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Conserved domains on  [gi|499818471|ref|WP_011499205|]
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indolepyruvate ferredoxin oxidoreductase subunit alpha [Methanococcoides burtonii]

Protein Classification

indolepyruvate ferredoxin oxidoreductase subunit alpha( domain architecture ID 11496621)

indolepyruvate ferredoxin oxidoreductase subunit alpha is part of the heterodimer enzyme complex that catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IOR_alpha TIGR03336
indolepyruvate ferredoxin oxidoreductase, alpha subunit; Indolepyruvate ferredoxin ...
 3-596 0e+00

indolepyruvate ferredoxin oxidoreductase, alpha subunit; Indolepyruvate ferredoxin oxidoreductase (IOR) is an alpha 2/beta 2 tetramer related to ketoacid oxidoreductases for pyruvate (1.2.7.1, POR), 2-ketoglutarate (1.2.7.3, KOR), and 2-oxoisovalerate (1.2.7.7, VOR). These multi-subunit enzymes typically are found in anaerobes and are inactiviated by oxygen. IOR in Pyrococcus acts in fermentation of all three aromatic amino acids, following removal of the amino group by transamination. In Methanococcus maripaludis, by contrast, IOR acts in the opposite direction, in pathways of amino acid biosynthesis from phenylacetate, indoleacetate, and p-hydroxyphenylacetate. In M. maripaludis and many other species, iorA and iorB are found next to an apparent phenylacetate-CoA ligase.


:

Pssm-ID: 274526 [Multi-domain]  Cd Length: 595  Bit Score: 1057.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471    3 TREYMLGNVAIARGIVEGGGRVISGYPGTPSSEIVDTLSKMKERD-FYVEWSVNEKVAMEVAAGAGMTGVRSVVTMKHVG 81
Cdd:TIGR03336   1 MKELLLGNEAIARGALEAGVGVAAAYPGTPSSEITDTLAKVAKRAgVYFEWSVNEKVAVEVAAGAAWSGLRAFCTMKHVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471   82 LNVAADPLMTLSYMGVKGGMVVIVADDPGCHSSQNEQDSRIYSEFSLMPCLDPSTPQEAKDMIPYAFELSEKFELPVIFR 161
Cdd:TIGR03336  81 LNVAADPLMTLAYTGVKGGLVVVVADDPSMHSSQNEQDTRHYAKFAKIPCLEPSTPQEAKDMVKYAFELSEKFGLPVILR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  162 PTTRISHGKADIELGEITDHRVEAKFEKDPSRWVMVPSNAVVRHPHLLSIQDGIQEELEISPWNELTINEAsRIGVIAAG 241
Cdd:TIGR03336 161 PTTRISHMRGDVELGEIPKEEVVKGFEKDPERYVMVPAIARVRHKKLLSKQHKLREELNESPLNRLEINGA-KIGVIASG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  242 IASVYAKEAIDNLGVSASYLKIG-AYPVPEGLIKRMYEQVDTVLVIEELEPIVEDRCKIIAKDMESSIKIIGKTDGTVPR 320
Cdd:TIGR03336 240 IAYNYVKEALERLGVDVSVLKIGfTYPVPEGLVEEFLSGVEEVLVVEELEPVVEEQVKALAGTAGLNIKVHGKEDGFLPR 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  321 VGELNVDHCVKAIADvFKIESGLPVIKEIEMELPLRPPAMCAGCSHRATYYAMKKVFGKNAVFPGDIGCYTLGIQ--NGT 398
Cdd:TIGR03336 320 EGELNPDIVVNALAK-FGLAPSVTHEKPVPKPLPVRPPSLCAGCPHRATFYAMKKVADREAIFPSDIGCYTLGIQppLGT 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  399 VDTTLCMGGSITVASGIYHSGEKQPICCSIGDSTFFHTGMNGLLNAVYNKANITVAILDNRITAMTGHQPNPGMGLTSTG 478
Cdd:TIGR03336 399 VDTTLCMGASIGVASGLSKAGEKQRIVAFIGDSTFFHTGIPGLINAVYNKANITVVILDNRITAMTGHQPNPGTGVTGMG 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  479 ETTKEIDLEQLCRGLGAEFVEVVDSFDVNATVEAFKRAKDYEGTSVIISKQPCIIYARRTGIRLTPFKVDHDKCVGCRMC 558
Cdd:TIGR03336 479 EATKEISIEELCRASGVEFVEVVDPLNVKETIEVFKAALAAEGVSVIIAKQPCVLSNKRAGKRAGPYKVDQDKCIGCKKC 558

                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 499818471  559 VN-LGCPAIEfdKENKKSTINATCTGCGLCAEVCKFDAI 596
Cdd:TIGR03336 559 IKeLGCPAIE--PEDKEAVIDPLCTGCGVCAQICPFDAI 595
 
Name Accession Description Interval E-value
IOR_alpha TIGR03336
indolepyruvate ferredoxin oxidoreductase, alpha subunit; Indolepyruvate ferredoxin ...
 3-596 0e+00

indolepyruvate ferredoxin oxidoreductase, alpha subunit; Indolepyruvate ferredoxin oxidoreductase (IOR) is an alpha 2/beta 2 tetramer related to ketoacid oxidoreductases for pyruvate (1.2.7.1, POR), 2-ketoglutarate (1.2.7.3, KOR), and 2-oxoisovalerate (1.2.7.7, VOR). These multi-subunit enzymes typically are found in anaerobes and are inactiviated by oxygen. IOR in Pyrococcus acts in fermentation of all three aromatic amino acids, following removal of the amino group by transamination. In Methanococcus maripaludis, by contrast, IOR acts in the opposite direction, in pathways of amino acid biosynthesis from phenylacetate, indoleacetate, and p-hydroxyphenylacetate. In M. maripaludis and many other species, iorA and iorB are found next to an apparent phenylacetate-CoA ligase.


Pssm-ID: 274526 [Multi-domain]  Cd Length: 595  Bit Score: 1057.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471    3 TREYMLGNVAIARGIVEGGGRVISGYPGTPSSEIVDTLSKMKERD-FYVEWSVNEKVAMEVAAGAGMTGVRSVVTMKHVG 81
Cdd:TIGR03336   1 MKELLLGNEAIARGALEAGVGVAAAYPGTPSSEITDTLAKVAKRAgVYFEWSVNEKVAVEVAAGAAWSGLRAFCTMKHVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471   82 LNVAADPLMTLSYMGVKGGMVVIVADDPGCHSSQNEQDSRIYSEFSLMPCLDPSTPQEAKDMIPYAFELSEKFELPVIFR 161
Cdd:TIGR03336  81 LNVAADPLMTLAYTGVKGGLVVVVADDPSMHSSQNEQDTRHYAKFAKIPCLEPSTPQEAKDMVKYAFELSEKFGLPVILR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  162 PTTRISHGKADIELGEITDHRVEAKFEKDPSRWVMVPSNAVVRHPHLLSIQDGIQEELEISPWNELTINEAsRIGVIAAG 241
Cdd:TIGR03336 161 PTTRISHMRGDVELGEIPKEEVVKGFEKDPERYVMVPAIARVRHKKLLSKQHKLREELNESPLNRLEINGA-KIGVIASG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  242 IASVYAKEAIDNLGVSASYLKIG-AYPVPEGLIKRMYEQVDTVLVIEELEPIVEDRCKIIAKDMESSIKIIGKTDGTVPR 320
Cdd:TIGR03336 240 IAYNYVKEALERLGVDVSVLKIGfTYPVPEGLVEEFLSGVEEVLVVEELEPVVEEQVKALAGTAGLNIKVHGKEDGFLPR 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  321 VGELNVDHCVKAIADvFKIESGLPVIKEIEMELPLRPPAMCAGCSHRATYYAMKKVFGKNAVFPGDIGCYTLGIQ--NGT 398
Cdd:TIGR03336 320 EGELNPDIVVNALAK-FGLAPSVTHEKPVPKPLPVRPPSLCAGCPHRATFYAMKKVADREAIFPSDIGCYTLGIQppLGT 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  399 VDTTLCMGGSITVASGIYHSGEKQPICCSIGDSTFFHTGMNGLLNAVYNKANITVAILDNRITAMTGHQPNPGMGLTSTG 478
Cdd:TIGR03336 399 VDTTLCMGASIGVASGLSKAGEKQRIVAFIGDSTFFHTGIPGLINAVYNKANITVVILDNRITAMTGHQPNPGTGVTGMG 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  479 ETTKEIDLEQLCRGLGAEFVEVVDSFDVNATVEAFKRAKDYEGTSVIISKQPCIIYARRTGIRLTPFKVDHDKCVGCRMC 558
Cdd:TIGR03336 479 EATKEISIEELCRASGVEFVEVVDPLNVKETIEVFKAALAAEGVSVIIAKQPCVLSNKRAGKRAGPYKVDQDKCIGCKKC 558

                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 499818471  559 VN-LGCPAIEfdKENKKSTINATCTGCGLCAEVCKFDAI 596
Cdd:TIGR03336 559 IKeLGCPAIE--PEDKEAVIDPLCTGCGVCAQICPFDAI 595
TPP_IOR_alpha cd02008
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ...
 356-531 2.61e-90

Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.


Pssm-ID: 238966 [Multi-domain]  Cd Length: 178  Bit Score: 276.47  E-value: 2.61e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 356 RPPAMCAGCSHRATYYAMKKVFGKNAVFPGDIGCYTLGIQNG--TVDTTLCMGGSITVASGIYHSGEKQPICCSIGDSTF 433
Cdd:cd02008    2 RPPGLCPGCPHRPSFYALRKAFKKDSIVSGDIGCYTLGALPPlnAIDTCTCMGASIGVAIGMAKASEDKKVVAVIGDSTF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 434 FHTGMNGLLNAVYNKANITVAILDNRITAMTGHQPNPGMGLTSTGETTKeIDLEQLCRGLGAEFVEVVDSFDVNATVEAF 513
Cdd:cd02008   82 FHSGILGLINAVYNKANITVVILDNRTTAMTGGQPHPGTGKTLTEPTTV-IDIEALVRAIGVKRVVVVDPYDLKAIREEL 160

                        170
                 ....*....|....*...
gi 499818471 514 KRAKDYEGTSVIISKQPC 531
Cdd:cd02008  161 KEALAVPGVSVIIAKRPC 178
PRK13030 PRK13030
indolepyruvate ferredoxin oxidoreductase family protein;
14-589 7.43e-35

indolepyruvate ferredoxin oxidoreductase family protein;


Pssm-ID: 237279 [Multi-domain]  Cd Length: 1159  Bit Score: 141.27  E-value: 7.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471   14 ARGIVEGGgrVISGYPGTPSSEIVDTLSKMKER----DFYVEWSVNEKVA------MEVAAGAGMTGVRSVVTM---KHV 80
Cdd:PRK13030   39 ARGLNTAG--FVSGYRGSPLGGVDQALWKAKKLldasDIRFLPGINEELAatavlgTQQVEADPERTVDGVFAMwygKGP 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471   81 GLNVAADPLMTLSYMGV--KGGMVVIVADDPGCHSS----QneqdsriySEFSL----MPCLDPSTPQEAKDMIPYAFEL 150
Cdd:PRK13030  117 GVDRAGDALKHGNAYGSspHGGVLVVAGDDHGCVSSsmphQ--------SDFALiawhMPVLNPANVQEYLDFGLYGWAL 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  151 SEKFELPVIFRPTTRISHGKADIELGEitdhrvEAKFEKDPSRWVMVPSNAVVRHPHLLS--IQDGIQEELE-------I 221
Cdd:PRK13030  189 SRYSGAWVGFKAISETVESGSTVDLDP------DRTRWPAPEDFTPPAGGLHNRWPDLPSlaIEARLAAKLPavrafarA 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  222 SPWNELTI-NEASRIGVIAAGIASVYAKEAIDNLGVSA--------SYLKIGA-YPVPEGLIKRMYEQVDTVLVIEELEP 291
Cdd:PRK13030  263 NSIDRWVApSPDARVGIVTCGKAHLDLMEALRRLGLDDadlraagiRIYKVGLsWPLEPTRLREFADGLEEILVIEEKRP 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  292 IVEDRCKIIAKDMESSI--KIIGKTD--GT--VPRVGELNVDHCVKAIA----DVFKIESG--------LPVIKEIEMEL 353
Cdd:PRK13030  343 VIEQQIKDYLYNRPGGArpRVVGKHDedGAplLSELGELRPSLIAPVLAarlaRHKPALDRrarvvdlvAPQILSNEADA 422

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  354 PLRPPAMCAGCSHRATyyamKKVFGKNAVFPGdIGCYTLGI-QNGTVDTTLCMGGSITVASGIYHSGEKQPICCSIGDST 432
Cdd:PRK13030  423 VVRTPYFCSGCPHNTS----TKVPEGSIAQAG-IGCHFMASwMDRDTTGLTQMGGEGVDWIGHAPFTETKHVFQNLGDGT 497

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  433 FFHTGMNGLLNAVYNKANITVAILDNRITAMTGHQPNPGmgltstgettkEIDLEQLCRGLGAEFVE--VVDSFDVN--- 507
Cdd:PRK13030  498 YFHSGSLAIRQAVAAGANITYKILYNDAVAMTGGQPVDG-----------SISVPQIARQVEAEGVSriVVVSDEPEkyr 566

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  508 -----ATVEAFKRA---------KDYEGTSVIISKQPCIIYARRTGIRltpfkvdhdkcvGcrmcvnlgcpaiEFDKENK 573
Cdd:PRK13030  567 ghhlpAGVTVHHRDeldavqrelRETPGVTVLIYDQTCAAEKRRRRKR------------G------------EFPDPDR 622

                         650
                  ....*....|....*..
gi 499818471  574 KSTIN-ATCTGCGLCAE 589
Cdd:PRK13030  623 RLFINeAVCEGCGDCGV 639
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
386-526 1.28e-22

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 94.19  E-value: 1.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  386 DIGCYTLGIQ--------NGTVDTTL--CMGGSITVASGIYHSGEKQPICCSIGDSTFFHTgMNGLLNAVYNKANITVAI 455
Cdd:pfam02775   1 DIGCHQMWAAqyyrfrppRRYLTSGGlgTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMN-LQELATAVRYNLPITVVV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499818471  456 LDNRITAMTGHQPNPGMGLTSTGET---TKEIDLEQLCRGLGAEfVEVVDSFDvnATVEAFKRAKDYEGTSVII 526
Cdd:pfam02775  80 LNNGGYGMTRGQQTPFGGGRYSGPSgkiLPPVDFAKLAEAYGAK-GARVESPE--ELEEALKEALEHDGPALID 150
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 531-597 7.02e-18

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 78.16  E-value: 7.02e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499818471 531 CIIYARRTGIRltpFKVDHDKCVGCRMCVNLgCPAIEFDKENKKSTIN-ATCTGCGLCAEVCKFDAIK 597
Cdd:COG4231    6 KILDNRTTAMR---YVIDEDKCTGCGACVKV-CPADAIEEGDGKAVIDpDLCIGCGSCVQVCPVDAIK 69
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
 62-162 4.71e-03

Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.


Pssm-ID: 214865 [Multi-domain]  Cd Length: 136  Bit Score: 37.85  E-value: 4.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471    62 VAAGAGMTGVRSVVTMKHVGLNVAADPLMtlsyMGVK-GGMVVIVADDPG--------CHSSQneqdsRIYSEFSLMPCL 132
Cdd:smart00861  30 FAAGLALHGLRPVVEIFFTFFDRAKDQIR----SAGAsGNVPVVFRHDGGggvgedgpTHHSI-----EDEALLRAIPGL 100

                           90       100       110
                   ....*....|....*....|....*....|...
gi 499818471   133 D---PSTPQEAKDMIPYAFELSEKfelPVIFRP 162
Cdd:smart00861 101 KvvaPSDPAEAKGLLRAAIRDDGP---VVIRLE 130
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 544-584 7.56e-03

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 38.30  E-value: 7.56e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 499818471 544 PFKVDhDKCVGCRMCVNLgCPA--IEFdkENKKSTINATCTGC 584
Cdd:NF038196 180 KFHVT-DKCIGCGICAKV-CPVnnIEM--EDGKPVWGHNCTHC 218
 
Name Accession Description Interval E-value
IOR_alpha TIGR03336
indolepyruvate ferredoxin oxidoreductase, alpha subunit; Indolepyruvate ferredoxin ...
 3-596 0e+00

indolepyruvate ferredoxin oxidoreductase, alpha subunit; Indolepyruvate ferredoxin oxidoreductase (IOR) is an alpha 2/beta 2 tetramer related to ketoacid oxidoreductases for pyruvate (1.2.7.1, POR), 2-ketoglutarate (1.2.7.3, KOR), and 2-oxoisovalerate (1.2.7.7, VOR). These multi-subunit enzymes typically are found in anaerobes and are inactiviated by oxygen. IOR in Pyrococcus acts in fermentation of all three aromatic amino acids, following removal of the amino group by transamination. In Methanococcus maripaludis, by contrast, IOR acts in the opposite direction, in pathways of amino acid biosynthesis from phenylacetate, indoleacetate, and p-hydroxyphenylacetate. In M. maripaludis and many other species, iorA and iorB are found next to an apparent phenylacetate-CoA ligase.


Pssm-ID: 274526 [Multi-domain]  Cd Length: 595  Bit Score: 1057.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471    3 TREYMLGNVAIARGIVEGGGRVISGYPGTPSSEIVDTLSKMKERD-FYVEWSVNEKVAMEVAAGAGMTGVRSVVTMKHVG 81
Cdd:TIGR03336   1 MKELLLGNEAIARGALEAGVGVAAAYPGTPSSEITDTLAKVAKRAgVYFEWSVNEKVAVEVAAGAAWSGLRAFCTMKHVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471   82 LNVAADPLMTLSYMGVKGGMVVIVADDPGCHSSQNEQDSRIYSEFSLMPCLDPSTPQEAKDMIPYAFELSEKFELPVIFR 161
Cdd:TIGR03336  81 LNVAADPLMTLAYTGVKGGLVVVVADDPSMHSSQNEQDTRHYAKFAKIPCLEPSTPQEAKDMVKYAFELSEKFGLPVILR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  162 PTTRISHGKADIELGEITDHRVEAKFEKDPSRWVMVPSNAVVRHPHLLSIQDGIQEELEISPWNELTINEAsRIGVIAAG 241
Cdd:TIGR03336 161 PTTRISHMRGDVELGEIPKEEVVKGFEKDPERYVMVPAIARVRHKKLLSKQHKLREELNESPLNRLEINGA-KIGVIASG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  242 IASVYAKEAIDNLGVSASYLKIG-AYPVPEGLIKRMYEQVDTVLVIEELEPIVEDRCKIIAKDMESSIKIIGKTDGTVPR 320
Cdd:TIGR03336 240 IAYNYVKEALERLGVDVSVLKIGfTYPVPEGLVEEFLSGVEEVLVVEELEPVVEEQVKALAGTAGLNIKVHGKEDGFLPR 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  321 VGELNVDHCVKAIADvFKIESGLPVIKEIEMELPLRPPAMCAGCSHRATYYAMKKVFGKNAVFPGDIGCYTLGIQ--NGT 398
Cdd:TIGR03336 320 EGELNPDIVVNALAK-FGLAPSVTHEKPVPKPLPVRPPSLCAGCPHRATFYAMKKVADREAIFPSDIGCYTLGIQppLGT 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  399 VDTTLCMGGSITVASGIYHSGEKQPICCSIGDSTFFHTGMNGLLNAVYNKANITVAILDNRITAMTGHQPNPGMGLTSTG 478
Cdd:TIGR03336 399 VDTTLCMGASIGVASGLSKAGEKQRIVAFIGDSTFFHTGIPGLINAVYNKANITVVILDNRITAMTGHQPNPGTGVTGMG 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  479 ETTKEIDLEQLCRGLGAEFVEVVDSFDVNATVEAFKRAKDYEGTSVIISKQPCIIYARRTGIRLTPFKVDHDKCVGCRMC 558
Cdd:TIGR03336 479 EATKEISIEELCRASGVEFVEVVDPLNVKETIEVFKAALAAEGVSVIIAKQPCVLSNKRAGKRAGPYKVDQDKCIGCKKC 558

                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 499818471  559 VN-LGCPAIEfdKENKKSTINATCTGCGLCAEVCKFDAI 596
Cdd:TIGR03336 559 IKeLGCPAIE--PEDKEAVIDPLCTGCGVCAQICPFDAI 595
TPP_IOR_alpha cd02008
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ...
 356-531 2.61e-90

Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.


Pssm-ID: 238966 [Multi-domain]  Cd Length: 178  Bit Score: 276.47  E-value: 2.61e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 356 RPPAMCAGCSHRATYYAMKKVFGKNAVFPGDIGCYTLGIQNG--TVDTTLCMGGSITVASGIYHSGEKQPICCSIGDSTF 433
Cdd:cd02008    2 RPPGLCPGCPHRPSFYALRKAFKKDSIVSGDIGCYTLGALPPlnAIDTCTCMGASIGVAIGMAKASEDKKVVAVIGDSTF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 434 FHTGMNGLLNAVYNKANITVAILDNRITAMTGHQPNPGMGLTSTGETTKeIDLEQLCRGLGAEFVEVVDSFDVNATVEAF 513
Cdd:cd02008   82 FHSGILGLINAVYNKANITVVILDNRTTAMTGGQPHPGTGKTLTEPTTV-IDIEALVRAIGVKRVVVVDPYDLKAIREEL 160

                        170
                 ....*....|....*...
gi 499818471 514 KRAKDYEGTSVIISKQPC 531
Cdd:cd02008  161 KEALAVPGVSVIIAKRPC 178
TPP_PYR_PFOR_IOR-alpha_like cd07034
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ...
 9-164 5.29e-54

Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ferredoxin oxidoreductase alpha subunit (IOR-alpha), and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain, of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit (IOR-alpha), and related proteins, subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzyme Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit. This subfamily includes proteins characterized as pyruvate NADP+ oxidoreductase (PNO). PFOR and PNO catalyze the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. The facultative anaerobic mitochondrion of the photosynthetic protist Euglena gracilis oxidizes pyruvate with PNO. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate.


Pssm-ID: 132917 [Multi-domain]  Cd Length: 160  Bit Score: 180.78  E-value: 5.29e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471   9 GNVAIARGIVEGGGRVISGYPGTPSSEIVDTLSKM---KERDFYVEWSvNEKVAMEVAAGAGMTGVRSVVTMKHVGLNVA 85
Cdd:cd07034    1 GNEAVARGALAAGVDVVAAYPITPSTEIAETLAKAvlgELGGVVVQAE-SEHAAAEAAIGASAAGARAMTATSGPGLNLM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  86 ADPLMTLSYMGvkGGMVVIVADDPGCHSS-----QNEQDSRIYSEFSlMPCLDPSTPQEAKDMIPYAFELSEKFELPVIF 160
Cdd:cd07034   80 AEALYLAAGAE--LPLVIVVAQRPGPSTGlpkpdQSDLMAARYGGHP-WPVLAPSSVQEAFDLALEAFELAEKYRLPVIV 156


                 ....
gi 499818471 161 RPTT 164
Cdd:cd07034  157 LSDG 160
PRK13030 PRK13030
indolepyruvate ferredoxin oxidoreductase family protein;
14-589 7.43e-35

indolepyruvate ferredoxin oxidoreductase family protein;


Pssm-ID: 237279 [Multi-domain]  Cd Length: 1159  Bit Score: 141.27  E-value: 7.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471   14 ARGIVEGGgrVISGYPGTPSSEIVDTLSKMKER----DFYVEWSVNEKVA------MEVAAGAGMTGVRSVVTM---KHV 80
Cdd:PRK13030   39 ARGLNTAG--FVSGYRGSPLGGVDQALWKAKKLldasDIRFLPGINEELAatavlgTQQVEADPERTVDGVFAMwygKGP 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471   81 GLNVAADPLMTLSYMGV--KGGMVVIVADDPGCHSS----QneqdsriySEFSL----MPCLDPSTPQEAKDMIPYAFEL 150
Cdd:PRK13030  117 GVDRAGDALKHGNAYGSspHGGVLVVAGDDHGCVSSsmphQ--------SDFALiawhMPVLNPANVQEYLDFGLYGWAL 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  151 SEKFELPVIFRPTTRISHGKADIELGEitdhrvEAKFEKDPSRWVMVPSNAVVRHPHLLS--IQDGIQEELE-------I 221
Cdd:PRK13030  189 SRYSGAWVGFKAISETVESGSTVDLDP------DRTRWPAPEDFTPPAGGLHNRWPDLPSlaIEARLAAKLPavrafarA 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  222 SPWNELTI-NEASRIGVIAAGIASVYAKEAIDNLGVSA--------SYLKIGA-YPVPEGLIKRMYEQVDTVLVIEELEP 291
Cdd:PRK13030  263 NSIDRWVApSPDARVGIVTCGKAHLDLMEALRRLGLDDadlraagiRIYKVGLsWPLEPTRLREFADGLEEILVIEEKRP 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  292 IVEDRCKIIAKDMESSI--KIIGKTD--GT--VPRVGELNVDHCVKAIA----DVFKIESG--------LPVIKEIEMEL 353
Cdd:PRK13030  343 VIEQQIKDYLYNRPGGArpRVVGKHDedGAplLSELGELRPSLIAPVLAarlaRHKPALDRrarvvdlvAPQILSNEADA 422

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  354 PLRPPAMCAGCSHRATyyamKKVFGKNAVFPGdIGCYTLGI-QNGTVDTTLCMGGSITVASGIYHSGEKQPICCSIGDST 432
Cdd:PRK13030  423 VVRTPYFCSGCPHNTS----TKVPEGSIAQAG-IGCHFMASwMDRDTTGLTQMGGEGVDWIGHAPFTETKHVFQNLGDGT 497

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  433 FFHTGMNGLLNAVYNKANITVAILDNRITAMTGHQPNPGmgltstgettkEIDLEQLCRGLGAEFVE--VVDSFDVN--- 507
Cdd:PRK13030  498 YFHSGSLAIRQAVAAGANITYKILYNDAVAMTGGQPVDG-----------SISVPQIARQVEAEGVSriVVVSDEPEkyr 566

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  508 -----ATVEAFKRA---------KDYEGTSVIISKQPCIIYARRTGIRltpfkvdhdkcvGcrmcvnlgcpaiEFDKENK 573
Cdd:PRK13030  567 ghhlpAGVTVHHRDeldavqrelRETPGVTVLIYDQTCAAEKRRRRKR------------G------------EFPDPDR 622

                         650
                  ....*....|....*..
gi 499818471  574 KSTIN-ATCTGCGLCAE 589
Cdd:PRK13030  623 RLFINeAVCEGCGDCGV 639
PRK09193 PRK09193
indolepyruvate ferredoxin oxidoreductase; Validated
 98-587 2.12e-27

indolepyruvate ferredoxin oxidoreductase; Validated


Pssm-ID: 236404 [Multi-domain]  Cd Length: 1165  Bit Score: 118.01  E-value: 2.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471   98 KGGMVVIVADDPGCHSS----QneqdsriySEFSL----MPCLDPSTPQEAKDMIPYAFELSEKFELPVIFRPTTRISHG 169
Cdd:PRK09193  144 HGGVLALAGDDHAAKSStlphQ--------SEHAFkaagMPVLFPANVQEILDYGLHGWAMSRYSGLWVGMKTVTDVVES 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  170 KADIELGeitDHRVEAKFekdPSRWVMVPSNAVVRHPHLLsiqdGIQEELEISP-W------------NELTINEA-SRI 235
Cdd:PRK09193  216 SASVDVD---PDRVQIVL---PEDFEMPPGGLNIRWPDPP----LEQEARLLDYkLyaalayaranklDRVVIDSPnARL 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  236 GVIAAGIASVYAKEAIDNLGVSA--------SYLKIGA-YPV-PEGlIKRMYEQVDTVLVIEELEPIVEDRCKIIAKDME 305
Cdd:PRK09193  286 GIVAAGKAYLDVRQALRDLGLDEetaarlgiRLYKVGMvWPLePQG-VRAFAEGLDEILVVEEKRQIIEYQLKEELYNWP 364

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  306 SSI--KIIGKTDGT----VPRVGELNVDHCVKAIADVFK-----------IESGLPVIKEIEMELPL------RPPAMCA 362
Cdd:PRK09193  365 DDVrpRVIGKFDPQgnwlLPAHGELSPAIIAKAIARRLLklelpgdvrarIAARLAVLEAKEAALALprvtaaRTPYFCS 444

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  363 GCSH-RATyyamkKV-FGKNAVfpGDIGCYTLGIQNGTVDTTLC-MGGS----ITVASgiyHSGEKQpICCSIGDSTFFH 435
Cdd:PRK09193  445 GCPHnTST-----RVpEGSRAL--AGIGCHYMATWMDRNTSTFTqMGGEgvpwIGQAP---FTDEKH-VFQNLGDGTYFH 513

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  436 TGMNGLLNAVYNKANITVAILDNRITAMTGHQPNPGmgltstgettkEIDLEQLCRGLGAEFVE---VV----------D 502
Cdd:PRK09193  514 SGLLAIRAAVAAGVNITYKILYNDAVAMTGGQPVDG-----------GLSVPQITRQLAAEGVKrivVVtdepekydgvA 582

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  503 SFDVNATV-------EAFKRAKDYEGTSVIISKQPCIIYARRTGIRLTpfkvdhdkcvgcrmcvnlgcpaieFDKENKKS 575
Cdd:PRK09193  583 RLAPGVTVhhrdeldAVQRELREIPGVTVLIYDQTCAAEKRRRRKRGT------------------------LPDPAKRV 638

                         570
                  ....*....|...
gi 499818471  576 TIN-ATCTGCGLC 587
Cdd:PRK09193  639 FINeAVCEGCGDC 651
PRK13029 PRK13029
indolepyruvate ferredoxin oxidoreductase family protein;
25-589 7.06e-24

indolepyruvate ferredoxin oxidoreductase family protein;


Pssm-ID: 237278 [Multi-domain]  Cd Length: 1186  Bit Score: 107.18  E-value: 7.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471   25 ISGYPGTPSSEIVDTLSKMK----ERDFYVEWSVNEKVA---------MEVAAGAGMTGVRSVVTMKHVGLNVAADPLMT 91
Cdd:PRK13029   59 ISGYRGSPLGALDQALWKAKkhlaAADVVFQPGVNEELAatavwgsqqLELDPGAKRDGVFGMWYGKGPGVDRSGDALRH 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471   92 LSYMGV--KGGMVVIVADDPGCHSSQNEQDSriysEFSLM----PCLDPSTPQEAKDMIPYAFELSEKFELPVIFRPTTR 165
Cdd:PRK13029  139 ANLAGTspLGGVLVLAGDDHGAKSSSVAHQS----DHTFIawgiPVLYPASVQDYLDYGLHGWAMSRYSGLWVGMKCVTE 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  166 ISHGKADIELgeitdhrveakfekDPSRWVMVPSNAVVRHPHLLSIQ----DGIQEE-------------LEISPWNELT 228
Cdd:PRK13029  215 VVESTASVDL--------------DPDRVDIVLPDDFVLPPGGLHIRwpddPLAQEErmlefkwyaalayVRANRLNRLV 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  229 INEAS-RIGVIAAGIASVYAKEAIDNLGVSAS--------YLKIG-AYPVPEGLIKRMYEQVDTVLVIEELEPIVEDRCK 298
Cdd:PRK13029  281 IDGPNpRLGIIAAGKAYLDVRQALRDLGLDDAtcaalgirLLKVGcVWPLDPQSVREFAQGLEEVLVVEEKRAVIEYQLK 360

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  299 I----IAKDMESsiKIIGKTDGT---------------VPRVGELNVDHCVKAIADVFKiESGLPV---------IKEIE 350
Cdd:PRK13029  361 EelynWREDVRP--AIFGKFDHRdgaggewsvpagrwlLPAHAELSPALIAKAIARRLA-ALGLPAdvaarmdarVADIE 437

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  351 ME---------LPLRPPAMCAGCSHRATyyamKKVfGKNAVFPGDIGCYTLGIQ-NGTVDTTLCMGGSITVASGIYHSGE 420
Cdd:PRK13029  438 AKeraaaqprlLTERKPWFCSGCPHNTS----TRV-PEGSRALAGIGCHYMAMWmDRSTEGFSQMGGEGVAWIGQMPFSR 512

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  421 KQPICCSIGDSTFFHTGMNGLLNAVYNKANITVAILDNRITAMTGHQPNPGmgltstgettkEIDLEQLCRGLGAEFVE- 499
Cdd:PRK13029  513 RRHVFQNLGDGTYFHSGLLAIRQAIAAGVNITYKILYNDAVAMTGGQPVDG-----------VLTVPQIARQVHAEGVRr 581

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  500 ---VVDSFDVNATVEAF----------------KRAKDYEGTSVIISKQPCIIYARRTGIRLTpfkvdhdkcvgcrmcvn 560
Cdd:PRK13029  582 ivvVTDEPGKYRGVARLpagvtvhhrdeldavqRELREVPGVSVLIYDQTCATEKRRRRKRGT----------------- 644

                         650       660       670
                  ....*....|....*....|....*....|
gi 499818471  561 lgCPAiefdkENKKSTIN-ATCTGCGLCAE 589
Cdd:PRK13029  645 --YPD-----PARRVFINeLVCEGCGDCSV 667
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
386-526 1.28e-22

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 94.19  E-value: 1.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  386 DIGCYTLGIQ--------NGTVDTTL--CMGGSITVASGIYHSGEKQPICCSIGDSTFFHTgMNGLLNAVYNKANITVAI 455
Cdd:pfam02775   1 DIGCHQMWAAqyyrfrppRRYLTSGGlgTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMN-LQELATAVRYNLPITVVV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499818471  456 LDNRITAMTGHQPNPGMGLTSTGET---TKEIDLEQLCRGLGAEfVEVVDSFDvnATVEAFKRAKDYEGTSVII 526
Cdd:pfam02775  80 LNNGGYGMTRGQQTPFGGGRYSGPSgkiLPPVDFAKLAEAYGAK-GARVESPE--ELEEALKEALEHDGPALID 150
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 531-597 7.02e-18

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 78.16  E-value: 7.02e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499818471 531 CIIYARRTGIRltpFKVDHDKCVGCRMCVNLgCPAIEFDKENKKSTIN-ATCTGCGLCAEVCKFDAIK 597
Cdd:COG4231    6 KILDNRTTAMR---YVIDEDKCTGCGACVKV-CPADAIEEGDGKAVIDpDLCIGCGSCVQVCPVDAIK 69
PorA COG0674
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha ...
 2-324 2.52e-17

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


Pssm-ID: 440438 [Multi-domain]  Cd Length: 372  Bit Score: 83.97  E-value: 2.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471   2 STREYMLGNVAIARGIVEGGGRVISGYPGTPSSEIVDTLSKMKERdfyvewsVNEKV--------AMEVAAGAGMTGVRS 73
Cdd:COG0674    1 GKRVLMDGNEAVALGAIAAGCRVIAAYPITPSTEIAEYLAEWLAE-------LGGVVvqaeseiaAIGAVIGASAAGARA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  74 vvtmkhvglnvaadplMT------LSYM----GVKGGM----VVIVADDPGchSSQ-----NEQ------------DSRi 122
Cdd:COG0674   74 ----------------MTatsgpgLSLMqeglGLAAGAelplVIVVVQRAG--PSTglpikGDQsdlmqalygghgDTG- 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 123 ysefslMPCLDPSTPQEAKDMIPYAFELSEKFELPVI-----FrpttrISHGKADIEL---GEITDHRVEAKFE-----K 189
Cdd:COG0674  135 ------WIVLAPSSVQEAFDLTIIAFNLAEKYRVPVIvlfdgF-----LGSHEEPVELpddEEVKILPRPEEYRpyaldE 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 190 DPsrwVMVP-----------------SNAVVRHPHLLSIQD---GIQEELeisPWNELTINEASRIGVIAAGIASVYAKE 249
Cdd:COG0674  204 DP---RAIPgtaqpdvyftglehdetEDPENAEKMVEKRMRkfeKIRDEL---PRVEYYGAEDAEVVIVAMGSTAGTAKE 277

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 250 AIDNL---GVSASYLKIGAY-PVPEGLIKRMYEQVDTVLVIEelepivedRCK--IIAKDMESSIKI------IGKTDGT 317
Cdd:COG0674  278 AVDRLreeGIKVGLLRVRLLrPFPAEALREALKGVKKVAVVE--------RNKsgQLALDVRAALGAdrvvggIYGLGGR 349


                 ....*..
gi 499818471 318 VPRVGEL 324
Cdd:COG0674  350 PFTPEEI 356
PRK08659 PRK08659
2-oxoacid:acceptor oxidoreductase subunit alpha;
1-337 3.78e-17

2-oxoacid:acceptor oxidoreductase subunit alpha;


Pssm-ID: 181526 [Multi-domain]  Cd Length: 376  Bit Score: 83.37  E-value: 3.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471   1 MSTREYMLGNVAIARGIVEGGGRVISGYPGTPSSEIVDTLSKM--KERDFYVEwsvnekvaME-----VAA--GAGMTGV 71
Cdd:PRK08659   1 MTKVDFLQGNEACAEGAIAAGCRFFAGYPITPSTEIAEVMARElpKVGGVFIQ--------MEdeiasMAAviGASWAGA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  72 RSV-VT--------MKHVGLNVAAD-PLMTLSYM--GVKGGMvvivaddPGCHSSQNEQDSRI-----YSefslMPCLDP 134
Cdd:PRK08659  73 KAMtATsgpgfslmQENIGYAAMTEtPCVIVNVQrgGPSTGQ-------PTKPAQGDMMQARWgthgdHP----IIALSP 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 135 STPQEAKDMIPYAFELSEKFELPVIFRPTTRISHGKADIELGEITD-HRVEAKFEKDPSRWV--------MVPSNAVVRH 205
Cdd:PRK08659 142 SSVQECFDLTIRAFNLAEKYRTPVIVLADEVVGHMREKVVLPEPDEiEIIERKLPKVPPEAYkpfddpegGVPPMPAFGD 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 206 PH------LLSIQDG-------IQEEL-------------EISPWNELTINEASrIGVIAAGIASVYAKEAIDNL---GV 256
Cdd:PRK08659 222 GYrfhvtgLTHDERGfpttdpeTHEKLvrrlvrkieknrdDIVLYEEYMLEDAE-VVVVAYGSVARSARRAVKEAreeGI 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 257 SASYLK-IGAYPVPEGLIKRMYEQVDTVLVIE--------ELEPIVEDRCKiiakdmessIKIIGKTDGTVPRVGELnvd 327
Cdd:PRK08659 301 KVGLFRlITVWPFPEEAIRELAKKVKAIVVPEmnlgqmslEVERVVNGRAK---------VEGINKIGGELITPEEI--- 368

                        410
                 ....*....|
gi 499818471 328 hcVKAIADVF 337
Cdd:PRK08659 369 --LEKIKEVA 376
oorA PRK09627
2-oxoglutarate synthase subunit alpha;
9-287 1.22e-14

2-oxoglutarate synthase subunit alpha;


Pssm-ID: 182002 [Multi-domain]  Cd Length: 375  Bit Score: 75.90  E-value: 1.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471   9 GNVAIARGIVEGGGRVISGYPGTPSSEIVDTLSKMKERDFYVEWSVNEKVA-MEVAAGAGMTGVRSV-------VTMK-- 78
Cdd:PRK09627   8 GNELVAKAAIECGCRFFGGYPITPSSEIAHEMSVLLPKCGGTFIQMEDEISgISVALGASMSGVKSMtassgpgISLKae 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  79 HVGLNVAAD-PLMTLSYM--GVKGGMVVIVAddpgcHSSQNEQDSRIYSEFSlMPCLDPSTPQEAKDMIPYAFELSEKFE 155
Cdd:PRK09627  88 QIGLGFIAEiPLVIVNVMrgGPSTGLPTRVA-----QGDVNQAKNPTHGDFK-SIALAPGSLEEAYTETVRAFNLAERFM 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 156 LPVIFRPTTRISH--GKADI-ELGEITDHRV-EAKFEKDPSRW--VMVPSN--AVVR------HPHLLSIQDG------- 214
Cdd:PRK09627 162 TPVFLLLDETVGHmyGKAVIpDLEEVQKMIInRKEFDGDKKDYkpYGVAQDepAVLNpffkgyRYHVTGLHHGpigfpte 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 215 ---------------IQEEL-EISPWNELTINEASrIGVIAAGIASVYAKEAIDNL---GVSASYLK-IGAYPVPEGLIK 274
Cdd:PRK09627 242 dakicgklidrlfnkIESHQdEIEEYEEYMLDDAE-ILIIAYGSVSLSAKEAIKRLreeGIKVGLFRpITLWPSPAKKLK 320

                        330
                 ....*....|...
gi 499818471 275 RMYEQVDTVLVIE 287
Cdd:PRK09627 321 EIGDKFEKILVIE 333
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
 372-526 3.31e-14

Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.


Pssm-ID: 238318 [Multi-domain]  Cd Length: 168  Bit Score: 70.75  E-value: 3.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 372 AMKKVFGKNAVFPGDIGCYTLGIQNGT---------VDTTLC-MGGSITVASGIYHSGEKQPICCSIGDSTFFHTGMnGL 441
Cdd:cd00568    5 ALRAALPEDAIVVNDAGNSAYWAYRYLplrrgrrflTSTGFGaMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQ-EL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 442 LNAVYNKANITVAILDNRITAMTGHQPNPGMGLTSTGETTKEIDLEQLCRGLGAEFVEVVDSFDVNAtveAFKRAKDYEG 521
Cdd:cd00568   84 ATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDLSNPDFAALAEAYGAKGVRVEDPEDLEA---ALAEALAAGG 160


                 ....*
gi 499818471 522 TSVII 526
Cdd:cd00568  161 PALIE 165
POR_N pfam01855
Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N ...
 20-204 1.70e-13

Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N terminal structural domain of the pyruvate ferredoxin oxidoreductase. This domain binds thiamine diphosphate, and along with domains II and IV, is involved in inter subunit contacts. The family also includes pyruvate flavodoxin oxidoreductase as encoded by the nifJ gene in cyanobacterium which is required for growth on molecular nitrogen when iron is limited.


Pssm-ID: 396432  Cd Length: 230  Bit Score: 70.36  E-value: 1.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471   20 GGGRVISGYPGTPSSEIVDTLSKMKeRDFYVEWSV-----NEKVAMEVAAGAGMTGVRSVVTMKHVGLNvaadpLMtLSY 94
Cdd:pfam01855   5 AGVDVIAAYPITPSSEIAEEAAEWA-ANGEKGDVVviqmeSEIGAISAVIGAAAAGARAATATSGQGLL-----LM-IEN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471   95 MGVKGGM----VVIVADDPGCHSSQNeqdsrIYSEFS-LMPCLD-------PSTPQEAKDMIPYAFELSEKFELPVI-FR 161
Cdd:pfam01855  78 LGKAAGErlpvVIHVVARAGPSPGLS-----IFGDHSdVMAARDtgwivlaSENVQEAFDFALVAFNLAEKVRTPVIhLF 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 499818471  162 PTTRISHGKADIEL---GEITDHRVEAKFEKDPSRWVMVPSNAVVR 204
Cdd:pfam01855 153 DGFRTSHEREKVELppdEDEKDLIDEFLPPYKRKRYGLDPEMPIAR 198
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 357-534 4.35e-13

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


Pssm-ID: 440637 [Multi-domain]  Cd Length: 262  Bit Score: 69.40  E-value: 4.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 357 PPAMCAGCSH----RATYYAMKKVF-GKNAVFPGDIGCytLGIQNGTVDT----TLcMGGSITVASGI---YHsgEKQPI 424
Cdd:COG1013   12 GHRWCPGCGHgiilRLLLKALDELLdGDKTVVVSGIGC--SSVAPGYFNVpgfhTL-HGRAAAVATGIklaNP--DLTVI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 425 CCSiGDSTFFHTGMNGLLNAVYNKANITVAILDNRITAMTGHQPNP----GMGLTST--GETTKEIDLEQLCRGLGAEFV 498
Cdd:COG1013   87 VFG-GDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPttplGAKTTTTpyGKPEPPKDPAEIAAAHGATYV 165

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 499818471 499 EVVDSFDVNATVEAFKRAKDYEGTSVIISKQPCIIY 534
Cdd:COG1013  166 ARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTG 201
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 546-601 1.11e-12

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 63.21  E-value: 1.11e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499818471 546 KVDHDKCVGCRMCVNLgCP--AIEFDKENKKSTINATCTGCGLCAEVCKFDAIKEIQK 601
Cdd:COG1149    7 VIDEEKCIGCGLCVEV-CPegAIKLDDGGAPVVDPDLCTGCGACVGVCPTGAITLEER 63
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 361-534 6.60e-12

Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) subfamily, TPP-binding module; OGFOR catalyzes the oxidative decarboxylation of 2-oxo-acids, with ferredoxin acting as an electron acceptor. In the TCA cycle, OGFOR catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA. In the reductive tricarboxylic acid cycle found in the anaerobic autotroph Hydrogenobacter thermophilus, OGFOR catalyzes the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate. Thauera aromatica OGFOR has been shown to provide reduced ferredoxin to benzoyl-CoA reductase, a key enzyme in the anaerobic metabolism of aromatic compounds. OGFOR is dependent on TPP and a divalent metal cation for activity.


Pssm-ID: 239470 [Multi-domain]  Cd Length: 193  Bit Score: 64.85  E-value: 6.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 361 CAGCSHRATYYAMKKVF-------GKNAVFPGdIGC------YtlgIQNGTVDTTlcMGGSITVASGIYHSG-EKQPICC 426
Cdd:cd03375    2 CPGCGDGSILKALAKALaelgidpEKVVVVSG-IGCssrlpyY---FNTYGFHTL--HGRALAVATGVKLANpDLTVIVV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 427 SiGDSTFFHTGMNGLLNAVYNKANITVAILDNRITAMTGHQPNP----GMGLTSTGETTKE--IDLEQLCRGLGAEFVEV 500
Cdd:cd03375   76 S-GDGDLAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPttpeGFKTKTTPYGNIEepFNPLALALAAGATFVAR 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 499818471 501 VDSFDVNATVEAFKRAKDYEGTSVIISKQPCIIY 534
Cdd:cd03375  155 GFSGDIKQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 547-597 7.86e-12

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: 61.22  E-value: 7.86e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499818471 547 VDHDKCVGCRMCVnLGCP--AIEFDKENKKSTINATCTGCGLCAEVCKFDAIK 597
Cdd:COG1144   27 VDEDKCIGCGLCW-IVCPdgAIRVDDGKYYGIDYDYCKGCGICAEVCPVKAIE 78
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
545-597 4.56e-11

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 58.97  E-value: 4.56e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499818471 545 FKVDHDKCVGCRMCVNLgCP--AIEFdkENKKSTINA-TCTGCGLCAEVCKFDAIK 597
Cdd:COG2768    6 PYVDEEKCIGCGACVKV-CPvgAISI--EDGKAVIDPeKCIGCGACIEVCPVGAIK 58
PRK07119 PRK07119
2-ketoisovalerate ferredoxin reductase; Validated
 1-287 4.64e-11

2-ketoisovalerate ferredoxin reductase; Validated


Pssm-ID: 235942 [Multi-domain]  Cd Length: 352  Bit Score: 64.50  E-value: 4.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471   1 MSTREYMLGNVAIARGIVEGGGRVISGYPGTPSSEIVDTLSK---MKERDFYVEWSvnekvamEVAA-----GAGMTGVR 72
Cdd:PRK07119   1 MMEKVLMKGNEAIAEAAIRAGCRCYFGYPITPQSEIPEYMSRrlpEVGGVFVQAES-------EVAAinmvyGAAATGKR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471  73 SVVTMKHVGLNvaadpLMT--LSYMG---VKGGMVVIVADDPGCHSSQNEQ-------------DSRiysefslMPCLDP 134
Cdd:PRK07119  74 VMTSSSSPGIS-----LKQegISYLAgaeLPCVIVNIMRGGPGLGNIQPSQgdyfqavkggghgDYR-------LIVLAP 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 135 STPQEAKDMIPYAFELSEKFELPVIFRpttrishgkADIELGEITDHRV---EAKFEKDPSRWvmvpsnAVV----RHPH 207
Cdd:PRK07119 142 SSVQEMVDLTMLAFDLADKYRNPVMVL---------GDGVLGQMMEPVEfppRKKRPLPPKDW------AVTgtkgRRKN 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 208 L---LSIQDGIQEEL---------EISP----WNELTINEASRIgVIAAGIASVYAKEAIDNL---GVSASYLK-IGAYP 267
Cdd:PRK07119 207 IitsLFLDPEELEKHnlrlqekyaKIEEnevrYEEYNTEDAELV-LVAYGTSARIAKSAVDMAreeGIKVGLFRpITLWP 285

                        330       340
                 ....*....|....*....|
gi 499818471 268 VPEGLIKRMYEQVDTVLVIE 287
Cdd:PRK07119 286 FPEKALEELADKGKGFLSVE 305
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 545-597 1.17e-10

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 59.33  E-value: 1.17e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499818471 545 FKVDHDKCVGCRMCVNLgCP--AIEFDKENKKSTINATCTGCGLCAEVCKFDAIK 597
Cdd:cd10549   73 AEIDEEKCIGCGLCVKV-CPvdAITLEDELEIVIDKEKCIGCGICAEVCPVNAIK 126
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 544-597 1.69e-10

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 56.98  E-value: 1.69e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499818471 544 PFKVDHDKCVGCRMCVNLgCP--AIEFDkeNKKSTINAT-CTGCGLCAEVCKFDAIK 597
Cdd:COG2221    9 PPKIDEEKCIGCGLCVAV-CPtgAISLD--DGKLVIDEEkCIGCGACIRVCPTGAIK 62
PRK11867 PRK11867
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
 358-534 3.51e-10

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 61.40  E-value: 3.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 358 PAMCAGCSHRATYYAMKKVFGK------NAVFPGDIGC------YtlgIQNGTVDTTlcMGGSITVASGIYHSGEKQPIC 425
Cdd:PRK11867  17 PRWCPGCGDGSILAALQRALAElgldpeNVAVVSGIGCsgrlpgY---INTYGFHTI--HGRALAIATGLKLANPDLTVI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 426 CSIGDSTFFHTGMNGLLNAVYNKANITVAILDNRITAMTGHQPNPgmgLTSTGETTKE---------IDLEQLCRGLGAE 496
Cdd:PRK11867  92 VVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSP---TSPVGFVTKTtpygsieppFNPVELALGAGAT 168

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 499818471 497 FVEVVDSFDVNATVEAFKRAKDYEGTSVIISKQPCIIY 534
Cdd:PRK11867 169 FVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTF 206
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 550-597 4.42e-10

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: 55.91  E-value: 4.42e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499818471 550 DKCVGCRMCVNLgCPA----IEFDKENKKSTINAT-CTGCGLCAEVCKFDAIK 597
Cdd:COG1143    2 DKCIGCGLCVRV-CPVdaitIEDGEPGKVYVIDPDkCIGCGLCVEVCPTGAIS 53
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
531-596 6.28e-10

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 61.80  E-value: 6.28e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 531 CIIYARRTGIRLTPF--KVDHDKCVGCRMCVNLgCP--AIEFDKENKKSTINATCTGCGLCAEVCKFDAI 596
Cdd:COG1148  475 AIQLLSKGELGVEPSvaEVDPEKCTGCGRCVEV-CPygAISIDEKGVAEVNPALCKGCGTCAAACPSGAI 543
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 538-597 8.23e-10

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


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 56.82  E-value: 8.23e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499818471 538 TGIRLtpfkVDHDKCVGCRMCVNlGCP--AIEFDKENKKSTINATCTGCGLCAEVCKFDAIK 597
Cdd:cd10550   72 TGAVV----VDEDKCIGCGMCVE-ACPfgAIRVDPETGKAIKCDLCGGDPACVKVCPTGALE 128
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 530-597 2.46e-09

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 56.88  E-value: 2.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 530 PCI-------IYARRTGIRLtpfkVDHDKCVGCRMCVNlGCP--AIEFDKENKKSTInatCTGCG---------LCAEVC 591
Cdd:COG0437   67 PCVkvcptgaTYKREDGIVL----VDYDKCIGCRYCVA-ACPygAPRFNPETGVVEK---CTFCAdrldegllpACVEAC 138


                 ....*.
gi 499818471 592 KFDAIK 597
Cdd:COG0437  139 PTGALV 144
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 543-597 2.81e-09

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 53.56  E-value: 2.81e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499818471 543 TPFKVDHDKCVGCRMCVNLgCP--AIEFDKENKKST-INA-TCTGCGLCAEVCKFDAIK 597
Cdd:COG1146    1 MMPVIDTDKCIGCGACVEV-CPvdVLELDEEGKKALvINPeECIGCGACELVCPVGAIT 58
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 543-597 3.24e-09

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 55.10  E-value: 3.24e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499818471 543 TPFKVDHDKCVGCRMCVNLgCP--AIEFDKEN-------KKSTIN-ATCTGCGLCAEVCKFDAIK 597
Cdd:cd10549   33 RGPEIDEDKCVFCGACVEV-CPtgAIELTPEGkeyvpkeKEAEIDeEKCIGCGLCVKVCPVDAIT 96
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 548-597 2.42e-08

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 52.53  E-value: 2.42e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499818471 548 DHDKCVGCRMCVNLgCPA--IEFDKENKKSTI-NATCTGCGLCAEVCKFDAIK 597
Cdd:PRK08348  40 DVDKCVGCRMCVTV-CPAgvFVYLPEIRKVALwTGRCVFCGQCVDVCPTGALQ 91
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 537-598 2.48e-08

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: 52.42  E-value: 2.48e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499818471  537 RTGIRLTPFKVDHDKCVGCRMCVNLgCPAI------EFDKENKKS----TIN-ATCTGCGLCAEVCKFDAIKE 598
Cdd:TIGR01971  30 RGRIVLTRDPNGEEKCIGCTLCAAV-CPADairvvpAEGEDGKRRlkfyEINfGRCIFCGLCEEACPTDAIVL 101
NapF COG1145
Ferredoxin [Energy production and conversion];
532-597 2.50e-08

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 55.11  E-value: 2.50e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499818471 532 IIYARRTGIRLTPFKVDHDKCVGCRMCVNLgCP--AIEFDKENKKSTINAT-CTGCGLCAEVCKFDAIK 597
Cdd:COG1145  164 IEEELKIAIKKAKAVIDAEKCIGCGLCVKV-CPtgAIRLKDGKPQIVVDPDkCIGCGACVKVCPVGAIS 231
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
540-598 3.82e-08

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 52.96  E-value: 3.82e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 540 IRLTPFKVDHDKCVGCRMCVNLgCP--AI----EFDKENKKST----IN-ATCTGCGLCAEVCKFDAIKE 598
Cdd:PRK05888  48 HALRRDPNGEERCIACKLCAAI-CPadAItieaAEREDGRRRTtrydINfGRCIFCGFCEEACPTDAIVE 116
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 530-597 4.74e-08

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: 52.01  E-value: 4.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 530 PCI-------IYARRTGIRLtpfkVDHDKCVGCRMCVnLGCP--AIEFDKENKKSTInatCTGCG---------LCAEVC 591
Cdd:cd04410   57 PCVkacptgaIYKDEDGIVL----IDEDKCIGCGSCV-EACPygAIVFDPEPGKAVK---CDLCGdrldeglepACVKAC 128


                 ....*.
gi 499818471 592 KFDAIK 597
Cdd:cd04410  129 PTGALT 134
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 533-597 1.48e-07

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


Pssm-ID: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 50.64  E-value: 1.48e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499818471 533 IYARRTGIRLtpfkVDHDKCVGCRMCVNlGCP--AIEFDKENKKSTinaTCTGC------GL---CAEVCKFDAIK 597
Cdd:cd16371   71 ITKREDGIVV----VDQDKCIGCGYCVW-ACPygAPQYNPETGKMD---KCDMCvdrldeGEkpaCVAACPTRALD 138
Fer4_21 pfam14697
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 546-591 1.78e-07

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


Pssm-ID: 434137 [Multi-domain]  Cd Length: 59  Bit Score: 48.05  E-value: 1.78e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 499818471  546 KVDHDKCVGCRMCVnLGCP-----AIEFDKENKKSTINATCTGCGLCAEVC 591
Cdd:pfam14697   2 RIDEDTCIGCGKCY-IACPdtshqAIVGDGKRHHTVIEDECTGCNLCVSVC 51
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
541-597 2.12e-07

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 52.37  E-value: 2.12e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499818471 541 RLTPFKV--DHDKCVGCRMCVNlGCP---AIEfdkenKKSTINATCTGCGLCAEVCKFDAIK 597
Cdd:COG0348  199 DLSTLRVryDRGDCIDCGLCVK-VCPmgiDIR-----KGEINQSECINCGRCIDACPKDAIR 254
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
524-598 3.00e-07

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 53.11  E-value: 3.00e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499818471 524 VIISKQPCIIYARRTGIRltPFKVDHDKCVGCRMCVNlGCPAIEFDKENKKSTINAT-CTGCGLCAEVCKFDAIKE 598
Cdd:COG4624   67 AISCIQVRGIIIIDKRGP--SIIRDKEKCKNCYPCVR-ACPVKAIKVDDGKAEIDEEkCISCGQCVAVCPFGAITE 139
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
547-597 3.34e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 53.27  E-value: 3.34e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499818471 547 VDHDKCVG--CRM-CVNLgCP-------AIEFDKENKKSTIN-ATCTGCGLCAEVCKFDAIK 597
Cdd:PRK13409   7 VDYDRCQPkkCNYeCIKY-CPvvrtgeeTIEIDEDDGKPVISeELCIGCGICVKKCPFDAIS 67
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 546-597 3.59e-07

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: 49.32  E-value: 3.59e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499818471 546 KVDHDKCVGCRMCVNLgCP--AIEFDKE---NKKSTINAT-CTGCGLCAEVCKFDAIK 597
Cdd:cd10549    2 KYDPEKCIGCGICVKA-CPtdAIELGPNgaiARGPEIDEDkCVFCGACVEVCPTGAIE 58
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 547-597 9.74e-07

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 51.71  E-value: 9.74e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499818471 547 VDHDKCVG--CRM-CVNLgCP-------AIEFDKENKKSTIN-ATCTGCGLCAEVCKFDAIK 597
Cdd:COG1245    7 VDRDRCQPkkCNYeCIKY-CPvnrtgkeAIEIDEDDGKPVISeELCIGCGICVKKCPFDAIS 67
Fer4_9 pfam13187
4Fe-4S dicluster domain;
551-596 1.08e-06

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 45.62  E-value: 1.08e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 499818471  551 KCVGCRMCVNlGCPAIEFDKENKKSTI-----NATCTGCGLCAEVCKFDAI 596
Cdd:pfam13187   1 KCTGCGACVA-ACPAGAIVPDLVGQTIrgdiaGLACIGCGACVDACPRGAI 50
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 552-595 1.40e-06

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: 45.60  E-value: 1.40e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 499818471  552 CVGCRMCVNlGCP--AIEFDKENKKSTI------NATCTGCGLCAEVCKFDA 595
Cdd:pfam12838   1 CIGCGACVA-ACPvgAITLDEVGEKKGTktvvidPERCVGCGACVAVCPTGA 51
PRK05778 PRK05778
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
 357-551 3.27e-06

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated


Pssm-ID: 235604 [Multi-domain]  Cd Length: 301  Bit Score: 49.11  E-value: 3.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 357 PPAMCAGCSHRATYYAMKKVFG-------KNAVFPGdIGC------YTLGiqnGTVDTTlcMGGSITVASGIY------- 416
Cdd:PRK05778  17 PTTWCPGCGNFGILNAIIQALAelgldpdKVVVVSG-IGCsskipgYFLS---HGLHTL--HGRAIAFATGAKlanpdle 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 417 ---HSGEkqpiccsiGDSTffHTGMNGLLNAVYNKANITVAILDNRITAMTGHQPNP----GMGLTSTGETTKE--IDLE 487
Cdd:PRK05778  91 vivVGGD--------GDLA--SIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPttpeGSKTKTAPYGNIEppIDPC 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499818471 488 QLCRGLGAEFVEVVDSFDVNATVEAFKRAKDYEGTSVIISKQPCIIY-ARRTGIRLTPFKVDHDK 551
Cdd:PRK05778 161 ALALAAGATFVARSFAGDVKQLVELIKKAISHKGFAFIDVLSPCVTFnGRNTSTKSPAYMREYYK 225
porD PRK09624
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
 546-601 6.47e-06

pyruvate ferredoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 170017 [Multi-domain]  Cd Length: 105  Bit Score: 45.40  E-value: 6.47e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499818471 546 KVDHDKCVGCRMCVNLgCP--AIEFDKENKKSTINATCTGCGLCAEVCKFDAIKEIQK 601
Cdd:PRK09624  47 EFNRDKCVRCYLCYIY-CPepAIYLDEEGYPVFDYDYCKGCGICANECPTKAIEMVRE 103
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 547-597 7.29e-06

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: 46.53  E-value: 7.29e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499818471 547 VDHDKCVGCRMCVNlGCP--AIEFDKENKKSTinaTCTGC------GL---CAEVCKFDAIK 597
Cdd:cd10562   97 VDEDKCIGCGYCVA-ACPfdVPRYDETTNKIT---KCTLCfdrienGMqpaCVKTCPTGALT 154
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 530-596 1.29e-05

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: 45.99  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 530 PCI-------IYARRTGIRLtpfkVDHDKCVGCRMCVNlGCP--AIEFDKENKKSTINAT---------CTGC------G 585
Cdd:cd10551   60 PCVkvcptgaTYKREDGIVL----VDYDKCIGCRYCMA-ACPygARYFNPEEPHEFGEVPvrpkgvvekCTFCyhrldeG 134

                         90
                 ....*....|....
gi 499818471 586 L---CAEVCKFDAI 596
Cdd:cd10551  135 LlpaCVEACPTGAR 148
PRK11866 PRK11866
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 356-536 1.43e-05

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183347 [Multi-domain]  Cd Length: 279  Bit Score: 47.06  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 356 RPPAMCAGCSHRATYYAMKKVFG------KNAVFPGDIGCY--------TLGIQNgtvdttlCMGGSITVASGIYHSGEK 421
Cdd:PRK11866   5 RPPIWCPGCGNYGILEALRKALAelgippENVVVVSGIGCSsnlpeflnTYGIHG-------IHGRVLPIATGVKWANPK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 422 QPICCSIGDSTFFHTGMNGLLNAVYNKANITVAILDNRITAMTGHQPNPGMGLTSTGETTKEIDLEQ------LCRGLGA 495
Cdd:PRK11866  78 LTVIGYGGDGDGYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEpfnpiaLALAAGA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 499818471 496 EFVEVVDSFDVNATVEAFKRAKDYEGTSVIISKQPCIIYAR 536
Cdd:PRK11866 158 TFVARGFSGDVKHLKEIIKEAIKHKGFSFIDVLSPCVTFNK 198
TPP_ComE cd03372
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ...
 405-528 1.76e-05

Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.


Pssm-ID: 239469 [Multi-domain]  Cd Length: 179  Bit Score: 45.74  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 405 MGGSITVASGIYHS---GEKQPICCSIGDSTFFhTGMNGLLNAVYNKA-NITVAILDNRITAMTGHQPNPgmgltstgeT 480
Cdd:cd03372   40 MLGSMGLASSIGLGlalAQPRKVIVIDGDGSLL-MNLGALATIAAEKPkNLIIVVLDNGAYGSTGNQPTH---------A 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 499818471 481 TKEIDLEQLCRGLGAEFVEVVDSfdvnatVEAFKRAK--DYEGTSVIISK 528
Cdd:cd03372  110 GKKTDLEAVAKACGLDNVATVAS------EEAFEKAVeqALDGPSFIHVK 153
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 547-597 2.47e-05

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


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 44.19  E-value: 2.47e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499818471 547 VDHDKCVGCRMCVnLGCP--AIEFDKENKkstINATCTGCG---------LCAEVCKFDAIK 597
Cdd:cd16374   70 VDPDKCIGCGMCA-MACPfgVPRFDPSLK---VAVKCDLCIdrrregklpACVEACPTGALK 127
PRK13795 PRK13795
hypothetical protein; Provisional
 551-591 2.73e-05

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 47.30  E-value: 2.73e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 499818471 551 KCVGCRMCVNLgCP--AIEFDKENKKSTINA-TCTGCGLCAEVC 591
Cdd:PRK13795 582 ECVGCGVCVGA-CPtgAIRIEEGKRKISVDEeKCIHCGKCTEVC 624
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 547-599 3.40e-05

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


Pssm-ID: 319885 [Multi-domain]  Cd Length: 140  Bit Score: 44.17  E-value: 3.40e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 547 VDHDKCVGCRMCVnLGCP--AIEFDKENKKStinATCTGCG-----LCAEVCKFDAIKEI 599
Cdd:cd10563   85 HDEEKCVGCWMCV-MVCPygAIRPDKERKVA---LKCDLCPdretpACVEACPTGALVLE 140
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
546-597 4.06e-05

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 43.88  E-value: 4.06e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499818471 546 KVDHDKCVGCRMCVNLgCP--AIEFDKENKKSTIN-----ATCTGCGLCAEVCKFDAIK 597
Cdd:COG1142   77 VVDEEKCIGCGLCVLA-CPfgAITMVGEKSRAVAVkcdlcGGREGGPACVEACPTGALR 134
PRK09898 PRK09898
ferredoxin-like protein;
505-600 4.45e-05

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 44.83  E-value: 4.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 505 DVNATVEAFKRAKDYEGTSViiskqpCIIYARRTGIRLTPFKVDHDKCVGCRMCVNlGCPAI--EFDKENKKSTinaTCT 582
Cdd:PRK09898 115 DLNYTADTCRQCKEPQCMNV------CPIGAITWQQKEGCITVDHKRCIGCSACTT-ACPWMmaTVNTESKKSS---KCV 184

                         90
                 ....*....|....*...
gi 499818471 583 GCGLCAEVCKFDAIKEIQ 600
Cdd:PRK09898 185 LCGECANACPTGALKIIE 202
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
546-597 4.53e-05

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 45.69  E-value: 4.53e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499818471 546 KVDHDKCVGCRMCVNLgCP--AIEFDKENKKSTIN---------------ATCTGCGLCAEVCKFDAIK 597
Cdd:PRK07118 164 VVDEDKCTGCGACVKA-CPrnVIELIPKSARVFVAcnskdkgkavkkvceVGCIGCGKCVKACPAGAIT 231
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 546-596 9.36e-05

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


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 42.56  E-value: 9.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 546 KVDHDKCVGCRMC------VNLG------------------------------------CP--AIEFDKENKKSTINA-T 580
Cdd:cd10550    2 VVDPEKCTGCRTCelacslKHEGvfnpslsrirvvrfepegldvpvvcrqcedapcveaCPvgAISRDEETGAVVVDEdK 81

                         90
                 ....*....|....*.
gi 499818471 581 CTGCGLCAEVCKFDAI 596
Cdd:cd10550   82 CIGCGMCVEACPFGAI 97
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 546-591 9.64e-05

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


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 43.01  E-value: 9.64e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499818471 546 KVDHDKCV------GCRMCVNLgCP----AIEFDKENKKSTINAT-CTGCGLCAEVC 591
Cdd:cd16373   87 VIDKDRCLawqggtDCGVCVEA-CPteaiAIVLEDDVLRPVVDEDkCVGCGLCEYVC 142
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 548-596 9.65e-05

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


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 42.64  E-value: 9.65e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499818471 548 DHDKCVGCRMCVNlGCP--AIEFDKENKKSTInatCTGCGLCAEVCKFDAI 596
Cdd:cd16370   81 DKEKCIGCGNCVK-ACIvgAIFWDEETNKPII---CIHCGYCARYCPHDVL 127
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 546-591 1.13e-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: 40.31  E-value: 1.13e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 499818471  546 KVDHDKCVGCRMCVNlGCPA-------IEFDKENKKSTINAT-CTGCGLCAEVC 591
Cdd:pfam13237   3 VIDPDKCIGCGRCTA-ACPAgltrvgaIVERLEGEAVRIGVWkCIGCGACVEAC 55
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 548-597 1.43e-04

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


Pssm-ID: 319883 [Multi-domain]  Cd Length: 196  Bit Score: 43.35  E-value: 1.43e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499818471 548 DHDKCVGCRMCVnLGCP----AIEFDKENKKSTinaTCTGC------GL---CAEVCKFDAIK 597
Cdd:cd10561   97 DEDKCIGCRYCM-VACPfnipKYEWDSANPKIR---KCTMCydrlkeGKqpaCVEACPTGALL 155
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 546-598 1.83e-04

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


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 41.55  E-value: 1.83e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499818471 546 KVDHDKCVGCRMCVNlGCPAIEFDKENK-KSTIN----------ATCTGCGLCAEVCKFDAIKE 598
Cdd:cd16372    4 VTDPEKCIGCLQCEE-ACSKTFFKEEDReKSCIRiteteggyaiNVCNQCGECIDVCPTGAITR 66
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 555-597 1.85e-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: 319889 [Multi-domain]  Cd Length: 138  Bit Score: 41.91  E-value: 1.85e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 499818471 555 CRMCVN----LGCP--AIEFDkENKKSTINATCTGCGLCAEVCKFDAIK 597
Cdd:cd16367   57 CRHCVDpvcmIGCPtgAIHRD-DGGEVVISDACCGCGNCASACPYGAIQ 104
PRK08764 PRK08764
Rnf electron transport complex subunit RnfB;
530-597 2.08e-04

Rnf electron transport complex subunit RnfB;


Pssm-ID: 181550 [Multi-domain]  Cd Length: 135  Bit Score: 41.83  E-value: 2.08e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499818471 530 PCIIYARRTGIRLTP---FKVDHDkCVGCRMCVNlGCP--AIEFDKENKKSTINATCTGCGLCAEVCKFDAIK 597
Cdd:PRK08764  63 PARPYDRSRGTHKLPqvaWIVEAD-CIGCTKCIQ-ACPvdAIVGGAKHMHTVIAPLCTGCELCVPACPVDCIE 133
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 547-597 2.18e-04

beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family contains beta FeS subunits of several dehydrogenases in the DMSO reductase superfamily, including formate dehydrogenase N (FDH-N), tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N is a major component of nitrate respiration of Escherichia coli; it catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate to a cytochrome. W-FDH contains a tungsten instead of molybdenum at the catalytic center and seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate.


Pssm-ID: 319888 [Multi-domain]  Cd Length: 156  Bit Score: 42.00  E-value: 2.18e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499818471 547 VDHDKCVGCRMCVNlGCP--AIEFDKENKKStinATCTGC------GL---CAEVCKFDAIK 597
Cdd:cd16366   97 VDPETCIGCGYCVN-ACPfdIPRFDEETGRV---AKCTLCydrisnGLqpaCVKTCPTGALT 154
TPP_SHCHC_synthase cd02009
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ...
 407-525 2.42e-04

Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of proteins similar to Escherichia coli 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylic acid (SHCHC) synthase (also called MenD). SHCHC synthase plays a key role in the menaquinone biosynthetic pathway, converting isochorismate and 2-oxoglutarate to SHCHC, pyruvate and carbon dioxide. The enzyme requires TPP and a divalent metal cation for activity.


Pssm-ID: 238967 [Multi-domain]  Cd Length: 175  Bit Score: 42.20  E-value: 2.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 407 GSITVASGIYHsGEKQPICCSIGDSTFFHTgMNGLLNAVYNKANITVAILDNR---ITAM-TGHQPNPgmGLTSTGETTK 482
Cdd:cd02009   55 GTLSTALGIAL-ATDKPTVLLTGDLSFLHD-LNGLLLGKQEPLNLTIVVINNNgggIFSLlPQASFED--EFERLFGTPQ 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 499818471 483 EIDLEQLCRGLGAEFVEVVDSFDVNatvEAFKRAKDYEGTSVI 525
Cdd:cd02009  131 GLDFEHLAKAYGLEYRRVSSLDELE---QALESALAQDGPHVI 170
PRK11869 PRK11869
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 406-550 2.43e-04

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183349 [Multi-domain]  Cd Length: 280  Bit Score: 43.23  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 406 GGSITVASGIYHSGEKQPICCSIGDSTFFHTGMNGLLNAVYNKANITVAILDNRITAMTGHQPNP----GMGlTST---G 478
Cdd:PRK11869  63 GRAIPAATAVKATNPELTVIAEGGDGDMYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPttlkGFK-TPTqpwG 141

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499818471 479 ETTKEIDLEQLCRGLGAEFVEVVDSFDVNATVEAFKRAKDYEGTSVIISKQPCIIYARRTGIRL----TPFKVDHD 550
Cdd:PRK11869 142 VFEEPFNPIALAIALDASFVARTFSGDIEETKEILKEAIKHKGLAIVDIFQPCVSFNKVNTYQWyrenTYYLKDHD 217
PRK14028 PRK14028
pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional
 539-601 3.38e-04

pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional


Pssm-ID: 172522 [Multi-domain]  Cd Length: 312  Bit Score: 43.06  E-value: 3.38e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499818471 539 GIRLTPFKVDHDKCVGCRMCVnLGCP---AIEFDKEN--------KKSTIN---ATCTGCGLCAEVCKFDAIKEIQK 601
Cdd:PRK14028 236 GWRIDKPVIDHSKCIMCRKCW-LYCPddaIIEAWREAegprgrkfRMKMIDfdyQYCKGCGVCAEVCPTGAIQMVRE 311
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
546-591 6.13e-04

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 42.62  E-value: 6.13e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499818471 546 KVDHDKCVGCRMCvNLGC-----PAIEFDKENKK--STINATCTGCGLCAEVC 591
Cdd:PRK08318 338 RIDQDKCIGCGRC-YIACedtshQAIEWDEDGTRtpEVIEEECVGCNLCAHVC 389
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 547-597 1.21e-03

beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes beta subunit of formate dehydrogenase family O (FDH-O), which is highly homologous to formate dehydrogenase N (FDH-N), a member of the DMSO reductase family. In E. coli three formate dehydrogenases are synthesized that are capable of oxidizing formate; Fdh-H, couples formate disproportionation to hydrogen and CO2, and is part of the cytoplasmically oriented formate hydrogenlyase complex, while FDH-N and FDH-O indicate their respective induction after growth with nitrate and oxygen. Little is known about FDH-O, although it shows formate oxidase activity during aerobic growth and is also synthesized during nitrate respiration, similar to FDH-N.


Pssm-ID: 319882 [Multi-domain]  Cd Length: 225  Bit Score: 40.83  E-value: 1.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499818471 547 VDHDKCVGCRMCVNlGCP--AIEFDKENKKStinATCTGC------GL---CAEVCKFDAIK 597
Cdd:cd10560  105 IQPDICNGCGYCVA-ACPfgVIDRNEETGRA---HKCTLCydrlkdGLepaCAKACPTGSIQ 162
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 547-597 1.44e-03

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


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 38.86  E-value: 1.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499818471 547 VDHDKCVGCRMCVNLgCPAIEFDKENKKSTiNATCTGCGLCAEVCKFDAIK 597
Cdd:cd16372   74 INKKLCVGCLMCVGF-CPEGAMFKHEDYPE-PFKCIACGICVKACPTGALE 122
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
552-601 1.91e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 40.69  E-value: 1.91e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499818471 552 CVGCRMCVNLgCPAIEFDKENKKSTINAT-CTGCGLCAEVCKFDAIKEIQK 601
Cdd:PRK07118 215 CIGCGKCVKA-CPAGAITMENNLAVIDQEkCTSCGKCVEKCPTKAIRILNK 264
napF TIGR00402
ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of ...
 537-592 1.95e-03

ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of the periplasmic nitrate reductase system, as in Escherichia coli. NapF interacts with the catalytic subunit, NapA, and may be an accessory protein for NapA maturation. [Energy metabolism, Electron transport]


Pssm-ID: 273060 [Multi-domain]  Cd Length: 101  Bit Score: 38.00  E-value: 1.95e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499818471  537 RTGIRlTPFKVDHD----KCVGCRMCVNL-----------GCPAIEFDkenkkstiNATCTGCGLCAEVCK 592
Cdd:TIGR00402  18 KTQIR-PPWSARESlfsaVCTRCGECASAcennilqlgqqGQPTVEFD--------NAECDFCGKCAEACP 79
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
553-596 1.98e-03

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 38.87  E-value: 1.98e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499818471 553 VGCRMCVN----LGCP--AIEFDkeNKKSTIN-ATCTGCGLCAEVCKFDAI 596
Cdd:COG1142   50 VQCRHCEDapcaEVCPvgAITRD--DGAVVVDeEKCIGCGLCVLACPFGAI 98
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
 548-597 2.82e-03

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 39.25  E-value: 2.82e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499818471 548 DHDKCVGCRMCVNlGCPA----IEFDKENKKST--IN-ATCTGCGLCAEVCKFDAIK 597
Cdd:PRK12387  36 NPQQCIGCAACVN-ACPSnaltVETDLATGELAweFNlGRCIFCGRCEEVCPTAAIK 91
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 546-597 3.48e-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: 38.39  E-value: 3.48e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499818471 546 KVDHDKCVGCRMCVnLGCP--AIEFDKENKKSTINATCTG-----CGLCA---------EVCKFDAIK 597
Cdd:cd10554   81 QVDEERCIGCKLCV-LACPfgAIEMAPTTVPGVDWERGPRavavkCDLCAgreggpacvEACPTKALT 147
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 581-597 4.33e-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: 34.92  E-value: 4.33e-03
                          10
                  ....*....|....*..
gi 499818471  581 CTGCGLCAEVCKFDAIK 597
Cdd:pfam00037   8 CIGCGACVEVCPVGAIT 24
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
 62-162 4.71e-03

Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.


Pssm-ID: 214865 [Multi-domain]  Cd Length: 136  Bit Score: 37.85  E-value: 4.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471    62 VAAGAGMTGVRSVVTMKHVGLNVAADPLMtlsyMGVK-GGMVVIVADDPG--------CHSSQneqdsRIYSEFSLMPCL 132
Cdd:smart00861  30 FAAGLALHGLRPVVEIFFTFFDRAKDQIR----SAGAsGNVPVVFRHDGGggvgedgpTHHSI-----EDEALLRAIPGL 100

                           90       100       110
                   ....*....|....*....|....*....|...
gi 499818471   133 D---PSTPQEAKDMIPYAFELSEKfelPVIFRP 162
Cdd:smart00861 101 KvvaPSDPAEAKGLLRAAIRDDGP---VVIRLE 130
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
 384-519 5.03e-03

Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).


Pssm-ID: 238958 [Multi-domain]  Cd Length: 293  Bit Score: 39.40  E-value: 5.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499818471 384 PGDIGCYTLGI--QNGTVdttlcmGGSITVASGIYHS----GEKQPICCSIGDST----FFHTGMNglLNAVYnKANITV 453
Cdd:cd02000   89 SMHIGDKEKNFfgGNGIV------GGQVPLAAGAALAlkyrGEDRVAVCFFGDGAtnegDFHEALN--FAALW-KLPVIF 159

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499818471 454 AILDNRItamtghqpnpGMGlTSTGETTKEIDLEQLCRGLGAEFVEVvDSFDVNATVEAFKRAKDY 519
Cdd:cd02000  160 VCENNGY----------AIS-TPTSRQTAGTSIADRAAAYGIPGIRV-DGNDVLAVYEAAKEAVER 213
PRK07569 PRK07569
bidirectional hydrogenase complex protein HoxU; Validated
 545-596 5.76e-03

bidirectional hydrogenase complex protein HoxU; Validated


Pssm-ID: 181037 [Multi-domain]  Cd Length: 234  Bit Score: 38.87  E-value: 5.76e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499818471 545 FKVDHDKCVGCRMCVNLgCPAIE----FDKENK--KSTINA----------TCTGCGLCAEVCKFDAI 596
Cdd:PRK07569 141 FGIDHNRCVLCTRCVRV-CDEIEgahtWDVAGRgaKSRVITdlnqpwgtseTCTSCGKCVQACPTGAI 207
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
547-596 6.06e-03

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 36.85  E-value: 6.06e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499818471 547 VDHDKCVGCRMCVNLgCP--AIeFDKENKKSTINAT-CTGCGLCAEVCKFDAI 596
Cdd:PRK09623  48 VDESKCVKCYICWKF-CPepAI-YIKEDGYVAIDYDyCKGCGICANECPTKAI 98
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 550-597 7.55e-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: 37.22  E-value: 7.55e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499818471 550 DKC-----VGCRMCVNlGCP--AIEFDKENKKS---TINAT-CTGCGLCAEVCKFDAIK 597
Cdd:cd10564   78 DSClalqgVECRSCQD-ACPtqAIRFRPRLGGIalpELDADaCTGCGACVSVCPVGAIT 135
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 544-584 7.56e-03

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 38.30  E-value: 7.56e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 499818471 544 PFKVDhDKCVGCRMCVNLgCPA--IEFdkENKKSTINATCTGC 584
Cdd:NF038196 180 KFHVT-DKCIGCGICAKV-CPVnnIEM--EDGKPVWGHNCTHC 218
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 558-598 8.10e-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: 38.52  E-value: 8.10e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 499818471 558 CVNLGCPAIEFDKEnkkstinaTCTGCGLCAEVCKFDAIKE 598
Cdd:cd03110   51 EDFVGGKKAFIDQE--------KCIRCGNCERVCKFGAILE 83
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 551-591 8.51e-03

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: 433287 [Multi-domain]  Cd Length: 61  Bit Score: 35.13  E-value: 8.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 499818471  551 KCVGCRMCVNLgCPAIEFDKENKKSTINA----------------TCTGCGLCAEVC 591
Cdd:pfam13534   1 RCIQCGCCVDE-CPRYLLNGDEPKKLMRAaylgdleelqankvanLCSECGLCEYAC 56
 
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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