|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
1-384 |
0e+00 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 616.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 1 MIEITVPVLPESVTEGTLTTWCKQEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGSTVTSAQLLAHLK---- 76
Cdd:PRK05704 2 MVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDegaa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 77 -----------------PQAVIEETVTPVTETLAMPSARLEAQRSGVELADVAGSGRNGRILKEDVQR-VTPAPVIQPER 138
Cdd:PRK05704 82 agaaaaaaaaaaaaaaaPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAaLAAAAAAPAAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 139 VAEIAPAKPLTPGARQERREPMSRLRQRIAERLLASQQNNAILTTFNEVNMQSVMDLRARWKDRFAEKHGVKLGFMSFFV 218
Cdd:PRK05704 162 AAAAPAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSFFV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 219 KAVTRALERFPVVNASVDGNEIIWRDYCDIGIAVSSNRGLVVPVLRNAQSLSLVEIERQIAEYATQARNGKLPLEALQGG 298
Cdd:PRK05704 242 KAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 299 TFSITNGGTFGSMMSTPIINPPQSAILGMHAITPRPVAENGQVVIRPMMYLALSYDHRIIDGQEAVQTLVAIRELLESPE 378
Cdd:PRK05704 322 TFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPE 401
|
....*.
gi 446492375 379 QLLLDL 384
Cdd:PRK05704 402 RLLLDL 407
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
2-384 |
0e+00 |
|
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: 542.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 2 IEITVPVLPESVTEGTLTTWCKQEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGSTVTSAQLLAHLK----- 76
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEegnda 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 77 ----PQAVIEETVTPVTETL------------AMPSARLEAQRSGVELADVAGSGRNGRILKEDVQRVTPAPVIQPERVA 140
Cdd:TIGR01347 81 taapPAKSGEEKEETPAASAaaaptaaanrpsLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 141 EIAPAKPLTpGARQERREPMSRLRQRIAERLLASQQNNAILTTFNEVNMQSVMDLRARWKDRFAEKHGVKLGFMSFFVKA 220
Cdd:TIGR01347 161 AAAAAAPAA-ATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 221 VTRALERFPVVNASVDGNEIIWRDYCDIGIAVSSNRGLVVPVLRNAQSLSLVEIERQIAEYATQARNGKLPLEALQGGTF 300
Cdd:TIGR01347 240 VVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 301 SITNGGTFGSMMSTPIINPPQSAILGMHAITPRPVAENGQVVIRPMMYLALSYDHRIIDGQEAVQTLVAIRELLESPEQL 380
Cdd:TIGR01347 320 TITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRL 399
|
....
gi 446492375 381 LLDL 384
Cdd:TIGR01347 400 LLDL 403
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
4-384 |
4.75e-163 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 463.39 E-value: 4.75e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 4 ITVPVLPESVTEGTLTTWCKQEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGSTVTSAqllahlKPQAVIEE 83
Cdd:PTZ00144 47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVG------APLSEIDT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 84 TVTPvtetlamPSARLEAQRSGVELADVAGSGRNGRILKEDVQRVTPAPVIQPERVAEIAPAK----PLTPGARQERREP 159
Cdd:PTZ00144 121 GGAP-------PAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPPEPAPAAKppptPVARADPRETRVP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 160 MSRLRQRIAERLLASQQNNAILTTFNEVNMQSVMDLRARWKDRFAEKHGVKLGFMSFFVKAVTRALERFPVVNASVDGNE 239
Cdd:PTZ00144 194 MSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGDE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 240 IIWRDYCDIGIAVSSNRGLVVPVLRNAQSLSLVEIERQIAEYATQARNGKLPLEALQGGTFSITNGGTFGSMMSTPIINP 319
Cdd:PTZ00144 274 IVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINP 353
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446492375 320 PQSAILGMHAITPRPVAENGQVVIRPMMYLALSYDHRIIDGQEAVQTLVAIRELLESPEQLLLDL 384
Cdd:PTZ00144 354 PQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLDL 418
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-383 |
4.96e-137 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 396.85 E-value: 4.96e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 1 MIEITVPVLPESVTEGTLTTWCKQEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGSTVTSAQLLAHL----- 75
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIeeege 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 76 ----------------KPQAVIEETVTPVTET------------LAMPSARLEAQRSGVELADVAGSGRNGRILKEDVQR 127
Cdd:PRK11856 82 aeaaaaaeaapeapapEPAPAAAAAAAAAPAAaaapaapaaaaaKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 128 VTPAPVIQPERVAEIAPAKPLTPGARqERREPMSRLRQRIAERLLASQQNNAILTTFNEVNMQSVMDLRARWKdrfaeKH 207
Cdd:PRK11856 162 AAAAAAPAAAAAAAAAAAPPAAAAEG-EERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLK-----AI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 208 GVKLGFMSFFVKAVTRALERFPVVNASVDGNEIIWRDYCDIGIAVSSNRGLVVPVLRNAQSLSLVEIERQIAEYATQARN 287
Cdd:PRK11856 236 GVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKARE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 288 GKLPLEALQGGTFSITNGGTFGSMMSTPIINPPQSAILGMHAITPRPVAENGQVVIRPMMYLALSYDHRIIDGQEAVQTL 367
Cdd:PRK11856 316 GKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFL 395
|
410
....*....|....*.
gi 446492375 368 VAIRELLESPEQLLLD 383
Cdd:PRK11856 396 KALKELLENPALLLLE 411
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
2-384 |
2.40e-119 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 354.06 E-value: 2.40e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 2 IEITVPVLPESVTEGTLTTWCKQEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGSTV----------TSAQL 71
Cdd:PLN02226 92 VEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVepgtkvaiisKSEDA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 72 LAHLKPQAVIEETvtpvTETLAMPSARlEAQRSGVELADVAGSGRngrilkedvqrvTPAPVIQPERVAEiapaKPLTPG 151
Cdd:PLN02226 172 ASQVTPSQKIPET----TDPKPSPPAE-DKQKPKVESAPVAEKPK------------APSSPPPPKQSAK----EPQLPP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 152 ARQERREPMSRLRQRIAERLLASQQNNAILTTFNEVNMQSVMDLRARWKDRFAEKHGVKLGFMSFFVKAVTRALERFPVV 231
Cdd:PLN02226 231 KERERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYEKHGVKLGLMSGFIKAAVSALQHQPVV 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 232 NASVDGNEIIWRDYCDIGIAVSSNRGLVVPVLRNAQSLSLVEIERQIAEYATQARNGKLPLEALQGGTFSITNGGTFGSM 311
Cdd:PLN02226 311 NAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSL 390
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446492375 312 MSTPIINPPQSAILGMHAITPRPVAENGQVVIRPMMYLALSYDHRIIDGQEAVQTLVAIRELLESPEQLLLDL 384
Cdd:PLN02226 391 ISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLLDI 463
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-382 |
1.37e-114 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 344.50 E-value: 1.37e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 2 IEITVPVLPEsVTEGTLTTWCKQEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGSTVTSAQLLAHLK----- 76
Cdd:PRK11855 120 VEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEvaaaa 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 77 ------------------------------PQAVIEETVTPVTETLAMPSARLEAQRSGVELADVAGSGRNGRILKEDVQ 126
Cdd:PRK11855 199 paaaaapaaaapaaaaaaapapapaaaaapAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQ 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 127 R-----VTPAPVIQPERVAEIAPAKPLTPGAR-------QERREPMSRLRQRIAERLLASQQNNAILTTFNEVNMQSVMD 194
Cdd:PRK11855 279 AfvkgaMSAAAAAAAAAAAAGGGGLGLLPWPKvdfskfgEIETKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEA 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 195 LRARWKDRFaEKHGVKLGFMSFFVKAVTRALERFPVVNASVD--GNEIIWRDYCDIGIAVSSNRGLVVPVLRNAQSLSLV 272
Cdd:PRK11855 359 LRKQLKKEA-EKAGVKLTMLPFFIKAVVAALKEFPVFNASLDedGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLL 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 273 EIERQIAEYATQARNGKLPLEALQGGTFSITN----GGTFgsmmSTPIINPPQSAILGMHAITPRPVAENGQVVIRPMMY 348
Cdd:PRK11855 438 EIAREIAELAKKARDGKLKPDDMQGGCFTISSlggiGGTA----FTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLP 513
|
410 420 430
....*....|....*....|....*....|....
gi 446492375 349 LALSYDHRIIDGQEAVQTLVAIRELLESPEQLLL 382
Cdd:PRK11855 514 LSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
171-381 |
5.38e-94 |
|
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: 280.20 E-value: 5.38e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 171 LLASQQNNAILTTFNEVNMQSVMDLRARWKDRFAEKHGvKLGFMSFFVKAVTRALERFPVVNASVDGN--EIIWRDYCDI 248
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 249 GIAVSSNRGLVVPVLRNAQSLSLVEIERQIAEYATQARNGKLPLEALQGGTFSITNGGTFGSMMSTPIINPPQSAILGMH 328
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446492375 329 AITPRPVAENGQVVIRPMMYLALSYDHRIIDGQEAVQTLVAIRELLESPEQLL 381
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
3-382 |
1.54e-88 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 279.97 E-value: 1.54e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 3 EITVPVLpeSVTEGTLTTWCKQEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGSTVTSAQLLAHL------- 75
Cdd:PRK11854 208 DVNVPDI--GGDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFevegaap 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 76 --------------------KPQAVIEETVTPVTETL-------AMPSARLEAQRSGVELADVAGSGRNGRILKEDVQRV 128
Cdd:PRK11854 286 aaapakqeaaapapaaakaeAPAAAPAAKAEGKSEFAendayvhATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQAY 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 129 TPAPVIQPERVAEIAPAKPLTPG---------ARQERRE--PMSRLRQRIAERLLASQQNNAILTTFNEVNMQSVMDLR- 196
Cdd:PRK11854 366 VKDAVKRAEAAPAAAAAGGGGPGllpwpkvdfSKFGEIEevELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRk 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 197 ARWKDRFAEKHGVKLGFMSFFVKAVTRALERFPVVNASV--DGNEIIWRDYCDIGIAVSSNRGLVVPVLRNAQSLSLVEI 274
Cdd:PRK11854 446 QQNAEAEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLseDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIEL 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 275 ERQIAEYATQARNGKLPLEALQGGTFSITNGGTFGSMMSTPIINPPQSAILGMHAITPRPVAENGQVVIRPMMYLALSYD 354
Cdd:PRK11854 526 SRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGKEFAPRLMLPLSLSYD 605
|
410 420
....*....|....*....|....*...
gi 446492375 355 HRIIDGQEAVQTLVAIRELLESPEQLLL 382
Cdd:PRK11854 606 HRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
3-376 |
2.82e-87 |
|
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817).
Pssm-ID: 200219 [Multi-domain] Cd Length: 579 Bit Score: 274.97 E-value: 2.82e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 3 EITVPVLPESVTEGTLTTWCKQEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGSTVTSAQLLAHL------- 75
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIgdanaap 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 76 ------KPQAVIEETVTPVTETLAMPSARLE-------------------------------------AQRSGVELADVA 112
Cdd:TIGR02927 208 aepaeeEAPAPSEAGSEPAPDPAARAPHAAPdppapapapaktaapaaaapvssgdsgpyvtplvrklAKDKGVDLSTVK 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 113 GSGRNGRILKEDV----------QRVTPAPVIQPERVAEIAPAKPLTPGARQER--REPMSRLRQRIAERLLASQQNNAI 180
Cdd:TIGR02927 288 GTGVGGRIRKQDVlaaakaaeeaRAAAAAPAAAAAPAAPAAAAKPAEPDTAKLRgtTQKMNRIRQITADKTIESLQTSAQ 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 181 LTTFNEVNMQSVMDLRARWKDRFAEKHGVKLGFMSFFVKAVTRALERFPVVNASV--DGNEIIWRDYCDIGIAVSSNRGL 258
Cdd:TIGR02927 368 LTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYnaETKEVTYHDVEHVGIAVDTPRGL 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 259 VVPVLRNAQSLSLVEIERQIAEYATQARNGKLPLEALQGGTFSITNGGTFGSMMSTPIINPPQSAILGMHAITPRPV--- 335
Cdd:TIGR02927 448 LVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRvik 527
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 446492375 336 -AENGQVV-IRPMMYLALSYDHRIIDGQEAVQTLVAIRELLES 376
Cdd:TIGR02927 528 dEDGGESIaIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEE 570
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
3-382 |
5.84e-83 |
|
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: 259.73 E-value: 5.84e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 3 EITVPVLPESVTEGTLTTWCKQEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGS------------------ 64
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTkdvpvnkpiavlveeked 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 65 ----------------------TVTSAQLLAHLKPQAVIEETVTPVTET-----------LAMPSARLEAQRSGVELADV 111
Cdd:TIGR01349 81 vadafknyklessaspapkpseIAPTAPPSAPKPSPAPQKQSPEPSSPAplsdkesgdriFASPLAKKLAKEKGIDLSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 112 AGSGRNGRILKEDVQRVTP-APVIQPERVAEIAPA--KPLTPGARQERRE-PMSRLRQRIAERLLASQQNNAILTTFNEV 187
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPqSPASANQQAAATTPAtyPAAAPVSTGSYEDvPLSNIRKIIAKRLLESKQTIPHYYVSIEC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 188 NMQSVMDLRARWKDRFAEKhgVKLGFMSFFVKAVTRALERFPVVNASVDGNEIIWRDYCDIGIAVSSNRGLVVPVLRNAQ 267
Cdd:TIGR01349 241 NVDKLLALRKELNAMASEV--YKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNAD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 268 SLSLVEIERQIAEYATQARNGKLPLEALQGGTFSITNGGTFGSMMSTPIINPPQSAILGMHAITPRPVAENGQ---VVIR 344
Cdd:TIGR01349 319 AKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEekgFAVA 398
|
410 420 430
....*....|....*....|....*....|....*...
gi 446492375 345 PMMYLALSYDHRIIDGQEAVQTLVAIRELLESPEQLLL 382
Cdd:TIGR01349 399 SIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
2-382 |
4.15e-70 |
|
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: 229.38 E-value: 4.15e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 2 IEITVPVLpESVTEGTLTTWCKQEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGSTVTSAQLLAHLK----- 76
Cdd:TIGR01348 117 QEVTVPDI-GDIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSvagst 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 77 ----------------PQAVIEE-------------------TVTPVTETLAMPSARLEAQRSGVELADVAGSGRNGRIL 121
Cdd:TIGR01348 196 patapapasaqpaaqsPAATQPEpaaapaaakaqapapqqagTQNPAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRIL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 122 KEDVQRVTPAPVIQPER--VAEIAPAKPLTPGARQE-------RREPMSRLRQRIAERLLASQQNNAILTTFNEVNMQSV 192
Cdd:TIGR01348 276 REDVQRFVKEPSVRAQAaaASAAGGAPGALPWPNVDfskfgevEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEM 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 193 MDLRARWKDRfAEKHGVKLGFMSFFVKAVTRALERFPVVNASVD--GNEIIWRDYCDIGIAVSSNRGLVVPVLRNAQSLS 270
Cdd:TIGR01348 356 EAFRKQQNAA-VEKEGVKLTVLHILMKAVAAALKKFPKFNASLDlgGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKG 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 271 LVEIERQIAEYATQARNGKLPLEALQGGTFSITNGGTFGSMMSTPIINPPQSAILGMHAITPRPVAENGQVVIRPMMYLA 350
Cdd:TIGR01348 435 ITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLS 514
|
410 420 430
....*....|....*....|....*....|..
gi 446492375 351 LSYDHRIIDGQEAVQTLVAIRELLESPEQLLL 382
Cdd:TIGR01348 515 LSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
92-380 |
1.78e-67 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 215.43 E-value: 1.78e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 92 LAMPSARLEAQRSGVELADVAGSGRNGRILKEDVQR--------VTPAPVIQPERVAEIAPAKPLTPGARQ--ERREPMS 161
Cdd:PRK11857 3 LATPIARALAKKLGIDISLLKGSGRDGKILAEDVENfikslksaPTPAEAASVSSAQQAAKTAAPAAAPPKleGKREKVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 162 RLRQRIAERLLASQQNNAILTTFNEVNMQSVMDLRARWKDRFAEKHGVKLGFMSFFVKAVTRALERFPVVNASVD--GNE 239
Cdd:PRK11857 83 PIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDeaTSE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 240 IIWRDYCDIGIAVSSNRGLVVPVLRNAQSLSLVEIERQIAEYATQARNGKLPLEALQGGTFSITNGGTFGSMMSTPIINP 319
Cdd:PRK11857 163 LVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINY 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446492375 320 PQSAILGMHAITPRPVAENGQVVIRPMMYLALSYDHRIIDGQEAVQTLVAIRELLESPEQL 380
Cdd:PRK11857 243 PELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
11-384 |
4.19e-53 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 181.46 E-value: 4.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 11 ESVTEGTLTTWCKQEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGSTVTSAQLL--------AHLKPQAVIE 82
Cdd:PLN02528 8 EGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLlkimvedsQHLRSDSLLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 83 ETVTP--------------VTETLAMPSARLEAQRSGVELADVAGSGRNGRILKEDVQRVTP----------APVIQPER 138
Cdd:PLN02528 88 PTDSSnivslaesdergsnLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAqkgvvkdsssAEEATIAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 139 VAEIAPAKPLTPGARQERREPMSRLRQRIAERLLASQQNNAILTTFNEVNMQSVMDLRARWKDRfAEKHGVKLGFMSFFV 218
Cdd:PLN02528 168 QEEFSTSVSTPTEQSYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQEN-NTDPTVKHTFLPFLI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 219 KAVTRALERFPVVNASVDG--NEIIWRDYCDIGIAVSSNRGLVVPVLRNAQSLSLVEIERQIAEYATQARNGKLPLEALQ 296
Cdd:PLN02528 247 KSLSMALSKYPLLNSCFNEetSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDIT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 297 GGTFSITN----GGTFGSmmstPIINPPQSAILGMHAI--TPRPVaENGQVVIRPMMYLALSYDHRIIDGQEAVQTLVAI 370
Cdd:PLN02528 327 GGTITLSNigaiGGKFGS----PVLNLPEVAIIALGRIqkVPRFV-DDGNVYPASIMTVTIGADHRVLDGATVARFCNEW 401
|
410
....*....|....
gi 446492375 371 RELLESPEQLLLDL 384
Cdd:PLN02528 402 KSYVEKPELLMLHM 415
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
95-382 |
3.13e-52 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 177.40 E-value: 3.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 95 PSARLEAQRSGVELADVAGSGRNGRILKEDVQRVTPAPV----IQPERVAEIAPAKPLTPGARQE-RREPMSRLRQRIAE 169
Cdd:PRK14843 53 PLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIendsIKSPAQIEKVEEVPDNVTPYGEiERIPMTPMRKVIAQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 170 RLLASQQNNAILTTFNEVNMQSVMDLRARWKDRFAEKHGVKLGFMSFFVKAVTRALERFPVVNASV--DGNEIIWRDYCD 247
Cdd:PRK14843 133 RMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLteDGKTIITHNYVN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 248 IGIAVSSNRGLVVPVLRNAQSLSLVEIERQIAEYATQARNGKLPLEALQGGTFSITNGGTFGSMMSTPIINPPQSAILGM 327
Cdd:PRK14843 213 LAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILGV 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446492375 328 HAITPRPVAENGQVVIRPMMYLALSYDHRIIDGQEAVQTLVAIRELLESPEQLLL 382
Cdd:PRK14843 293 SSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
3-382 |
1.72e-49 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 174.66 E-value: 1.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 3 EITVPVLPESVTEGTLTTWCKQEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGS-----------TVTSAQL 71
Cdd:PLN02744 114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAkeikvgeviaiTVEEEED 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 72 LAHLK---------------------------------PQAVIEETVTPVT---ETLAMPSARLEAQRSGVELADVAGSG 115
Cdd:PLN02744 194 IGKFKdykpsssaapaapkakpsppppkeeevekpassPEPKASKPSAPPSsgdRIFASPLARKLAEDNNVPLSSIKGTG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 116 RNGRILKEDVQRVTPApviqperVAEIAPAKPLTPGARQERRE---PMSRLRQRIAERLLASQQN--NAILTTfnEVNMQ 190
Cdd:PLN02744 274 PDGRIVKADIEDYLAS-------GGKGATAPPSTDSKAPALDYtdiPNTQIRKVTASRLLQSKQTipHYYLTV--DTRVD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 191 SVMDLRARWKDRFAEKHGVKLGFMSFFVKAVTRALERFPVVNASVDGNEIiwRDY--CDIGIAVSSNRGLVVPVLRNAQS 268
Cdd:PLN02744 345 KLMALRSQLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYI--RQYhnVNINVAVQTENGLYVPVVKDADK 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 269 LSLVEIERQIAEYATQARNGKLPLEALQGGTFSITN-GGTFGSMMSTPIINPPQSAILGMHAITPR--PVAENGQVVIRP 345
Cdd:PLN02744 423 KGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNlGGPFGIKQFCAIINPPQSAILAVGSAEKRviPGSGPDQYNFAS 502
|
410 420 430
....*....|....*....|....*....|....*..
gi 446492375 346 MMYLALSYDHRIIDGQEAVQTLVAIRELLESPEQLLL 382
Cdd:PLN02744 503 FMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-73 |
2.31e-28 |
|
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: 105.92 E-value: 2.31e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446492375 1 MIEITVPVLPESVTEGTLTTWCKQEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGSTVTSAQLLA 73
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIA 74
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
2-73 |
4.43e-27 |
|
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: 102.48 E-value: 4.43e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446492375 2 IEITVPVLPESVTEGTLTTWCKQEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGSTVTSAQLLA 73
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIA 72
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
129-374 |
8.55e-21 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 94.57 E-value: 8.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 129 TPAPVIQPERVAEIAPAKPLTPGARQERREpMSRLR---QRIAERLLASqqnnaiL-----TTFNEVNMQSVMDLRARWK 200
Cdd:PRK12270 87 AAAAAAAAAPAAPPAAAAAAAPAAAAVEDE-VTPLRgaaAAVAKNMDAS------LevptaTSVRAVPAKLLIDNRIVIN 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 201 DRFAEKHGVKLGFMSFFVKAVTRALERFPVVNAS---VDGN-EIIWRDYCDIGIAV-----SSNRGLVVPVLRNAQSLSL 271
Cdd:PRK12270 160 NHLKRTRGGKVSFTHLIGYALVQALKAFPNMNRHyaeVDGKpTLVTPAHVNLGLAIdlpkkDGSRQLVVPAIKGAETMDF 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 272 VEIERQIAEYATQARNGKLPLEALQGGTFSITNGGTFGSMMSTPIINPPQSAILGMHAI---------TPRPVAENGqvv 342
Cdd:PRK12270 240 AQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMeypaefqgaSEERLAELG--- 316
|
250 260 270
....*....|....*....|....*....|..
gi 446492375 343 IRPMMYLALSYDHRIIDGQEAVQTLVAIRELL 374
Cdd:PRK12270 317 ISKVMTLTSTYDHRIIQGAESGEFLRTIHQLL 348
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
3-125 |
7.19e-20 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 90.00 E-value: 7.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 3 EITVPVLPESVTEGTLTTWCKQEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGSTVTSAQLLAHLKPQAVIE 82
Cdd:PRK14875 4 PITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVSD 83
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446492375 83 ETVTPVTETLAMPSArleaqRSGVELADVAGSGRNGRILKEDV 125
Cdd:PRK14875 84 AEIDAFIAPFARRFA-----PEGIDEEDAGPAPRKARIGGRTV 121
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
3-73 |
4.56e-15 |
|
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: 69.55 E-value: 4.56e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446492375 3 EITVPVLPESVTEGTlTTWCKQEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGSTVTSAQLLA 73
Cdd:pfam00364 2 EIKSPMIGESVREGV-VEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLA 71
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-169 |
9.76e-15 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 75.34 E-value: 9.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 1 MIEITVPVLPESVTEGTLTTWCKQEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGStvtsaQLLAHLKPQAV 80
Cdd:PRK11892 2 AIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGT-----EGVKVNTPIAV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 81 IEETVTPVTETLAMPSARLEAQRSGVELADVAgsgrngrilKEDVQRVTPAPVIQPERVAEIAPAKPL-TPGARQERREP 159
Cdd:PRK11892 77 LLEEGESASDAGAAPAAAAEAAAAAPAAAAAA---------AAKKAAPAPAAPAAPAAEVAADPDIPAgTEMVTMTVREA 147
|
170
....*....|
gi 446492375 160 msrLRQRIAE 169
Cdd:PRK11892 148 ---LRDAMAE 154
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
3-72 |
1.30e-13 |
|
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: 65.54 E-value: 1.30e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 3 EITVPVLPESVTEGTLTTWCKQEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGSTVTSAQLL 72
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPL 70
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-73 |
8.70e-11 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 63.48 E-value: 8.70e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446492375 2 IEITVPVLpeSVTEGTLTTWCKQEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGSTVTSAQLLA 73
Cdd:PRK11854 3 IEIKVPDI--GADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIM 72
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
16-75 |
6.95e-10 |
|
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: 54.73 E-value: 6.95e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 16 GTLTTWCKQEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGSTVTSAQLLAHL 75
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
92-126 |
8.75e-10 |
|
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: 8.75e-10
10 20 30
....*....|....*....|....*....|....*
gi 446492375 92 LAMPSARLEAQRSGVELADVAGSGRNGRILKEDVQ 126
Cdd:pfam02817 2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
3-77 |
2.52e-06 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 49.46 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446492375 3 EITVPVLPESVTEGTLTTWCK--------QEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGSTVTSAQLLAH 74
Cdd:PRK09282 510 EIVVGGRPRASAPGAVTSPMPgtvvkvkvKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLME 589
|
...
gi 446492375 75 LKP 77
Cdd:PRK09282 590 IEP 592
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
24-76 |
9.96e-06 |
|
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: 44.89 E-value: 9.96e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446492375 24 QEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGSTVTSAQLLAHLK 76
Cdd:COG0511 84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
24-75 |
3.09e-05 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 43.70 E-value: 3.09e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 446492375 24 QEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGSTVTSAQLLAHL 75
Cdd:PRK05641 101 REGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
24-72 |
9.95e-05 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 44.15 E-value: 9.95e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 446492375 24 QEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGSTVTSAQLL 72
Cdd:PRK14040 541 TEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTL 589
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
16-72 |
4.78e-03 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 39.29 E-value: 4.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446492375 16 GTLTTWCKQEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGSTVTSAQLL 72
Cdd:COG1038 1085 GTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLL 1141
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
23-75 |
5.44e-03 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 35.37 E-value: 5.44e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446492375 23 KQEGEHVKRDDVIAELETDKVILEIPAPHDGVLSNIIVSEGSTVTSAQLLAHL 75
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARI 78
|
|
| |
