|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
5-449 |
2.82e-151 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 435.76 E-value: 2.82e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 5 NFNLPDVGEGLTEAEIVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGSPIITFVTDARDD 84
Cdd:PRK11856 4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 85 AGPGKIATAEAPAPEEGGGSVlvgygtgGGATSRRKRPAERPVRSSVGVIAKPPIRKLARDLGVDLTTVTPTGADGEVTR 164
Cdd:PRK11856 84 AAAAAEAAPEAPAPEPAPAAA-------AAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 165 DDVMTHASQAsvfrnietpewgavreetvpapqstPAGLARGVSAAPASAPVSDDRTESIPVKGVRKATSSAMVQSAYSA 244
Cdd:PRK11856 157 EDVEAAAAAA-------------------------APAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 245 PHVTVWKEIDASRTMELVKRLKASPdyadIRVSPLLIMARAVIWAARRTPMVNAAWIEteggAEIAVRHYVNLGIAAATP 324
Cdd:PRK11856 212 PHFTLTDEVDVTALLALRKQLKAIG----VKLTVTDFLIKAVALALKKFPELNASWDD----DAIVLKKYVNIGIAVATD 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 325 RGLLVPNIKDAQDLSMKDLARALNRLTLTAREGKTSPADQQGGTITITNIGVFGMDAGTPIINPGEAGIVAMGTISQKPW 404
Cdd:PRK11856 284 GGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPV 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 914699459 405 VVDGEVRPRWVTTVAGSFDHRVIDGDGMSRFIADVASVLEEPALL 449
Cdd:PRK11856 364 VVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALL 408
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
237-449 |
1.14e-84 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 258.63 E-value: 1.14e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 237 MVQSAYSAPHVTVWKEIDASRTMELVKRLKASPDYADIRVSPLLIMARAVIWAARRTPMVNAAWIETEGgaEIAVRHYVN 316
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEG--EIVYKKYVN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 317 LGIAAATPRGLLVPNIKDAQDLSMKDLARALNRLTLTAREGKTSPADQQGGTITITNIGVFGMDAGTPIINPGEAGIVAM 396
Cdd:pfam00198 79 IGIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 914699459 397 GTISQKPWVVDGEVRPRWVTTVAGSFDHRVIDGDGMSRFIADVASVLEEPALL 449
Cdd:pfam00198 159 GRIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
5-449 |
1.26e-77 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 247.34 E-value: 1.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 5 NFNLPDVGEGLTEAEIVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGSPIITFvtdaRDD 84
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAIL----EEG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 85 AGPGKIATAEAPAPEEGGGsvlvgygtgggATSRRKRPAERPVRSSvgviAKPPIRKLARDLGVDLTTVTPTGADGEVTR 164
Cdd:TIGR01347 78 NDATAAPPAKSGEEKEETP-----------AASAAAAPTAAANRPS----LSPAARRLAKEHGIDLSAVPGTGVTGRVTK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 165 DDVMTHASqasvfrnietpewgavreetvpAPQSTPAGLARGVSAAPASAPVSDDRtesIPVKGVRKATSSAMVQSAYSA 244
Cdd:TIGR01347 143 EDIIKKTE----------------------APASAQPPAAAAAAAAPAAATRPEER---VKMTRLRQRIAERLKEAQNST 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 245 PHVTVWKEIDASRTMELVKRLK-ASPDYADIRVSPLLIMARAVIWAARRTPMVNAAwIEtegGAEIAVRHYVNLGIAAAT 323
Cdd:TIGR01347 198 AMLTTFNEVDMSAVMELRKRYKeEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNAE-ID---GDDIVYKDYYDISVAVST 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 324 PRGLLVPNIKDAQDLSMKDLARALNRLTLTAREGKTSPADQQGGTITITNIGVFGMDAGTPIINPGEAGIVAMGTISQKP 403
Cdd:TIGR01347 274 DRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERP 353
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 914699459 404 WVVDGEVRPRWVTTVAGSFDHRVIDGDGMSRFIADVASVLEEPALL 449
Cdd:TIGR01347 354 VAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRL 399
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
6-78 |
9.22e-27 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 102.45 E-value: 9.22e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 914699459 6 FNLPDVGEGLTEAEIVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGSPIITFV 78
Cdd:COG0508 5 IKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
6-77 |
3.80e-25 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 97.86 E-value: 3.80e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914699459 6 FNLPDVGEGLTEAEIVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGSPIITF 77
Cdd:cd06849 3 IKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
5-449 |
2.82e-151 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 435.76 E-value: 2.82e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 5 NFNLPDVGEGLTEAEIVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGSPIITFVTDARDD 84
Cdd:PRK11856 4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 85 AGPGKIATAEAPAPEEGGGSVlvgygtgGGATSRRKRPAERPVRSSVGVIAKPPIRKLARDLGVDLTTVTPTGADGEVTR 164
Cdd:PRK11856 84 AAAAAEAAPEAPAPEPAPAAA-------AAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 165 DDVMTHASQAsvfrnietpewgavreetvpapqstPAGLARGVSAAPASAPVSDDRTESIPVKGVRKATSSAMVQSAYSA 244
Cdd:PRK11856 157 EDVEAAAAAA-------------------------APAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 245 PHVTVWKEIDASRTMELVKRLKASPdyadIRVSPLLIMARAVIWAARRTPMVNAAWIEteggAEIAVRHYVNLGIAAATP 324
Cdd:PRK11856 212 PHFTLTDEVDVTALLALRKQLKAIG----VKLTVTDFLIKAVALALKKFPELNASWDD----DAIVLKKYVNIGIAVATD 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 325 RGLLVPNIKDAQDLSMKDLARALNRLTLTAREGKTSPADQQGGTITITNIGVFGMDAGTPIINPGEAGIVAMGTISQKPW 404
Cdd:PRK11856 284 GGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPV 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 914699459 405 VVDGEVRPRWVTTVAGSFDHRVIDGDGMSRFIADVASVLEEPALL 449
Cdd:PRK11856 364 VVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALL 408
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-450 |
1.27e-102 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 316.38 E-value: 1.27e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 2 STQNFNLPDVGEgLTEAEIVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGSPIITFvtda 81
Cdd:PRK11855 118 GVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVI---- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 82 rDDAGPGKIATAEAPAPEEGGGSVLVGYGTGGGATSRRKRPAERPVRSSVGVIAKPPIRKLARDLGVDLTTVTPTGADGE 161
Cdd:PRK11855 193 -EVAAAAPAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGR 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 162 VTRDDVMTHASQASvfrnietpewgavreeTVPAPQSTPAGLARGVSAAPASAPVSD----DRTESIPVKGVRKATSSAM 237
Cdd:PRK11855 272 ITKEDVQAFVKGAM----------------SAAAAAAAAAAAAGGGGLGLLPWPKVDfskfGEIETKPLSRIKKISAANL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 238 VQSAYSAPHVTVWKEIDASRTMELVKRLKASPDYADIRVSPLLIMARAVIWAARRTPMVNAAWieTEGGAEIAVRHYVNL 317
Cdd:PRK11855 336 HRSWVTIPHVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASL--DEDGDELTYKKYFNI 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 318 GIAAATPRGLLVPNIKDAQDLSMKDLARALNRLTLTAREGKTSPADQQGGTITITNIGVFGMDAGTPIINPGEAGIVAMG 397
Cdd:PRK11855 414 GFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVG 493
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 914699459 398 TISQKPWVVDGEVRPRWVTTVAGSFDHRVIDGDGMSRFIADVASVLEEPALLV 450
Cdd:PRK11855 494 KSQMKPVWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRML 546
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
237-449 |
1.14e-84 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 258.63 E-value: 1.14e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 237 MVQSAYSAPHVTVWKEIDASRTMELVKRLKASPDYADIRVSPLLIMARAVIWAARRTPMVNAAWIETEGgaEIAVRHYVN 316
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEG--EIVYKKYVN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 317 LGIAAATPRGLLVPNIKDAQDLSMKDLARALNRLTLTAREGKTSPADQQGGTITITNIGVFGMDAGTPIINPGEAGIVAM 396
Cdd:pfam00198 79 IGIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 914699459 397 GTISQKPWVVDGEVRPRWVTTVAGSFDHRVIDGDGMSRFIADVASVLEEPALL 449
Cdd:pfam00198 159 GRIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
9-450 |
1.41e-78 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 249.75 E-value: 1.41e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 9 PDVGEGLTEAEIVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGSPIitfvtdARDDAGPG 88
Cdd:PRK05704 8 PTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVL------GRIDEGAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 89 KIATAEAPAPEEGggsvlvgygtgggATSRRKRPAERPVRSSVGVIAKPPIRKLARDLGVDLTTVTPTGADGEVTRDDVM 168
Cdd:PRK05704 82 AGAAAAAAAAAAA-------------AAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 169 THASQASvfrnietpewgavreetvPAPQSTPAglargVSAAPASAPVSDDRTESIPVKGVRKATSSAMVQSAYSAPHVT 248
Cdd:PRK05704 149 AALAAAA------------------AAPAAPAA-----AAPAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNTTAMLT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 249 VWKEIDASRTMELVKRLK-ASPDYADIRvspLLIMA---RAVIWAARRTPMVNAAwIEtegGAEIAVRHYVNLGIAAATP 324
Cdd:PRK05704 206 TFNEVDMTPVMDLRKQYKdAFEKKHGVK---LGFMSffvKAVVEALKRYPEVNAS-ID---GDDIVYHNYYDIGIAVGTP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 325 RGLLVPNIKDAQDLSMKDLARALNRLTLTAREGKTSPADQQGGTITITNIGVFGMDAGTPIINPGEAGIVAMGTISQKPW 404
Cdd:PRK05704 279 RGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPV 358
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 914699459 405 VVDGEVRPRWVTTVAGSFDHRVIDGDGMSRFIADVASVLEEPALLV 450
Cdd:PRK05704 359 AVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLL 404
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
5-449 |
1.26e-77 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 247.34 E-value: 1.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 5 NFNLPDVGEGLTEAEIVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGSPIITFvtdaRDD 84
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAIL----EEG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 85 AGPGKIATAEAPAPEEGGGsvlvgygtgggATSRRKRPAERPVRSSvgviAKPPIRKLARDLGVDLTTVTPTGADGEVTR 164
Cdd:TIGR01347 78 NDATAAPPAKSGEEKEETP-----------AASAAAAPTAAANRPS----LSPAARRLAKEHGIDLSAVPGTGVTGRVTK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 165 DDVMTHASqasvfrnietpewgavreetvpAPQSTPAGLARGVSAAPASAPVSDDRtesIPVKGVRKATSSAMVQSAYSA 244
Cdd:TIGR01347 143 EDIIKKTE----------------------APASAQPPAAAAAAAAPAAATRPEER---VKMTRLRQRIAERLKEAQNST 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 245 PHVTVWKEIDASRTMELVKRLK-ASPDYADIRVSPLLIMARAVIWAARRTPMVNAAwIEtegGAEIAVRHYVNLGIAAAT 323
Cdd:TIGR01347 198 AMLTTFNEVDMSAVMELRKRYKeEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNAE-ID---GDDIVYKDYYDISVAVST 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 324 PRGLLVPNIKDAQDLSMKDLARALNRLTLTAREGKTSPADQQGGTITITNIGVFGMDAGTPIINPGEAGIVAMGTISQKP 403
Cdd:TIGR01347 274 DRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERP 353
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 914699459 404 WVVDGEVRPRWVTTVAGSFDHRVIDGDGMSRFIADVASVLEEPALL 449
Cdd:TIGR01347 354 VAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRL 399
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
6-450 |
6.07e-73 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 235.38 E-value: 6.07e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 6 FNLPDVGEGLTEAEIVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGSPIITFVTDARDDA 85
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 86 GPGKIATaeapaPEEGGGSVLVGYGTGGGATSRrkrpaerpvrssvGVIAKPPIRKLARDLGVDLTTVTPTGADGEVTRD 165
Cdd:PLN02528 81 RSDSLLL-----PTDSSNIVSLAESDERGSNLS-------------GVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 166 DVMTHASQASVFRN-IETPEWGAVREETVPAPQSTPAGlargvsaapasaPVSDDRTesIPVKGVRKATSSAMVQSAySA 244
Cdd:PLN02528 143 DVLKYAAQKGVVKDsSSAEEATIAEQEEFSTSVSTPTE------------QSYEDKT--IPLRGFQRAMVKTMTAAA-KV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 245 PHVTVWKEIDASRTMELVKRLKASPDYADIRVSPLLIMARAVIWAARRTPMVNAAWIETEggAEIAVRHYVNLGIAAATP 324
Cdd:PLN02528 208 PHFHYVEEINVDALVELKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEET--SEIRLKGSHNIGVAMATE 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 325 RGLLVPNIKDAQDLSMKDLARALNRLTLTAREGKTSPADQQGGTITITNIGVFGMDAGTPIINPGEAGIVAMGTISQKPW 404
Cdd:PLN02528 286 HGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPR 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 914699459 405 VVD-GEVRPRWVTTVAGSFDHRVIDGDGMSRFIADVASVLEEPALLV 450
Cdd:PLN02528 366 FVDdGNVYPASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLM 412
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-444 |
6.49e-70 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 233.36 E-value: 6.49e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 2 STQNFNLPDVGegLTEAEIVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGSPIITFVTDA 81
Cdd:PRK11854 205 GVKDVNVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEG 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 82 RDDAGPGKIATAEAPAPEEgggsvlvgygtgggatSRRKRPAERPVRSSVG----------VIAKPPIRKLARDLGVDLT 151
Cdd:PRK11854 283 AAPAAAPAKQEAAAPAPAA----------------AKAEAPAAAPAAKAEGksefaendayVHATPLVRRLAREFGVNLA 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 152 TVTPTGADGEVTRDDVMTHASQAsvfrnietpewgavreetVPAPQSTPAGLARGVSAAPASA-PVSD----DRTESIPV 226
Cdd:PRK11854 347 KVKGTGRKGRILKEDVQAYVKDA------------------VKRAEAAPAAAAAGGGGPGLLPwPKVDfskfGEIEEVEL 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 227 KGVRKATSSAMVQSAYSAPHVTVWKEIDASRTMELVKRLK--ASPDYADIRVSPLLIMARAVIWAARRTPMVNAAWieTE 304
Cdd:PRK11854 409 GRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRKQQNaeAEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSL--SE 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 305 GGAEIAVRHYVNLGIAAATPRGLLVPNIKDAQDLSMKDLARALNRLTLTAREGKTSPADQQGGTITITNIGVFGMDAGTP 384
Cdd:PRK11854 487 DGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTP 566
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914699459 385 IINPGEAGIVAMGTISQKPwVVDG-EVRPRWVTTVAGSFDHRVIDGDGMSRFIADVASVLE 444
Cdd:PRK11854 567 IVNAPEVAILGVSKSAMEP-VWNGkEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLS 626
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
7-450 |
9.62e-66 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 216.86 E-value: 9.62e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 7 NLPDVGEGLTEAEIVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGSPIITfvtdarddag 86
Cdd:PTZ00144 48 KVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSE---------- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 87 pgkIATAEAPAPEegggsvlvgygtgggatsrrkrPAERPvrssvgviakppirklardlgvdlttvtptgadgevtrdd 166
Cdd:PTZ00144 118 ---IDTGGAPPAA----------------------APAAA---------------------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 167 vmthASQASVFRNIETPEWGAVREETVPAPQSTPAGLARGVSAAPASAPV-----SDDRTE-SIPVKGVRKATSSAMVQS 240
Cdd:PTZ00144 133 ----AAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPPEPAPAAKPPptpvaRADPREtRVPMSRMRQRIAERLKAS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 241 AYSAPHVTVWKEIDASRTMELVKRLKasPDYADIR------VSPLLimaRAVIWAARRTPMVNAAWieteGGAEIAVRHY 314
Cdd:PTZ00144 209 QNTCAMLTTFNECDMSALMELRKEYK--DDFQKKHgvklgfMSAFV---KASTIALKKMPIVNAYI----DGDEIVYRNY 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 315 VNLGIAAATPRGLLVPNIKDAQDLSMKDLARALNRLTLTAREGKTSPADQQGGTITITNIGVFGMDAGTPIINPGEAGIV 394
Cdd:PTZ00144 280 VDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAIL 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 914699459 395 AMGTISQKPWVVDGEVRPRWVTTVAGSFDHRVIDGDGMSRFIADVASVLEEPALLV 450
Cdd:PTZ00144 360 GMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARML 415
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
5-450 |
7.16e-62 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273567 [Multi-domain] Cd Length: 436 Bit Score: 206.95 E-value: 7.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 5 NFNLPDVGEGLTEAEIVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGA-TVEVGSPIITFVTDARD 83
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTkDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 84 DA-----GPGKIATAEAPAPEEGGGSVLVGYGTGGGATSRRKRPAERPVRSSVG-----VIAKPPIRKLARDLGVDLTTV 153
Cdd:TIGR01349 81 VAdafknYKLESSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKesgdrIFASPLAKKLAKEKGIDLSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 154 TPTGADGEVTRDDVMTHASQAsvfrnietpewgavreetvPAPQSTPAgLARGVSAAPASAPVSDDRTESIPVKGVRKAT 233
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQS-------------------PASANQQA-AATTPATYPAAAPVSTGSYEDVPLSNIRKII 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 234 SSAMVQSAYSAPHVTVWKEIDASRTMELVKRLKAS-PDYADIRVSPLLIMARAViwAARRTPMVNAAWIETEggaeIAVR 312
Cdd:TIGR01349 221 AKRLLESKQTIPHYYVSIECNVDKLLALRKELNAMaSEVYKLSVNDFIIKASAL--ALREVPEANSSWTDNF----IRRY 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 313 HYVNLGIAAATPRGLLVPNIKDAQDLSMKDLARALNRLTLTAREGKTSPADQQGGTITITNIGVFGMDAGTPIINPGEAG 392
Cdd:TIGR01349 295 KNVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQAC 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914699459 393 IVAMGTISQKPWVVDGEVRPRWVTT---VAGSFDHRVIDGDGMSRFIADVASVLEEPALLV 450
Cdd:TIGR01349 375 ILAVGAVEDVAVVDNDEEKGFAVASimsVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEML 435
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
2-450 |
3.60e-60 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 205.49 E-value: 3.60e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 2 STQNFNLPDVGeGLTEAEIVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGSPIITFVTDA 81
Cdd:TIGR01348 115 GVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAG 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 82 RDDAGPGKIATAEAPAPEEGGGSVLVGyGTGGGATSRRKRPAERPVRSSVGVI-AKPPIRKLARDLGVDLTTVTPTGADG 160
Cdd:TIGR01348 194 STPATAPAPASAQPAAQSPAATQPEPA-AAPAAAKAQAPAPQQAGTQNPAKVDhAAPAVRRLAREFGVDLSAVKGTGIKG 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 161 EVTRDDVmthasQASVfrnietpewgavrEETVPAPQSTPAGLARGVSAAPASAPVSDDR---TESIPVKGVRKATSSAM 237
Cdd:TIGR01348 273 RILREDV-----QRFV-------------KEPSVRAQAAAASAAGGAPGALPWPNVDFSKfgeVEEVDMSRIRKISGANL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 238 VQSAYSAPHVTVWKEIDASRTMELVKRLKASPDYADIRVSPLLIMARAVIWAARRTPMVNAAWieTEGGAEIAVRHYVNL 317
Cdd:TIGR01348 335 TRNWTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASL--DLGGEQLILKKYVNI 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 318 GIAAATPRGLLVPNIKDAQDLSMKDLARALNRLTLTAREGKTSPADQQGGTITITNIGVFGMDAGTPIINPGEAGIVAMG 397
Cdd:TIGR01348 413 GVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVS 492
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 914699459 398 TISQKPwVVDG-EVRPRWVTTVAGSFDHRVIDGDGMSRFIADVASVLEEPALLV 450
Cdd:TIGR01348 493 KSGMEP-VWNGkEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLL 545
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
133-449 |
1.73e-48 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 168.05 E-value: 1.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 133 VIAKPPIRKLARDLGVDLTTVTPTGADGEVTRDDVMTHasqasvfrnIETPEWGAVREETVPAPQSTpaglargvSAAPA 212
Cdd:PRK11857 2 ILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENF---------IKSLKSAPTPAEAASVSSAQ--------QAAKT 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 213 SAPVSDDRT---ESIPVKGVRKATSSAMVQSAYSAPHVTVWKEIDASRTMELVKRLKAS-PDYADIRVSPLLIMARAVIW 288
Cdd:PRK11857 65 AAPAAAPPKlegKREKVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPvLKTEGVKLTFLPFIAKAILI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 289 AARRTPMVNAAWieTEGGAEIAVRHYVNLGIAAATPRGLLVPNIKDAQDLSMKDLARALNRLTLTAREGKTSPADQQGGT 368
Cdd:PRK11857 145 ALKEFPIFAAKY--DEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 369 ITITNIGVFGMDAGTPIINPGEAGIVAMGTISQKPWVVDGEVRPRWVTTVAGSFDHRVIDGDGMSRFIADVASVLEEPAL 448
Cdd:PRK11857 223 FTITNYGSVGSLYGVPVINYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEI 302
|
.
gi 914699459 449 L 449
Cdd:PRK11857 303 L 303
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
4-446 |
5.43e-45 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 164.26 E-value: 5.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 4 QNFNLPDVGEGLTEAEIVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGAT-VEVGSPIITFVTDAR 82
Cdd:PLN02744 113 QEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKeIKVGEVIAITVEEEE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 83 D-----DAGPGKIATAEAPAPEEGGGSVLVGYGTGGGATSRRKRP-AERPVRSSVGVIAKPPIRKLARDLGVDLTTVTPT 156
Cdd:PLN02744 193 DigkfkDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASkPSAPPSSGDRIFASPLARKLAEDNNVPLSSIKGT 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 157 GADGEVTRDDVMTHASQasvfrnietpewgAVREETVPAPQstpaglargVSAAPASAPVsddrteSIPVKGVRKATSSA 236
Cdd:PLN02744 273 GPDGRIVKADIEDYLAS-------------GGKGATAPPST---------DSKAPALDYT------DIPNTQIRKVTASR 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 237 MVQSAYSAPHVTVWKEIDASRTMELVKRLKASPDYA---DIRVSPLLIMARAViwAARRTPMVNAAWIETeggaEIAVRH 313
Cdd:PLN02744 325 LLQSKQTIPHYYLTVDTRVDKLMALRSQLNSLQEASggkKISVNDLVIKAAAL--ALRKVPQCNSSWTDD----YIRQYH 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 314 YVNLGIAAATPRGLLVPNIKDAQDLSMKDLARALNRLTLTAREGKTSPADQQGGTITITNI-GVFGMDAGTPIINPGEAG 392
Cdd:PLN02744 399 NVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLgGPFGIKQFCAIINPPQSA 478
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 914699459 393 IVAMGTISQK--PWVVDGEVRPRWVTTVAGSFDHRVIDGDGMSRFIADVASVLEEP 446
Cdd:PLN02744 479 ILAVGSAEKRviPGSGPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENP 534
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
135-450 |
9.84e-45 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 159.30 E-value: 9.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 135 AKPPIRKLARDLGVDLTTVTPTGADGEVTRDDVMTHASQASVF-----------RNIETPEW------GAVREETV---- 193
Cdd:PRK14843 8 ATPAARKLADDLGINLYDVSGSGANGRVHKEDVETYKDTNVVRisplakrialeHNIAWQEIqgtghrGKIMKKDVlall 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 194 PAPQST-----PAGLARGVSAAPASAPVSDdrTESIPVKGVRKATSSAMVQSAYSAPHVTVWKEIDASRTMELVKR-LKA 267
Cdd:PRK14843 88 PENIENdsiksPAQIEKVEEVPDNVTPYGE--IERIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKvLEP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 268 SPDYADIRVSPLLIMARAVIWAARRTPMVNAAWieTEGGAEIAVRHYVNLGIAAATPRGLLVPNIKDAQDLSMKDLARAL 347
Cdd:PRK14843 166 IMEATGKKTTVTDLLSLAVVKTLMKHPYINASL--TEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 348 NRLTLTAREGKTSPADQQGGTITITNIGVFGMDAGTPIINPGEAGIVAMGTISQKPWVVDGEVRPRWVTTVAGSFDHRVI 427
Cdd:PRK14843 244 KDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVV 323
|
330 340
....*....|....*....|....
gi 914699459 428 DGDGMSRFIADVASVLEEP-ALLV 450
Cdd:PRK14843 324 DGMAGAKFMKDLKELIETPiSMLI 347
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
8-450 |
1.47e-41 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 153.76 E-value: 1.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 8 LPDVGEGLTEAEIVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGS--PIITFVTDARDDA 85
Cdd:PLN02226 96 VPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTkvAIISKSEDAASQV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 86 GPGKIAtAEAPAPEegggsvlvgygtgggaTSRRKRPAERPVRSSVGVIAKPpirklardlgvdlttvtptgadgevtrd 165
Cdd:PLN02226 176 TPSQKI-PETTDPK----------------PSPPAEDKQKPKVESAPVAEKP---------------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 166 dvmthasqasvfrnietpewgavreeTVPAPQSTPAGLARGVSAAPasapvsDDRTESIPVKGVRKATSSAMVQSAYSAP 245
Cdd:PLN02226 211 --------------------------KAPSSPPPPKQSAKEPQLPP------KERERRVPMTRLRKRVATRLKDSQNTFA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 246 HVTVWKEIDASRTMELVKRLK-ASPDYADIRVSPLLIMARAVIWAARRTPMVNAAWieteGGAEIAVRHYVNLGIAAATP 324
Cdd:PLN02226 259 LLTTFNEVDMTNLMKLRSQYKdAFYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVI----DGDDIIYRDYVDISIAVGTS 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 325 RGLLVPNIKDAQDLSMKDLARALNRLTLTAREGKTSPADQQGGTITITNIGVFGMDAGTPIINPGEAGIVAMGTISQKPW 404
Cdd:PLN02226 335 KGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPM 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 914699459 405 VVDGEVRPRWVTTVAGSFDHRVIDGDGMSRFIADVASVLEEPALLV 450
Cdd:PLN02226 415 VVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLL 460
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
6-78 |
9.22e-27 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 102.45 E-value: 9.22e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 914699459 6 FNLPDVGEGLTEAEIVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGSPIITFV 78
Cdd:COG0508 5 IKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
6-77 |
3.80e-25 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 97.86 E-value: 3.80e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914699459 6 FNLPDVGEGLTEAEIVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGSPIITF 77
Cdd:cd06849 3 IKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
191-443 |
6.84e-18 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 86.87 E-value: 6.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 191 ETVPAPQSTPAGLARGVSAAPASAPVSDdrtESIPVKGVRKATSSAMVQS-----AYSAPHVTVwKEIDASRTMeLVKRL 265
Cdd:PRK12270 88 AAAAAAAAPAAPPAAAAAAAPAAAAVED---EVTPLRGAAAAVAKNMDASlevptATSVRAVPA-KLLIDNRIV-INNHL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 266 KASpdyADIRVSPLLIMARAVIWAARRTPMVNAAWIETEGGAEIAVRHYVNLGIAAATP-----RGLLVPNIKDAQDLSM 340
Cdd:PRK12270 163 KRT---RGGKVSFTHLIGYALVQALKAFPNMNRHYAEVDGKPTLVTPAHVNLGLAIDLPkkdgsRQLVVPAIKGAETMDF 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 341 KDLARALNRLTLTAREGKTSPADQQGGTITITNIGVFGMDAGTPIINPGEAGIVAMGTI---------SQKPWVVDGEVR 411
Cdd:PRK12270 240 AQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMeypaefqgaSEERLAELGISK 319
|
250 260 270
....*....|....*....|....*....|..
gi 914699459 412 prwVTTVAGSFDHRVIDGDGMSRFIADVASVL 443
Cdd:PRK12270 320 ---VMTLTSTYDHRIIQGAESGEFLRTIHQLL 348
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
6-77 |
3.23e-17 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 75.71 E-value: 3.23e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914699459 6 FNLPDVGEGLTEAeIVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGSPIITF 77
Cdd:pfam00364 3 IKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
8-102 |
9.44e-14 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 72.28 E-value: 9.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 8 LPDVGEGLTEAEIVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGSPI-ITFVTDARDDAG 86
Cdd:PRK14875 7 MPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLaVVADAEVSDAEI 86
|
90
....*....|....*.
gi 914699459 87 PGKIATAEAPAPEEGG 102
Cdd:PRK14875 87 DAFIAPFARRFAPEGI 102
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
20-77 |
1.58e-11 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 59.35 E-value: 1.58e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 914699459 20 IVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGSPIITF 77
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
133-167 |
1.13e-09 |
|
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.
Pssm-ID: 460710 [Multi-domain] Cd Length: 36 Bit Score: 53.46 E-value: 1.13e-09
10 20 30
....*....|....*....|....*....|....*
gi 914699459 133 VIAKPPIRKLARDLGVDLTTVTPTGADGEVTRDDV 167
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDV 35
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
15-101 |
1.16e-08 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 56.85 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 15 LTEAEIVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGAT-VEVGSPIITFVTDARDDAGPGKIATA 93
Cdd:PRK11892 14 MEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEgVKVNTPIAVLLEEGESASDAGAAPAA 93
|
....*...
gi 914699459 94 EAPAPEEG 101
Cdd:PRK11892 94 AAEAAAAA 101
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
8-77 |
4.16e-08 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 50.13 E-value: 4.16e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914699459 8 LPDVGEGLTEAEIVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGSPIITF 77
Cdd:cd06663 4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
25-76 |
7.50e-08 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 51.05 E-value: 7.50e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 914699459 25 VAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGSPIIT 76
Cdd:COG0511 83 VKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFV 134
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
20-75 |
3.35e-06 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 49.46 E-value: 3.35e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 914699459 20 IVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGSPII 75
Cdd:PRK09282 533 VVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLM 588
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
23-78 |
4.54e-05 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 45.69 E-value: 4.54e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 914699459 23 WK--VAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGSPIITFV 78
Cdd:PRK14040 536 FKviVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTLA 593
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
25-74 |
1.75e-04 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 40.00 E-value: 1.75e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 914699459 25 VAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGSPI 74
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVL 75
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
9-75 |
7.51e-03 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 37.15 E-value: 7.51e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914699459 9 PDVGEGLTEA----EIVAWKVAPGDSVAINDVICEIETAKSLVELPSPHAGVVGELLAAEGATVEVGSPII 75
Cdd:PRK05641 80 ASAGENVVTApmpgKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLI 150
|
|
| |
