|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
2-405 |
0e+00 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 745.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 2 SSVDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGN 81
Cdd:PRK05704 1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 82 SAGK--ETSAKSEEKASTPAQRQQASLEEQNNDALSPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKHLAKAPAKESA 159
Cdd:PRK05704 81 AAGAaaAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 160 PAAAAPAAQPALVA-RSEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFY 238
Cdd:PRK05704 161 PAAAAPAAAPAPLGaRPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 239 VKAVVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTG 318
Cdd:PRK05704 241 VKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 319 GNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNGLVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDP 398
Cdd:PRK05704 321 GTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDP 400
|
....*..
gi 446021972 399 TRLLLDV 405
Cdd:PRK05704 401 ERLLLDL 407
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
4-405 |
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: 686.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 4 VDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNSA 83
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 84 GKETSAKS-EEKASTPAQRQQASLEEQNN-DALSPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKHLAKAPAKESAPA 161
Cdd:TIGR01347 81 TAAPPAKSgEEKEETPAASAAAAPTAAANrPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 162 AAAPAAQPALVaRSEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFYVKA 241
Cdd:TIGR01347 161 AAAAAAPAAAT-RPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 242 VVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTGGNF 321
Cdd:TIGR01347 240 VVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 322 TITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNGLVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRL 401
Cdd:TIGR01347 320 TITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRL 399
|
....
gi 446021972 402 LLDV 405
Cdd:TIGR01347 400 LLDL 403
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
192-402 |
8.57e-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: 292.91 E-value: 8.57e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 192 LLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGiRLGFMSFYVKAVVEALKRYPEVNASIDGDD--VVYHNYFDV 269
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 270 SMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMH 349
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446021972 350 AIKDRPMAVNGLVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRLL 402
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
2-77 |
5.37e-26 |
|
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: 99.76 E-value: 5.37e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446021972 2 SSVDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRL 77
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
4-77 |
1.63e-24 |
|
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: 95.55 E-value: 1.63e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446021972 4 VDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRL 77
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
2-405 |
0e+00 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 745.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 2 SSVDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGN 81
Cdd:PRK05704 1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 82 SAGK--ETSAKSEEKASTPAQRQQASLEEQNNDALSPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKHLAKAPAKESA 159
Cdd:PRK05704 81 AAGAaaAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 160 PAAAAPAAQPALVA-RSEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFY 238
Cdd:PRK05704 161 PAAAAPAAAPAPLGaRPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 239 VKAVVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTG 318
Cdd:PRK05704 241 VKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 319 GNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNGLVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDP 398
Cdd:PRK05704 321 GTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDP 400
|
....*..
gi 446021972 399 TRLLLDV 405
Cdd:PRK05704 401 ERLLLDL 407
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
4-405 |
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: 686.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 4 VDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNSA 83
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 84 GKETSAKS-EEKASTPAQRQQASLEEQNN-DALSPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKHLAKAPAKESAPA 161
Cdd:TIGR01347 81 TAAPPAKSgEEKEETPAASAAAAPTAAANrPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 162 AAAPAAQPALVaRSEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFYVKA 241
Cdd:TIGR01347 161 AAAAAAPAAAT-RPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 242 VVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTGGNF 321
Cdd:TIGR01347 240 VVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 322 TITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNGLVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRL 401
Cdd:TIGR01347 320 TITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRL 399
|
....
gi 446021972 402 LLDV 405
Cdd:TIGR01347 400 LLDL 403
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
6-405 |
4.15e-158 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 451.83 E-value: 4.15e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 6 ILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLregnsagK 85
Cdd:PTZ00144 47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEI-------D 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 86 ETSAKSEEKASTPAQRQQASLEEQNNDALSPAirrllaehnldASAIKgtgvggrltrEDVEKHLAKAPAKESAPAAAAP 165
Cdd:PTZ00144 120 TGGAPPAAAPAAAAAAKAEKTTPEKPKAAAPT-----------PEPPA----------ASKPTPPAAAKPPEPAPAAKPP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 166 AAQPALVARSEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFYVKAVVEA 245
Cdd:PTZ00144 179 PTPVARADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGVKLGFMSAFVKASTIA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 246 LKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTGGNFTITN 325
Cdd:PTZ00144 259 LKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 326 GGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNGLVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRLLLDV 405
Cdd:PTZ00144 339 GGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLDL 418
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
4-404 |
1.14e-136 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 396.85 E-value: 1.14e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 4 VDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNSA 83
Cdd:PRK11856 3 FEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 84 GKETSAKSEEKASTPAQRQQASLEEQNNDAL--------------SPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKH 149
Cdd:PRK11856 83 EAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAaaapaapaaaaakaSPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 150 LAKAPAKESAPAAAAPAAQPALVARSEkRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYgeafeKRHG 229
Cdd:PRK11856 163 AAAAAPAAAAAAAAAAAPPAAAAEGEE-RVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQL-----KAIG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 230 IRLGFMSFYVKAVVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDG 309
Cdd:PRK11856 237 VKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 310 KLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNGLVEILPMMYLALSYDHRLIDGRESVGFLV 389
Cdd:PRK11856 317 KLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLK 396
|
410
....*....|....*
gi 446021972 390 TIKELLEDPTRLLLD 404
Cdd:PRK11856 397 ALKELLENPALLLLE 411
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
3-405 |
5.54e-118 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 351.36 E-value: 5.54e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 3 SVDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNS 82
Cdd:PLN02226 91 TVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSED 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 83 AGKETsAKSEEKASTPAQRQQASLEeqnnDALSPAIrrllaEHNLDASAIKGTGVGGRLTREDVEKHLAKAPakesapaa 162
Cdd:PLN02226 171 AASQV-TPSQKIPETTDPKPSPPAE----DKQKPKV-----ESAPVAEKPKAPSSPPPPKQSAKEPQLPPKE-------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 163 aapaaqpalvarSEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFYVKAV 242
Cdd:PLN02226 233 ------------RERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYEKHGVKLGLMSGFIKAA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 243 VEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTGGNFT 322
Cdd:PLN02226 301 VSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFT 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 323 ITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNGLVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRLL 402
Cdd:PLN02226 381 VSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLL 460
|
...
gi 446021972 403 LDV 405
Cdd:PLN02226 461 LDI 463
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-403 |
2.19e-107 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 326.78 E-value: 2.19e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 2 SSVDILVPDLPEsVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGN 81
Cdd:PRK11855 118 GVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 82 SAGKETSAKSEEK---------------ASTPAQRQQASLEEQNNDAL-SPAIRRLLAEHNLDASAIKGTGVGGRLTRED 145
Cdd:PRK11855 197 AAPAAAAAPAAAApaaaaaaapapapaaAAAPAAAAPAAAAAPGKAPHaSPAVRRLARELGVDLSQVKGTGKKGRITKED 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 146 VEKHL--AKAPAKESAPAAAAPAAQPALVARSEK----------RVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPI 213
Cdd:PRK11855 277 VQAFVkgAMSAAAAAAAAAAAAGGGGLGLLPWPKvdfskfgeieTKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 214 MDLRKQYGEAFEKrHGIRLGFMSFYVKAVVEALKRYPEVNASID--GDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLG 291
Cdd:PRK11855 357 EALRKQLKKEAEK-AGVKLTMLPFFIKAVVAALKEFPVFNASLDedGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKS 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 292 MADIEKKIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNGLVEILPMMYLA 371
Cdd:PRK11855 436 LLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLS 515
|
410 420 430
....*....|....*....|....*....|..
gi 446021972 372 LSYDHRLIDGRESVGFLVTIKELLEDPTRLLL 403
Cdd:PRK11855 516 LSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
192-402 |
8.57e-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: 292.91 E-value: 8.57e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 192 LLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGiRLGFMSFYVKAVVEALKRYPEVNASIDGDD--VVYHNYFDV 269
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 270 SMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMH 349
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446021972 350 AIKDRPMAVNGLVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRLL 402
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-403 |
2.61e-93 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 293.06 E-value: 2.61e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 2 SSVDILVPDLpeSVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGN 81
Cdd:PRK11854 205 GVKDVNVPDI--GGDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEG 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 82 SAG------------KETSAKSEEKASTPAQRQQASLEEQNNDAL---SPAIRRLLAEHNLDASAIKGTGVGGRLTREDV 146
Cdd:PRK11854 283 AAPaaapakqeaaapAPAAAKAEAPAAAPAAKAEGKSEFAENDAYvhaTPLVRRLAREFGVNLAKVKGTGRKGRILKEDV 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 147 EKHLAKAPAKESAPAAAAPAAQPALVARSEKRV-----------PMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMD 215
Cdd:PRK11854 363 QAYVKDAVKRAEAAPAAAAAGGGGPGLLPWPKVdfskfgeieevELGRIQKISGANLHRNWVMIPHVTQFDKADITELEA 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 216 LRK-QYGEAFEKRHGIRLGFMSFYVKAVVEALKRYPEVNASI--DGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGM 292
Cdd:PRK11854 443 FRKqQNAEAEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLseDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGI 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 293 ADIEKKIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPmaVNGLVEILP--MMYL 370
Cdd:PRK11854 523 IELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEP--VWNGKEFAPrlMLPL 600
|
410 420 430
....*....|....*....|....*....|...
gi 446021972 371 ALSYDHRLIDGRESVGFLVTIKELLEDPTRLLL 403
Cdd:PRK11854 601 SLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
2-397 |
4.84e-92 |
|
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: 288.45 E-value: 4.84e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 2 SSVDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGN 81
Cdd:TIGR02927 125 EATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDAN 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 82 SAGKETS--------------------------------AKSEEKASTPAQRQQASlEEQNNDALSPAIRRLLAEHNLDA 129
Cdd:TIGR02927 205 AAPAEPAeeeapapseagsepapdpaaraphaapdppapAPAPAKTAAPAAAAPVS-SGDSGPYVTPLVRKLAKDKGVDL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 130 SAIKGTGVGGRLTREDVEKHLAKAPAKESAPAAAAPAAQPALVARSEKRV------------PMTRLRKRVAERLLEAKN 197
Cdd:TIGR02927 284 STVKGTGVGGRIRKQDVLAAAKAAEEARAAAAAPAAAAAPAAPAAAAKPAepdtaklrgttqKMNRIRQITADKTIESLQ 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 198 STAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFYVKAVVEALKRYPEVNASI--DGDDVVYHNYFDVSMAVST 275
Cdd:TIGR02927 364 TSAQLTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYnaETKEVTYHDVEHVGIAVDT 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 276 PRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRP 355
Cdd:TIGR02927 444 PRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRP 523
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 446021972 356 MAV-----NGLVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLED 397
Cdd:TIGR02927 524 RVIkdedgGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEE 570
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
6-403 |
9.75e-85 |
|
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: 265.12 E-value: 9.75e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 6 ILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTT-----------------V 68
Cdd:TIGR01349 2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKdvpvnkpiavlveekedV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 69 TSRQILGRLREGNSAGKETSAK--------------SEEKASTPAQRQQASLEEQNND-ALSPAIRRLLAEHNLDASAIK 133
Cdd:TIGR01349 82 ADAFKNYKLESSASPAPKPSEIaptappsapkpspaPQKQSPEPSSPAPLSDKESGDRiFASPLAKKLAKEKGIDLSAVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 134 GTGVGGRLTREDVEKHLAKAPAKESAPAAAAPAAQPALVARSE----KRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVN 209
Cdd:TIGR01349 162 GSGPNGRIVKKDIESFVPQSPASANQQAAATTPATYPAAAPVStgsyEDVPLSNIRKIIAKRLLESKQTIPHYYVSIECN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 210 MKPIMDLRKQYGEAFEKRhgIRLGFMSFYVKAVVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDT 289
Cdd:TIGR01349 242 VDKLLALRKELNAMASEV--YKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 290 LGMADIEKKIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNG---LVEILP 366
Cdd:TIGR01349 320 KGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDeekGFAVAS 399
|
410 420 430
....*....|....*....|....*....|....*..
gi 446021972 367 MMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRLLL 403
Cdd:TIGR01349 400 IMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
5-403 |
1.86e-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: 231.30 E-value: 1.86e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 5 DILVPDLpESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLR--EGNS 82
Cdd:TIGR01348 118 EVTVPDI-GDIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSvaGSTP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 83 AGKETSAKSEEKASTPAQRQQA-------------------SLEEQNNDALSPAIRRLLAEHNLDASAIKGTGVGGRLTR 143
Cdd:TIGR01348 197 ATAPAPASAQPAAQSPAATQPEpaaapaaakaqapapqqagTQNPAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILR 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 144 EDVEKHLAKAPAKESAPAAAAPAAQPALVARSE---------KRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIM 214
Cdd:TIGR01348 277 EDVQRFVKEPSVRAQAAAASAAGGAPGALPWPNvdfskfgevEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEME 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 215 DLRKQYGEAFEKRhGIRLGFMSFYVKAVVEALKRYPEVNASID--GDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGM 292
Cdd:TIGR01348 357 AFRKQQNAAVEKE-GVKLTVLHILMKAVAAALKKFPKFNASLDlgGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGI 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 293 ADIEKKIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAvNGlVEILP--MMYL 370
Cdd:TIGR01348 436 TELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVW-NG-KEFEPrlMLPL 513
|
410 420 430
....*....|....*....|....*....|...
gi 446021972 371 ALSYDHRLIDGRESVGFLVTIKELLEDPTRLLL 403
Cdd:TIGR01348 514 SLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
5-403 |
2.46e-63 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 212.41 E-value: 2.46e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 5 DILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGT-----------TVTSRQI 73
Cdd:PLN02744 114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAkeikvgeviaiTVEEEED 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 74 LGRLREGNSAGKETSAKSEEKASTPA-----QRQQASLEEQNNDAL------------SPAIRRLLAEHNLDASAIKGTG 136
Cdd:PLN02744 194 IGKFKDYKPSSSAAPAAPKAKPSPPPpkeeeVEKPASSPEPKASKPsappssgdrifaSPLARKLAEDNNVPLSSIKGTG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 137 VGGRLTREDVEKHLAKAPAKESAPAAAAPAAQPAlvarSEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDL 216
Cdd:PLN02744 274 PDGRIVKADIEDYLASGGKGATAPPSTDSKAPAL----DYTDIPNTQIRKVTASRLLQSKQTIPHYYLTVDTRVDKLMAL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 217 RKQYGEAFEKRHGIRLGFMSFYVKAVVEALKRYPEVNASIDGDDV-VYHNyFDVSMAVSTPRGLVTPVLRDVDTLGMADI 295
Cdd:PLN02744 350 RSQLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIrQYHN-VNINVAVQTENGLYVPVVKDADKKGLSTI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 296 EKKIKELAVKGRDGKLTVEDLTGGNFTITN-GGVFGSLMSTPIINPPQSAILGMHAIKDR--PMAVNGLVEILPMMYLAL 372
Cdd:PLN02744 429 AEEVKQLAQKARENSLKPEDYEGGTFTVSNlGGPFGIKQFCAIINPPQSAILAVGSAEKRviPGSGPDQYNFASFMSVTL 508
|
410 420 430
....*....|....*....|....*....|.
gi 446021972 373 SYDHRLIDGRESVGFLVTIKELLEDPTRLLL 403
Cdd:PLN02744 509 SCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
115-401 |
5.22e-55 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 183.84 E-value: 5.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 115 SPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKHL----------AKAPAKESAPAAAAPAAQPALVARSEKRVPMTRL 184
Cdd:PRK11857 5 TPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIkslksaptpaEAASVSSAQQAAKTAAPAAAPPKLEGKREKVAPI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 185 RKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFYVKAVVEALKRYPEVNASID--GDDVV 262
Cdd:PRK11857 85 RKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDeaTSELV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 263 YHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQ 342
Cdd:PRK11857 165 YPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINYPE 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446021972 343 SAILGMHAIKDRPMAVNGLVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRL 401
Cdd:PRK11857 245 LAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
104-403 |
6.19e-54 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 182.41 E-value: 6.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 104 ASLEEQNNDALSPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKHLAKAPAKESAPAAAAPAAQPALVARSEK-----R 178
Cdd:PRK14843 41 ETYKDTNVVRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEEVPDNVTPygeieR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 179 VPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFYVKAVVEALKRYPEVNASI-- 256
Cdd:PRK14843 121 IPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLte 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 257 DGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTP 336
Cdd:PRK14843 201 DGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGP 280
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446021972 337 IINPPQSAILGMHAIKDRPMAVNGLVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRLLL 403
Cdd:PRK14843 281 IINQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
6-403 |
2.73e-48 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 169.51 E-value: 2.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 6 ILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNSAGK 85
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 86 ETSAKSEEKASTPAQRQQASLEEQNNDA---LSPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKHL-----------A 151
Cdd:PLN02528 81 RSDSLLLPTDSSNIVSLAESDERGSNLSgvlSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAaqkgvvkdsssA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 152 KAPAKESAPAAAAPAAQPALVARSEKRVPMtrlrkRVAERLLeAKNSTAMLTT-----FNEVNMKPIMDLRKQYGEAfEK 226
Cdd:PLN02528 161 EEATIAEQEEFSTSVSTPTEQSYEDKTIPL-----RGFQRAM-VKTMTAAAKVphfhyVEEINVDALVELKASFQEN-NT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 227 RHGIRLGFMSFYVKAVVEALKRYPEVNASIDGD--DVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAV 304
Cdd:PLN02528 234 DPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEEtsEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 305 KGRDGKLTVEDLTGGNFTITN----GGVFGSlmstPIINPPQSAILGMHAIKDRPMAVN-GLVEILPMMYLALSYDHRLI 379
Cdd:PLN02528 314 LAAENKLNPEDITGGTITLSNigaiGGKFGS----PVLNLPEVAIIALGRIQKVPRFVDdGNVYPASIMTVTIGADHRVL 389
|
410 420
....*....|....*....|....
gi 446021972 380 DGRESVGFLVTIKELLEDPTRLLL 403
Cdd:PLN02528 390 DGATVARFCNEWKSYVEKPELLML 413
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
2-77 |
5.37e-26 |
|
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: 99.76 E-value: 5.37e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446021972 2 SSVDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRL 77
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
4-77 |
1.63e-24 |
|
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: 95.55 E-value: 1.63e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446021972 4 VDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRL 77
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
5-77 |
4.15e-24 |
|
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: 94.43 E-value: 4.15e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446021972 5 DILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRL 77
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
241-395 |
7.53e-22 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 98.04 E-value: 7.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 241 AVVEALKRYPEVNASIDGDD----VVYHNYFDVSMAVSTP-----RGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKL 311
Cdd:PRK12270 179 ALVQALKAFPNMNRHYAEVDgkptLVTPAHVNLGLAIDLPkkdgsRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 312 TVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIkDRPMAVNGLVE-------ILPMMYLALSYDHRLIDGRES 384
Cdd:PRK12270 259 TADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAM-EYPAEFQGASEerlaelgISKVMTLTSTYDHRIIQGAES 337
|
170
....*....|.
gi 446021972 385 VGFLVTIKELL 395
Cdd:PRK12270 338 GEFLRTIHQLL 348
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
6-113 |
2.25e-14 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 73.82 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 6 ILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNSAGK 85
Cdd:PRK14875 5 ITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVSDA 84
|
90 100
....*....|....*....|....*...
gi 446021972 86 ETSAkseekASTPAQRQQASLEEQNNDA 113
Cdd:PRK14875 85 EIDA-----FIAPFARRFAPEGIDEEDA 107
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
3-118 |
1.54e-12 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 68.79 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 3 SVDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGT------TVTSRqILGr 76
Cdd:PRK11892 2 AIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTegvkvnTPIAV-LLE- 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 446021972 77 lrEGNSAGKETSAKSEEKASTPAQRQQASLEEQNNDALSPAI 118
Cdd:PRK11892 80 --EGESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAA 119
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
4-77 |
3.41e-12 |
|
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: 61.46 E-value: 3.41e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446021972 4 VDILVPDLPESVAdATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRL 77
Cdd:pfam00364 1 TEIKSPMIGESVR-EGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
3-107 |
2.20e-10 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 62.33 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446021972 3 SVDILVPDLpeSVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNS 82
Cdd:PRK11854 2 AIEIKVPDI--GADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADG 79
|
90 100
....*....|....*....|....*
gi 446021972 83 AGKETSAKSEEKASTPAQRQQASLE 107
Cdd:PRK11854 80 AADAAPAQAEEKKEAAPAAAPAAAA 104
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
115-147 |
6.50e-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: 53.84 E-value: 6.50e-10
10 20 30
....*....|....*....|....*....|...
gi 446021972 115 SPAIRRLLAEHNLDASAIKGTGVGGRLTREDVE 147
Cdd:pfam02817 4 SPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
19-77 |
1.39e-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: 1.39e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 446021972 19 TVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRL 77
Cdd:cd06850 9 TVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
26-74 |
6.79e-03 |
|
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: 36.80 E-value: 6.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 446021972 26 KPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQIL 74
Cdd:COG0511 84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPL 132
|
|
| |
