|
Name |
Accession |
Description |
Interval |
E-value |
| pyruv_ox_red |
TIGR02176 |
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single ... |
5-1171 |
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: 2271.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 5 LKTMDGNEAAAYASYAFTDVAAIYPITPSTPMAELVDNWSSHGRKNIFGQPVKIVEMQSEAGAAGTVHGSLIAGALTTTY 84
Cdd:TIGR02176 1 MKTMDGNTAAAHVAYAFSEVAAIYPITPSSTMGEYVDDWAAQGRKNIFGQTVKVVEMQSEAGAAGAVHGALQTGALTTTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 85 TASQGLLLMIPNMYKMAGELLPCVFHVSARAIATHALSIFGDHQDVMAARQTGFVLLASSNVQEVMDLAMVSHLAAIKAR 164
Cdd:TIGR02176 81 TASQGLLLMIPNMYKIAGELLPCVFHVSARAIAAHALSIFGDHQDVMAARQTGFAMLASSSVQEVMDLALVAHLATIEAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 165 VPFMHFFDGFRTSHEYQKIEMIDYNDVAPLVDYESIKAFRSRALNPEHPTVRGTAQNPDIYFQGREASNNFYTAVPDIVE 244
Cdd:TIGR02176 161 VPFMHFFDGFRTSHEIQKIEVLDYEDMASLVNQELVAAFRKRSMNPEHPHVRGTAQNPDIYFQGREAVNPYYLAVPGIVQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 245 SYMREIEKITGRVYHPFDYYGDPEAEDIIIAMGSVCDTVEETVDYLRSKGQKVGLLKVHLYRPFSTDYFFKYLPKTIKRI 324
Cdd:TIGR02176 241 KYMDKIAKLTGRSYHLFDYYGAPDAERVIIAMGSVAETIEETVDYLNAKGEKVGLLKVRLYRPFSAETFFAALPKSVKRI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 325 AVLDRTKEPGSAGEPLYLDVVNAFYNH-PNKPVIVGGRFGLGSKDTRPSQILSVFDNLRAQSPKNRFTIGIVDDVSNTSL 403
Cdd:TIGR02176 321 AVLDRTKEPGAAGEPLYLDVVSAFYEMgEAMPVILGGRYGLGSKEFTPAMVKAVFDNLSGEAPKNHFTVGIEDDVTGTSL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 404 PEGEIIDTTPQGTIRCKFYGLGSDGTVGANKSAIKIIGDNTDMYCQAYFSYDSKKSGGSTVSHLRFGNKPIKSPYLVYEA 483
Cdd:TIGR02176 401 PVDEFFDTTPKGTIQAKFYGLGSDGTVGANKNAIKIIGDNTDNYAQGYFSYDSKKSGGITISHLRFGEKPIRSTYLVTEA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 484 DYIACHNKSFIYNINVLKGLKKNGIFVLNCPFKDNELDEHLPNAMKKYIADNNIQFYTIDAVSIAQEVGLGSRINMIMQS 563
Cdd:TIGR02176 481 DFVACHNPAYLEMYDVLKGLKKGGTFLLNSPWAPEDLDKHLPNGVKRYIADKEIKFYTIDAVKIAQEVGLGGRINTIMQT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 564 AFFKLANIIPVDKAVQYLKDSIEYTYGKKGATIVDANKKAVDAGVNAAHKVTVPEAWKNAESNYQP-LKGLPDFVQRIER 642
Cdd:TIGR02176 561 AFFKLAGVLPFEKAVDLLKKSIEKSYGKKGEKIVQKNIKAVDQAVESLHEVKVPAEWKDAPAEPKAiEGDAPEFVKNVVR 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 643 PMARHEGDELPVSAFKGmeDGVFPLGITAYEKRGIAVNVPEWQIDKCIQCNQCAYVCPHSVIRACLLDDEEKENAPERFV 722
Cdd:TIGR02176 641 PINAQEGDDLPVSAFPA--DGTFPLGTTAFEKRGVAINVPVWVPDNCIQCNQCAFVCPHAAIRPKLADEEELENAPAGFK 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 723 TKKPVGKGLEHLHYKIQISPLDCTGCGNCADICPAPGKALIMKPAAEQIEEQSENFEYALKVKPKEGIMDIHTVKGSQFS 802
Cdd:TIGR02176 719 SLDAKGKELEGMKFRIQISPLDCTGCGNCVDICPAKEKALVMQPLAEQREAQVANWEFAINIPEKDNKLNIDTVKGSQFQ 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 803 RPLLEFNGACPGCGETPYIKLLTQLYGDRMMIANATGCSSIWGASAPSIAYTTNNFGKGPSWGNSLFEDNAEYGYGMFLG 882
Cdd:TIGR02176 799 RPLFEFSGACSGCGETPYVKLLTQLFGDRMVIANATGCSSIWGASAPSTPYTTNEQGQGPAWSNSLFEDNAEFGYGMRLS 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 883 VKQMRERLAELMEEAINSNINSD-LKDAFSLWLDGFDDGDKSKEASNKILRIMENEDfkgDKLLSEIYDKKDYLVKKSHW 961
Cdd:TIGR02176 879 MDKRRERLAELAAKALESDIASGdLKAALNGWLAGKNDIEKSKERVAKLKKLLAGEK---DDLLKEIYAVSDLFVKKSVW 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 962 LIGGDGWAYDIGFGGVDQVLALGDDVNIFVMDTEIYSNTGGQSSKSTPTGAIAKFASAGKKTRKKDLGLMAMTYGNVYVT 1041
Cdd:TIGR02176 956 IIGGDGWAYDIGYGGLDHVLASGKDVNVLVMDTEVYSNTGGQSSKATPTGAIAKFAAAGKRTSKKDLGMMAMTYGYVYVA 1035
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 1042 QIAMGANMTHTIKAITEAEAYKGPSLVIAYAPCISHGIKTGMGTSIAQEKKAVEAGYWHLYRYNPLLKEQGKNPFILDSK 1121
Cdd:TIGR02176 1036 QVSMGANMQQTLKAFREAEAYDGPSIVIAYSPCINHGIKKGMGKSQAEQKTAVESGYWPLYRYNPRLAEQGKNPFQLDSK 1115
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|
gi 15025520 1122 EPTESYTDFINGELRYSSLKTIFPDKVEDAFNKSAENAKERYSLYKKLSE 1171
Cdd:TIGR02176 1116 EPDSSVAEFLNGEVRFASLKKSFPDDAERLFNKAAHEAKRRFKEYEHLAA 1165
|
|
| TPP_PFOR_PNO |
cd03377 |
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ... |
804-1171 |
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: 646.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 804 PLLEFNGACPGCGETPYIKLLTQLYGDRMMIANATGCSSIWGASAPSIAYTTNNFGKGPSWGNSLFEDNAEYGYGMFLGV 883
Cdd:cd03377 1 PLFEFSGACAGCGETPYVKLLTQLFGDRMVIANATGCSSIYGGSAPTTPYTTNAKGRGPAWANSLFEDNAEFGLGMRLAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 884 KQMRERLAELMEEAINSNINSDLKDAFSLWLDGFDDGDKSKEASNKILRIMENEDfkgDKLLSEIYDKKDYLVKKSHWLI 963
Cdd:cd03377 81 DQRRERARELVQKLIEKIGDEELKTLLNAWLATEDDIEESRERVAKLKPLLAAEK---DELAKELLSLADYLVKKSVWII 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 964 GGDGWAYDIGFGGVDQVLALGDDVNIFVMDTEIYSNTGGQSSKSTPTGAIAKFASAGKKTRKKDLGLMAMTYGNVYVTQI 1043
Cdd:cd03377 158 GGDGWAYDIGYGGLDHVLASGENVNILVLDTEVYSNTGGQASKATPLGAVAKFAAAGKRTGKKDLGMIAMSYGNVYVAQI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 1044 AMGANMTHTIKAITEAEAYKGPSLVIAYAPCISHGIKTGMGTSIAQEKKAVEAGYWHLYRYNPLLKEQGKNPFILDSKEP 1123
Cdd:cd03377 238 ALGANDNQTLKAFREAEAYDGPSLIIAYSPCIAHGIKGGMTKSQEQQKLAVESGYWPLYRYNPRLVEEGKNPLQLDSKEP 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 15025520 1124 TESYTDFINGELRYSSLKTIFPDKVEDAFNKSAENAKERYSLYKKLSE 1171
Cdd:cd03377 318 DGPVEEFLNNENRFAALKKANPERAEQLFEQLQADAKERYKRYKRLAA 365
|
|
| PorA |
COG0674 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha ... |
3-392 |
1.01e-145 |
|
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: 442.98 E-value: 1.01e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 3 KKLKTMDGNEAAAY-ASYAFTDVAAIYPITPSTPMAELVDNWSShgRKNifgqpVKIVEMQSEAGAAGTVHGSLIAGALT 81
Cdd:COG0674 1 GKRVLMDGNEAVALgAIAAGCRVIAAYPITPSTEIAEYLAEWLA--ELG-----GVVVQAESEIAAIGAVIGASAAGARA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 82 TTYTASQGLLLMIPNMYKMAGELLPCVFHVSARAIATHALSIFGDHQDVMAA-----RQTGFVLLASSNVQEVMDLAMVS 156
Cdd:COG0674 74 MTATSGPGLSLMQEGLGLAAGAELPLVIVVVQRAGPSTGLPIKGDQSDLMQAlygghGDTGWIVLAPSSVQEAFDLTIIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 157 HLAAIKARVPFMHFFDGFRTSHEYqKIEMIDYNDVAPLvdyESIKAFRSRALNpEHP-TVRGTAQnPDIYFQG---REAS 232
Cdd:COG0674 154 FNLAEKYRVPVIVLFDGFLGSHEE-PVELPDDEEVKIL---PRPEEYRPYALD-EDPrAIPGTAQ-PDVYFTGlehDETE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 233 NNfyTAVPDIVESYMREIEKITGRVyHPFDYYGDPEAEDIIIAMGSVCDTVEETVDYLRSKGQKVGLLKVHLYRPFSTDY 312
Cdd:COG0674 228 DP--ENAEKMVEKRMRKFEKIRDEL-PRVEYYGAEDAEVVIVAMGSTAGTAKEAVDRLREEGIKVGLLRVRLLRPFPAEA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 313 FFKYLpKTIKRIAVLDRTKEpGsagePLYLDVVNAFynhpNKPVIVGGRFGLGSKDTRPSQILSVFDNLRAQSPKnrFTI 392
Cdd:COG0674 305 LREAL-KGVKKVAVVERNKS-G----QLALDVRAAL----GADRVVGGIYGLGGRPFTPEEILAVIEELLKGAPK--FTL 372
|
|
| POR_N |
pfam01855 |
Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N ... |
14-248 |
1.74e-97 |
|
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: 309.57 E-value: 1.74e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 14 AAYAsyAFTDVAAIYPITPSTPMAELVDNWSSHGRKNIfgqpVKIVEMQSEAGAAGTVHGSLIAGALTTTYTASQGLLLM 93
Cdd:pfam01855 1 AAIA--AGVDVIAAYPITPSSEIAEEAAEWAANGEKGD----VVVIQMESEIGAISAVIGAAAAGARAATATSGQGLLLM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 94 IPNMYKMAGELLPCVFHVSARAIATHALSIFGDHQDVMAARQTGFVLLASSNVQEVMDLAMVSHLAAIKARVPFMHFFDG 173
Cdd:pfam01855 75 IENLGKAAGERLPVVIHVVARAGPSPGLSIFGDHSDVMAARDTGWIVLASENVQEAFDFALVAFNLAEKVRTPVIHLFDG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15025520 174 FRTSHEYQKIEMIDYNDVAPLVDYESIKAFRSR-ALNPEHPTVRGTAQNPDIYFQGREASNNFYTAVPDIVESYMR 248
Cdd:pfam01855 155 FRTSHEREKVELPPDEDEKDLIDEFLPPYKRKRyGLDPEMPIARGTAQNPDTYFEHREYGNPAYDAAEVVIEEVMK 230
|
|
| TPP_PFOR |
cd02018 |
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ... |
805-1106 |
1.06e-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: 250.10 E-value: 1.06e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 805 LLEFNGACPGCGETPYIKLLTQLYG--DRMMIANATGCSSIWGASAPSIAYttnnfgkGPSWGNSLFEDNAEYGYGMFLG 882
Cdd:cd02018 1 LTEEHGACAGCGEVTAVRVVLAALPapEDTVIANSTGCSSVYASTAPFNSW-------AVPWVNSLFEDANAVASGLKRG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 883 VKQMRERLAELmeeainsninsdlkdafslwldgfddgdkskeasnkilrimenedfkgdkllseiyDKKdylvkKSHWL 962
Cdd:cd02018 74 LKARFPKDREL--------------------------------------------------------DKK-----KDVVV 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 963 IGGDGWAYDIGFGGVDQVLALGDDVNIFVMDTEIYSNTGGQSSKSTPTGAIAKFASAGKKTRKKDLGLMAMTYGNVYVTQ 1042
Cdd:cd02018 93 IGGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGKKEDKKDLVLIAATHGCVYVAR 172
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15025520 1043 IAMgANMTHTIKAITEAEAYK-GPSLVIAYAPCISHGiKTGMGTSIAQEKKAVEAGYWHLYRYNP 1106
Cdd:cd02018 173 LSP-ALKKHFLKVVKEAISRTdGPTFIHAYTPCITEW-GIGSGKSLELARKAVKSRMFPLFEYDP 235
|
|
| PorG |
COG1014 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, gamma ... |
415-850 |
1.05e-66 |
|
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: 231.50 E-value: 1.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 415 GTIRCKFYGLGSDGTVGANKSAIKIIgDNTDMYCQAYFSYDSKKSGGSTVSHLRFGNKPIKSPyLVYEADYIACHNKSFI 494
Cdd:COG1014 3 MDLEIRIAGVGGQGVVTAGKILAKAA-MREGYYVQGYPSYGSEQRGGPVVSHVRISDEPIRSP-LIDEADVLIALDPEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 495 YniNVLKGLKKNGIFVLNCPFKDNELDeHLPnamKKYIADNNIQFYTIDAVSIAQEvGLGS--RINMIMQSAFFKLANiI 572
Cdd:COG1014 81 D--RVLDGLKPGGVLIVNSSLVPPEVW-RLP---QEALERKDIRVYVIDATKIAKE-LLGNarVANTVMLGALAALLG-L 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 573 PVDkavqYLKDSIEYTYGKKGATIVDANKKAVDAGVNAAHKV-TVPEAWKNAESNyqplkGLPDFVQRIERPMARHEGDE 651
Cdd:COG1014 153 PLE----ALEEAIEETFGKKGEKVVELNLKAFEAGYEAAKEVfALAAAPAPLVLL-----AGNAAAALGAAAGGAAFAAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 652 LPVSAFkgMEDGVFPLGITAYEKRGIAVNVPEWQIDKCIQCNQCAYVCPHSVIR-ACLLDDEEKENAPERFVTKKPVGKG 730
Cdd:COG1014 224 YPITPS--TSLIEAAAAAAAKVGGVVAEEEAAAAAAAAAAAAAAAGAAAAAAGGgGGAALATEGLGLAGMTETPVVAVAA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 731 LEHLHYKIQISPLDCTGCGNCADICPAPGKALIMKPAAEQIEEQSENFEYALKVKPKEG-IMDIHTVKGSQFSRPLLEFN 809
Cdd:COG1014 302 PRPGPGTGTPTEEEQGLLLLAAGGGGGEAPALALAPDTEEELLFAAAAAFALAEYAQALlLLLLLQLLVLLLTDLLLLLL 381
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 15025520 810 GACPGCGETPYIKLLTQLYGDRMMIANATGCSSIWGASAPS 850
Cdd:COG1014 382 DLLRRRAGLGAEEAEARRKLLAAEGRAARAAGGGGGGGGGG 422
|
|
| TPP_PYR_PFOR_IOR-alpha_like |
cd07034 |
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ... |
10-173 |
2.86e-56 |
|
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: 191.95 E-value: 2.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 10 GNEAAAYASYAFT-DVAAIYPITPSTPMAELVDNWSshgrknIFGQPVKIVEMQSEAGAAGTVHGSLIAGALTTTYTASQ 88
Cdd:cd07034 1 GNEAVARGALAAGvDVVAAYPITPSTEIAETLAKAV------LGELGGVVVQAESEHAAAEAAIGASAAGARAMTATSGP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 89 GLLLMIPNMYKMAGELLPCVFHVSARAIATHALsIFGDHQDVMAARQTG--FVLLASSNVQEVMDLAMVSHLAAIKARVP 166
Cdd:cd07034 75 GLNLMAEALYLAAGAELPLVIVVAQRPGPSTGL-PKPDQSDLMAARYGGhpWPVLAPSSVQEAFDLALEAFELAEKYRLP 153
|
....*..
gi 15025520 167 FMHFFDG 173
Cdd:cd07034 154 VIVLSDG 160
|
|
| porA |
PRK09622 |
2-oxoacid:ferredoxin oxidoreductase subunit alpha; |
1-391 |
1.28e-53 |
|
2-oxoacid:ferredoxin oxidoreductase subunit alpha;
Pssm-ID: 181999 [Multi-domain] Cd Length: 407 Bit Score: 193.44 E-value: 1.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 1 MAKKL-----KTMDGNEAAAYA-SYAFTDVAAIYPITPSTPmaeLVDNWSS-HGRKNIFGQpvkIVEMQSEAGAAGTVHG 73
Cdd:PRK09622 1 MAKKIelqeiEVWDGNTAASNAlRQAQIDVVAAYPITPSTP---IVQNYGSfKANGYVDGE---FVMVESEHAAMSACVG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 74 SLIAGALTTTYTASQGLLLMIPNMYKMAGELLPCVFHVSARAIAThALSIFGDHQDVMAARQTGFVLLASSNVQEVMDLA 153
Cdd:PRK09622 75 AAAAGGRVATATSSQGLALMVEVLYQASGMRLPIVLNLVNRALAA-PLNVNGDHSDMYLSRDSGWISLCTCNPQEAYDFT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 154 MVSHLAA--IKARVPFMHFFDGFRTSHEYQkiemidynDVAPLVD---YESIKAFRSR--ALNPEHPTVRGTAQNPDIYF 226
Cdd:PRK09622 154 LMAFKIAedQKVRLPVIVNQDGFLCSHTAQ--------NVRPLSDevaYQFVGEYQTKnsMLDFDKPVTYGAQTEEDWHF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 227 QGREASNNFYTAVPDIVESYMREIEKITGRVYHPFDYYGDPEAEDIIIAMGSVCDTVEETVDYLRSKGQKVGLLKVHLYR 306
Cdd:PRK09622 226 EHKAQLHHALMSSSSVIEEVFNDFAKLTGRKYNLVETYQLEDAEVAIVALGTTYESAIVAAKEMRKEGIKAGVATIRVLR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 307 PFSTDYFFKYLpKTIKRIAVLDRTKEPGSAGEpLYLDVVNAFYNH--PNKPVIVGGRFGLGSKDTRPSQILSVFDNLRAQ 384
Cdd:PRK09622 306 PFPYERLGQAL-KNLKALAILDRSSPAGAMGA-LFNEVTSAVYQTqgTKHPVVSNYIYGLGGRDMTIAHLCEIFEELNEN 383
|
....*..
gi 15025520 385 SPKNRFT 391
Cdd:PRK09622 384 ALAGKLT 390
|
|
| porA |
PRK08367 |
pyruvate ferredoxin oxidoreductase subunit alpha; Reviewed |
6-368 |
2.82e-51 |
|
pyruvate ferredoxin oxidoreductase subunit alpha; Reviewed
Pssm-ID: 181403 [Multi-domain] Cd Length: 394 Bit Score: 186.24 E-value: 2.82e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 6 KTMDGNEAAAYAS-YAFTDVAAIYPITPSTPMAELVDNWSSHGRKNifgqpVKIVEMQSEAGAAGTVHGSLIAGALTTTY 84
Cdd:PRK08367 5 TVMKANEAAAWAAkLAKPKVIAAFPITPSTLVPEKISEFVANGELD-----AEFIKVESEHSAISACVGASAAGVRTFTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 85 TASQGLLLMIPNMYKMAGELLPCVFHVSARAIAThALSIFGDHQDVMAARQTGFVLLASSNVQEVMDLAMVSHLAAIKAR 164
Cdd:PRK08367 80 TASQGLALMHEVLFIAAGMRLPIVMAIGNRALSA-PINIWNDWQDTISQRDTGWMQFYAENNQEALDLILIAFKVAEDER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 165 V--PFMHFFDGFRTSHEYQKIEMIDYNDVAP-LVDYESIKAFrsraLNPEHPTVRGTAQNPDIYFQGR----EASNNfyt 237
Cdd:PRK08367 159 VllPAMVGFDAFILTHTVEPVEIPDQEVVDEfLGEYEPKHAY----LDPARPITQGALAFPAHYMEARytvwEAMEN--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 238 aVPDIVESYMREIEKITGRVYHPFDYYGDPEAEDIIIAMGSVCDTVEETVDYLRSKGQKVGLLKVHLYRPFSTDYfFKYL 317
Cdd:PRK08367 232 -AKKVIDEAFAEFEKKFGRKYQKIEEYRTEDAEIIFVTMGSLAGTLKEFVDKLREEGYKVGAAKLTVYRPFPVEE-IRAL 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 15025520 318 PKTIKRIAVLDRTKEPGSAGePLYLDVVNAFYNHPNKPVIVGGRFGLGSKD 368
Cdd:PRK08367 310 AKKAKVLAFLEKNISFGLGG-AVFADASAALVNESEKPKILDFIIGLGGRD 359
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
807-1137 |
1.95e-46 |
|
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: 167.63 E-value: 1.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 807 EFNGACPGCGETPYIKLLTQ-----LYGDRMMIANATGCSSIWGAsapsiAYTTNNFgkgpswgNSLFEDNAEYGYGMfl 881
Cdd:COG1013 11 PGHRWCPGCGHGIILRLLLKaldelLDGDKTVVVSGIGCSSVAPG-----YFNVPGF-------HTLHGRAAAVATGI-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 882 gvkqmreRLAelmeeainsniNSDLKdafslwldgfddgdkskeasnkilrimenedfkgdkllseiydkkdylVkkshW 961
Cdd:COG1013 77 -------KLA-----------NPDLT------------------------------------------------V----I 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 962 LIGGDGWAYDIGFGGVDQVLALGDDVNIFVMDTEIYSNTGGQSSKSTPTGAIAKFASAGKKTRKKDLGLMAMTYGNVYVT 1041
Cdd:COG1013 87 VFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHGATYVA 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 1042 QIAMGaNMTHTIKAITEAEAYKGPSLVIAYAPCIshgikTGMGTSIAQEKKAVEAGYWHLYRYNPLLKEQgknpFILDSK 1121
Cdd:COG1013 167 RASVG-DPKDLKKKIKKAIEHKGFSFIEVLSPCP-----TGWGRDPSKTIEWAKEGMWPLYEYDPGEKLR----LTYEPK 236
|
330
....*....|....*...
gi 15025520 1122 E--PTEsytDFINGELRY 1137
Cdd:COG1013 237 DkiPVG---EFLKNQGRF 251
|
|
| vorA |
PRK08366 |
2-ketoisovalerate ferredoxin oxidoreductase subunit alpha; Reviewed |
6-383 |
1.29e-45 |
|
2-ketoisovalerate ferredoxin oxidoreductase subunit alpha; Reviewed
Pssm-ID: 169406 [Multi-domain] Cd Length: 390 Bit Score: 169.41 E-value: 1.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 6 KTMDGNEAAAYAS-YAFTDVAAIYPITPSTPMAELVDNWSSHGRKNIfgqpvKIVEMQSEAGAAGTVHGSLIAGALTTTY 84
Cdd:PRK08366 4 KVVSGNYAAAYAAlHARVQVVAAYPITPQTSIIEKIAEFIANGEADI-----QYVPVESEHSAMAACIGASAAGARAFTA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 85 TASQGLLLMIPNMYKMAGELLPCVFHVSARAIAThALSIFGDHQDVMAARQTGFVLLASSNVQEVMDLAMVSHLAAIKAR 164
Cdd:PRK08366 79 TSAQGLALMHEMLHWAAGARLPIVMVDVNRAMAP-PWSVWDDQTDSLAQRDTGWMQFYAENNQEVYDGVLMAFKVAETVN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 165 VPFMHFFDGFRTSHEYQKIEMIDYNDV----APLVDYESIKAFrsralnpEHPTVRGTAQNPDIYFQGREASNNFYTAVP 240
Cdd:PRK08366 158 LPAMVVESAFILSHTYDVVEMIPQELVdeflPPRKPLYSLADF-------DNPISVGALATPADYYEFRYKIAKAMEEAK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 241 DIVESYMREIEKITGRVYHPF--DYYGDpEAEDIIIAMGSVCDTVEETVDYLRSKGQKVGLLKVHLYRPFSTDYFFKyLP 318
Cdd:PRK08366 231 KVIKEVGKEFGERFGRDYSQMieTYYTD-DADFVFMGMGSLMGTVKEAVDLLRKEGYKVGYAKVRWFRPFPKEELYE-IA 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15025520 319 KTIKRIAVLDRTKEPGSAGePLYLDVVNAFYNHPNKPVIVGGRFGLGSKDTRPSQILSVFDNLRA 383
Cdd:PRK08366 309 ESVKGIAVLDRNFSFGQEG-ILFTEAKGALYNTDARPIMKNYIVGLGGRDFTVNDVKAIAEDMKK 372
|
|
| POR |
pfam01558 |
Pyruvate ferredoxin/flavodoxin oxidoreductase; This family includes a region of the large ... |
425-609 |
2.28e-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: 132.42 E-value: 2.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 425 GSDGTVGANKSAIKIIgDNTDMYCQAYFSYDSKKSGGSTVSHLRFGNKPIKSPYLVYEADYIACHNKSFIYniNVLKGLK 504
Cdd:pfam01558 1 GGQGVVTAGKILAKAA-ARAGYYVQATPEYGSEIRGGPVVSHVRISDEPIVPAIPVGEADLLVALDPETLD--RHLDGLK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 505 KNGIFVLNCPFKDNELDEhlpnaMKKYIADNNIQFYTIDAVSIAQEVGLGSR-INMIMQSAFFKLANiIPVDkavqYLKD 583
Cdd:pfam01558 78 PGGIIIYNSSEVPPELLE-----KDLPAYPRLARVYGVPATEIAKEAGGNSRaANTVMLGALAALLG-LPLE----ALEE 147
|
170 180
....*....|....*....|....*.
gi 15025520 584 SIEYTYGKKGAtIVDANKKAVDAGVN 609
Cdd:pfam01558 148 AIKKRFPGKAK-VIELNLKAFRAGYE 172
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
23-173 |
3.23e-27 |
|
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: 108.59 E-value: 3.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 23 DVAAIYPITPSTPMAELVDNwsshgrknifGQPVKIVEMQSEAGAAGTVHGSLIAGALTTTY-TASQGLLLMIPNMYKMA 101
Cdd:cd06586 13 RHVFGYPGDEISSLLDALRE----------GDKRIIDTVIHELGAAGAAAGYARAGGPPVVIvTSGTGLLNAINGLADAA 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15025520 102 GELLPCVFHVSARAIATHALSIFGDHQDVMAARQTGFVLLASSNVQEVMDLAMVSHLAAIKARVPFMHFFDG 173
Cdd:cd06586 83 AEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYASQGPVVVRLPR 154
|
|
| TPP_PFOR_porB_like |
cd03376 |
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ... |
809-1104 |
3.87e-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: 3.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 809 NGACPGCGETPYIKLLTQLYGDRMMIANATGCSSIWGASAPSIAYTTNnfgkgpsWGNSLFEDNAeygyGMFLGVKQMRE 888
Cdd:cd03376 5 HRACAGCGAALALRHVLKALGPDTVVVNPTGCLEVITTPYPYTAWRVP-------WIHVAFENAA----AVASGIEAALK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 889 RLAElmeeainsninsdlkdafslwldgfddgdkskeasnkilrimenedfkgdkllseiydKKDYLVkkshWLIGGDGW 968
Cdd:cd03376 74 ALGR----------------------------------------------------------GKDITV----VAFAGDGG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 969 AYDIGFGGVDQVLALGDDVNIFVMDTEIYSNTGGQSSKSTPTGAIAKFASAGK-----KTRKKDLGLMAMTYGNVYVTQi 1043
Cdd:cd03376 92 TADIGFQALSGAAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTTTTPVGKvsfgkKQPKKDLPLIMAAHNIPYVAT- 170
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15025520 1044 AMGANMTHTIKAITEAEAYKGPSLVIAYAPCISH-GIKTGMGTSIAqeKKAVEAGYWHLYRY 1104
Cdd:cd03376 171 ASVAYPEDLYKKVKKALSIEGPAYIHILSPCPTGwRFDPSKTIEIA--RLAVETGFWPLYEY 230
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
509-770 |
1.19e-24 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 104.03 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 509 FVLNCPFKDNELDEHLPNAMKKYIADNNIQFYTIDAVSIAQEVGLGSRINMIMQSAFFKLANIIPVDKAVQYLKDSIEYT 588
Cdd:COG1145 3 LLLDLKEALSPKLKVLYAVVTGILGKIILNVIAGALLKAVALGGLLPIIGILAKEAFDALKDVLGILGAIVIGIGAGEIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 589 YGKKGATIVDANKKAVDAGVNAAHKVTVP-EAWKNAESNYQPLKGLPDFVQRIERPMARHEGDELPVSAFKgmEDGVFPL 667
Cdd:COG1145 83 RVGIAAADLNLKAVALVLLLALAVAGAAKrLIISAVKLVAGLVVAAGEVLLVIAAALAEAGLAILGAAAPV--DALAISG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 668 GITAYEKRGIAVNVPEWQID--KCIQCNQCAYVCPHSVIRaclLDDEEkenaperfvtkkpvgkglehlhYKIQISPLDC 745
Cdd:COG1145 161 GKKIEEELKIAIKKAKAVIDaeKCIGCGLCVKVCPTGAIR---LKDGK----------------------PQIVVDPDKC 215
|
250 260
....*....|....*....|....*
gi 15025520 746 TGCGNCADICPApgKALIMKPAAEQ 770
Cdd:COG1145 216 IGCGACVKVCPV--GAISLEPKEIE 238
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
664-769 |
1.43e-24 |
|
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: 98.59 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 664 VFPLGITAYEKRGIAVNVPEWQIDKCIQCNQCAYVCPHSVIRAclldDEEKenaperfvtkkpvgkglehlhyKIQISPL 743
Cdd:COG1144 7 TEPGGTAAYKTGGWRVERPVVDEDKCIGCGLCWIVCPDGAIRV----DDGK----------------------YYGIDYD 60
|
90 100
....*....|....*....|....*.
gi 15025520 744 DCTGCGNCADICPApgKALIMKPAAE 769
Cdd:COG1144 61 YCKGCGICAEVCPV--KAIEMVPEEK 84
|
|
| PFOR_II |
pfam17147 |
Pyruvate:ferredoxin oxidoreductase core domain II; PFOR_II is a core domain of the anaerobic ... |
269-374 |
1.16e-22 |
|
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: 93.48 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 269 AEDIIIAMGSVCDTVEETVDYLRSKGQKVGLLKVHLYRPFSTDYFFKYLpKTIKRIAVLDRTKEPGSAGePLYLDVVNAF 348
Cdd:pfam17147 1 AEVVIVAMGSVAGTAKSAVDRLREEGIKVGLLRLRTFRPFPEEELKELL-AGVKKVVVLDRNISFGSPG-QLGTEVKAAL 78
|
90 100
....*....|....*....|....*.
gi 15025520 349 YNHPNKPVIVGGrfGLGSKDTRPSQI 374
Cdd:pfam17147 79 YDSDPPVVNFIA--GLGGRDITPEDI 102
|
|
| PRK11865 |
PRK11865 |
pyruvate synthase subunit beta; |
811-1104 |
3.13e-21 |
|
pyruvate synthase subunit beta;
Pssm-ID: 183346 [Multi-domain] Cd Length: 299 Bit Score: 95.55 E-value: 3.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 811 ACPGCGETPYIKLLTQLYGDRMMIANATGCSSIWGASAPSIAYttnnfgKGPsWGNSLFEDNAEYGYGMFLGVKqmrerl 890
Cdd:PRK11865 20 ACAGCGAAIAMRLALKALGKNTVIVVATGCLEVITTPYPETAW------NVP-WIHVAFENAAAVASGIERAVK------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 891 aelmeeAINSNINsdlkdafslwldgfddgdkskeasnkILrimenedfkgdkllseiydkkdylvkkshwLIGGDGWAY 970
Cdd:PRK11865 87 ------ALGKKVN--------------------------VV------------------------------AIGGDGGTA 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 971 DIGFGGVDQVLALGDDVnIFVM-DTEIYSNTGGQSSKSTPTGAIAKFASAGKKTR-----KKDLGLMAMTYGNVYVTQIA 1044
Cdd:PRK11865 105 DIGFQSLSGAMERGHNI-LYLMyDNEAYMNTGIQRSGSTPFGASTTTSPAGKYSRgedrpKKNMPLIMAAHGIPYVATAS 183
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15025520 1045 MGaNMTHTIKAITEAEAYKGPSLVIAYAPCIshgikTGMGT----SIAQEKKAVEAGYWHLYRY 1104
Cdd:PRK11865 184 IG-YPEDFMEKVKKAKEVEGPAYIQVLQPCP-----TGWGFppekTIEIGRLAVETGYWPLFEI 241
|
|
| EKR |
smart00890 |
Domain of unknown function; EKR is a short, 33 residue, domain found in bacterial and some ... |
631-679 |
3.79e-21 |
|
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: 87.67 E-value: 3.79e-21
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 15025520 631 KGLPDFVQRIERPMARHEGDELPVSAFKgmEDGVFPLGITAYEKRGIAV 679
Cdd:smart00890 11 EEAPEFVKNVVAPMNAGEGDDLPVSAFP--EDGTFPTGTAAYEKRGIAV 57
|
|
| EKR |
pfam10371 |
Domain of unknown function; EKR is a short, 33 residue, domain found in bacterial and some ... |
631-678 |
2.95e-20 |
|
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: 85.21 E-value: 2.95e-20
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 15025520 631 KGLPDFVQRIERPMARHEGDELPVSAFKgmEDGVFPLGITAYEKRGIA 678
Cdd:pfam10371 9 EDAPEFVKNVLAPMNAGEGDELPVSAFP--EDGTFPTGTSAYEKRGIA 54
|
|
| PorC_KorC |
TIGR02175 |
2-oxoacid:acceptor oxidoreductase, gamma subunit, pyruvate/2-ketoisovalerate family; A number ... |
417-607 |
1.85e-19 |
|
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: 87.02 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 417 IRCKFYGLGSDGTVGAN----KSAIkiigdNTDMYCQAYFSYDSKKSGGSTVSHLRFGNKPIKSPYLVYEADYIACHNKS 492
Cdd:TIGR02175 2 IEIRFHGRGGQGAVTASqllaEAAF-----LEGKYAQAFPEFGAERRGAPVRAFLRISDRPIRVHSQIYEPDYVVVLDPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 493 FIYNINVLKGLKKNGIFVLNCPFKDNELdehlpnamkkyiaDNNIQFYTIDAVSIAQEVgLGSRI-NMIMQSAFFKLANI 571
Cdd:TIGR02175 77 LLKTVNVTAGLKEDGILIVNTKKDPEEL-------------RKELKVYTVDATKIALVV-LGRPIvNTPMLGAFAKVTGL 142
|
170 180 190
....*....|....*....|....*....|....*.
gi 15025520 572 IPVDKavqyLKDSIEYTYGKKGAtivDANKKAVDAG 607
Cdd:TIGR02175 143 VSLES----LEKAIEESFPGKLA---EANAKAVERA 171
|
|
| PRK11864 |
PRK11864 |
3-methyl-2-oxobutanoate dehydrogenase subunit beta; |
809-1123 |
2.18e-17 |
|
3-methyl-2-oxobutanoate dehydrogenase subunit beta;
Pssm-ID: 237005 [Multi-domain] Cd Length: 300 Bit Score: 84.37 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 809 NGACPGCGETPYIKLLTQLYGDRMMIANATGCSSIWGASAPSIAYTTNNFgkgpswgNSLFEDNAeygygmflgvkqmre 888
Cdd:PRK11864 18 NAACPGCGAPLGLRYLLKALGEKTVLVIPASCSTVIQGDTPKSPLTVPVL-------HTAFAATA--------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 889 rlaelmeeAINSNINSDLKdafslwldgfddgdkskeasnkilrimenedFKGdkllseiydKKDYLVkkSHWliGGDGW 968
Cdd:PRK11864 76 --------AVASGIEEALK-------------------------------ARG---------EKGVIV--VGW--AGDGG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 969 AYDIGFGGVDQVLALGDDVnIFVM-DTEIYSNTGGQSSKSTPTGAIAKFASAGKKTRKKDLGLMAMTYGNVYV--TQIAM 1045
Cdd:PRK11864 104 TADIGFQALSGAAERNHDI-LYIMyDNEAYMNTGIQRSSSTPYGAWTTTTPGGKREHKKPVPDIMAAHKVPYVatASIAY 182
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15025520 1046 GANMthtIKAITEAEAYKGPSLVIAYAPCIShGIKTGMGTSIAQEKKAVEAGYWHLYRY-NPLLKEQGKNPFILDSKEP 1123
Cdd:PRK11864 183 PEDF---IRKLKKAKEIRGFKFIHLLAPCPP-GWRFDPDKTIEIARLAVETGVWPLFEYeNGKFKLNSPSKTLLDKKKR 257
|
|
| PRK08534 |
PRK08534 |
pyruvate ferredoxin oxidoreductase subunit gamma; Reviewed |
417-604 |
6.56e-17 |
|
pyruvate ferredoxin oxidoreductase subunit gamma; Reviewed
Pssm-ID: 181460 [Multi-domain] Cd Length: 181 Bit Score: 79.70 E-value: 6.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 417 IRCKFYGLGSDGTVGANKsAIKIIGDNTDMYCQAYFSYDSKKSGGSTVSHLRFGNKPIKSPYLVYEADYIACHNKSFIYN 496
Cdd:PRK08534 2 IEIRFHGRGGQGAVTAAE-ILAKAAFEDGKFSQAFPFFGVERRGAPVMAFTRIDDKPIRLRSQIYEPDYVIVQDPTLLDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 497 INVLKGLKKNGIFVLNCPFKDNELDEhlpnamkkyiaDNNIQFYTIDAVSIAQEVgLGSRI-NMIMQSAFFKLANIIPVD 575
Cdd:PRK08534 81 VDVTSGLKKDGIIIINTTKDPEDLKY-----------DTKAKVYTIDATKIALDV-LGVPIvNTTMLGAFAGATGEVSLE 148
|
170 180
....*....|....*....|....*....
gi 15025520 576 kavqYLKDSIEYTYGKKgatIVDANKKAV 604
Cdd:PRK08534 149 ----SLKKAILERFPGK---LGEKNAEAV 170
|
|
| PRK08659 |
PRK08659 |
2-oxoacid:acceptor oxidoreductase subunit alpha; |
2-319 |
7.67e-15 |
|
2-oxoacid:acceptor oxidoreductase subunit alpha;
Pssm-ID: 181526 [Multi-domain] Cd Length: 376 Bit Score: 77.59 E-value: 7.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 2 AKKLKTMDGNEAAAY-ASYAFTDVAAIYPITPSTPMAE-------LVDNwsshgrknifgqpvKIVEMQSEAGAAGTVHG 73
Cdd:PRK08659 1 MTKVDFLQGNEACAEgAIAAGCRFFAGYPITPSTEIAEvmarelpKVGG--------------VFIQMEDEIASMAAVIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 74 SLIAGALTTTYTASQGLLLMIPNM-YKMAGElLPCVFHVSARAIATHALSIFGDHQDVMAARQtG------FVLLASSNV 146
Cdd:PRK08659 67 ASWAGAKAMTATSGPGFSLMQENIgYAAMTE-TPCVIVNVQRGGPSTGQPTKPAQGDMMQARW-GthgdhpIIALSPSSV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 147 QEVMDLAMVSHLAAIKARVPFMHFFDGFrTSHEYQKIEMIDYNDV------APLVDYESIKAFrsralnpeHPTVRGTAQ 220
Cdd:PRK08659 145 QECFDLTIRAFNLAEKYRTPVIVLADEV-VGHMREKVVLPEPDEIeiierkLPKVPPEAYKPF--------DDPEGGVPP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 221 NPDIyfqGR----------EASNNFYTAVPDIVESYMREI-EKITG--RVYHPFDYYGDPEAEDIIIAMGSVCDTVEETV 287
Cdd:PRK08659 216 MPAF---GDgyrfhvtgltHDERGFPTTDPETHEKLVRRLvRKIEKnrDDIVLYEEYMLEDAEVVVVAYGSVARSARRAV 292
|
330 340 350
....*....|....*....|....*....|..
gi 15025520 288 DYLRSKGQKVGLLKVHLYRPFSTDYFFKYLPK 319
Cdd:PRK08659 293 KEAREEGIKVGLFRLITVWPFPEEAIRELAKK 324
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
687-773 |
1.23e-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: 69.39 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 687 DKCIQCNQCAYVCPHSVIRaclLDDEEKenaperfvtkkpvgkglehlHYKIQISPLDCTGCGNCADICPApgKALIMKP 766
Cdd:COG1143 2 DKCIGCGLCVRVCPVDAIT---IEDGEP--------------------GKVYVIDPDKCIGCGLCVEVCPT--GAISMTP 56
|
90
....*....|
gi 15025520 767 ---AAEQIEE 773
Cdd:COG1143 57 felAVEDREE 66
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
961-1076 |
1.96e-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: 67.17 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 961 WLIGGDGWAYDIGFGGVDQVLALGDDVNIFVMDTEIYSNTGGQSSKSTPTGAIAKFASAGKKTRKKDLGLMAMTYGNVYV 1040
Cdd:cd03375 73 IVVSGDGDLAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFV 152
|
90 100 110
....*....|....*....|....*....|....*.
gi 15025520 1041 TQiAMGANMTHTIKAITEAEAYKGPSLVIAYAPCIS 1076
Cdd:cd03375 153 AR-GFSGDIKQLKEIIKKAIQHKGFSFVEVLSPCPT 187
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
677-766 |
8.75e-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: 61.67 E-value: 8.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 677 IAVNVPEWQIDKCIQCNQCAYVCPHSVIRAclldDEEKenaperfvtkkpvgkglehlhyKIQISPLDCTGCGNCADICP 756
Cdd:COG1149 1 VKRKIPVIDEEKCIGCGLCVEVCPEGAIKL----DDGG----------------------APVVDPDLCTGCGACVGVCP 54
|
90
....*....|
gi 15025520 757 ApgKALIMKP 766
Cdd:COG1149 55 T--GAITLEE 62
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
961-1075 |
3.08e-11 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 65.63 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 961 WLIGGDGWAYDIGfGG---------VDqvlalgddVNIFVMDTEIYSNTGGQSSKSTPTGAIAKFASAGKKTRKKDLGLM 1031
Cdd:PRK11867 91 IVVTGDGDALAIG-GNhfihalrrnID--------ITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVEL 161
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 15025520 1032 AMTYGNVYVTQiAMGANMTHTIKAITEAEAYKGPSLVIAYAPCI 1075
Cdd:PRK11867 162 ALGAGATFVAR-GFDSDVKQLTELIKAAINHKGFSFVEILQPCP 204
|
|
| PRK06853 |
PRK06853 |
indolepyruvate oxidoreductase subunit beta; Reviewed |
454-613 |
3.78e-11 |
|
indolepyruvate oxidoreductase subunit beta; Reviewed
Pssm-ID: 180732 [Multi-domain] Cd Length: 197 Bit Score: 63.73 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 454 YDSKKS--------GGSTVSHLRFGnKPIKSPyLVYE--ADYI-------ACHNKSFiyninvlkgLKKNGIFVLNcpfk 516
Cdd:PRK06853 32 YDVKVSevhgmsqrGGSVVSHVRFG-DEVYSP-LIPEgkADLLlafepleALRYLPY---------LKKGGKVVVN---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 517 dnelDEHLPNA-----MKKY---------IADNNIQFYTIDAVSIAQEvgLGSRI--NMIMQSAffkLANIIPVDKAVqy 580
Cdd:PRK06853 97 ----TQPIVPVpvslgLAKYpedeeileeLKKLGIKVYVIDAEKIAKE--AGNIKaaNVVLLGA---LAKFLPIDEET-- 165
|
170 180 190
....*....|....*....|....*....|...
gi 15025520 581 LKDSIEYTYGKKgatIVDANKKAVDAGVNAAHK 613
Cdd:PRK06853 166 LEEAIKERVPPK---FVEVNLKAFEAGREAAEK 195
|
|
| PRK14029 |
PRK14029 |
pyruvate/ketoisovalerate ferredoxin oxidoreductase subunit gamma; Provisional |
417-594 |
1.62e-10 |
|
pyruvate/ketoisovalerate ferredoxin oxidoreductase subunit gamma; Provisional
Pssm-ID: 172523 [Multi-domain] Cd Length: 185 Bit Score: 61.58 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 417 IRCKFYGLGSDGTVgankSAIKIIGDNTDM---YCQAYFSYDSKKSGGSTVSHLRFGNKPIKSPYLVYEADYIACHNKSF 493
Cdd:PRK14029 2 IEIRFHGRGGQGAV----TAANILAEAAFLegkYVQAFPFFGVERRGAPVTAFTRIDEKPIRIKTQIYEPDVVVVLDPSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 494 IYNINVLKGLKKNGIFVLNCPFKDNELDEHLPNAMKKyiadnniqFYTIDAVSIAQEVgLGSRI-NMIMQSAFFKLANII 572
Cdd:PRK14029 78 LDTVDVTAGLKDGGIVIVNTEKSKEEVLEKLKKKPKK--------LALVDATTIALEI-LGLPItNTAILGAVAKATGLV 148
|
170 180
....*....|....*....|..
gi 15025520 573 PVDKAVQYLKDSIEYTYGKKGA 594
Cdd:PRK14029 149 KIESVEEAIKDTFSGELGEKNA 170
|
|
| PRK07119 |
PRK07119 |
2-ketoisovalerate ferredoxin reductase; Validated |
1-324 |
3.39e-10 |
|
2-ketoisovalerate ferredoxin reductase; Validated
Pssm-ID: 235942 [Multi-domain] Cd Length: 352 Bit Score: 63.34 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 1 MAKKLktMDGNEAAAYAS-YAFTDVAAIYPITPSTPMAE-LVDNWSSHGRKnifgqpvkIVEMQSEAGAAGTVHGSLIAG 78
Cdd:PRK07119 2 MEKVL--MKGNEAIAEAAiRAGCRCYFGYPITPQSEIPEyMSRRLPEVGGV--------FVQAESEVAAINMVYGAAATG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 79 ALTTTYTASQGLLLMIPNMYKMAGELLPCVFHVSARA------IATHALSIF-----GDHQDvmaARqtgFVLLASSNVQ 147
Cdd:PRK07119 72 KRVMTSSSSPGISLKQEGISYLAGAELPCVIVNIMRGgpglgnIQPSQGDYFqavkgGGHGD---YR---LIVLAPSSVQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 148 EVMDLAMVSHLAAIKARVPFMHFFDGFRTsheyQKIEmidyndvaPLVdyesIKAFRSRALNPEHPTVRGTAQNP----- 222
Cdd:PRK07119 146 EMVDLTMLAFDLADKYRNPVMVLGDGVLG----QMME--------PVE----FPPRKKRPLPPKDWAVTGTKGRRkniit 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 223 --DIYFQGREASNNfytavpDIVESYmREIEKITGRvyhpFDYYGDPEAEDIIIAMGSVCDTVEETVDYLRSKGQKVGLL 300
Cdd:PRK07119 210 slFLDPEELEKHNL------RLQEKY-AKIEENEVR----YEEYNTEDAELVLVAYGTSARIAKSAVDMAREEGIKVGLF 278
|
330 340
....*....|....*....|....*
gi 15025520 301 K-VHLYrPFSTDyFFKYLPKTIKRI 324
Cdd:PRK07119 279 RpITLW-PFPEK-ALEELADKGKGF 301
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
689-756 |
3.95e-10 |
|
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: 56.38 E-value: 3.95e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15025520 689 CIQCNQCAYVCPHSVIRAcllddEEKENAPERFvtkkpvgkglehlhyKIQISPLDCTGCGNCADICP 756
Cdd:pfam12838 1 CIGCGACVAACPVGAITL-----DEVGEKKGTK---------------TVVIDPERCVGCGACVAVCP 48
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
687-756 |
2.14e-09 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 54.72 E-value: 2.14e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 687 DKCIQCNQCAYVCPHSVIRAclldDEEKENAperfvtkkpvgkglehlhykIQISPLDCTGCGNCADICP 756
Cdd:COG1146 8 DKCIGCGACVEVCPVDVLEL----DEEGKKA--------------------LVINPEECIGCGACELVCP 53
|
|
| NuoI |
TIGR01971 |
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ... |
687-780 |
5.17e-09 |
|
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: 55.50 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 687 DKCIQCNQCAYVCPHSVIRaclLDDEEKENAPERFvtkkpvgkglehlhYKIQISPLDCTGCGNCADICPApgKALIMKP 766
Cdd:TIGR01971 43 EKCIGCTLCAAVCPADAIR---VVPAEGEDGKRRL--------------KFYEINFGRCIFCGLCEEACPT--DAIVLTP 103
|
90
....*....|....
gi 15025520 767 AAEQIEEQSENFEY 780
Cdd:TIGR01971 104 EFELATYTRSDLVY 117
|
|
| Fer4_16 |
pfam13484 |
4Fe-4S double cluster binding domain; |
689-757 |
7.58e-09 |
|
4Fe-4S double cluster binding domain;
Pssm-ID: 463893 [Multi-domain] Cd Length: 65 Bit Score: 53.26 E-value: 7.58e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15025520 689 CIQCNQCAYVCPHSVIRAclldDEEKENAPERFVTKKPVGKGLEHLHYKIQISPlDCTGCGNCADICPA 757
Cdd:pfam13484 1 CGSCGKCIDACPTGAIVG----PEGVLDARRCISYLTIEKKGLIPDELRCLLGN-RCYGCDICQDVCPW 64
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
673-756 |
2.92e-08 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 53.55 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 673 EKRGIAVNVPEWQIDKCIQCNQCAYVCPHSVIRaclLDDEEKENAPerfvtkkpvgkglEHLHYKIQISplDCTGCGNCA 752
Cdd:cd10549 26 GPNGAIARGPEIDEDKCVFCGACVEVCPTGAIE---LTPEGKEYVP-------------KEKEAEIDEE--KCIGCGLCV 87
|
....
gi 15025520 753 DICP 756
Cdd:cd10549 88 KVCP 91
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
682-779 |
4.79e-08 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 52.78 E-value: 4.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 682 PEWQIDKCIQCNQCAYVCPHSVIracllddeekenapeRFVTKKPVGKGLEhlhykiqISPLDCTGCGNCADICpaPGKA 761
Cdd:cd10549 1 LKYDPEKCIGCGICVKACPTDAI---------------ELGPNGAIARGPE-------IDEDKCVFCGACVEVC--PTGA 56
|
90
....*....|....*...
gi 15025520 762 LIMKPAAEQIEEQSENFE 779
Cdd:cd10549 57 IELTPEGKEYVPKEKEAE 74
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
963-1083 |
7.77e-08 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 55.27 E-value: 7.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 963 IGGDGWAYDIGFGgvdQVLALGD---DVNIFVMDTEIYSNTGGQSSKSTPTGAIAKFASAGKKTRKKDLGLMAMTYGNVY 1039
Cdd:PRK05778 94 VGGDGDLASIGGG---HFIHAGRrniDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCALALAAGATF 170
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 15025520 1040 VTQiAMGANMTHTIKAITEAEAYKGPSLVIAYAPCISH-GIKTGM 1083
Cdd:PRK05778 171 VAR-SFAGDVKQLVELIKKAISHKGFAFIDVLSPCVTFnGRNTST 214
|
|
| PRK05844 |
PRK05844 |
pyruvate flavodoxin oxidoreductase subunit gamma; Validated |
443-612 |
9.88e-08 |
|
pyruvate flavodoxin oxidoreductase subunit gamma; Validated
Pssm-ID: 180284 [Multi-domain] Cd Length: 186 Bit Score: 53.24 E-value: 9.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 443 NTDMYCQAYFSYDSKKSGGSTVSHLRFGNKPIKSPYLVYEADYIACHNKSFIYNINVLKGLKKNGIFVLNCPFKDNELDE 522
Cdd:PRK05844 27 KTGKEVQAFAFYGSAKRGAAMTAYNRIDDEPILNHEKFMQPDYVLVIDPGLVFIENIFANEKEDTKYIITTHLSKEELIE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 523 HLPNAMKKyiadnniQFYTIDAVSIAQEVgLGSRI-NMIMQSAFFKLANIIPVDkavqYLKDSIEYTYGKK-GATIVDAN 600
Cdd:PRK05844 107 KKPELKGK-------KVFLVDCIKISMET-IGRPIpNTPMLGALMKVSGMLEID----AFKEAFKKVLGKKlPQKVIDAN 174
|
170
....*....|..
gi 15025520 601 KKAVDAGVNAAH 612
Cdd:PRK05844 175 MLAIQRAYEEVQ 186
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
687-756 |
1.00e-07 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 50.43 E-value: 1.00e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 687 DKCIQCNQCAYVCPHSVIRaclLDDEekenaperfvtkkpvgkglehlhyKIQISPLDCTGCGNCADICP 756
Cdd:COG4231 22 DKCTGCGACVKVCPADAIE---EGDG------------------------KAVIDPDLCIGCGSCVQVCP 64
|
|
| porD |
PRK09625 |
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed |
679-787 |
1.09e-07 |
|
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 236596 [Multi-domain] Cd Length: 133 Bit Score: 52.06 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 679 VNVPEWQIDKCIQCNQCAYVCPHSVIracllddEEKEnaperfvtKKPVGKGLEHlhykiqispldCTGCGNCADICPAP 758
Cdd:PRK09625 51 VEKPVHNNEICINCFNCWVYCPDAAI-------LSRD--------KKLKGVDYSH-----------CKGCGVCVEVCPTN 104
|
90 100
....*....|....*....|....*....
gi 15025520 759 GKALIMKPaaeqieEQSENfEYALKVKPK 787
Cdd:PRK09625 105 PKSLLMFE------EQIEN-ETALTQWPK 126
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
682-766 |
1.66e-07 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 49.73 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 682 PEWQIDKCIQCNQCAYVCPHSVIRaclLDDEekenaperfvtkkpvgkglehlhyKIQISPLDCTGCGNCADICPApgKA 761
Cdd:COG2768 6 PYVDEEKCIGCGACVKVCPVGAIS---IEDG------------------------KAVIDPEKCIGCGACIEVCPV--GA 56
|
....*
gi 15025520 762 LIMKP 766
Cdd:COG2768 57 IKIEW 61
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
673-765 |
5.82e-07 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 53.71 E-value: 5.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 673 EKRGIAVNVPEWQIDKCIQCNQCAYVCPHSVIRacllDDEEKenaperfvtkkpvgkglehlhyKIQISPLDCTGCGNCA 752
Cdd:COG1148 482 GELGVEPSVAEVDPEKCTGCGRCVEVCPYGAIS----IDEKG----------------------VAEVNPALCKGCGTCA 535
|
90
....*....|...
gi 15025520 753 DICPApgKALIMK 765
Cdd:COG1148 536 AACPS--GAISLK 546
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
687-756 |
7.05e-07 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 47.25 E-value: 7.05e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 687 DKCIQCNQCAYVCPhSVIRACLLDDEEKENAPERFVtkkpvgkglehlhykiqisPLDCTGCGNCADICP 756
Cdd:pfam13237 7 DKCIGCGRCTAACP-AGLTRVGAIVERLEGEAVRIG-------------------VWKCIGCGACVEACP 56
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
677-757 |
8.27e-07 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 47.35 E-value: 8.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 677 IAVNVPEWQIDKCIQCNQCAYVCPHSVIRaclLDDEekenaperfvtkkpvgkglehlhyKIQISPLDCTGCGNCADICP 756
Cdd:COG2221 5 IGTWPPKIDEEKCIGCGLCVAVCPTGAIS---LDDG------------------------KLVIDEEKCIGCGACIRVCP 57
|
.
gi 15025520 757 A 757
Cdd:COG2221 58 T 58
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
688-757 |
1.35e-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: 46.92 E-value: 1.35e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 688 KCIQCNQCAYVCPhsvirACLLDDEEKENAPERFVTKKpvgKGLEHLHYKIQISPLDCTGCGNCADICPA 757
Cdd:pfam13183 1 RCIRCGACLAACP-----VYLVTGGRFPGDPRGGAAAL---LGRLEALEGLAEGLWLCTLCGACTEVCPV 62
|
|
| PRK05888 |
PRK05888 |
NADH-quinone oxidoreductase subunit NuoI; |
688-781 |
1.68e-06 |
|
NADH-quinone oxidoreductase subunit NuoI;
Pssm-ID: 235637 [Multi-domain] Cd Length: 164 Bit Score: 49.11 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 688 KCIQCNQCAYVCPHSVIRACLLDDEEKENAPERFvtkkpvgkglehlhykiQISPLDCTGCGNCADICPApgKALIMkpa 767
Cdd:PRK05888 59 RCIACKLCAAICPADAITIEAAEREDGRRRTTRY-----------------DINFGRCIFCGFCEEACPT--DAIVE--- 116
|
90
....*....|....
gi 15025520 768 aeqieeqSENFEYA 781
Cdd:PRK05888 117 -------TPDFELA 123
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
688-756 |
2.58e-06 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 45.62 E-value: 2.58e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15025520 688 KCIQCNQCAYVCPHSVIRAcllddeekenaperfvtkKPVGKGLEhlhykIQISPLDCTGCGNCADICP 756
Cdd:pfam13187 1 KCTGCGACVAACPAGAIVP------------------DLVGQTIR-----GDIAGLACIGCGACVDACP 46
|
|
| Fer4_6 |
pfam12837 |
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ... |
681-704 |
8.76e-06 |
|
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: 43.37 E-value: 8.76e-06
|
| Fer4_21 |
pfam14697 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
687-759 |
2.19e-05 |
|
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: 43.04 E-value: 2.19e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15025520 687 DKCIQCNQCAYVCPHSVIRACLLDDEEkenaperfvtkkpvgkglehlHYKIqISPlDCTGCGNCADICPAPG 759
Cdd:pfam14697 6 DTCIGCGKCYIACPDTSHQAIVGDGKR---------------------HHTV-IED-ECTGCNLCVSVCPVDD 55
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
961-1070 |
2.26e-05 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 45.65 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 961 WLIGGDGwaydiGFGGVDQVLA----LGDDVNIFVMDTEIYSNTGGQsskSTPTGAIAKFASAGKKTRKKDLGLMAMTYG 1036
Cdd:pfam02775 50 VAIAGDG-----GFQMNLQELAtavrYNLPITVVVLNNGGYGMTRGQ---QTPFGGGRYSGPSGKILPPVDFAKLAEAYG 121
|
90 100 110
....*....|....*....|....*....|....*.
gi 15025520 1037 --NVYVTQIAmganmtHTIKAITEAEAYKGPSLVIA 1070
Cdd:pfam02775 122 akGARVESPE------ELEEALKEALEHDGPALIDV 151
|
|
| fdxN_nitrog |
TIGR02936 |
ferredoxin III, nif-specific; Members of this family are homodimeric ferredoxins from nitrogen ... |
687-756 |
4.46e-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: 43.16 E-value: 4.46e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 687 DKCIQCNQCAYVCPHSVIRACLLDDEEKENAPERFvtkkpvGKGLEHLHYKIqISPLDCTGCGNCADICP 756
Cdd:TIGR02936 21 EKCIGCGRCYKVCGRDVLTLKGINEEGELVASDDD------DDEIERKVMVV-ANPGNCIGCGACARVCP 83
|
|
| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
964-1076 |
5.05e-05 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 46.67 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 964 GGDGWAYDIGFGGVDQVLALGDDVNIFVMDTEIYSNTGGQSSKSTPTGAIAKFASAGKKTRKKDLGLMAMTYGNVYVTQi 1043
Cdd:PRK11866 84 GGDGDGYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEPFNPIALALAAGATFVAR- 162
|
90 100 110
....*....|....*....|....*....|...
gi 15025520 1044 AMGANMTHTIKAITEAEAYKGPSLVIAYAPCIS 1076
Cdd:PRK11866 163 GFSGDVKHLKEIIKEAIKHKGFSFIDVLSPCVT 195
|
|
| ACS_1 |
cd01916 |
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ... |
686-843 |
1.41e-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: 46.25 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 686 IDKCIQCNQCAYVCPHSviracLLDDEEKENAperfvtKKPVGKGLEHLHYKiqispldCTGCGNCADICPA--PGKALI 763
Cdd:cd01916 364 AAKCTDCGWCTRACPNS-----LRIKEAMEAA------KEGDFSGLADLFDQ-------CVGCGRCEQECPKeiPIINMI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 764 MKPAAEQIEEQsenfeyalKVKPKEGIMDIHTVKGSQFSRPLLEfnGACPG------CGETP----YIKLLTQLYGDRMM 833
Cdd:cd01916 426 EKAARERIKEE--------KGKMRAGRGPIKDTEIRKVGAPIVL--GDIPGvialvgCSNYPngtkDVYKIAEEFLERNY 495
|
170
....*....|
gi 15025520 834 IANATGCSSI 843
Cdd:cd01916 496 IVVTTGCMAM 505
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
686-766 |
1.42e-04 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319895 [Multi-domain] Cd Length: 154 Bit Score: 43.40 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 686 IDKCIQCNQCAYVCPHSVIRACLLDDEEK---------ENAPERFVTKK-----PVG----KGLEHLHYKI---QISPLD 744
Cdd:cd16373 13 LALCIRCGLCVEACPTGVIQPAGLEDGLEggrtpyldpREGPCDLCCDAcvevcPTGalrpLDLEEQKVKMgvaVIDKDR 92
|
90 100
....*....|....*....|....*...
gi 15025520 745 C------TGCGNCADICPAPGKALIMKP 766
Cdd:cd16373 93 ClawqggTDCGVCVEACPTEAIAIVLED 120
|
|
| PRK14028 |
PRK14028 |
pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional |
423-756 |
1.44e-04 |
|
pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional
Pssm-ID: 172522 [Multi-domain] Cd Length: 312 Bit Score: 45.37 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 423 GLGSDGTVgankSAIKIIGDNTDM---YCQAYFSYDSKKSGGSTVSHLRFGNKPIKSPYLVYEADYIACHNKSFIYNIN- 498
Cdd:PRK14028 9 GRGGQGIV----TATYIIANAAVIdgfYAIANPEFGAERRGAPVKAFLTISKNPIEDQEPVKTPDVAVIFDDKLIDPMRf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 499 VLKGLKKNGIFVLNCPFKdneldehlPNAMKKYIADNNIQFYTIDAVSIAQE-VGLGSRiNMIMQSAFFKLANIipvdKA 577
Cdd:PRK14028 85 AIDAVKPGGYVILNTGKQ--------PEEARKLVGRDDVYIVVLDAIGIARKhLKLDVP-NGPLAGAFSKVMGF----PS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 578 VQYLKDSIEYTYGKKGATIVDANKKAVD-AGVNAAHKVTVPEAWKNAESNYQP-LKGLPDFV--QRIERPMArhegdelp 653
Cdd:PRK14028 152 LESIRTAFETQLGKAVEENFAATKEAYEvAVVIPPEKVDASAKPKGIISTTSAfLTGPYELVgwQEVNKAGA-------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 654 vsafkgmedgVFPLGITAYEKRGIAVNVPEWQIDKCIQCNQCAYVCPhsviracllDDEEKENAPERfvtKKPVGKgleh 733
Cdd:PRK14028 224 ----------VFPGSSFPYLTGGWRIDKPVIDHSKCIMCRKCWLYCP---------DDAIIEAWREA---EGPRGR---- 277
|
330 340
....*....|....*....|....*.
gi 15025520 734 lHYKIQISPLD---CTGCGNCADICP 756
Cdd:PRK14028 278 -KFRMKMIDFDyqyCKGCGVCAEVCP 302
|
|
| Fer4_18 |
pfam13746 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
693-756 |
1.92e-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: 404610 [Multi-domain] Cd Length: 114 Bit Score: 42.00 E-value: 1.92e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15025520 693 NQCAYVCPHSVIRACLLDDEEKE-----NAPERFVTKKPVGKGLEHLHYKIQISPLDCTGCGNCADICP 756
Cdd:pfam13746 4 NFCIYACPYGRFQSVMYDEDTLTvvydaVRGEGIYGRKPPKAGLKTKELRQQKGVGDCIDCESCVQVCP 72
|
|
| glpC |
PRK11168 |
anaerobic glycerol-3-phosphate dehydrogenase subunit C; |
686-776 |
3.72e-04 |
|
anaerobic glycerol-3-phosphate dehydrogenase subunit C;
Pssm-ID: 236869 [Multi-domain] Cd Length: 396 Bit Score: 44.47 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 686 IDKCIQCNQCAYVCPhsVIRAcllDDE---EKENAP--ERFVTKKPVgKGLEHLHYkiqispldCTGCGNCADICPA--P 758
Cdd:PRK11168 6 FDSCIKCTVCTTACP--VARV---NPLypgPKQAGPdgERLRLKDGA-LYDESLKY--------CSNCKRCEVACPSgvK 71
|
90
....*....|....*...
gi 15025520 759 GKALIMKPAAEQIEEQSE 776
Cdd:PRK11168 72 IGDIIQRARAKYVTERGP 89
|
|
| Fer4_17 |
pfam13534 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
688-756 |
6.27e-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: 433287 [Multi-domain] Cd Length: 61 Bit Score: 38.98 E-value: 6.27e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15025520 688 KCIQCNQCAYVC---------PHSVIRACLLDDEEKENAPERFvtkkpvgkglehlhykiqispLDCTGCGNCADICP 756
Cdd:pfam13534 1 RCIQCGCCVDECpryllngdePKKLMRAAYLGDLEELQANKVA---------------------NLCSECGLCEYACP 57
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
733-756 |
7.16e-04 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 39.33 E-value: 7.16e-04
10 20
....*....|....*....|....
gi 15025520 733 HLHYKIQISPLDCTGCGNCADICP 756
Cdd:COG2768 1 HSLGKPYVDEEKCIGCGACVKVCP 24
|
|
| DMSOR_beta-like |
cd04410 |
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ... |
689-756 |
1.21e-03 |
|
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: 40.45 E-value: 1.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 689 CIQCNQ--CAYVCPHSVIracllddeekenaperfvTKKPVGKglehlhykIQISPLDCTGCGNCADICP 756
Cdd:cd04410 50 CMHCEDppCVKACPTGAI------------------YKDEDGI--------VLIDEDKCIGCGSCVEACP 93
|
|
| Fer4 |
pfam00037 |
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ... |
738-756 |
2.05e-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: 2.05e-03
|
| PRK06274 |
PRK06274 |
indolepyruvate oxidoreductase subunit beta; |
460-615 |
2.28e-03 |
|
indolepyruvate oxidoreductase subunit beta;
Pssm-ID: 235765 [Multi-domain] Cd Length: 197 Bit Score: 40.42 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 460 GGSTVSHLRFGNKpIKSPyLVYE--AD-YIACHNKSFIYNinvLKGLKKNGIFVLNC----PFKDNELDEHLPNAMKKYI 532
Cdd:PRK06274 45 EGSVISHLRFGDE-ISSP-LIPEgqADlLLALEPAEVARN---LHFLKKGGKIIVNAyaihPATTVGSEKYDPEKEIKFA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 533 ADNNIQFYTIDAVSIAQEVGLGSRINMIMQSAFFKlANIIPVDKavQYLKDSIEYTYGKKgatIVDANKKAVDAGVNAAH 612
Cdd:PRK06274 120 KEKICDVICIDFTKLADEIGNPRSLNVIMLGAAFG-AGLLPLSK--ESVLETIEAELPEK---LREINLAAFELGIELIS 193
|
...
gi 15025520 613 KVT 615
Cdd:PRK06274 194 LIS 196
|
|
| Fer4 |
pfam00037 |
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ... |
687-705 |
2.48e-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: 2.48e-03
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
662-756 |
3.64e-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: 41.22 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 662 DGVFPLGITAYEKRGIavNVPEWQ-----IDKCIQCNQCAYVCP---------HS------VIRAcLLDDEEKENAPERF 721
Cdd:COG0247 50 PGVELLGDGDLHDKNL--KTLPWKelldaLDACVGCGFCRAMCPsykatgdekDSprgrinLLRE-VLEGELPLDLSEEV 126
|
90 100 110
....*....|....*....|....*....|....*
gi 15025520 722 VtkkpvgkglEHLHYkiqispldCTGCGNCADICP 756
Cdd:COG0247 127 Y---------EVLDL--------CLTCKACETACP 144
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
687-766 |
5.05e-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: 40.06 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 687 DKCIQCNQCAYVCphsviracllddeekenapeRFVTKKPVGKGLEhlhykiqISPLDCTGCGNCADICPApgKALIMKP 766
Cdd:cd03110 64 EKCIRCGNCERVC--------------------KFGAILEFFQKLI-------VDESLCEGCGACVIICPR--GAIYLKD 114
|
|
| PRK08537 |
PRK08537 |
2-oxoacid:ferredoxin oxidoreductase subunit gamma; |
453-609 |
5.36e-03 |
|
2-oxoacid:ferredoxin oxidoreductase subunit gamma;
Pssm-ID: 181462 [Multi-domain] Cd Length: 177 Bit Score: 39.26 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 453 SYDSKKSGGSTVSHLRFGNKPIKSPYlVYEADYIAC--HNKSFIYninvLKGLKKNGIFVLncpfkDNELDEHLPNAMKK 530
Cdd:PRK08537 39 SYGPEARGGASKSEVVISDEEIDYPK-VISPDILVAmsQEAYDKY----LDDLKEGGTVIV-----DPDLVPIREIEYEK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 531 yiadnNIQFYTIDAVSIAQE-VGLGSRINMIMQSAFFKLANIIPVDKAVQYLKDSIeytygKKGATivDANKKAVDAGVN 609
Cdd:PRK08537 109 -----KVKVYKVPFTEIAEEeIGLSIVANIVMLGALTKLTGIVSKEAIEKAILDSV-----PKGTE--EKNLMAFEKGYE 176
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
668-756 |
5.57e-03 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 40.78 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15025520 668 GITAYEKRGIAVNVPEwqiDKCIQCNQCAYVCPHSVIRAcllDDEEKENAPERfvtkkpvgkglehlhykiqispldCTG 747
Cdd:COG4624 75 GIIIIDKRGPSIIRDK---EKCKNCYPCVRACPVKAIKV---DDGKAEIDEEK------------------------CIS 124
|
....*....
gi 15025520 748 CGNCADICP 756
Cdd:COG4624 125 CGQCVAVCP 133
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
737-763 |
7.43e-03 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 36.56 E-value: 7.43e-03
10 20 30
....*....|....*....|....*....|...
gi 15025520 737 KIQISPLDCTGCGNCADICPA------PGKALI 763
Cdd:COG4231 16 RYVIDEDKCTGCGACVKVCPAdaieegDGKAVI 48
|
|
| |
