167  Bit Score: 41.67  E-value: 5.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023   79 HLN---IQIHTLSEvKDITGEagSFQAKIfqrarYIDMDKCIACGTCAEKCP--RKVTD-EYNAGLGKRKAayvkfpqav 152
Cdd:CHL00014    29 HANrlpVTIQYPYE-KLITSE--RFRGRI-----HFEFDKCIACEVCVRVCPidLPVVDwKLETDIRKKRL--------- 91

                           90       100
                   ....*....|....*....|....*...
gi 1867174023  153 pLKYVIDKDHCIYfekgkCRACEKFCPT 180
Cdd:CHL00014    92 -LNYSIDFGVCIF-----CGNCVEYCPT 113
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
111-187 6.72e-04

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 42.61  E-value: 6.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  111 IDMDKCIACGTCAEKCPRKVTDeynagLGKRKAAYvkfpqavplkYVidkdHCIYFEKGK------------CRACEKFC 178
Cdd:PRK07118   165 VDEDKCTGCGACVKACPRNVIE-----LIPKSARV----------FV----ACNSKDKGKavkkvcevgcigCGKCVKAC 225


                   ....*....
gi 1867174023  179 PTQAVNFDD 187
Cdd:PRK07118   226 PAGAITMEN 234
PRK12409 PRK12409
D-amino acid dehydrogenase small subunit; Provisional
 602-632 7.03e-04

D-amino acid dehydrogenase small subunit; Provisional


Pssm-ID: 237093 [Multi-domain]  Cd Length: 410  Bit Score: 43.09  E-value: 7.03e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1867174023  602 KSALVVGGGIAGMTAALTLADQGYPVTLVER 632
Cdd:PRK12409     2 SHIAVIGAGITGVTTAYALAQRGYQVTVFDR 32
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 110-130 7.28e-04

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 40.46  E-value: 7.28e-04
                           10        20
                   ....*....|....*....|.
gi 1867174023  110 YIDMDKCIACGTCAEKCPRKV 130
Cdd:cd10549    104 VIDKEKCIGCGICAEVCPVNA 124
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 603-682 7.51e-04

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: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 39.11  E-value: 7.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  603 SALVVGGGIAGMTAALTLADQGYPVTLVERKDVLgghGRKLystwDGQPVAPFLDELIKRveahpEITVLTKARITDVQG 682
Cdd:pfam00070    1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRL---LPGF----DPEIAKILQEKLEKN-----GIEFLLNTTVEAIEG 68
NapF COG1145
Ferredoxin [Energy production and conversion];
963-1000 8.70e-04

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 42.40  E-value: 8.70e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1867174023  963 PFGAIDYLEREGKCEVNQALCKGCGTCAATCPSEAITL 1000
Cdd:COG1145    195 PTGAIRLKDGKPQIVVDPDKCIGCGACVKVCPVGAISL 232
porD PRK09624
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
 969-1001 9.22e-04

pyruvate ferredoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 170017 [Multi-domain]  Cd Length: 105  Bit Score: 39.63  E-value: 9.22e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1867174023  969 YLEREGKCEVNQALCKGCGTCAATCPSEAITLL 1001
Cdd:PRK09624    69 YLDEEGYPVFDYDYCKGCGICANECPTKAIEMV 101
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 110-127 9.58e-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: 38.57  E-value: 9.58e-04
                           10
                   ....*....|....*...
gi 1867174023  110 YIDMDKCIACGTCAEKCP 127
Cdd:COG1143     31 VIDPDKCIGCGLCVEVCP 48
PRK06475 PRK06475
FAD-binding protein;
14-92 1.01e-03

FAD-binding protein;


Pssm-ID: 180582 [Multi-domain]  Cd Length: 400  Bit Score: 42.89  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023   14 GSVLVVGGGIAGVQAALDLADTGYFVHLIEKT---SAIGGAMSMLDKtfptddcAMUILS-----PKLVEVGrhlnIQIH 85
Cdd:PRK06475     3 GSPLIAGAGVAGLSAALELAARGWAVTIIEKAqelSEVGAGLQLAPN-------AMRHLErlgvaDRLSGTG----VTPK 71


                   ....*..
gi 1867174023   86 TLsEVKD 92
Cdd:PRK06475    72 AL-YLMD 77
TrmFO COG1206
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ...
 606-631 1.02e-03

Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and biogenesis]; Folate-dependent tRNA-U54 methylase TrmFO/GidA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440819  Cd Length: 436  Bit Score: 42.74  E-value: 1.02e-03
                           10        20
                   ....*....|....*....|....*.
gi 1867174023  606 VVGGGIAGMTAALTLADQGYPVTLVE 631
Cdd:COG1206      6 VIGGGLAGSEAAWQLAERGVPVRLYE 31
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
609-639 1.09e-03

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 42.26  E-value: 1.09e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1867174023  609 GGIAGMTAALTLADQGYPVTLVERKDVLGGH 639
Cdd:COG0644      1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDK 31
PRK08274 PRK08274
FAD-dependent tricarballylate dehydrogenase TcuA;
605-661 1.17e-03

FAD-dependent tricarballylate dehydrogenase TcuA;


Pssm-ID: 236214 [Multi-domain]  Cd Length: 466  Bit Score: 42.55  E-value: 1.17e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  605 LVVGGGIAGMTAALTLADQGYPVTLVER--KDVLGG---HGRKLYSTWDG-QPVAP-------FLDELIK 661
Cdd:PRK08274     8 LVIGGGNAALCAALAAREAGASVLLLEAapREWRGGnsrHTRNLRCMHDApQDVLVgaypeeeFWQDLLR 77
PLN02487 PLN02487
zeta-carotene desaturase
 606-638 1.45e-03

zeta-carotene desaturase


Pssm-ID: 215268 [Multi-domain]  Cd Length: 569  Bit Score: 42.48  E-value: 1.45e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1867174023  606 VVGGGIAGMTAALTLADQGYPVTLVERKDVLGG 638
Cdd:PLN02487    80 IIGAGLAGMSTAVELLDQGHEVDIYESRPFIGG 112
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 111-188 1.46e-03

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: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  111 IDMDK--CIACGTCAEKCPRKVTDeynaglgkrkaayVKFPQAVPLKYVIDkDHCIYFEKGKCRACEKFCPTQAVNFDDQ 188
Cdd:cd10564     40 LDFSRgeCTFCGACAEACPEGALD-------------PAREAPWPLRAEIG-DSCLALQGVECRSCQDACPTQAIRFRPR 105
PRK06475 PRK06475
FAD-binding protein;
600-636 1.48e-03

FAD-binding protein;


Pssm-ID: 180582 [Multi-domain]  Cd Length: 400  Bit Score: 42.12  E-value: 1.48e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1867174023  600 VTKSALVVGGGIAGMTAALTLADQGYPVTLVERKDVL 636
Cdd:PRK06475     1 TRGSPLIAGAGVAGLSAALELAARGWAVTIIEKAQEL 37
PRK12842 PRK12842
putative succinate dehydrogenase; Reviewed
 605-638 1.54e-03

putative succinate dehydrogenase; Reviewed


Pssm-ID: 237224 [Multi-domain]  Cd Length: 574  Bit Score: 42.37  E-value: 1.54e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1867174023  605 LVVGGGIAGMTAALTLADQGYPVTLVERKDVLGG 638
Cdd:PRK12842    13 LVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGG 46
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 110-180 1.59e-03

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 40.32  E-value: 1.59e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1867174023  110 YIDMDKCIA------CGTCAEKCPRKvtdeynaglgkrkaAYVKFPQAVPLKYVIDKDHCIyfekGkCRACEKFCPT 180
Cdd:cd16373     87 VIDKDRCLAwqggtdCGVCVEACPTE--------------AIAIVLEDDVLRPVVDEDKCV----G-CGLCEYVCPV 144
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 963-1002 1.75e-03

HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 39.94  E-value: 1.75e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1867174023  963 PFGAIDYleREGKCEVNQALCKGCGTCAATCPSEAITLLG 1002
Cdd:cd10554     69 PVGAISQ--EDGVVQVDEERCIGCKLCVLACPFGAIEMAP 106
PRK06134 PRK06134
putative FAD-binding dehydrogenase; Reviewed
 605-638 1.77e-03

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 180419 [Multi-domain]  Cd Length: 581  Bit Score: 42.01  E-value: 1.77e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1867174023  605 LVVGGGIAGMTAALTLADQGYPVTLVERKDVLGG 638
Cdd:PRK06134    16 LVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGG 49
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 940-1000 1.82e-03

bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 41.22  E-value: 1.82e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1867174023  940 AGGVVAVVNKDLCCGCQGCVQCCPFGAIdyLEREGKCEVNQALCKGCGTCAATCPSEAITL 1000
Cdd:cd03110     54 VGGKKAFIDQEKCIRCGNCERVCKFGAI--LEFFQKLIVDESLCEGCGACVIICPRGAIYL 112
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 963-1000 1.88e-03

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 39.30  E-value: 1.88e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1867174023  963 PFGAIDyLEREGKC----EVNQALCKGCGTCAATCPSEAITL 1000
Cdd:cd10549     19 PTDAIE-LGPNGAIargpEIDEDKCVFCGACVEVCPTGAIEL 59
PRK07121 PRK07121
FAD-binding protein;
16-54 1.94e-03

FAD-binding protein;


Pssm-ID: 180854 [Multi-domain]  Cd Length: 492  Bit Score: 41.80  E-value: 1.94e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1867174023   16 VLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIGGAMSM 54
Cdd:PRK07121    23 VVVVGFGAAGACAAIEAAAAGARVLVLERAAGAGGATAL 61
HI0933_like pfam03486
HI0933-like protein;
604-641 2.07e-03

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 41.80  E-value: 2.07e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1867174023  604 ALVVGGGIAGMTAALTLADQGYPVTLVERKDVLG------GHGR 641
Cdd:pfam03486    3 VIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGrkilisGGGR 46
PLN02487 PLN02487
zeta-carotene desaturase
 15-57 2.24e-03

zeta-carotene desaturase


Pssm-ID: 215268 [Multi-domain]  Cd Length: 569  Bit Score: 41.71  E-value: 2.24e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1867174023   15 SVLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIGGAM-SMLDK 57
Cdd:PLN02487    77 KVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGGKVgSFVDK 120
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 602-652 2.32e-03

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 41.76  E-value: 2.32e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1867174023  602 KSALVVGGGIAGMTAALTLADQGYP--VTLVERKDVLGGhgrKLYS-TWDGQPV 652
Cdd:PRK11883     1 KKVAIIGGGITGLSAAYRLHKKGPDadITLLEASDRLGG---KIQTvRKDGFPI 51
PRK12844 PRK12844
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 596-638 2.40e-03

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 183787 [Multi-domain]  Cd Length: 557  Bit Score: 41.66  E-value: 2.40e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1867174023  596 MQLGVTKSALVVGGGIAGMTAALTLADQGYPVTLVERKDVLGG 638
Cdd:PRK12844     1 ATWDETYDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGG 43
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 107-127 2.53e-03

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 37.71  E-value: 2.53e-03
                           10        20
                   ....*....|....*....|.
gi 1867174023  107 RARYIDMDKCIACGTCAEKCP 127
Cdd:COG4231     44 GKAVIDPDLCIGCGSCVQVCP 64
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
110-187 2.66e-03

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 39.26  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  110 YIDMDKCIACGTCAEKCPRKV--TDEYNaglgkrkaayvkfPQAVPLKYvidkDHCIYFEKGkcRACEKFCPTQAVNFDD 187
Cdd:COG1142     77 VVDEEKCIGCGLCVLACPFGAitMVGEK-------------SRAVAVKC----DLCGGREGG--PACVEACPTGALRLVD 137
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
16-51 2.67e-03

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 41.43  E-value: 2.67e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1867174023   16 VLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIGGA 51
Cdd:COG0665      5 VVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGSGA 40
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 601-635 2.71e-03

tRNA (uracil-5-)-methyltransferase Gid; Reviewed


Pssm-ID: 235416  Cd Length: 436  Bit Score: 41.28  E-value: 2.71e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1867174023  601 TKSALVVGGGIAGMTAALTLADQGYPVTLVERKDV 635
Cdd:PRK05335     2 MKPVNVIGAGLAGSEAAWQLAKRGVPVELYEMRPV 36
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 116-182 2.89e-03

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


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 36.74  E-value: 2.89e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1867174023  116 CIACGTCAEKCPRKVTDEYNAGLGKRKAayvkfpqavplKYVIDKDHCIYfekgkCRACEKFCPTQA 182
Cdd:pfam12838    1 CIGCGACVAACPVGAITLDEVGEKKGTK-----------TVVIDPERCVG-----CGACVAVCPTGA 51
PRK07538 PRK07538
hypothetical protein; Provisional
 604-631 3.10e-03

hypothetical protein; Provisional


Pssm-ID: 236046 [Multi-domain]  Cd Length: 413  Bit Score: 41.04  E-value: 3.10e-03
                           10        20
                   ....*....|....*....|....*...
gi 1867174023  604 ALVVGGGIAGMTAALTLADQGYPVTLVE 631
Cdd:PRK07538     3 VLIAGGGIGGLTLALTLHQRGIEVVVFE 30
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 963-1000 3.12e-03

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 37.00  E-value: 3.12e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1867174023  963 PFGAIdYLEREGK--CEVNQALCKGCGTCAATCPSEAITL 1000
Cdd:COG1146     21 PVDVL-ELDEEGKkaLVINPEECIGCGACELVCPVGAITV 59
PLN02268 PLN02268
probable polyamine oxidase
 15-50 3.13e-03

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 41.21  E-value: 3.13e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1867174023   15 SVLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIGG 50
Cdd:PLN02268     2 SVIVIGGGIAGIAAARALHDASFKVTLLESRDRIGG 37
PRK07236 PRK07236
hypothetical protein; Provisional
 604-632 3.18e-03

hypothetical protein; Provisional


Pssm-ID: 235980 [Multi-domain]  Cd Length: 386  Bit Score: 41.06  E-value: 3.18e-03
                           10        20
                   ....*....|....*....|....*....
gi 1867174023  604 ALVVGGGIAGMTAALTLADQGYPVTLVER 632
Cdd:PRK07236     9 AVVIGGSLGGLFAALLLRRAGWDVDVFER 37
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 110-183 3.38e-03

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 39.16  E-value: 3.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  110 YIDMDK--CIACGT-CAEKCP-----RKVTDEYNAGLGKrkaayvkfpqAVplkyvIDKDHCI-YFEKGKCRACEKFCPT 180
Cdd:cd16373     47 YLDPREgpCDLCCDaCVEVCPtgalrPLDLEEQKVKMGV----------AV-----IDKDRCLaWQGGTDCGVCVEACPT 111


                   ...
gi 1867174023  181 QAV 183
Cdd:cd16373    112 EAI 114
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
 4-50 3.48e-03

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 41.30  E-value: 3.48e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1867174023    4 ATRTASSNPiGSVLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIGG 50
Cdd:PTZ00306   401 KKRIAGSLP-ARVIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGG 446
PRK12843 PRK12843
FAD-dependent oxidoreductase;
605-638 3.68e-03

FAD-dependent oxidoreductase;


Pssm-ID: 237225 [Multi-domain]  Cd Length: 578  Bit Score: 41.26  E-value: 3.68e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1867174023  605 LVVGGGIAGMTAALTLADQGYPVTLVERKDVLGG 638
Cdd:PRK12843    20 IVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGG 53
PRK07208 PRK07208
hypothetical protein; Provisional
 15-50 3.70e-03

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 41.03  E-value: 3.70e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1867174023   15 SVLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIGG 50
Cdd:PRK07208     6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGG 41
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 977-1000 4.43e-03

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 38.53  E-value: 4.43e-03
                           10        20
                   ....*....|....*....|....
gi 1867174023  977 EVNQALCKGCGTCAATCPSEAITL 1000
Cdd:cd10549      2 KYDPEKCIGCGICVKACPTDAIEL 25
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 977-999 4.49e-03

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: 35.30  E-value: 4.49e-03
                           10        20
                   ....*....|....*....|...
gi 1867174023  977 EVNQALCKGCGTCAATCPSEAIT 999
Cdd:pfam00037    2 VIDEEKCIGCGACVEVCPVGAIT 24
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 110-185 4.58e-03

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


Pssm-ID: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 38.70  E-value: 4.58e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1867174023  110 YIDMDKCIACGTCAEKCPrkvtdeYNAglgkrkaayvkfPQAVPLKYVIDK-DHCI-YFEKGKCRACEKFCPTQAVNF 185
Cdd:cd16371     80 VVDQDKCIGCGYCVWACP------YGA------------PQYNPETGKMDKcDMCVdRLDEGEKPACVAACPTRALDF 139
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
7-57 5.03e-03

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 40.27  E-value: 5.03e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023    7 TASSNPIGSVLVVGGGIAGVQAALDLADTGYFVHLIE--------KTSA-IGGAMSMLDK 57
Cdd:PRK07494     1 SLMEKEHTDIAVIGGGPAGLAAAIALARAGASVALVApeppyadlRTTAlLGPSIRFLER 60
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 16-49 5.27e-03

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 40.31  E-value: 5.27e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1867174023   16 VLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIG 49
Cdd:COG0654      6 VLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
111-190 5.83e-03

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 37.62  E-value: 5.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  111 IDMDKCIACGTCAEKCPrkvtdeynaglgkRKAAYVKfpqavPLKYV-IDKDHCiyfeKGkCRACEKFCPTQAVNFDDQD 189
Cdd:PRK09623    48 VDESKCVKCYICWKFCP-------------EPAIYIK-----EDGYVaIDYDYC----KG-CGICANECPTKAITMVKEE 104


                   .
gi 1867174023  190 R 190
Cdd:PRK09623   105 K 105
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
16-101 6.00e-03

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 39.90  E-value: 6.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023   16 VLVVGGGIAGVQAALDLADTGYFVHLIEKTSAIGGAMSMLDKTfptddcamuiLSP----KLVEVGRHLNIQIHTLSEVK 91
Cdd:pfam13738  158 VVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRDSDPSYS----------LSPdtlnRLEELVKNGKIKAHFNAEVK 227

                           90
                   ....*....|
gi 1867174023   92 DITGEAGSFQ 101
Cdd:pfam13738  228 EITEVDVSYK 237
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
 974-1000 6.19e-03

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 38.86  E-value: 6.19e-03
                           10        20
                   ....*....|....*....|....*..
gi 1867174023  974 GKCEVNQALCKGCGTCAATCPSEAITL 1000
Cdd:PRK12387    31 GKPEYNPQQCIGCAACVNACPSNALTV 57
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
963-1000 6.22e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 39.92  E-value: 6.22e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1867174023  963 PFGAIdYLErEGKCEVNQALCKGCGTCAATCPSEAITL 1000
Cdd:PRK07118   152 PFDAI-HIE-NGLPVVDEDKCTGCGACVKACPRNVIEL 187
PRK06185 PRK06185
FAD-dependent oxidoreductase;
596-667 6.45e-03

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 40.23  E-value: 6.45e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1867174023  596 MQLGVTKSALVVGGGIAGMTAALTLADQGYPVTLVERkdvlggHGRKLYStWDGQPVAP----FLDE--LIKRVEAHP 667
Cdd:PRK06185     1 MAEVETTDCCIVGGGPAGMMLGLLLARAGVDVTVLEK------HADFLRD-FRGDTVHPstleLMDElgLLERFLELP 71
glycerol3P_GlpB TIGR03378
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ...
 605-667 6.57e-03

glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are the B subunit, product of the glpB gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase. [Energy metabolism, Anaerobic]


Pssm-ID: 213807  Cd Length: 419  Bit Score: 40.00  E-value: 6.57e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1867174023  605 LVVGGGIAGMTAALTLADQGYPVTLVERK-----------DVLGghgrklySTWDGQPV-APF--LDELIKRVEAHP 667
Cdd:TIGR03378    4 IIIGGGLAGLSCALRLAEAGKKCAIIAAGqsalhfssgslDLLS-------RLPDGQAVeQPMdaLEALAQQAPEHP 73
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
963-999 7.44e-03

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 37.71  E-value: 7.44e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1867174023  963 PFGAIDYleREGKCEVNQALCKGCGTCAATCPSEAIT 999
Cdd:COG1142     65 PVGAITR--DDGAVVVDEEKCIGCGLCVLACPFGAIT 99
PRK06126 PRK06126
hypothetical protein; Provisional
 596-635 8.29e-03

hypothetical protein; Provisional


Pssm-ID: 235704 [Multi-domain]  Cd Length: 545  Bit Score: 39.98  E-value: 8.29e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1867174023  596 MQLGVTKSALVVGGGIAGMTAALTLADQGYPVTLVERKDV 635
Cdd:PRK06126     2 MENTSETPVLIVGGGPVGLALALDLGRRGVDSILVERKDG 41
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
111-188 8.59e-03

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 39.84  E-value: 8.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867174023  111 IDMDKCIACGTCAEKCPrkvtdeYNAglgkrkaayvkfpqavplkYVIDKDHCIYFEKGKCR---ACEKFCPTQAVNF-- 185
Cdd:COG1148    493 VDPEKCTGCGRCVEVCP------YGA-------------------ISIDEKGVAEVNPALCKgcgTCAAACPSGAISLkg 547


                   ....*
gi 1867174023  186 --DDQ 188
Cdd:COG1148    548 ftDDQ 552
PRK08401 PRK08401
L-aspartate oxidase; Provisional
 595-630 8.94e-03

L-aspartate oxidase; Provisional


Pssm-ID: 236259 [Multi-domain]  Cd Length: 466  Bit Score: 39.78  E-value: 8.94e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1867174023  595 EMQLGVtksalvVGGGIAGMTAALTLADQGYPVTLV 630
Cdd:PRK08401     1 MMKVGI------VGGGLAGLTAAISLAKKGFDVTII 30
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 111-189 9.63e-03

bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 38.91  E-value: 9.63e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1867174023  111 IDMDKCIACGTCAEKCprkvtdeynaglgkRKAAYVKFPQAVPlkyvIDKDHCiyfeKGkCRACEKFCPTQAVNFDDQD 189
Cdd:cd03110     61 IDQEKCIRCGNCERVC--------------KFGAILEFFQKLI----VDESLC----EG-CGACVIICPRGAIYLKDRD 116
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
109-182 9.93e-03

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 37.94  E-value: 9.93e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1867174023  109 RYIDMD-KCIACGTCAEKCPR---KVTDEYNAGlGKRKaayvkfpqavPLKYVIDKDHCIYfekgkCRACEKFCPTQA 182
Cdd:PRK05888    52 RDPNGEeRCIACKLCAAICPAdaiTIEAAERED-GRRR----------TTRYDINFGRCIF-----CGFCEEACPTDA 113
 
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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