|
Name |
Accession |
Description |
Interval |
E-value |
| pyruv_ox_red |
TIGR02176 |
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single ... |
6-1173 |
0e+00 |
|
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single chain form of pyruvate:ferredoxin (or flavodoxin) oxidoreductase. This enzyme may transfer electrons to nitrogenase in nitrogen-fixing species. Portions of this protein are homologous to gamma subunit of the four subunit pyruvate:ferredoxin (flavodoxin) oxidoreductase.
Pssm-ID: 131231 [Multi-domain] Cd Length: 1165 Bit Score: 1976.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 6 KTLNGNEAAAHISYPFTEVAAIYPITPSSPMAEITDKWAAHGKKNMFGQRVRVVELQSEAGASGTIHGSLAAGALTTTYT 85
Cdd:TIGR02176 2 KTMDGNTAAAHVAYAFSEVAAIYPITPSSTMGEYVDDWAAQGRKNIFGQTVKVVEMQSEAGAAGAVHGALQTGALTTTFT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 86 ASQGLLLMIPNMYKLVGELLPGVFHVSARALATHALSIFGDHQDVMACRQTGFGFLAASNAQEVMDLGCLAHLAAIKSRM 165
Cdd:TIGR02176 82 ASQGLLLMIPNMYKIAGELLPCVFHVSARAIAAHALSIFGDHQDVMAARQTGFAMLASSSVQEVMDLALVAHLATIEARV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 166 PFLHFFDGFRTSHEYQNVNVIDFEDIQDLVDYQAIKEFRARALSPEKPVVRGTAQNPDIYFQGKELPNPYYKAVPEVVEN 245
Cdd:TIGR02176 162 PFMHFFDGFRTSHEIQKIEVLDYEDMASLVNQELVAAFRKRSMNPEHPHVRGTAQNPDIYFQGREAVNPYYLAVPGIVQK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 246 YMQELEKIIGRSYNLFDYHGDPQAKHIIIAMGSVCDTIEETVDHLNEQGRKVGLIKVRLYRPFSAEHLLSAIPDTVKKIA 325
Cdd:TIGR02176 242 YMDKIAKLTGRSYHLFDYYGAPDAERVIIAMGSVAETIEETVDYLNAKGEKVGLLKVRLYRPFSAETFFAALPKSVKRIA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 326 VLDRTKEPGSLGEPLYQDVVHAYKNSQLN-PEIIGGRYGLGSKETRPSHIISVFDNLAEDKPKDNFTIGIVDDVSHTSLP 404
Cdd:TIGR02176 322 VLDRTKEPGAAGEPLYLDVVSAFYEMGEAmPVILGGRYGLGSKEFTPAMVKAVFDNLSGEAPKNHFTVGIEDDVTGTSLP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 405 ETGDVDITPSDTISCKFWGLGSDGTVGANQSAVKIIGDHTDLYAQAYFSYDSKKSGGTTVSHLRFGKQPIRAPYLVYNAD 484
Cdd:TIGR02176 402 VDEFFDTTPKGTIQAKFYGLGSDGTVGANKNAIKIIGDNTDNYAQGYFSYDSKKSGGITISHLRFGEKPIRSTYLVTEAD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 485 YVACHNPAFVNNYDLLQGLKAGGTFVLNCPWSKEDLEEKLPASMKRYLAENDINFYIIDAISIAGEIGLGNRINMIMQSA 564
Cdd:TIGR02176 482 FVACHNPAYLEMYDVLKGLKKGGTFLLNSPWAPEDLDKHLPNGVKRYIADKEIKFYTIDAVKIAQEVGLGGRINTIMQTA 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 565 FFKLADVIPIEDAVKYLKESVVENYGDKGQKVVDMNNLAIDKGIDSLIKVDIPKAWKDAQEEEYEESESEPEFVTNIQKP 644
Cdd:TIGR02176 562 FFKLAGVLPFEKAVDLLKKSIEKSYGKKGEKIVQKNIKAVDQAVESLHEVKVPAEWKDAPAEPKAIEGDAPEFVKNVVRP 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 645 MAKHEGDDLPVSAFKGmeDGTFPLRTTAYEKRGIAVNIPEWQIDKCIQCNQCSYICPHAVIRPYLLDEEEVQRAPETFET 724
Cdd:TIGR02176 642 INAQEGDDLPVSAFPA--DGTFPLGTTAFEKRGVAINVPVWVPDNCIQCNQCAFVCPHAAIRPKLADEEELENAPAGFKS 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 725 KQATGKDMDDLSYRIQVSPLDCTGCGNCADICPAKGKALIMEPAEEQIEQQEDNWEFAQTITEKTDRVNTKTLKGSQFVK 804
Cdd:TIGR02176 720 LDAKGKELEGMKFRIQISPLDCTGCGNCVDICPAKEKALVMQPLAEQREAQVANWEFAINIPEKDNKLNIDTVKGSQFQR 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 805 PLFEFHGACPGCGETPYYRLLTQLFGDRMLIANATGCSSIYCASAPSIPFTINSEGRGPAWANSLFEDNAEYGYGMYLAS 884
Cdd:TIGR02176 800 PLFEFSGACSGCGETPYVKLLTQLFGDRMVIANATGCSSIWGASAPSTPYTTNEQGQGPAWSNSLFEDNAEFGYGMRLSM 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 885 DYIQDRLAELAREVLETQQGDQDLNQALEEWLHVRKDGEKSKEAAKKLINLLNNRNLDantTLKHIAEYQDYLIKRSQWL 964
Cdd:TIGR02176 880 DKRRERLAELAAKALESDIASGDLKAALNGWLAGKNDIEKSKERVAKLKKLLAGEKDD---LLKEIYAVSDLFVKKSVWI 956
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 965 IGGDGWAYDIGFGGLDHVLSTGEDVNTLVMDTEVYSNTGGQSSKATQTAAMAKFASSGKATMKKDLGMMAMSYGYVYVAQ 1044
Cdd:TIGR02176 957 IGGDGWAYDIGYGGLDHVLASGKDVNVLVMDTEVYSNTGGQSSKATPTGAIAKFAAAGKRTSKKDLGMMAMTYGYVYVAQ 1036
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 1045 VSMGANMNQTLKAFLEAEQYPGPSLIIAYSPCINHGIRSGMGTSISQEKAAVDSGYWHLYRYNPQLKEEGKNPFILDSKE 1124
Cdd:TIGR02176 1037 VSMGANMQQTLKAFREAEAYDGPSIVIAYSPCINHGIKKGMGKSQAEQKTAVESGYWPLYRYNPRLAEQGKNPFQLDSKE 1116
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....*....
gi 501422877 1125 PKESLQDFLMSEVRFASLQKVFPETAEKLFEKAKQDARTKYETYKTLSE 1173
Cdd:TIGR02176 1117 PDSSVAEFLNGEVRFASLKKSFPDDAERLFNKAAHEAKRRFKEYEHLAA 1165
|
|
| TPP_PFOR_PNO |
cd03377 |
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ... |
805-1173 |
0e+00 |
|
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of proteins similar to the single subunit pyruvate ferredoxin oxidoreductase (PFOR) of Desulfovibrio Africanus, present in bacteria and amitochondriate eukaryotes. This subfamily also includes proteins characterized as pyruvate NADP+ oxidoreductase (PNO). These enzymes are dependent on TPP and a divalent metal cation as cofactors. PFOR and PNO catalyze the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. The PFOR from cyanobacterium Anabaena (NifJ) is required for the transfer of electrons from pyruvate to flavodoxin, which reduces nitrogenase. The facultative anaerobic mitochondrion of the photosynthetic protist Euglena gracilis oxidizes pyruvate with PNO.
Pssm-ID: 239472 Cd Length: 365 Bit Score: 653.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 805 PLFEFHGACPGCGETPYYRLLTQLFGDRMLIANATGCSSIYCASAPSIPFTINSEGRGPAWANSLFEDNAEYGYGMYLAS 884
Cdd:cd03377 1 PLFEFSGACAGCGETPYVKLLTQLFGDRMVIANATGCSSIYGGSAPTTPYTTNAKGRGPAWANSLFEDNAEFGLGMRLAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 885 DYIQDRLAELAREVLEtQQGDQDLNQALEEWLHVRKDGEKSKEAAKKLINLLNNRNLDAnttLKHIAEYQDYLIKRSQWL 964
Cdd:cd03377 81 DQRRERARELVQKLIE-KIGDEELKTLLNAWLATEDDIEESRERVAKLKPLLAAEKDEL---AKELLSLADYLVKKSVWI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 965 IGGDGWAYDIGFGGLDHVLSTGEDVNTLVMDTEVYSNTGGQSSKATQTAAMAKFASSGKATMKKDLGMMAMSYGYVYVAQ 1044
Cdd:cd03377 157 IGGDGWAYDIGYGGLDHVLASGENVNILVLDTEVYSNTGGQASKATPLGAVAKFAAAGKRTGKKDLGMIAMSYGNVYVAQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 1045 VSMGANMNQTLKAFLEAEQYPGPSLIIAYSPCINHGIRSGMGTSISQEKAAVDSGYWHLYRYNPQLKEEGKNPFILDSKE 1124
Cdd:cd03377 237 IALGANDNQTLKAFREAEAYDGPSLIIAYSPCIAHGIKGGMTKSQEQQKLAVESGYWPLYRYNPRLVEEGKNPLQLDSKE 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 501422877 1125 PKESLQDFLMSEVRFASLQKVFPETAEKLFEKAKQDARTKYETYKTLSE 1173
Cdd:cd03377 317 PDGPVEEFLNNENRFAALKKANPERAEQLFEQLQADAKERYKRYKRLAA 365
|
|
| PorA |
COG0674 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha ... |
3-392 |
2.93e-134 |
|
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: 412.94 E-value: 2.93e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 3 QKSKTLNGNEAAA-HISYPFTEVAAIYPITPSSPMAEITDKWAAhgKKNmfgqrVRVVELQSEAGASGTIHGSLAAGALT 81
Cdd:COG0674 1 GKRVLMDGNEAVAlGAIAAGCRVIAAYPITPSTEIAEYLAEWLA--ELG-----GVVVQAESEIAAIGAVIGASAAGARA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 82 TTYTASQGLLLMIPNMYKLVGELLPGVFHVSARALATHALSIFGDHQDVMAC-----RQTGFGFLAASNAQEVMDLGCLA 156
Cdd:COG0674 74 MTATSGPGLSLMQEGLGLAAGAELPLVIVVVQRAGPSTGLPIKGDQSDLMQAlygghGDTGWIVLAPSSVQEAFDLTIIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 157 HLAAIKSRMPFLHFFDGFRTSHEYqNVNVIDFEDIQDLVDYqaiKEFRARALSpEKPVVR-GTAQnPDIYFQG---KELP 232
Cdd:COG0674 154 FNLAEKYRVPVIVLFDGFLGSHEE-PVELPDDEEVKILPRP---EEYRPYALD-EDPRAIpGTAQ-PDVYFTGlehDETE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 233 NPyyKAVPEVVENYMQELEKIIgRSYNLFDYHGDPQAKHIIIAMGSVCDTIEETVDHLNEQGRKVGLIKVRLYRPFSAEH 312
Cdd:COG0674 228 DP--ENAEKMVEKRMRKFEKIR-DELPRVEYYGAEDAEVVIVAMGSTAGTAKEAVDRLREEGIKVGLLRVRLLRPFPAEA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 313 LLSAIpDTVKKIAVLDRTKEpGslgePLYQDVVHAYKNSQlnpeIIGGRYGLGSKETRPSHIISVFDNLAEDKPKdnFTI 392
Cdd:COG0674 305 LREAL-KGVKKVAVVERNKS-G----QLALDVRAALGADR----VVGGIYGLGGRPFTPEEILAVIEELLKGAPK--FTL 372
|
|
| POR_N |
pfam01855 |
Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N ... |
23-247 |
1.98e-89 |
|
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: 287.62 E-value: 1.98e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 23 EVAAIYPITPSSPMAEITDKWAAHGKKNmfgqRVRVVELQSEAGASGTIHGSLAAGALTTTYTASQGLLLMIPNMYKLVG 102
Cdd:pfam01855 8 DVIAAYPITPSSEIAEEAAEWAANGEKG----DVVVIQMESEIGAISAVIGAAAAGARAATATSGQGLLLMIENLGKAAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 103 ELLPGVFHVSARALATHALSIFGDHQDVMACRQTGFGFLAASNAQEVMDLGCLAHLAAIKSRMPFLHFFDGFRTSHEYQN 182
Cdd:pfam01855 84 ERLPVVIHVVARAGPSPGLSIFGDHSDVMAARDTGWIVLASENVQEAFDFALVAFNLAEKVRTPVIHLFDGFRTSHEREK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501422877 183 VNVIDFEDIQDLVDYQAIKEFRAR-ALSPEKPVVRGTAQNPDIYFQGKELPNPYYKAVPEVVENYM 247
Cdd:pfam01855 164 VELPPDEDEKDLIDEFLPPYKRKRyGLDPEMPIARGTAQNPDTYFEHREYGNPAYDAAEVVIEEVM 229
|
|
| TPP_PFOR |
cd02018 |
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ... |
806-1110 |
3.26e-75 |
|
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) subfamily, TPP-binding module; PFOR catalyzes the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. PFORs can be homodimeric, heterodimeric, or heterotetrameric, depending on the organism. These enzymes are dependent on TPP and a divalent metal cation as cofactors.
Pssm-ID: 238976 [Multi-domain] Cd Length: 237 Bit Score: 248.55 E-value: 3.26e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 806 LFEFHGACPGCGETPYYRLLTQLFG--DRMLIANATGCSSIYCASAPSIPFtinsegrGPAWANSLFEDNAEYGYGMyla 883
Cdd:cd02018 1 LTEEHGACAGCGEVTAVRVVLAALPapEDTVIANSTGCSSVYASTAPFNSW-------AVPWVNSLFEDANAVASGL--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 884 sdyiqdrlaELAREVLETQQGDQDLnqaleewlhvrkdgekskeaakklinllnnrnldanttlkhiaeyqdyliKRSQW 963
Cdd:cd02018 71 ---------KRGLKARFPKDRELDK--------------------------------------------------KKDVV 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 964 LIGGDGWAYDIGFGGLDHVLSTGEDVNTLVMDTEVYSNTGGQSSKATQTAAMAKFASSGKATMKKDLGMMAMSYGYVYVA 1043
Cdd:cd02018 92 VIGGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGKKEDKKDLVLIAATHGCVYVA 171
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501422877 1044 QVSMgANMNQTLKAFLEAEQY-PGPSLIIAYSPCIN-HGIrsGMGTSISQEKAAVDSGYWHLYRYNPQL 1110
Cdd:cd02018 172 RLSP-ALKKHFLKVVKEAISRtDGPTFIHAYTPCITeWGI--GSGKSLELARKAVKSRMFPLFEYDPRE 237
|
|
| PorG |
COG1014 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, gamma ... |
414-847 |
6.80e-65 |
|
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, gamma subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, gamma subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440638 [Multi-domain] Cd Length: 424 Bit Score: 226.50 E-value: 6.80e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 414 SDTISCKFWGLGSDGTVGANQSAVKIIgDHTDLYAQAYFSYDSKKSGGTTVSHLRFGKQPIRAPyLVYNADYVACHNPAF 493
Cdd:COG1014 2 AMDLEIRIAGVGGQGVVTAGKILAKAA-MREGYYVQGYPSYGSEQRGGPVVSHVRISDEPIRSP-LIDEADVLIALDPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 494 VNNYdlLQGLKAGGTFVLNCPWSKEDLeEKLPasmKRYLAENDINFYIIDAISIAGEiGLGN--RINMIMQSAFFKLADv 571
Cdd:COG1014 80 LDRV--LDGLKPGGVLIVNSSLVPPEV-WRLP---QEALERKDIRVYVIDATKIAKE-LLGNarVANTVMLGALAALLG- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 572 IPIEDavkyLKESVVENYGDKGQKVVDMNNLAIDKGIDSLIKVDIPKAWKDAQEEEYEESESEPEFVTNIQKPMAkhegd 651
Cdd:COG1014 152 LPLEA----LEEAIEETFGKKGEKVVELNLKAFEAGYEAAKEVFALAAAPAPLVLLAGNAAAALGAAAGGAAFAA----- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 652 DLPVSAFkgMEDGTFPLRTTAYEKRGIAVNIPEWQIDKCIQCNQCSYICPHAVIR-PYLLDEEEVQRAPETFETKQATGK 730
Cdd:COG1014 223 AYPITPS--TSLIEAAAAAAAKVGGVVAEEEAAAAAAAAAAAAAAAGAAAAAAGGgGGAALATEGLGLAGMTETPVVAVA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 731 DMDDLSYRIQVSPLDCTGCGNCADICPAKGKALIMEPAEEQIEQQEDNWEFAQTITEKTDRVNTKTLKGSQFVKPLFEFH 810
Cdd:COG1014 301 APRPGPGTGTPTEEEQGLLLLAAGGGGGEAPALALAPDTEEELLFAAAAAFALAEYAQALLLLLLLQLLVLLLTDLLLLL 380
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 501422877 811 ------GACPGCGETPYYRLLTQLFGDRMLIANATGCSSIYCA 847
Cdd:COG1014 381 ldllrrRAGLGAEEAEARRKLLAAEGRAARAAGGGGGGGGGGG 423
|
|
| TPP_PYR_PFOR_IOR-alpha_like |
cd07034 |
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ... |
10-173 |
9.90e-51 |
|
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: 176.15 E-value: 9.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 10 GNEAAAHISYPFT-EVAAIYPITPSSPMAEITDKWAahgkknMFGQRVRVVELQSEAGASGTIHGSLAAGALTTTYTASQ 88
Cdd:cd07034 1 GNEAVARGALAAGvDVVAAYPITPSTEIAETLAKAV------LGELGGVVVQAESEHAAAEAAIGASAAGARAMTATSGP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 89 GLLLMIPNMYKLVGELLPGVFHVSARALATHALsIFGDHQDVMACRQTGFGF--LAASNAQEVMDLGCLAHLAAIKSRMP 166
Cdd:cd07034 75 GLNLMAEALYLAAGAELPLVIVVAQRPGPSTGL-PKPDQSDLMAARYGGHPWpvLAPSSVQEAFDLALEAFELAEKYRLP 153
|
....*..
gi 501422877 167 FLHFFDG 173
Cdd:cd07034 154 VIVLSDG 160
|
|
| porA |
PRK09622 |
2-oxoacid:ferredoxin oxidoreductase subunit alpha; |
9-384 |
3.49e-50 |
|
2-oxoacid:ferredoxin oxidoreductase subunit alpha;
Pssm-ID: 181999 [Multi-domain] Cd Length: 407 Bit Score: 183.43 E-value: 3.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 9 NGNEAAAH-ISYPFTEVAAIYPITPSSPMAEITDKWAAHGKKNmfGQRVRVvelQSEAGASGTIHGSLAAGALTTTYTAS 87
Cdd:PRK09622 14 DGNTAASNaLRQAQIDVVAAYPITPSTPIVQNYGSFKANGYVD--GEFVMV---ESEHAAMSACVGAAAAGGRVATATSS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 88 QGLLLMIPNMYKLVGELLPGVFHVSARALAThALSIFGDHQDVMACRQTGFGFLAASNAQEVMDLGCLAHLAA--IKSRM 165
Cdd:PRK09622 89 QGLALMVEVLYQASGMRLPIVLNLVNRALAA-PLNVNGDHSDMYLSRDSGWISLCTCNPQEAYDFTLMAFKIAedQKVRL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 166 PFLHFFDGFRTSHEYQNVnvidfEDIQDLVDYQAIKEFRAR--ALSPEKPVVRGTAQNPDIYFQGK-ELPNPYYKAVPeV 242
Cdd:PRK09622 168 PVIVNQDGFLCSHTAQNV-----RPLSDEVAYQFVGEYQTKnsMLDFDKPVTYGAQTEEDWHFEHKaQLHHALMSSSS-V 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 243 VENYMQELEKIIGRSYNLFDYHGDPQAKHIIIAMGSVCDTIEETVDHLNEQGRKVGLIKVRLYRPFSAEHLLSAIpDTVK 322
Cdd:PRK09622 242 IEEVFNDFAKLTGRKYNLVETYQLEDAEVAIVALGTTYESAIVAAKEMRKEGIKAGVATIRVLRPFPYERLGQAL-KNLK 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501422877 323 KIAVLDRTKEPGSLGEpLYQDVVHAYKNSQ--LNPEIIGGRYGLGSKETRPSHIISVFDNLAED 384
Cdd:PRK09622 321 ALAILDRSSPAGAMGA-LFNEVTSAVYQTQgtKHPVVSNYIYGLGGRDMTIAHLCEIFEELNEN 383
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
808-1139 |
1.41e-49 |
|
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: 176.87 E-value: 1.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 808 EFHGACPGCGETPYYRLLTQLF-----GDRMLIANATGCSSIycasapsIPFTINSegrgpAWANSLFEDNAEYGYGMYL 882
Cdd:COG1013 11 PGHRWCPGCGHGIILRLLLKALdelldGDKTVVVSGIGCSSV-------APGYFNV-----PGFHTLHGRAAAVATGIKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 883 AsdyiqdrlaelarevletqqgdqdlnqaLEEwLHVrkdgekskeaakklinllnnrnldanttlkhiaeyqdylikrsq 962
Cdd:COG1013 79 A----------------------------NPD-LTV-------------------------------------------- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 963 WLIGGDGWAYDIGFGGLDHVLSTGEDVNTLVMDTEVYSNTGGQSSKATQTAAMAKFASSGKATMKKDLGMMAMSYGYVYV 1042
Cdd:COG1013 86 IVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHGATYV 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 1043 AQVSMGaNMNQTLKAFLEAEQYPGPSLIIAYSPCInhgirSGMGTSISQEKAAVDSGYWHLYRYNPQLKEEgknpFILDS 1122
Cdd:COG1013 166 ARASVG-DPKDLKKKIKKAIEHKGFSFIEVLSPCP-----TGWGRDPSKTIEWAKEGMWPLYEYDPGEKLR----LTYEP 235
|
330
....*....|....*..
gi 501422877 1123 KEPKeSLQDFLMSEVRF 1139
Cdd:COG1013 236 KDKI-PVGEFLKNQGRF 251
|
|
| porA |
PRK08367 |
pyruvate ferredoxin oxidoreductase subunit alpha; Reviewed |
6-383 |
3.19e-45 |
|
pyruvate ferredoxin oxidoreductase subunit alpha; Reviewed
Pssm-ID: 181403 [Multi-domain] Cd Length: 394 Bit Score: 168.52 E-value: 3.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 6 KTLNGNEAAA---HISYPftEVAAIYPITPSSPMAEITDKWAAHGKKNmfgqrVRVVELQSEAGASGTIHGSLAAGALTT 82
Cdd:PRK08367 5 TVMKANEAAAwaaKLAKP--KVIAAFPITPSTLVPEKISEFVANGELD-----AEFIKVESEHSAISACVGASAAGVRTF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 83 TYTASQGLLLMIPNMYKLVGELLPGVFHVSARALAThALSIFGDHQDVMACRQTGFGFLAASNAQEVMDLGCLAHLAAIK 162
Cdd:PRK08367 78 TATASQGLALMHEVLFIAAGMRLPIVMAIGNRALSA-PINIWNDWQDTISQRDTGWMQFYAENNQEALDLILIAFKVAED 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 163 SR--MPFLHFFDGFRTSHEYQNVNVIDFEDIQD-LVDYqaikEFRARALSPEKPVVRGTAQNPDIYFQGKELPNPYYKAV 239
Cdd:PRK08367 157 ERvlLPAMVGFDAFILTHTVEPVEIPDQEVVDEfLGEY----EPKHAYLDPARPITQGALAFPAHYMEARYTVWEAMENA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 240 PEVVENYMQELEKIIGRSYNLFDYHGDPQAKHIIIAMGSVCDTIEETVDHLNEQGRKVGLIKVRLYRPFSAEHlLSAIPD 319
Cdd:PRK08367 233 KKVIDEAFAEFEKKFGRKYQKIEEYRTEDAEIIFVTMGSLAGTLKEFVDKLREEGYKVGAAKLTVYRPFPVEE-IRALAK 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501422877 320 TVKKIAVLDRTKEPGsLGEPLYQDVVHAYKNSQLNPEIIGGRYGLGSKETrpshiisVFDNLAE 383
Cdd:PRK08367 312 KAKVLAFLEKNISFG-LGGAVFADASAALVNESEKPKILDFIIGLGGRDV-------TFKQLDE 367
|
|
| vorA |
PRK08366 |
2-ketoisovalerate ferredoxin oxidoreductase subunit alpha; Reviewed |
6-381 |
1.88e-40 |
|
2-ketoisovalerate ferredoxin oxidoreductase subunit alpha; Reviewed
Pssm-ID: 169406 [Multi-domain] Cd Length: 390 Bit Score: 154.39 E-value: 1.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 6 KTLNGNEAAAHIS-YPFTEVAAIYPITPSSPMAEITDKWAAHGKKNmfgqrVRVVELQSEAGASGTIHGSLAAGALTTTY 84
Cdd:PRK08366 4 KVVSGNYAAAYAAlHARVQVVAAYPITPQTSIIEKIAEFIANGEAD-----IQYVPVESEHSAMAACIGASAAGARAFTA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 85 TASQGLLLMIPNMYKLVGELLPGVFHVSARALAThALSIFGDHQDVMACRQTGFGFLAASNAQEVMDLGCLAHLAAIKSR 164
Cdd:PRK08366 79 TSAQGLALMHEMLHWAAGARLPIVMVDVNRAMAP-PWSVWDDQTDSLAQRDTGWMQFYAENNQEVYDGVLMAFKVAETVN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 165 MPFLHFFDGFRTSHEYQNVNVIDfediQDLVDyqaikEFraraLSPEKPVVRGTAQNPDIYFQGKELPNPYY-------K 237
Cdd:PRK08366 158 LPAMVVESAFILSHTYDVVEMIP----QELVD-----EF----LPPRKPLYSLADFDNPISVGALATPADYYefrykiaK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 238 AVPE---VVENYMQELEKIIGRSYN-LFDYHGDPQAKHIIIAMGSVCDTIEETVDHLNEQGRKVGLIKVRLYRPFSAEHL 313
Cdd:PRK08366 225 AMEEakkVIKEVGKEFGERFGRDYSqMIETYYTDDADFVFMGMGSLMGTVKEAVDLLRKEGYKVGYAKVRWFRPFPKEEL 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501422877 314 LSaIPDTVKKIAVLDRTKEPGSLGePLYQDVVHAYKNSQLNPEIIGGRYGLGSKETRPSHIISVFDNL 381
Cdd:PRK08366 305 YE-IAESVKGIAVLDRNFSFGQEG-ILFTEAKGALYNTDARPIMKNYIVGLGGRDFTVNDVKAIAEDM 370
|
|
| POR |
pfam01558 |
Pyruvate ferredoxin/flavodoxin oxidoreductase; This family includes a region of the large ... |
425-609 |
6.77e-35 |
|
Pyruvate ferredoxin/flavodoxin oxidoreductase; This family includes a region of the large protein pyruvate-flavodoxin oxidoreductase and the whole pyruvate ferredoxin oxidoreductase gamma subunit protein. It is not known whether the gamma subunit has a catalytic or regulatory role. Pyruvate oxidoreductase (POR) catalyzes the final step in the fermentation of carbohydrates in anaerobic microorganizms. This involves the oxidative decarboxylation of pyruvate with the participation of thiamine followed by the transfer of an acetyl moiety to coenzyme A for the synthesis of acetyl-CoA. 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: 426323 [Multi-domain] Cd Length: 172 Bit Score: 131.27 E-value: 6.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 425 GSDGTVGANqsavKIIG---DHTDLYAQAYFSYDSKKSGGTTVSHLRFGKQPIRAPYLVYNADYVACHNPAFVNNYdlLQ 501
Cdd:pfam01558 1 GGQGVVTAG----KILAkaaARAGYYVQATPEYGSEIRGGPVVSHVRISDEPIVPAIPVGEADLLVALDPETLDRH--LD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 502 GLKAGGTFVLNCPWSKEDLEEKlpasmKRYLAENDINFYIIDAISIAGEIGL-GNRINMIMQSAFFKLADvIPIEDAVKY 580
Cdd:pfam01558 75 GLKPGGIIIYNSSEVPPELLEK-----DLPAYPRLARVYGVPATEIAKEAGGnSRAANTVMLGALAALLG-LPLEALEEA 148
|
170 180
....*....|....*....|....*....
gi 501422877 581 LKESVvenygDKGQKVVDMNNLAIDKGID 609
Cdd:pfam01558 149 IKKRF-----PGKAKVIELNLKAFRAGYE 172
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
508-771 |
1.32e-26 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 109.81 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 508 TFVLNCPWSKEDLEEKLPASMKRYLAENDINFYIIDAISIAGEIGLGNRINMIMQSAFFKLADVIPIEDAVKYLKESVVE 587
Cdd:COG1145 1 AALLLDLKEALSPKLKVLYAVVTGILGKIILNVIAGALLKAVALGGLLPIIGILAKEAFDALKDVLGILGAIVIGIGAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 588 NYGDKGQKVVDMNNLAIDKGIDSLIKVDIPKAWKDAQEEEYEESESEPEFVTNIQKPMAKHEGDDLPVSAFKGmEDGTFP 667
Cdd:COG1145 81 IVRVGIAAADLNLKAVALVLLLALAVAGAAKRLIISAVKLVAGLVVAAGEVLLVIAAALAEAGLAILGAAAPV-DALAIS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 668 LRTTAYEKRGIAVNIPEWQID--KCIQCNQCSYICPHAVIRpylldeeevqrapetfetkqatgkdMDDLSYRIQVSPLD 745
Cdd:COG1145 160 GGKKIEEELKIAIKKAKAVIDaeKCIGCGLCVKVCPTGAIR-------------------------LKDGKPQIVVDPDK 214
|
250 260
....*....|....*....|....*.
gi 501422877 746 CTGCGNCADICPAkgKALIMEPAEEQ 771
Cdd:COG1145 215 CIGCGACVKVCPV--GAISLEPKEIE 238
|
|
| TPP_PFOR_porB_like |
cd03376 |
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ... |
810-1115 |
3.81e-26 |
|
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of proteins similar to the beta subunit (porB) of the Helicobacter pylori four-subunit pyruvate ferredoxin oxidoreductase (PFOR), which are also found in archaea and some hyperthermophilic bacteria. PFOR catalyzes the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. The 36-kDa porB subunit contains the binding sites for the cofactors, TPP and a divalent metal cation, which are required for activity.
Pssm-ID: 239471 [Multi-domain] Cd Length: 235 Bit Score: 108.09 E-value: 3.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 810 HGACPGCGETPYYRLLTQLFGDRMLIANATGCSSIYCASAPSIPFTINsegrgpaWANSLFEDNAEYGYGMylasdyiqd 889
Cdd:cd03376 5 HRACAGCGAALALRHVLKALGPDTVVVNPTGCLEVITTPYPYTAWRVP-------WIHVAFENAAAVASGI--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 890 rlaelarevletqqgdqdlnqalEEWLHVRKDGEKSKEAAkklinllnnrnldanttlkhiaeyqdylikrsqwlIGGDG 969
Cdd:cd03376 69 -----------------------EAALKALGRGKDITVVA-----------------------------------FAGDG 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 970 WAYDIGFGGLDHVLSTGEDVNTLVMDTEVYSNTGGQSSKATQTAAMAKFA-----SSGKATMKKDLGMMAMSYGYVYVAQ 1044
Cdd:cd03376 91 GTADIGFQALSGAAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTTTTpvgkvSFGKKQPKKDLPLIMAAHNIPYVAT 170
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501422877 1045 VSmGANMNQTLKAFLEAEQYPGPSLIIAYSPCINhGIRSGMGTSISQEKAAVDSGYWHLYRYnpqlkEEGK 1115
Cdd:cd03376 171 AS-VAYPEDLYKKVKKALSIEGPAYIHILSPCPT-GWRFDPSKTIEIARLAVETGFWPLYEY-----ENGK 234
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
665-770 |
8.46e-25 |
|
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: 98.97 E-value: 8.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 665 TFPLRTTAYEKRGIAVNIPEWQIDKCIQCNQCSYICPHAVIRPyllDEEEvqrapetfetkqatgkdmddlsyRIQVSPL 744
Cdd:COG1144 7 TEPGGTAAYKTGGWRVERPVVDEDKCIGCGLCWIVCPDGAIRV---DDGK-----------------------YYGIDYD 60
|
90 100
....*....|....*....|....*.
gi 501422877 745 DCTGCGNCADICPAkgKALIMEPAEE 770
Cdd:COG1144 61 YCKGCGICAEVCPV--KAIEMVPEEK 84
|
|
| PRK11865 |
PRK11865 |
pyruvate synthase subunit beta; |
810-1153 |
1.88e-23 |
|
pyruvate synthase subunit beta;
Pssm-ID: 183346 [Multi-domain] Cd Length: 299 Bit Score: 102.10 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 810 HGACPGCGETPYYRLLTQLFGDRMLIANATGCSSIYCASAPSIPFTInsegrgpAWANSLFEDNAEYGYGMYLAsdyiqd 889
Cdd:PRK11865 18 HRACAGCGAAIAMRLALKALGKNTVIVVATGCLEVITTPYPETAWNV-------PWIHVAFENAAAVASGIERA------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 890 rlaelarevletqqgdqdlnqaleewlhVRKDGEKSKEAAkklinllnnrnldanttlkhiaeyqdylikrsqwlIGGDG 969
Cdd:PRK11865 85 ----------------------------VKALGKKVNVVA-----------------------------------IGGDG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 970 WAYDIGFGGLDHVLSTGEDVNTLVMDTEVYSNTGGQSSKATQTAAMAKFASSGKATM-----KKDLGMMAMSYGYVYVAQ 1044
Cdd:PRK11865 102 GTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPAGKYSRgedrpKKNMPLIMAAHGIPYVAT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 1045 VSMGaNMNQTLKAFLEAEQYPGPSLIIAYSPCInHGIRSGMGTSISQEKAAVDSGYWHLYRYnpqlkEEGK-----NPFI 1119
Cdd:PRK11865 182 ASIG-YPEDFMEKVKKAKEVEGPAYIQVLQPCP-TGWGFPPEKTIEIGRLAVETGYWPLFEI-----ENGKfkityEPLH 254
|
330 340 350
....*....|....*....|....*....|....
gi 501422877 1120 LDsKEPKESLQDFLMSEVRFASLQkvfPETAEKL 1153
Cdd:PRK11865 255 LD-RRTRKPIEEYLKVQGRFKHLT---EEDIEIL 284
|
|
| PFOR_II |
pfam17147 |
Pyruvate:ferredoxin oxidoreductase core domain II; PFOR_II is a core domain of the anaerobic ... |
269-374 |
2.77e-21 |
|
Pyruvate:ferredoxin oxidoreductase core domain II; PFOR_II is a core domain of the anaerobic enzyme pyruvate:ferredoxin oxidoreductase and is necessary for inter subunit contacts in conjunction with domains I and IV.
Pssm-ID: 407280 [Multi-domain] Cd Length: 102 Bit Score: 89.63 E-value: 2.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 269 AKHIIIAMGSVCDTIEETVDHLNEQGRKVGLIKVRLYRPFSAEhLLSAIPDTVKKIAVLDRTKEPGSLGePLYQDVVHAY 348
Cdd:pfam17147 1 AEVVIVAMGSVAGTAKSAVDRLREEGIKVGLLRLRTFRPFPEE-ELKELLAGVKKVVVLDRNISFGSPG-QLGTEVKAAL 78
|
90 100
....*....|....*....|....*.
gi 501422877 349 KNSqlNPEIIGGRYGLGSKETRPSHI 374
Cdd:pfam17147 79 YDS--DPPVVNFIAGLGGRDITPEDI 102
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
23-173 |
1.07e-20 |
|
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; 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 group. 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. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. 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 enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.
Pssm-ID: 132915 [Multi-domain] Cd Length: 154 Bit Score: 89.71 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 23 EVAAIYPITPSSPMaeiTDKWAAHgkknmfgQRVRVVELQSEAGASGTIHGSLAAGALTTTY-TASQGLLLMIPNMYKLV 101
Cdd:cd06586 13 RHVFGYPGDEISSL---LDALREG-------DKRIIDTVIHELGAAGAAAGYARAGGPPVVIvTSGTGLLNAINGLADAA 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501422877 102 GELLPGVFHVSARALATHALSIFGDHQDVMACRQTGFGFLAASNAQEVMDLGCLAHLAAIKSRMPFLHFFDG 173
Cdd:cd06586 83 AEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYASQGPVVVRLPR 154
|
|
| PRK11864 |
PRK11864 |
3-methyl-2-oxobutanoate dehydrogenase subunit beta; |
810-1144 |
1.55e-19 |
|
3-methyl-2-oxobutanoate dehydrogenase subunit beta;
Pssm-ID: 237005 [Multi-domain] Cd Length: 300 Bit Score: 90.54 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 810 HGACPGCGETPYYRLLTQLFGDRMLIANATGCSSIYCASAPSIPFTINSegrgpawANSLFEDNAEYGYGMylasdyiqd 889
Cdd:PRK11864 18 NAACPGCGAPLGLRYLLKALGEKTVLVIPASCSTVIQGDTPKSPLTVPV-------LHTAFAATAAVASGI--------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 890 rlaelaREVLETQqgdqdlnqaleewlhvrkdGEKskeaakklinllnnrnlDANTTlkhiaeyqdylikrsQWliGGDG 969
Cdd:PRK11864 82 ------EEALKAR-------------------GEK-----------------GVIVV---------------GW--AGDG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 970 WAYDIGFGGLDHVLSTGEDVNTLVMDTEVYSNTGGQSSKATQTAAMAKFASSGKATMKKDLGMMAMSYGYVYVAQVSMG- 1048
Cdd:PRK11864 103 GTADIGFQALSGAAERNHDILYIMYDNEAYMNTGIQRSSSTPYGAWTTTTPGGKREHKKPVPDIMAAHKVPYVATASIAy 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 1049 -ANMNQTLKaflEAEQYPGPSLIIAYSPCINhGIRSGMGTSISQEKAAVDSGYWHLYRY-NPQLKEEGKNPFILDSKEPK 1126
Cdd:PRK11864 183 pEDFIRKLK---KAKEIRGFKFIHLLAPCPP-GWRFDPDKTIEIARLAVETGVWPLFEYeNGKFKLNSPSKTLLDKKKRK 258
|
330
....*....|....*...
gi 501422877 1127 EsLQDFLMSEVRFASLQK 1144
Cdd:PRK11864 259 P-VEEYLKLQGRFKHLTE 275
|
|
| EKR |
pfam10371 |
Domain of unknown function; EKR is a short, 33 residue, domain found in bacterial and some ... |
637-679 |
3.80e-19 |
|
Domain of unknown function; EKR is a short, 33 residue, domain found in bacterial and some lower eukaryotic species which lies between a POR (pyruvate ferredoxin/flavodoxin oxidoreductase) pfam01558 and the 4Fe-4S binding domain Fer4 pfam00037. It contains a characteriztic EKR sequence motif. The exact function of this domain is not known.
Pssm-ID: 431238 [Multi-domain] Cd Length: 54 Bit Score: 82.13 E-value: 3.80e-19
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 501422877 637 FVTNIQKPMAKHEGDDLPVSAFKgmEDGTFPLRTTAYEKRGIA 679
Cdd:pfam10371 14 FVKNVLAPMNAGEGDELPVSAFP--EDGTFPTGTSAYEKRGIA 54
|
|
| EKR |
smart00890 |
Domain of unknown function; EKR is a short, 33 residue, domain found in bacterial and some ... |
637-680 |
4.37e-19 |
|
Domain of unknown function; EKR is a short, 33 residue, domain found in bacterial and some lower eukaryotic species which lies between a POR (pyruvate ferredoxin/flavodoxin oxidoreductase) and the 4Fe-4S binding domain Fer4. It contains a characteristic EKR sequence motif. The exact function of this domain is not known.
Pssm-ID: 197958 [Multi-domain] Cd Length: 57 Bit Score: 81.89 E-value: 4.37e-19
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 501422877 637 FVTNIQKPMAKHEGDDLPVSAFKgmEDGTFPLRTTAYEKRGIAV 680
Cdd:smart00890 16 FVKNVVAPMNAGEGDDLPVSAFP--EDGTFPTGTAAYEKRGIAV 57
|
|
| PorC_KorC |
TIGR02175 |
2-oxoacid:acceptor oxidoreductase, gamma subunit, pyruvate/2-ketoisovalerate family; A number ... |
417-599 |
2.22e-18 |
|
2-oxoacid:acceptor oxidoreductase, gamma subunit, pyruvate/2-ketoisovalerate family; A number of anaerobic and microaerophilic species lack pyruvate dehydrogenase and have instead a four subunit, oxygen-sensitive pyruvate oxidoreductase, with either ferredoxins or flavodoxins (H. pylori) used as the acceptor. Several related four-subunit enzymes may exist in the same species. This model describes the gamma subunit. In Pyrococcus furious, enzymes active on pyruvate and 2-ketoisovalerate share a common gamma subunit.
Pssm-ID: 274014 [Multi-domain] Cd Length: 177 Bit Score: 83.94 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 417 ISCKFWGLGSDGTVGANQSAVKIIGdHTDLYAQAYFSYDSKKSGGTTVSHLRFGKQPIRAPYLVYNADYVACHNPAFVNN 496
Cdd:TIGR02175 2 IEIRFHGRGGQGAVTASQLLAEAAF-LEGKYAQAFPEFGAERRGAPVRAFLRISDRPIRVHSQIYEPDYVVVLDPTLLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 497 YDLLQGLKAGGTFVLNCPWSKEDLEEKLpasmkrylaendiNFYIIDAISIAGEIgLGNRI-NMIMQSAFFKLADVIPIE 575
Cdd:TIGR02175 81 VNVTAGLKEDGILIVNTKKDPEELRKEL-------------KVYTVDATKIALVV-LGRPIvNTPMLGAFAKVTGLVSLE 146
|
170 180
....*....|....*....|....
gi 501422877 576 DAVKYLKESVVENYGDKGQKVVDM 599
Cdd:TIGR02175 147 SLEKAIEESFPGKLAEANAKAVER 170
|
|
| PRK08534 |
PRK08534 |
pyruvate ferredoxin oxidoreductase subunit gamma; Reviewed |
417-614 |
3.03e-14 |
|
pyruvate ferredoxin oxidoreductase subunit gamma; Reviewed
Pssm-ID: 181460 [Multi-domain] Cd Length: 181 Bit Score: 71.99 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 417 ISCKFWGLGSDGTVGANQ---SAVKIIGDhtdlYAQAYFSYDSKKSGGTTVSHLRFGKQPIRAPYLVYNADYVACHNPAF 493
Cdd:PRK08534 2 IEIRFHGRGGQGAVTAAEilaKAAFEDGK----FSQAFPFFGVERRGAPVMAFTRIDDKPIRLRSQIYEPDYVIVQDPTL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 494 VNNYDLLQGLKAGGTFVLNCPWSKEDLEEKLPASMkrylaendinfYIIDAISIAGEIgLGNRI-NMIMQSAFFKLADVI 572
Cdd:PRK08534 78 LDSVDVTSGLKKDGIIIINTTKDPEDLKYDTKAKV-----------YTIDATKIALDV-LGVPIvNTTMLGAFAGATGEV 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 501422877 573 PIEdavkYLKESVVENYgdKGqKVVDMNNLAIDKGIDSLIKV 614
Cdd:PRK08534 146 SLE----SLKKAILERF--PG-KLGEKNAEAVEKAYNLMKEE 180
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
688-777 |
9.12e-14 |
|
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 67.08 E-value: 9.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 688 DKCIQCNQCSYICPHAVIRPylldeeevqrapetfetkqatgkDMDDLSYRIQVSPLDCTGCGNCADICPAkgKALIMEP 767
Cdd:COG1143 2 DKCIGCGLCVRVCPVDAITI-----------------------EDGEPGKVYVIDPDKCIGCGLCVEVCPT--GAISMTP 56
|
90
....*....|
gi 501422877 768 AEEQIEQQED 777
Cdd:COG1143 57 FELAVEDREE 66
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
963-1077 |
1.59e-13 |
|
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: 70.25 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 963 WLIGGDGWAYDIGFGGLDHVLSTGEDVNTLVMDTEVYSNTGGQSSkATqTAAMAKFASSGKATMKK--DLGMMAMSYGYV 1040
Cdd:cd03375 73 IVVSGDGDLAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQAS-PT-TPEGFKTKTTPYGNIEEpfNPLALALAAGAT 150
|
90 100 110
....*....|....*....|....*....|....*..
gi 501422877 1041 YVAQVSMGaNMNQTLKAFLEAEQYPGPSLIIAYSPCI 1077
Cdd:cd03375 151 FVARGFSG-DIKQLKEIIKKAIQHKGFSFVEVLSPCP 186
|
|
| PRK14029 |
PRK14029 |
pyruvate/ketoisovalerate ferredoxin oxidoreductase subunit gamma; Provisional |
417-595 |
3.30e-13 |
|
pyruvate/ketoisovalerate ferredoxin oxidoreductase subunit gamma; Provisional
Pssm-ID: 172523 [Multi-domain] Cd Length: 185 Bit Score: 69.28 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 417 ISCKFWGLGSDGTVganqSAVKIIGDHTDL---YAQAYFSYDSKKSGGTTVSHLRFGKQPIRAPYLVYNADYVACHNPAF 493
Cdd:PRK14029 2 IEIRFHGRGGQGAV----TAANILAEAAFLegkYVQAFPFFGVERRGAPVTAFTRIDEKPIRIKTQIYEPDVVVVLDPSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 494 VNNYDLLQGLKAGGTFVLNCPWSKEDLEEKLPASMKRyLAendinfyIIDAISIAGEIgLGNRI-NMIMQSAFFKLADVI 572
Cdd:PRK14029 78 LDTVDVTAGLKDGGIVIVNTEKSKEEVLEKLKKKPKK-LA-------LVDATTIALEI-LGLPItNTAILGAVAKATGLV 148
|
170 180
....*....|....*....|...
gi 501422877 573 PIEDAVKYLKESVVENYGDKGQK 595
Cdd:PRK14029 149 KIESVEEAIKDTFSGELGEKNAK 171
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
678-770 |
4.15e-11 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 59.74 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 678 IAVNIPEWQIDKCIQCNQCSYICPHAVIRpylldeeevqrapetfetkqatgkdMDDlSYRIQVSPLDCTGCGNCADICP 757
Cdd:COG1149 1 VKRKIPVIDEEKCIGCGLCVEVCPEGAIK-------------------------LDD-GGAPVVDPDLCTGCGACVGVCP 54
|
90
....*....|...
gi 501422877 758 AkgKALIMEPAEE 770
Cdd:COG1149 55 T--GAITLEEREA 65
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
963-1077 |
1.02e-09 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 61.01 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 963 WLIGGDGWAYDIGFGGLDHVLSTGEDVNTLVMDTEVYSNTGGQSSKATQTAAMAKfaSSGKATMKK--DLGMMAMSYGYV 1040
Cdd:PRK11867 91 IVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTK--TTPYGSIEPpfNPVELALGAGAT 168
|
90 100 110
....*....|....*....|....*....|....*..
gi 501422877 1041 YVAQvSMGANMNQTLKAFLEAEQYPGPSLIIAYSPCI 1077
Cdd:PRK11867 169 FVAR-GFDSDVKQLTELIKAAINHKGFSFVEILQPCP 204
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
690-759 |
2.52e-09 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 463724 [Multi-domain] Cd Length: 51 Bit Score: 54.07 E-value: 2.52e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 690 CIQCNQCSYICPHAVIRPylldeEEVQRAPETFetkqatgkdmddlsyRIQVSPLDCTGCGNCADICPAK 759
Cdd:pfam12838 1 CIGCGACVAACPVGAITL-----DEVGEKKGTK---------------TVVIDPERCVGCGACVAVCPTG 50
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
688-770 |
4.47e-09 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 53.94 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 688 DKCIQCNQCSYICPHAVIRPylldEEEVQRApetfetkqatgkdmddlsyrIQVSPLDCTGCGNCADICPAkgKALIMEP 767
Cdd:COG1146 8 DKCIGCGACVEVCPVDVLEL----DEEGKKA--------------------LVINPEECIGCGACELVCPV--GAITVED 61
|
...
gi 501422877 768 AEE 770
Cdd:COG1146 62 DEP 64
|
|
| PRK05844 |
PRK05844 |
pyruvate flavodoxin oxidoreductase subunit gamma; Validated |
432-609 |
5.08e-09 |
|
pyruvate flavodoxin oxidoreductase subunit gamma; Validated
Pssm-ID: 180284 [Multi-domain] Cd Length: 186 Bit Score: 57.09 E-value: 5.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 432 ANQSAV---KIIGD---HTDLYAQAYFSYDSKKSGGTTVSHLRFGKQPIRAPYLVYNADYVACHNPAFVNNYDLLQGLKA 505
Cdd:PRK05844 10 AGQGAVtgaKGLADviaKTGKEVQAFAFYGSAKRGAAMTAYNRIDDEPILNHEKFMQPDYVLVIDPGLVFIENIFANEKE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 506 GGTFVLNCPWSKEDLEEKLPAsmkryLAENDInfYIIDAISIAGEIgLGNRI-NMIMQSAFFKLADVIPIEdavkYLKES 584
Cdd:PRK05844 90 DTKYIITTHLSKEELIEKKPE-----LKGKKV--FLVDCIKISMET-IGRPIpNTPMLGALMKVSGMLEID----AFKEA 157
|
170 180
....*....|....*....|....*.
gi 501422877 585 VVENYGDK-GQKVVDMNNLAIDKGID 609
Cdd:PRK05844 158 FKKVLGKKlPQKVIDANMLAIQRAYE 183
|
|
| PRK14028 |
PRK14028 |
pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional |
423-766 |
6.71e-09 |
|
pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional
Pssm-ID: 172522 [Multi-domain] Cd Length: 312 Bit Score: 58.86 E-value: 6.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 423 GLGSDGTVganqSAVKIIGDHT---DLYAQAYFSYDSKKSGGTTVSHLRFGKQPIRAPYLVYNADYVACHNPAFVNNYDL 499
Cdd:PRK14028 9 GRGGQGIV----TATYIIANAAvidGFYAIANPEFGAERRGAPVKAFLTISKNPIEDQEPVKTPDVAVIFDDKLIDPMRF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 500 -LQGLKAGGTFVLNcpwskedlEEKLPASMKRYLAENDINFYIIDAISIA-GEIGLgNRINMIMQSAFFKLADVIPIEda 577
Cdd:PRK14028 85 aIDAVKPGGYVILN--------TGKQPEEARKLVGRDDVYIVVLDAIGIArKHLKL-DVPNGPLAGAFSKVMGFPSLE-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 578 vkylkeSVVENYGDKGQKVVDMNNLAIDKGIDslIKVDIPKAWKDAQEEEYEESESEPEFVTNIQKPMAKHEGDdlpvsa 657
Cdd:PRK14028 154 ------SIRTAFETQLGKAVEENFAATKEAYE--VAVVIPPEKVDASAKPKGIISTTSAFLTGPYELVGWQEVN------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 658 fKGmeDGTFPLRTTAYEKRGIAVNIPEWQIDKCIQCNQCSYICPH-AVIRPYLldEEEVQRApETFETKqatgkdMDDLS 736
Cdd:PRK14028 220 -KA--GAVFPGSSFPYLTGGWRIDKPVIDHSKCIMCRKCWLYCPDdAIIEAWR--EAEGPRG-RKFRMK------MIDFD 287
|
330 340 350
....*....|....*....|....*....|
gi 501422877 737 YRIqvspldCTGCGNCADICPAKGKALIME 766
Cdd:PRK14028 288 YQY------CKGCGVCAEVCPTGAIQMVRE 311
|
|
| PRK08659 |
PRK08659 |
2-oxoacid:acceptor oxidoreductase subunit alpha; |
4-326 |
1.09e-07 |
|
2-oxoacid:acceptor oxidoreductase subunit alpha;
Pssm-ID: 181526 [Multi-domain] Cd Length: 376 Bit Score: 55.64 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 4 KSKTLNGNEAAAHisypftevAAI---------YPITPSSPMAEITDKW--AAHGKknmfgqrvrVVELQSEAGASGTIH 72
Cdd:PRK08659 3 KVDFLQGNEACAE--------GAIaagcrffagYPITPSTEIAEVMARElpKVGGV---------FIQMEDEIASMAAVI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 73 GSLAAGALTTTYTASQGLLLMIPNM-YKLVGELlPGVFHVSARALATHALSIFGDHQDVMACRqtgFG--------FLAA 143
Cdd:PRK08659 66 GASWAGAKAMTATSGPGFSLMQENIgYAAMTET-PCVIVNVQRGGPSTGQPTKPAQGDMMQAR---WGthgdhpiiALSP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 144 SNAQEVMDLGCLAHLAAIKSRMPFLHFFDGFrTSHEYQNVNVIDFEDIQdLVDYQAIKEFRARALsPEKPVVRGTAQNPD 223
Cdd:PRK08659 142 SSVQECFDLTIRAFNLAEKYRTPVIVLADEV-VGHMREKVVLPEPDEIE-IIERKLPKVPPEAYK-PFDDPEGGVPPMPA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 224 ------IYFQG---KElpNPYYKAVPEVVENYMQEL-EKIIGRSYNLFDYHG----DpqAKHIIIAMGSVCDTIEETVDH 289
Cdd:PRK08659 219 fgdgyrFHVTGlthDE--RGFPTTDPETHEKLVRRLvRKIEKNRDDIVLYEEymleD--AEVVVVAYGSVARSARRAVKE 294
|
330 340 350
....*....|....*....|....*....|....*..
gi 501422877 290 LNEQGRKVGLIKVRLYRPFsAEHLLSAIPDTVKKIAV 326
Cdd:PRK08659 295 AREEGIKVGLFRLITVWPF-PEEAIRELAKKVKAIVV 330
|
|
| PRK06853 |
PRK06853 |
indolepyruvate oxidoreductase subunit beta; Reviewed |
454-609 |
2.67e-07 |
|
indolepyruvate oxidoreductase subunit beta; Reviewed
Pssm-ID: 180732 [Multi-domain] Cd Length: 197 Bit Score: 52.17 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 454 YDSKKS--------GGTTVSHLRFGKqPIRAPyLVYN--ADYVAchnpAF-----VNNYDLlqgLKAGGTFVLNC----P 514
Cdd:PRK06853 32 YDVKVSevhgmsqrGGSVVSHVRFGD-EVYSP-LIPEgkADLLL----AFepleaLRYLPY---LKKGGKVVVNTqpivP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 515 WSKEDLEEKLPASMKRY--LAENDINFYIIDAISIAGEigLGNRI--NMIMQSAffkLADVIPIEDavKYLKESVVENYg 590
Cdd:PRK06853 103 VPVSLGLAKYPEDEEILeeLKKLGIKVYVIDAEKIAKE--AGNIKaaNVVLLGA---LAKFLPIDE--ETLEEAIKERV- 174
|
170
....*....|....*....
gi 501422877 591 dkGQKVVDMNNLAIDKGID 609
Cdd:PRK06853 175 --PPKFVEVNLKAFEAGRE 191
|
|
| Fer4_16 |
pfam13484 |
4Fe-4S double cluster binding domain; |
690-759 |
1.33e-06 |
|
4Fe-4S double cluster binding domain;
Pssm-ID: 463893 [Multi-domain] Cd Length: 65 Bit Score: 46.71 E-value: 1.33e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501422877 690 CIQCNQCSYICPHAVIR--PYLLDEEEVqRAPETFETKQATGKDMDDLSYRiqvsplDCTGCGNCADICPAK 759
Cdd:pfam13484 1 CGSCGKCIDACPTGAIVgpEGVLDARRC-ISYLTIEKKGLIPDELRCLLGN------RCYGCDICQDVCPWN 65
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
689-757 |
1.34e-06 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 46.39 E-value: 1.34e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501422877 689 KCIQCNQCSYICPHAVIRPYLLDEEevqrapetfetkqatgkdmddlsYRIQVSPLDCTGCGNCADICP 757
Cdd:pfam13187 1 KCTGCGACVAACPAGAIVPDLVGQT-----------------------IRGDIAGLACIGCGACVDACP 46
|
|
| porD |
PRK09625 |
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed |
683-776 |
1.36e-06 |
|
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 236596 [Multi-domain] Cd Length: 133 Bit Score: 48.98 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 683 PEWQIDKCIQCNQCSYICPHAVIrpylldeeeVQRapetfeTKQATGKDMDDlsyriqvspldCTGCGNCADICPAKGKA 762
Cdd:PRK09625 54 PVHNNEICINCFNCWVYCPDAAI---------LSR------DKKLKGVDYSH-----------CKGCGVCVEVCPTNPKS 107
|
90
....*....|....
gi 501422877 763 LIMEPaeEQIEQQE 776
Cdd:PRK09625 108 LLMFE--EQIENET 119
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
683-767 |
1.44e-06 |
|
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: 48.55 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 683 PEWQIDKCIQCNQCSYICPHAVIRpyLLDEEEVQRAPETFETKqatgkdmddlsyriqvspldCTGCGNCADICPakGKA 762
Cdd:cd10549 1 LKYDPEKCIGCGICVKACPTDAIE--LGPNGAIARGPEIDEDK--------------------CVFCGACVEVCP--TGA 56
|
....*
gi 501422877 763 LIMEP 767
Cdd:cd10549 57 IELTP 61
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
683-776 |
1.45e-06 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 47.03 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 683 PEWQIDKCIQCNQCSYICPHAVIRpylldeeevqrapetfetkqatgkdMDDLSYRIqvSPLDCTGCGNCADICPAkgKA 762
Cdd:COG2768 6 PYVDEEKCIGCGACVKVCPVGAIS-------------------------IEDGKAVI--DPEKCIGCGACIEVCPV--GA 56
|
90
....*....|....
gi 501422877 763 LIMEPaEEQIEQQE 776
Cdd:COG2768 57 IKIEW-EEDEEFQE 69
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
689-759 |
1.68e-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: 433017 [Multi-domain] Cd Length: 64 Bit Score: 46.54 E-value: 1.68e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501422877 689 KCIQCNQCSYICP-------HAVIRPYLLDEEEVQRAPETFETKQAtgkdmddlsyriqvsPLDCTGCGNCADICPAK 759
Cdd:pfam13183 1 RCIRCGACLAACPvylvtggRFPGDPRGGAAALLGRLEALEGLAEG---------------LWLCTLCGACTEVCPVG 63
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
965-1077 |
2.03e-06 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 51.03 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 965 IGGDGWAYDIGFGGLDHVLSTGEDVNTLVMDTEVYSNTGGQSSKATQTAAMAKFASSGKATMKKDLGMMAMSYGYVYVAQ 1044
Cdd:PRK05778 94 VGGDGDLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCALALAAGATFVAR 173
|
90 100 110
....*....|....*....|....*....|...
gi 501422877 1045 vSMGANMNQTLKAFLEAEQYPGPSLIIAYSPCI 1077
Cdd:PRK05778 174 -SFAGDVKQLVELIKKAISHKGFAFIDVLSPCV 205
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
688-757 |
2.16e-06 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 46.09 E-value: 2.16e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 688 DKCIQCNQCSYICPhAVIRPYLLDEEEVQRAPetfetkqatgkdmddlsyrIQVSPLDCTGCGNCADICP 757
Cdd:pfam13237 7 DKCIGCGRCTAACP-AGLTRVGAIVERLEGEA-------------------VRIGVWKCIGCGACVEACP 56
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
963-1072 |
2.72e-06 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 48.35 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 963 WLIGGDGWAYDIGfGGLDHVLSTGEDVNTLVMDTEVYSNTGGQSSKATQTaamAKFASSGKATMKKDLGMMAMSYGyVYV 1042
Cdd:pfam02775 50 VAIAGDGGFQMNL-QELATAVRYNLPITVVVLNNGGYGMTRGQQTPFGGG---RYSGPSGKILPPVDFAKLAEAYG-AKG 124
|
90 100 110
....*....|....*....|....*....|
gi 501422877 1043 AQVSMGANMNQTLKaflEAEQYPGPSLIIA 1072
Cdd:pfam02775 125 ARVESPEELEEALK---EALEHDGPALIDV 151
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
674-766 |
3.50e-06 |
|
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: 47.39 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 674 EKRGIAVNIPEWQIDKCIQCNQCSYICPHAVIRpylLDEEEVQRAPetfETKQATGKDMddlsyriqvsplDCTGCGNCA 753
Cdd:cd10549 26 GPNGAIARGPEIDEDKCVFCGACVEVCPTGAIE---LTPEGKEYVP---KEKEAEIDEE------------KCIGCGLCV 87
|
90
....*....|...
gi 501422877 754 DICPAkgKALIME 766
Cdd:cd10549 88 KVCPV--DAITLE 98
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
688-759 |
4.15e-06 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 45.80 E-value: 4.15e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501422877 688 DKCIQCNQCSYICPHAVIrpylldeeevqrapetfetkqatgkDMDDLSYRIQvsPLDCTGCGNCADICPAK 759
Cdd:COG4231 22 DKCTGCGACVKVCPADAI-------------------------EEGDGKAVID--PDLCIGCGSCVQVCPVD 66
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
678-759 |
6.57e-06 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 45.04 E-value: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 678 IAVNIPEWQIDKCIQCNQCSYICPHAVIRpylldeeevqrapetfetkqatgkdMDDlsYRIQVSPLDCTGCGNCADICP 757
Cdd:COG2221 5 IGTWPPKIDEEKCIGCGLCVAVCPTGAIS-------------------------LDD--GKLVIDEEKCIGCGACIRVCP 57
|
..
gi 501422877 758 AK 759
Cdd:COG2221 58 TG 59
|
|
| porD |
PRK09624 |
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed |
680-766 |
8.81e-06 |
|
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 170017 [Multi-domain] Cd Length: 105 Bit Score: 45.79 E-value: 8.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 680 VNIPEWQIDKCIQCNQCSYICPHAVIrpyLLDEEevqrapetfetkqatGKDMDDLSYriqvspldCTGCGNCADICPAK 759
Cdd:PRK09624 43 VFMPEFNRDKCVRCYLCYIYCPEPAI---YLDEE---------------GYPVFDYDY--------CKGCGICANECPTK 96
|
....*..
gi 501422877 760 GKALIME 766
Cdd:PRK09624 97 AIEMVRE 103
|
|
| NuoI |
TIGR01971 |
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ... |
688-770 |
1.17e-05 |
|
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: 45.87 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 688 DKCIQCNQCSYICPHAVIRpyLLDEEevqrapetfetkqatGKDMDDLSYRIQVSPLDCTGCGNCADICPAkgKALIMEP 767
Cdd:TIGR01971 43 EKCIGCTLCAAVCPADAIR--VVPAE---------------GEDGKRRLKFYEINFGRCIFCGLCEEACPT--DAIVLTP 103
|
...
gi 501422877 768 AEE 770
Cdd:TIGR01971 104 EFE 106
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
674-759 |
1.39e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 49.09 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 674 EKRGIAVNIPEWQIDKCIQCNQCSYICPHAVIRpylLDEEEVqrapetfetkqatgkdmddlsyrIQVSPLDCTGCGNCA 753
Cdd:COG1148 482 GELGVEPSVAEVDPEKCTGCGRCVEVCPYGAIS---IDEKGV-----------------------AEVNPALCKGCGTCA 535
|
....*.
gi 501422877 754 DICPAK 759
Cdd:COG1148 536 AACPSG 541
|
|
| fdxN_nitrog |
TIGR02936 |
ferredoxin III, nif-specific; Members of this family are homodimeric ferredoxins from nitrogen ... |
688-759 |
1.89e-05 |
|
ferredoxin III, nif-specific; Members of this family are homodimeric ferredoxins from nitrogen fixation regions of many nitrogen-fixing bacteria. As characterized in Rhodobacter capsulatus, these proteins are homodimeric, with two 4Fe-4S clusters bound per monomer. Although nif-specific, this protein family is not usiveral, as other nitrogenase systems may substitute flavodoxins, or different types of ferredoxin. [Central intermediary metabolism, Nitrogen fixation]
Pssm-ID: 274356 [Multi-domain] Cd Length: 91 Bit Score: 44.32 E-value: 1.89e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501422877 688 DKCIQCNQCSYICPHAVIRPYLLDEEEVQRAPETFEtkqatgkDMDDLSYRIQVSPLDCTGCGNCADICPAK 759
Cdd:TIGR02936 21 EKCIGCGRCYKVCGRDVLTLKGINEEGELVASDDDD-------DEIERKVMVVANPGNCIGCGACARVCPKK 85
|
|
| PRK05888 |
PRK05888 |
NADH-quinone oxidoreductase subunit NuoI; |
689-757 |
2.24e-05 |
|
NADH-quinone oxidoreductase subunit NuoI;
Pssm-ID: 235637 [Multi-domain] Cd Length: 164 Bit Score: 46.03 E-value: 2.24e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501422877 689 KCIQCNQCSYICPHAVIRpylldeeeVQRAPETFETKQATgkdmddlSYRIqvsplD---CTGCGNCADICP 757
Cdd:PRK05888 59 RCIACKLCAAICPADAIT--------IEAAEREDGRRRTT-------RYDI-----NfgrCIFCGFCEEACP 110
|
|
| Fer4_6 |
pfam12837 |
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ... |
682-705 |
3.33e-05 |
|
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 432822 [Multi-domain] Cd Length: 24 Bit Score: 41.83 E-value: 3.33e-05
|
| PRK08537 |
PRK08537 |
2-oxoacid:ferredoxin oxidoreductase subunit gamma; |
446-607 |
1.53e-04 |
|
2-oxoacid:ferredoxin oxidoreductase subunit gamma;
Pssm-ID: 181462 [Multi-domain] Cd Length: 177 Bit Score: 43.89 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 446 LYAQAYFSYDSKKSGGTTVSHLRFGKQPIRAPYlVYNADY-VACHNPAFVNNYDLLqglKAGGTFVLNcpwskEDLeekL 524
Cdd:PRK08537 32 KYAVQTQSYGPEARGGASKSEVVISDEEIDYPK-VISPDIlVAMSQEAYDKYLDDL---KEGGTVIVD-----PDL---V 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 525 PASMKRYlaENDINFYIIDAISIAGE-IGLGNRINMIMQSAFFKLADVIPIEDAVKYLKESVvenygDKGQKvvDMNNLA 603
Cdd:PRK08537 100 PIREIEY--EKKVKVYKVPFTEIAEEeIGLSIVANIVMLGALTKLTGIVSKEAIEKAILDSV-----PKGTE--EKNLMA 170
|
....
gi 501422877 604 IDKG 607
Cdd:PRK08537 171 FEKG 174
|
|
| ACS_1 |
cd01916 |
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ... |
687-775 |
4.00e-04 |
|
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.
Pssm-ID: 238897 [Multi-domain] Cd Length: 731 Bit Score: 44.71 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 687 IDKCIQCNQCSYICPHAVirpylldeeevqRAPETFEtKQATGkdmdDLSYRIQVSPLdCTGCGNCADICPAKGK--ALI 764
Cdd:cd01916 364 AAKCTDCGWCTRACPNSL------------RIKEAME-AAKEG----DFSGLADLFDQ-CVGCGRCEQECPKEIPiiNMI 425
|
90
....*....|.
gi 501422877 765 MEPAEEQIEQQ 775
Cdd:cd01916 426 EKAARERIKEE 436
|
|
| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
966-1077 |
4.16e-04 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 43.59 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 966 GGDGWAYDIGFGGLDHVLSTGEDVNTLVMDTEVYSNTGGQSSKATQTAAMAKFASSGKATMKKDLGMMAMSYGYVYVAQV 1045
Cdd:PRK11866 84 GGDGDGYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEPFNPIALALAAGATFVARG 163
|
90 100 110
....*....|....*....|....*....|....
gi 501422877 1046 SMG--ANMNQTLKaflEAEQYPGPSLIIAYSPCI 1077
Cdd:PRK11866 164 FSGdvKHLKEIIK---EAIKHKGFSFIDVLSPCV 194
|
|
| oorA |
PRK09627 |
2-oxoglutarate synthase subunit alpha; |
178-326 |
7.19e-04 |
|
2-oxoglutarate synthase subunit alpha;
Pssm-ID: 182002 [Multi-domain] Cd Length: 375 Bit Score: 43.16 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 178 HEYQNVNVIDFEDIQDLVDYQAI-----KEFRARALSPEKPVVrgtaQNPdiYFQGKEL--------PNPYYKAVPEVVE 244
Cdd:PRK09627 174 HMYGKAVIPDLEEVQKMIINRKEfdgdkKDYKPYGVAQDEPAV----LNP--FFKGYRYhvtglhhgPIGFPTEDAKICG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 245 NYMQELE-KIIGR-----SYNLFDYHGdpqAKHIIIAMGSVCDTIEETVDHLNEQGRKVGlikvrLYRPF----SAEHLL 314
Cdd:PRK09627 248 KLIDRLFnKIESHqdeieEYEEYMLDD---AEILIIAYGSVSLSAKEAIKRLREEGIKVG-----LFRPItlwpSPAKKL 319
|
170
....*....|..
gi 501422877 315 SAIPDTVKKIAV 326
Cdd:PRK09627 320 KEIGDKFEKILV 331
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
693-767 |
2.06e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319895 [Multi-domain] Cd Length: 154 Bit Score: 39.93 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 693 CNQCSYICPHAVIRPYLLDEEEVQ--RA--------PETFETK----------QATGKDMDDLSYRIQVSPLDCTGCGNC 752
Cdd:cd16373 59 CDACVEVCPTGALRPLDLEEQKVKmgVAvidkdrclAWQGGTDcgvcveacptEAIAIVLEDDVLRPVVDEDKCVGCGLC 138
|
90
....*....|....*.
gi 501422877 753 ADICPAKG-KALIMEP 767
Cdd:cd16373 139 EYVCPVEPpKAIVVEP 154
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
731-764 |
2.29e-03 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 38.10 E-value: 2.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 501422877 731 DMDDLSYRIQVSPLDCTGCGNCADICPA------KGKALI 764
Cdd:COG4231 9 DNRTTAMRYVIDEDKCTGCGACVKVCPAdaieegDGKAVI 48
|
|
| Fer4 |
pfam00037 |
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ... |
739-757 |
2.56e-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: 36.46 E-value: 2.56e-03
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
687-759 |
2.94e-03 |
|
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];
Pssm-ID: 440017 [Multi-domain] Cd Length: 420 Bit Score: 41.60 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 687 IDKCIQCNQCSYICPHAVI----------RPYLLDEeeVQRAPETFETKQATGKDMDDlsyriqvspldCTGCGNCADIC 756
Cdd:COG0247 77 LDACVGCGFCRAMCPSYKAtgdekdsprgRINLLRE--VLEGELPLDLSEEVYEVLDL-----------CLTCKACETAC 143
|
...
gi 501422877 757 PAK 759
Cdd:COG0247 144 PSG 146
|
|
| Fer4_18 |
pfam13746 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
694-757 |
4.98e-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: 404610 [Multi-domain] Cd Length: 114 Bit Score: 38.15 E-value: 4.98e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501422877 694 NQCSYICPHAVIRPYLLDEEEVQ-------------RAPETFETKQatgKDMddlsyRIQVSPLDCTGCGNCADICP 757
Cdd:pfam13746 4 NFCIYACPYGRFQSVMYDEDTLTvvydavrgegiygRKPPKAGLKT---KEL-----RQQKGVGDCIDCESCVQVCP 72
|
|
| PRK11869 |
PRK11869 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
966-1077 |
5.55e-03 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183349 [Multi-domain] Cd Length: 280 Bit Score: 40.15 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 966 GGDGWAYDIGFGGLDHVLSTGEDVNTLVMDTEVYSNTGGQSSKATQTAAMAKFASSGKATMKKDLGMMAMSYGYVYVAQV 1045
Cdd:PRK11869 85 GGDGDMYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVFEEPFNPIALAIALDASFVART 164
|
90 100 110
....*....|....*....|....*....|..
gi 501422877 1046 SMGaNMNQTLKAFLEAEQYPGPSLIIAYSPCI 1077
Cdd:PRK11869 165 FSG-DIEETKEILKEAIKHKGLAIVDIFQPCV 195
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| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
963-1072 |
6.85e-03 |
|
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: 38.78 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501422877 963 WLIGGDGWAYDiGFGGLDHVLSTGEDVNTLVMDTEVYSNTGGQSSKATqtaamaKFASSGKATMKKDLGMMAMSYGyVYV 1042
Cdd:cd00568 68 VCIAGDGGFMM-TGQELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFY------GGRVSGTDLSNPDFAALAEAYG-AKG 139
|
90 100 110
....*....|....*....|....*....|
gi 501422877 1043 AQVSMGAnmnQTLKAFLEAEQYPGPSLIIA 1072
Cdd:cd00568 140 VRVEDPE---DLEAALAEALAAGGPALIEV 166
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