|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
2-428 |
0e+00 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 522.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 2 GTHVIKMPDIGEGIAEVELVEWHVQVGDSVNEDQVLAEVMTDKATVEIPSPVAGRILALGGQPGQVMAVGGELIRLEVEG 81
Cdd:PRK11856 1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 82 AGNLAESPAAATPAAPVAATPEKPKEAPVAApkaaaeapralrdSEAPRQRRQPGERPLASPAVRQRARDLGIELQFVQG 161
Cdd:PRK11856 81 EAEAAAAAEAAPEAPAPEPAPAAAAAAAAAP-------------AAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 162 SGPAGRVLHEDLDAYLTQDG---SVARSGGAAQGYAERHDEQAVPVIGLRRKIAQKMQDAKRRIPHFSYVEEIDVTDLEA 238
Cdd:PRK11856 148 SGPGGRITKEDVEAAAAAAApaaAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 239 LRAHLNQkwggQRGKLTLLPFLVRAMVVALRDFPQLNARYDDEAevVTRYGAVHVGIATQSDNGLMVPVLRHAESRDLWG 318
Cdd:PRK11856 228 LRKQLKA----IGVKLTVTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 319 NASEVARLAEAARSGKAQRQELSGSTITLSSLGVLGGIVSTPVINHPEVAIVGVNRIVERPMVVGGNIVVRKMMNLSSSF 398
Cdd:PRK11856 302 LAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSF 381
|
410 420 430
....*....|....*....|....*....|
gi 15597445 399 DHRVVDGMDAAAFIQAVRGLLEHPATLFLE 428
Cdd:PRK11856 382 DHRVIDGADAARFLKALKELLENPALLLLE 411
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
215-426 |
2.65e-99 |
|
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: 295.22 E-value: 2.65e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 215 MQDAKRRIPHFSYVEEIDVTDLEALRAHLNQKWGGQRGKLTLLPFLVRAMVVALRDFPQLNARYDDEAEVVTRYGAVHVG 294
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 295 IATQSDNGLMVPVLRHAESRDLWGNASEVARLAEAARSGKAQRQELSGSTITLSSLGVLGGIVSTPVINHPEVAIVGVNR 374
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15597445 375 IVERPMVVGGNIVVRKMMNLSSSFDHRVVDGMDAAAFIQAVRGLLEHPATLF 426
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
6-428 |
7.65e-85 |
|
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: 265.06 E-value: 7.65e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 6 IKMPDIGEGIAEVELVEWHVQVGDSVNEDQVLAEVMTDKATVEIPSPVAGRILALGGQPGQVMAVGGELIRLEvEGAGNL 85
Cdd:TIGR01347 3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILE-EGNDAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 86 AESPaaatpaapvaatpEKPKEAPVAAPKaaaeapralrdSEAPRQRRQPGERPLASPAVRQRARDLGIELQFVQGSGPA 165
Cdd:TIGR01347 82 AAPP-------------AKSGEEKEETPA-----------ASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 166 GRVLHEDLDAYLTQDGSVARSGGAAQGYAERHD---EQAVPVIGLRRKIAQKMQDAKRRIPHFSYVEEIDVTDLEALRAH 242
Cdd:TIGR01347 138 GRVTKEDIIKKTEAPASAQPPAAAAAAAAPAAAtrpEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 243 LNQKWGGQRG-KLTLLPFLVRAMVVALRDFPQLNARYDDEaEVVTRyGAVHVGIATQSDNGLMVPVLRHAESRDLWGNAS 321
Cdd:TIGR01347 218 YKEEFEKKHGvKLGFMSFFVKAVVAALKRFPEVNAEIDGD-DIVYK-DYYDISVAVSTDRGLVVPVVRNADRMSFADIEK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 322 EVARLAEAARSGKAQRQELSGSTITLSSLGVLGGIVSTPVINHPEVAIVGVNRIVERPMVVGGNIVVRKMMNLSSSFDHR 401
Cdd:TIGR01347 296 EIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHR 375
|
410 420
....*....|....*....|....*..
gi 15597445 402 VVDGMDAAAFIQAVRGLLEHPATLFLE 428
Cdd:TIGR01347 376 LIDGKEAVTFLVTIKELLEDPRRLLLD 402
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
3-77 |
1.17e-29 |
|
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: 110.16 E-value: 1.17e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597445 3 THVIKMPDIGEGIAEVELVEWHVQVGDSVNEDQVLAEVMTDKATVEIPSPVAGRILALGGQPGQVMAVGGELIRL 77
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
6-77 |
5.37e-28 |
|
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: 105.56 E-value: 5.37e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597445 6 IKMPDIGEGIAEVELVEWHVQVGDSVNEDQVLAEVMTDKATVEIPSPVAGRILALGGQPGQVMAVGGELIRL 77
Cdd:cd06849 3 IKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
2-428 |
0e+00 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 522.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 2 GTHVIKMPDIGEGIAEVELVEWHVQVGDSVNEDQVLAEVMTDKATVEIPSPVAGRILALGGQPGQVMAVGGELIRLEVEG 81
Cdd:PRK11856 1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 82 AGNLAESPAAATPAAPVAATPEKPKEAPVAApkaaaeapralrdSEAPRQRRQPGERPLASPAVRQRARDLGIELQFVQG 161
Cdd:PRK11856 81 EAEAAAAAEAAPEAPAPEPAPAAAAAAAAAP-------------AAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 162 SGPAGRVLHEDLDAYLTQDG---SVARSGGAAQGYAERHDEQAVPVIGLRRKIAQKMQDAKRRIPHFSYVEEIDVTDLEA 238
Cdd:PRK11856 148 SGPGGRITKEDVEAAAAAAApaaAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 239 LRAHLNQkwggQRGKLTLLPFLVRAMVVALRDFPQLNARYDDEAevVTRYGAVHVGIATQSDNGLMVPVLRHAESRDLWG 318
Cdd:PRK11856 228 LRKQLKA----IGVKLTVTDFLIKAVALALKKFPELNASWDDDA--IVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 319 NASEVARLAEAARSGKAQRQELSGSTITLSSLGVLGGIVSTPVINHPEVAIVGVNRIVERPMVVGGNIVVRKMMNLSSSF 398
Cdd:PRK11856 302 LAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSF 381
|
410 420 430
....*....|....*....|....*....|
gi 15597445 399 DHRVVDGMDAAAFIQAVRGLLEHPATLFLE 428
Cdd:PRK11856 382 DHRVIDGADAARFLKALKELLENPALLLLE 411
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-427 |
3.37e-136 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 401.51 E-value: 3.37e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 2 GTHVIKMPDIGEgIAEVELVEWHVQVGDSVNEDQVLAEVMTDKATVEIPSPVAGRILALGGQPGQVMAVGGELIRLEVEG 81
Cdd:PRK11855 118 GVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 82 AGNLAESPAAatpaapvaatpEKPKEAPVAAPKAAAEAPRALRDSEAPRQRRQPGERPLASPAVRQRARDLGIELQFVQG 161
Cdd:PRK11855 197 AAPAAAAAPA-----------AAAPAAAAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHASPAVRRLARELGVDLSQVKG 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 162 SGPAGRVLHEDLDAYLTQDGSVARSGGAAQG----------------YAERHDEQAVPVIGLRRKIAQKMQDAKRRIPHF 225
Cdd:PRK11855 266 TGKKGRITKEDVQAFVKGAMSAAAAAAAAAAaagggglgllpwpkvdFSKFGEIETKPLSRIKKISAANLHRSWVTIPHV 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 226 SYVEEIDVTDLEALRAHLNQKWGGQRGKLTLLPFLVRAMVVALRDFPQLNARYDDEAEVVTRYGAVHVGIATQSDNGLMV 305
Cdd:PRK11855 346 TQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGLVV 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 306 PVLRHAESRDLWGNASEVARLAEAARSGKAQRQELSGSTITLSSLGVLGGIVSTPVINHPEVAIVGVNRIVERPMVVGGN 385
Cdd:PRK11855 426 PVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKE 505
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 15597445 386 IVVRKMMNLSSSFDHRVVDGMDAAAFIQAVRGLLEHPATLFL 427
Cdd:PRK11855 506 FVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
215-426 |
2.65e-99 |
|
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: 295.22 E-value: 2.65e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 215 MQDAKRRIPHFSYVEEIDVTDLEALRAHLNQKWGGQRGKLTLLPFLVRAMVVALRDFPQLNARYDDEAEVVTRYGAVHVG 294
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 295 IATQSDNGLMVPVLRHAESRDLWGNASEVARLAEAARSGKAQRQELSGSTITLSSLGVLGGIVSTPVINHPEVAIVGVNR 374
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15597445 375 IVERPMVVGGNIVVRKMMNLSSSFDHRVVDGMDAAAFIQAVRGLLEHPATLF 426
Cdd:pfam00198 161 IRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
10-427 |
6.81e-88 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 273.13 E-value: 6.81e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 10 DIGEGIAEVELVEWHVQVGDSVNEDQVLAEVMTDKATVEIPSPVAGRILALGGQPGQVMAVGGELIRLEVEGAGNLAESP 89
Cdd:PLN02528 5 QTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHLRSDS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 90 AAATPAAPVAATPEKPKEApvaapkaaaeapralrdseaprqrrqpGERP---LASPAVRQRARDLGIELQFVQGSGPAG 166
Cdd:PLN02528 85 LLLPTDSSNIVSLAESDER---------------------------GSNLsgvLSTPAVRHLAKQYGIDLNDILGTGKDG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 167 RVLHEDLDAYLTQDGSVARSGGAAQGYAER---------------HDEQAVPVIGLRRKIAQKMQDAKRrIPHFSYVEEI 231
Cdd:PLN02528 138 RVLKEDVLKYAAQKGVVKDSSSAEEATIAEqeefstsvstpteqsYEDKTIPLRGFQRAMVKTMTAAAK-VPHFHYVEEI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 232 DVTDLEALRAHLNQKWGGQRGKLTLLPFLVRAMVVALRDFPQLNARYDDEAEVVTRYGAVHVGIATQSDNGLMVPVLRHA 311
Cdd:PLN02528 217 NVDALVELKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 312 ESRDLWGNASEVARLAEAARSGKAQRQELSGSTITLSSLGVLGGIVSTPVINHPEVAIVGVNRIVERPMVVG-GNIVVRK 390
Cdd:PLN02528 297 QSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDdGNVYPAS 376
|
410 420 430
....*....|....*....|....*....|....*..
gi 15597445 391 MMNLSSSFDHRVVDGMDAAAFIQAVRGLLEHPATLFL 427
Cdd:PLN02528 377 IMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLML 413
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
6-420 |
3.91e-86 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 275.34 E-value: 3.91e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 6 IKMPDIGEGiaEVELVEWHVQVGDSVNEDQVLAEVMTDKATVEIPSPVAGRILALGGQPGQVMAVGGELIRLEVEGAGNL 85
Cdd:PRK11854 209 VNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGAAPA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 86 AESPAAATPAAPVAATPEKPKEAPVAAPkaaaeapralrdSEAPRQRRQPGERPLASPAVRQRARDLGIELQFVQGSGPA 165
Cdd:PRK11854 287 AAPAKQEAAAPAPAAAKAEAPAAAPAAK------------AEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 166 GRVLHEDLDAYL------TQDGSVAR-SGGAAQG--------YAERHDEQAVPVIGLRRKIAQKMQDAKRRIPHFSYVEE 230
Cdd:PRK11854 355 GRILKEDVQAYVkdavkrAEAAPAAAaAGGGGPGllpwpkvdFSKFGEIEEVELGRIQKISGANLHRNWVMIPHVTQFDK 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 231 IDVTDLEALRAHLN-----QKWGGqrgKLTLLPFLVRAMVVALRDFPQLNARYDDEAEVVTRYGAVHVGIATQSDNGLMV 305
Cdd:PRK11854 435 ADITELEAFRKQQNaeaekRKLGV---KITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVV 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 306 PVLRHAESRDLWGNASEVARLAEAARSGKAQRQELSGSTITLSSLGVLGGIVSTPVINHPEVAIVGVNRIVERPMVVGGN 385
Cdd:PRK11854 512 PVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGKE 591
|
410 420 430
....*....|....*....|....*....|....*
gi 15597445 386 IVVRKMMNLSSSFDHRVVDGMDAAAFIQAVRGLLE 420
Cdd:PRK11854 592 FAPRLMLPLSLSYDHRVIDGADGARFITIINDRLS 626
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
6-428 |
7.65e-85 |
|
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: 265.06 E-value: 7.65e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 6 IKMPDIGEGIAEVELVEWHVQVGDSVNEDQVLAEVMTDKATVEIPSPVAGRILALGGQPGQVMAVGGELIRLEvEGAGNL 85
Cdd:TIGR01347 3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILE-EGNDAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 86 AESPaaatpaapvaatpEKPKEAPVAAPKaaaeapralrdSEAPRQRRQPGERPLASPAVRQRARDLGIELQFVQGSGPA 165
Cdd:TIGR01347 82 AAPP-------------AKSGEEKEETPA-----------ASAAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 166 GRVLHEDLDAYLTQDGSVARSGGAAQGYAERHD---EQAVPVIGLRRKIAQKMQDAKRRIPHFSYVEEIDVTDLEALRAH 242
Cdd:TIGR01347 138 GRVTKEDIIKKTEAPASAQPPAAAAAAAAPAAAtrpEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 243 LNQKWGGQRG-KLTLLPFLVRAMVVALRDFPQLNARYDDEaEVVTRyGAVHVGIATQSDNGLMVPVLRHAESRDLWGNAS 321
Cdd:TIGR01347 218 YKEEFEKKHGvKLGFMSFFVKAVVAALKRFPEVNAEIDGD-DIVYK-DYYDISVAVSTDRGLVVPVVRNADRMSFADIEK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 322 EVARLAEAARSGKAQRQELSGSTITLSSLGVLGGIVSTPVINHPEVAIVGVNRIVERPMVVGGNIVVRKMMNLSSSFDHR 401
Cdd:TIGR01347 296 EIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHR 375
|
410 420
....*....|....*....|....*..
gi 15597445 402 VVDGMDAAAFIQAVRGLLEHPATLFLE 428
Cdd:TIGR01347 376 LIDGKEAVTFLVTIKELLEDPRRLLLD 402
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
6-427 |
1.93e-83 |
|
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: 265.97 E-value: 1.93e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 6 IKMPDIGeGIAEVELVEWHVQVGDSVNEDQVLAEVMTDKATVEIPSPVAGRILALGGQPGQVMAVGGELIRLEVEGAGNL 85
Cdd:TIGR01348 119 VTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTPA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 86 AESPAAATPAAPVAATPEKPKEAPVAAPKAAaeapralrDSEAPRQR--RQPGERPLASPAVRQRARDLGIELQFVQGSG 163
Cdd:TIGR01348 198 TAPAPASAQPAAQSPAATQPEPAAAPAAAKA--------QAPAPQQAgtQNPAKVDHAAPAVRRLAREFGVDLSAVKGTG 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 164 PAGRVLHEDLDAYLTQDGSVARSGGAAQG-------------YAERHDEQAVPVIGLRRKIAQKMQDAKRRIPHFSYVEE 230
Cdd:TIGR01348 270 IKGRILREDVQRFVKEPSVRAQAAAASAAggapgalpwpnvdFSKFGEVEEVDMSRIRKISGANLTRNWTMIPHVTHFDK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 231 IDVTDLEALRAHLNQKWGGQRGKLTLLPFLVRAMVVALRDFPQLNARYDDEAEVVTRYGAVHVGIATQSDNGLMVPVLRH 310
Cdd:TIGR01348 350 ADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKD 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 311 AESRDLWGNASEVARLAEAARSGKAQRQELSGSTITLSSLGVLGGIVSTPVINHPEVAIVGVNRIVERPMVVGGNIVVRK 390
Cdd:TIGR01348 430 VDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGKEFEPRL 509
|
410 420 430
....*....|....*....|....*....|....*..
gi 15597445 391 MMNLSSSFDHRVVDGMDAAAFIQAVRGLLEHPATLFL 427
Cdd:TIGR01348 510 MLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
6-428 |
1.30e-81 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 256.68 E-value: 1.30e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 6 IKMPDIGEGIAEVELVEWHVQVGDSVNEDQVLAEVMTDKATVEIPSPVAGRILALGGQPGQVMAVGGELIRLEVEGAGNL 85
Cdd:PRK05704 5 IKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAAGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 86 AESPAaatpaapvaatpEKPKEAPVAapkaaaeapralrdSEAPRQRRQPGERPLA-SPAVRQRARDLGIELQFVQGSGP 164
Cdd:PRK05704 85 AAAAA------------AAAAAAAAA--------------PAQAQAAAAAEQSNDAlSPAARKLAAENGLDASAVKGTGK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 165 AGRVLHEDLDAYLTQDGS------VARSGGAAQGYAERHdEQAVPVIGLRRKIAQKMQDAKRRIPHFSYVEEIDVTDLEA 238
Cdd:PRK05704 139 GGRVTKEDVLAALAAAAAapaapaAAAPAAAPAPLGARP-EERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 239 LRAHLNQKWGGQRG-KLTLLPFLVRAMVVALRDFPQLNARYDDEaEVVTRyGAVHVGIATQSDNGLMVPVLRHAESRDLW 317
Cdd:PRK05704 218 LRKQYKDAFEKKHGvKLGFMSFFVKAVVEALKRYPEVNASIDGD-DIVYH-NYYDIGIAVGTPRGLVVPVLRDADQLSFA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 318 GNASEVARLAEAARSGKAQRQELSGSTITLSSLGVLGGIVSTPVINHPEVAIVGVNRIVERPMVVGGNIVVRKMMNLSSS 397
Cdd:PRK05704 296 EIEKKIAELAKKARDGKLSIEELTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALS 375
|
410 420 430
....*....|....*....|....*....|.
gi 15597445 398 FDHRVVDGMDAAAFIQAVRGLLEHPATLFLE 428
Cdd:PRK05704 376 YDHRIIDGKEAVGFLVTIKELLEDPERLLLD 406
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
5-428 |
4.83e-73 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 234.96 E-value: 4.83e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 5 VIKMPDIGEGIAEVELVEWHVQVGDSVNEDQVLAEVMTDKATVEIPSPVAGRILALGGQPGQVMAVGGELIRLEVEGAGN 84
Cdd:PTZ00144 46 VIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 85 lAESPAAATPAAPVAATPEKPKEAPVAAPKAAAeapralrDSEAPRQRRQPGERPLASPAVrqrardlgieLQFVQGSGP 164
Cdd:PTZ00144 126 -AAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAA-------SKPTPPAAAKPPEPAPAAKPP----------PTPVARADP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 165 AgrvlhedldayltqdgsvarsggaaqgyaerhdEQAVPVIGLRRKIAQKMQDAKRRIPHFSYVEEIDVTDLEALRAHLN 244
Cdd:PTZ00144 188 R---------------------------------ETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 245 QKWGGQRG-KLTLLPFLVRAMVVALRDFPQLNArYDDEAEVVTR-YgaVHVGIATQSDNGLMVPVLRHAESRDLWGNASE 322
Cdd:PTZ00144 235 DDFQKKHGvKLGFMSAFVKASTIALKKMPIVNA-YIDGDEIVYRnY--VDISVAVATPTGLVVPVIRNCENKSFAEIEKE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 323 VARLAEAARSGKAQRQELSGSTITLSSLGVLGGIVSTPVINHPEVAIVGVNRIVERPMVVGGNIVVRKMMNLSSSFDHRV 402
Cdd:PTZ00144 312 LADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRL 391
|
410 420
....*....|....*....|....*.
gi 15597445 403 VDGMDAAAFIQAVRGLLEHPATLFLE 428
Cdd:PTZ00144 392 IDGRDAVTFLKKIKDLIEDPARMLLD 417
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
6-420 |
2.40e-71 |
|
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: 235.29 E-value: 2.40e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 6 IKMPDIGEGIAEVELVEWHVQVGDSVNEDQVLAEVMTDKATVEIPSPVAGRILALGGQPGQVMAVGGELIRLevegaGNL 85
Cdd:TIGR02927 129 VKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAII-----GDA 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 86 AESPAAATPAAPVAATPEKPKEAPVAAPKAAAEAPRALRDSEAPRQRRQPGERPLAS---------PAVRQRARDLGIEL 156
Cdd:TIGR02927 204 NAAPAEPAEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPAPAKTAAPAAAAPVSsgdsgpyvtPLVRKLAKDKGVDL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 157 QFVQGSGPAGRVLHEDLDAYLTQDGSVARSGGAAQGYAERHDEQAVP----------------VIGLRRKIAQKMQDAKR 220
Cdd:TIGR02927 284 STVKGTGVGGRIRKQDVLAAAKAAEEARAAAAAPAAAAAPAAPAAAAkpaepdtaklrgttqkMNRIRQITADKTIESLQ 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 221 RIPHFSYVEEIDVTDLEALRAHLNQKWGGQRG-KLTLLPFLVRAMVVALRDFPQLNARYDDEAEVVTRYGAVHVGIATQS 299
Cdd:TIGR02927 364 TSAQLTQVHEVDMTRVAALRARAKNDFLEKNGvNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGIAVDT 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 300 DNGLMVPVLRHAESRDLWGNASEVARLAEAARSGKAQRQELSGSTITLSSLGVLGGIVSTPVINHPEVAIVGVNRIVERP 379
Cdd:TIGR02927 444 PRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRP 523
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 15597445 380 MVV-----GGNIVVRKMMNLSSSFDHRVVDGMDAAAFIQAVRGLLE 420
Cdd:TIGR02927 524 RVIkdedgGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLE 569
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
140-425 |
1.75e-60 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 198.86 E-value: 1.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 140 LASPAVRQRARDLGIELQFVQGSGPAGRVLHEDLDAYLTQDGSVARSGGAAQ--------------GYAERHDEQAVPVI 205
Cdd:PRK11857 3 LATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAASvssaqqaaktaapaAAPPKLEGKREKVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 206 GLRRKIAQKMQDAKRRIPHFSYVEEIDVTDLEALRAHLNQKWGGQRG-KLTLLPFLVRAMVVALRDFPQLNARYDDEAEV 284
Cdd:PRK11857 83 PIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGvKLTFLPFIAKAILIALKEFPIFAAKYDEATSE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 285 VTRYGAVHVGIATQSDNGLMVPVLRHAESRDLWGNASEVARLAEAARSGKAQRQELSGSTITLSSLGVLGGIVSTPVINH 364
Cdd:PRK11857 163 LVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINY 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597445 365 PEVAIVGVNRIVERPMVVGGNIVVRKMMNLSSSFDHRVVDGMDAAAFIQAVRGLLEHPATL 425
Cdd:PRK11857 243 PELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
6-427 |
6.07e-56 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 193.15 E-value: 6.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 6 IKMPDIGEGIAEVELVEWHVQVGDSVNEDQVLAEVMTDKATVEIPSP----VAGRILALGGQPGQVmavgGELIRLEVEG 81
Cdd:PLN02744 115 IGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMeegyLAKIVKGDGAKEIKV----GEVIAITVEE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 82 AGNLAE------SPAAATPAAPVAATPEKPKEAPVAAPKAAAEAPRAlRDSEAPrqrrQPGERPLASPAVRQRARDLGIE 155
Cdd:PLN02744 191 EEDIGKfkdykpSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKAS-KPSAPP----SSGDRIFASPLARKLAEDNNVP 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 156 LQFVQGSGPAGRVLHEDLDAYLTQDGSVARSGGAAQGYAERHDEQAVPVIGLRRKIAQKMQDAKRRIPHFSYVEEIDVTD 235
Cdd:PLN02744 266 LSSIKGTGPDGRIVKADIEDYLASGGKGATAPPSTDSKAPALDYTDIPNTQIRKVTASRLLQSKQTIPHYYLTVDTRVDK 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 236 LEALRAHLNQKWGGQRGK-LTLLPFLVRAMVVALRDFPQLNARYDDeaEVVTRYGAVHVGIATQSDNGLMVPVLRHAESR 314
Cdd:PLN02744 346 LMALRSQLNSLQEASGGKkISVNDLVIKAAALALRKVPQCNSSWTD--DYIRQYHNVNINVAVQTENGLYVPVVKDADKK 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 315 DLWGNASEVARLAEAARSGKAQRQELSGSTITLSSLGVLGGIVS-TPVINHPEVAIVGVNRIVER--PMVVGGNIVVRKM 391
Cdd:PLN02744 424 GLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGPFGIKQfCAIINPPQSAILAVGSAEKRviPGSGPDQYNFASF 503
|
410 420 430
....*....|....*....|....*....|....*.
gi 15597445 392 MNLSSSFDHRVVDGMDAAAFIQAVRGLLEHPATLFL 427
Cdd:PLN02744 504 MSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
142-427 |
4.04e-48 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 167.77 E-value: 4.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 142 SPAVRQRARDLGIELQFVQGSGPAGRVLHEDLDAYLTQDGSVARSGGAAQ-GYAERHDEQA--------VPVIGLRRKIA 212
Cdd:PRK14843 52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQiEKVEEVPDNVtpygeierIPMTPMRKVIA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 213 QKMQDAKRRIPHFSYVEEIDVTDLEALRAHLNQKWGGQRGK-LTLLPFLVRAMVVALRDFPQLNARYDDEAEVVTRYGAV 291
Cdd:PRK14843 132 QRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKkTTVTDLLSLAVVKTLMKHPYINASLTEDGKTIITHNYV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 292 HVGIATQSDNGLMVPVLRHAESRDLWGNASEVARLAEAARSGKAQRQELSGSTITLSSLGVLGGIVSTPVINHPEVAIVG 371
Cdd:PRK14843 212 NLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIINQPNSAILG 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 15597445 372 VNRIVERPMVVGGNIVVRKMMNLSSSFDHRVVDGMDAAAFIQAVRGLLEHPATLFL 427
Cdd:PRK14843 292 VSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
8-428 |
1.33e-46 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 166.85 E-value: 1.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 8 MPDIGEGIAEVELVEWHVQVGDSVNEDQVLAEVMTDKATVEIPSPVAGRILALGGQPGQVMAVGGELIRLevegagnlAE 87
Cdd:PLN02226 96 VPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAII--------SK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 88 SPAAATPAAPVAATPEKPKEAPVAAPkaaaeapralRDSEAPRQRRQP-GERPLAS---PAVRQRARDLGIElqfvqgsg 163
Cdd:PLN02226 168 SEDAASQVTPSQKIPETTDPKPSPPA----------EDKQKPKVESAPvAEKPKAPsspPPPKQSAKEPQLP-------- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 164 PAGRvlhedldayltqdgsvarsggaaqgyaerhdEQAVPVIGLRRKIAQKMQDAKRRIPHFSYVEEIDVTDLEALRAHL 243
Cdd:PLN02226 230 PKER-------------------------------ERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQY 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 244 NQKWGGQRG-KLTLLPFLVRAMVVALRDFPQLNARYDDEAEVVTRYgaVHVGIATQSDNGLMVPVLRHAESRDLWGNASE 322
Cdd:PLN02226 279 KDAFYEKHGvKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDY--VDISIAVGTSKGLVVPVIRGADKMNFAEIEKT 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 323 VARLAEAARSGKAQRQELSGSTITLSSLGVLGGIVSTPVINHPEVAIVGVNRIVERPMVVGGNIVVRKMMNLSSSFDHRV 402
Cdd:PLN02226 357 INGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRL 436
|
410 420
....*....|....*....|....*.
gi 15597445 403 VDGMDAAAFIQAVRGLLEHPATLFLE 428
Cdd:PLN02226 437 IDGREAVYFLRRVKDVVEDPQRLLLD 462
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
3-77 |
1.17e-29 |
|
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: 110.16 E-value: 1.17e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597445 3 THVIKMPDIGEGIAEVELVEWHVQVGDSVNEDQVLAEVMTDKATVEIPSPVAGRILALGGQPGQVMAVGGELIRL 77
Cdd:COG0508 2 AIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
6-77 |
5.37e-28 |
|
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: 105.56 E-value: 5.37e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597445 6 IKMPDIGEGIAEVELVEWHVQVGDSVNEDQVLAEVMTDKATVEIPSPVAGRILALGGQPGQVMAVGGELIRL 77
Cdd:cd06849 3 IKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
4-77 |
6.38e-18 |
|
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: 77.64 E-value: 6.38e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597445 4 HVIKMPDIGEGIAEVElVEWHVQVGDSVNEDQVLAEVMTDKATVEIPSPVAGRILALGGQPGQVMAVGGELIRL 77
Cdd:pfam00364 1 TEIKSPMIGESVREGV-VEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
184-419 |
8.30e-14 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 73.77 E-value: 8.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 184 ARSGGAAQGYAERHDEQAVPVIGLRRKIAQKMqDAKRRIPHFSYVEEIDVTDLEALRAHLNQKWGGQRG-KLTLLPFLVR 262
Cdd:PRK12270 100 PAAAAAAAPAAAAVEDEVTPLRGAAAAVAKNM-DASLEVPTATSVRAVPAKLLIDNRIVINNHLKRTRGgKVSFTHLIGY 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 263 AMVVALRDFPQLNARYD--DEAEVVTRYGAVHVGIA--TQSDNG---LMVPVLRHAES---RDLWGNASEVARlaeAARS 332
Cdd:PRK12270 179 ALVQALKAFPNMNRHYAevDGKPTLVTPAHVNLGLAidLPKKDGsrqLVVPAIKGAETmdfAQFWAAYEDIVR---RARD 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 333 GKAQRQELSGSTITLSSLGVLGGIVSTPVINHPEVAIVGVNRIvERPMVVGG-------NIVVRKMMNLSSSFDHRVVDG 405
Cdd:PRK12270 256 GKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAM-EYPAEFQGaseerlaELGISKVMTLTSTYDHRIIQG 334
|
250
....*....|....
gi 15597445 406 MDAAAFIQAVRGLL 419
Cdd:PRK12270 335 AESGEFLRTIHQLL 348
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
4-82 |
1.65e-10 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 62.27 E-value: 1.65e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597445 4 HVIKMPDIGEGIAEVELVEWHVQVGDSVNEDQVLAEVMTDKATVEIPSPVAGRILALGGQPGQVMAVGGELIRLEVEGA 82
Cdd:PRK14875 3 TPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEV 81
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
139-174 |
3.17e-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: 55.00 E-value: 3.17e-10
10 20 30
....*....|....*....|....*....|....*.
gi 15597445 139 PLASPAVRQRARDLGIELQFVQGSGPAGRVLHEDLD 174
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
6-77 |
1.02e-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: 51.67 E-value: 1.02e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597445 6 IKMPDIGEGIAEVELVEWHVQVGDSVNEDQVLAEVMTDKATVEIPSPVAGRILALGGQPGQVMAVGGELIRL 77
Cdd:cd06663 2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
20-77 |
1.46e-06 |
|
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: 45.48 E-value: 1.46e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 20 LVEWHVQVGDSVNEDQVLA--EVMtdKATVEIPSPVAGRILALGGQPGQVMAVGGELIRL 77
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAvlEAM--KMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| GcvH |
COG0509 |
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; ... |
15-87 |
6.29e-06 |
|
Glycine cleavage system protein H (lipoate-binding) [Amino acid transport and metabolism]; Glycine cleavage system protein H (lipoate-binding) is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440275 Cd Length: 128 Bit Score: 45.11 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597445 15 IAEVELVEwhvqVGDSVNEDQVLAEVMTDKATVEIPSPVAGRIL----ALGGQPGQVMA---VGGELIRLEVEGAGNLAE 87
Cdd:COG0509 39 IVFVELPE----VGTEVEAGEPFGVVESVKAVSDLYAPVSGEVVevneALEDDPELVNEdpyGEGWLFKIKPSDPAELDD 114
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
25-78 |
1.37e-04 |
|
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: 41.80 E-value: 1.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 15597445 25 VQVGDSVNEDQVLA--EVMtdKATVEIPSPVAGRILALGGQPGQVMAVGGELIRLE 78
Cdd:COG0511 83 VKVGDKVKAGDTLCiiEAM--KMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
6-49 |
2.53e-04 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 42.98 E-value: 2.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 15597445 6 IKMPDIGEGIAEVELVEWHVQVGDSVNEDQVLAEVMTDKATVEI 49
Cdd:PRK11892 5 ILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEV 48
|
|
| GCS_H |
cd06848 |
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ... |
17-59 |
1.17e-03 |
|
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue.
Pssm-ID: 133457 [Multi-domain] Cd Length: 96 Bit Score: 37.90 E-value: 1.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 15597445 17 EVELVEWHvQVGDSVNEDQVLAEVMTDKATVEIPSPVAGRILA 59
Cdd:cd06848 30 DIVFVELP-EVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVE 71
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