|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
2-407 |
0e+00 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 743.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 2 SSVDILVPDLPESVADATVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGN 81
Cdd:PRK05704 1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 82 STGK--ETSAKSEEKDSTPAQRQQASLAEQNNDALSPSIRRLLGEHNLEASAINGTGVGGRITREDVEKHLAKAPAAKAE 159
Cdd:PRK05704 81 AAGAaaAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 160 AKAPAAAPAPQaQLGARGEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGDAFEKRHGIRLGFMSF 239
Cdd:PRK05704 161 PAAAAPAAAPA-PLGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 240 YVKAVVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDLLGMADIEKNIKELAVKGRDGKLTVEDLT 319
Cdd:PRK05704 240 FVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 320 GGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVDGKVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLED 399
Cdd:PRK05704 320 GGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLED 399
|
....*...
gi 2330900463 400 PTRLLLDV 407
Cdd:PRK05704 400 PERLLLDL 407
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
4-407 |
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: 677.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 4 VDILVPDLPESVADATVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNST 83
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 84 GKETSAKS-EEKDSTPAQRQQASLAEQNN-DALSPSIRRLLGEHNLEASAINGTGVGGRITREDVEKHLAKAPAAKAEAK 161
Cdd:TIGR01347 81 TAAPPAKSgEEKEETPAASAAAAPTAAANrPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 162 APAAAPAPQAqlgARGEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGDAFEKRHGIRLGFMSFYV 241
Cdd:TIGR01347 161 AAAAAAPAAA---TRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 242 KAVVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDLLGMADIEKNIKELAVKGRDGKLTVEDLTGG 321
Cdd:TIGR01347 238 KAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 322 NFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVDGKVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPT 401
Cdd:TIGR01347 318 TFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPR 397
|
....*.
gi 2330900463 402 RLLLDV 407
Cdd:TIGR01347 398 RLLLDL 403
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
194-404 |
3.89e-98 |
|
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: 291.37 E-value: 3.89e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 194 LLEAKNSTAMLTTFNEVNMKPIMDLRKQYGDAFEKRHGiRLGFMSFYVKAVVEALKRYPEVNASIDGDD--VVYHNYFDV 271
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 272 SMAVSTPRGLVTPVLRDVDLLGMADIEKNIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMH 351
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2330900463 352 AIKDRPMAVDGKVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRLL 404
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
2-77 |
2.18e-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: 100.91 E-value: 2.18e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2330900463 2 SSVDILVPDLPESVADATVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRL 77
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
4-77 |
4.03e-25 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 97.48 E-value: 4.03e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2330900463 4 VDILVPDLPESVADATVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRL 77
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
2-407 |
0e+00 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 743.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 2 SSVDILVPDLPESVADATVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGN 81
Cdd:PRK05704 1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 82 STGK--ETSAKSEEKDSTPAQRQQASLAEQNNDALSPSIRRLLGEHNLEASAINGTGVGGRITREDVEKHLAKAPAAKAE 159
Cdd:PRK05704 81 AAGAaaAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 160 AKAPAAAPAPQaQLGARGEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGDAFEKRHGIRLGFMSF 239
Cdd:PRK05704 161 PAAAAPAAAPA-PLGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 240 YVKAVVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDLLGMADIEKNIKELAVKGRDGKLTVEDLT 319
Cdd:PRK05704 240 FVKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 320 GGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVDGKVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLED 399
Cdd:PRK05704 320 GGTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLED 399
|
....*...
gi 2330900463 400 PTRLLLDV 407
Cdd:PRK05704 400 PERLLLDL 407
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
4-407 |
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: 677.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 4 VDILVPDLPESVADATVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNST 83
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 84 GKETSAKS-EEKDSTPAQRQQASLAEQNN-DALSPSIRRLLGEHNLEASAINGTGVGGRITREDVEKHLAKAPAAKAEAK 161
Cdd:TIGR01347 81 TAAPPAKSgEEKEETPAASAAAAPTAAANrPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 162 APAAAPAPQAqlgARGEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGDAFEKRHGIRLGFMSFYV 241
Cdd:TIGR01347 161 AAAAAAPAAA---TRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 242 KAVVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDLLGMADIEKNIKELAVKGRDGKLTVEDLTGG 321
Cdd:TIGR01347 238 KAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 322 NFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVDGKVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPT 401
Cdd:TIGR01347 318 TFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPR 397
|
....*.
gi 2330900463 402 RLLLDV 407
Cdd:TIGR01347 398 RLLLDL 403
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
6-407 |
1.02e-156 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 448.36 E-value: 1.02e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 6 ILVPDLPESVADATVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNS-TG 84
Cdd:PTZ00144 47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGApPA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 85 KETSAKSEEKDSTPAQRQQASLAEQNNDALSPSIrrllgEHNLEASAINGTGVGGRITredvekhlakapaakaeakapa 164
Cdd:PTZ00144 127 AAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKP-----TPPAAAKPPEPAPAAKPPP---------------------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 165 aapaPQAQLGARGEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGDAFEKRHGIRLGFMSFYVKAV 244
Cdd:PTZ00144 180 ----TPVARADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGVKLGFMSAFVKAS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 245 VEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDLLGMADIEKNIKELAVKGRDGKLTVEDLTGGNFT 324
Cdd:PTZ00144 256 TIALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFT 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 325 ITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVDGKVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRLL 404
Cdd:PTZ00144 336 ISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARML 415
|
...
gi 2330900463 405 LDV 407
Cdd:PTZ00144 416 LDL 418
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
4-406 |
6.75e-136 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 394.93 E-value: 6.75e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 4 VDILVPDLPESVADATVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNST 83
Cdd:PRK11856 3 FEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 84 GKETSAKSEEKDSTPAQRQQASLAEQNNDAL--------------SPSIRRLLGEHNLEASAINGTGVGGRITREDVEKH 149
Cdd:PRK11856 83 EAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAaaapaapaaaaakaSPAVRKLARELGVDLSTVKGSGPGGRITKEDVEAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 150 LAKAPAAKAEAKAPAAAPAPQAqlgARGEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYgdafeKR 229
Cdd:PRK11856 163 AAAAAPAAAAAAAAAAAPPAAA---AEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQL-----KA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 230 HGIRLGFMSFYVKAVVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDLLGMADIEKNIKELAVKGR 309
Cdd:PRK11856 235 IGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 310 DGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVDGKVEILPMMYLALSYDHRLIDGRESVGF 389
Cdd:PRK11856 315 EGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARF 394
|
410
....*....|....*..
gi 2330900463 390 LVTIKELLEDPTRLLLD 406
Cdd:PRK11856 395 LKALKELLENPALLLLE 411
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
3-407 |
1.21e-119 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 355.60 E-value: 1.21e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 3 SVDILVPDLPESVADATVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNS 82
Cdd:PLN02226 91 TVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSED 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 83 TGKETSA------KSEEKDSTPAQRQQASLAEQNNDALSPSirrllgehnleasaingtgvggritredvekhlakapaa 156
Cdd:PLN02226 171 AASQVTPsqkipeTTDPKPSPPAEDKQKPKVESAPVAEKPK--------------------------------------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 157 KAEAKAPAAAPAPQAQLGARG-EKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGDAFEKRHGIRLG 235
Cdd:PLN02226 212 APSSPPPPKQSAKEPQLPPKErERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYEKHGVKLG 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 236 FMSFYVKAVVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDLLGMADIEKNIKELAVKGRDGKLTV 315
Cdd:PLN02226 292 LMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISI 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 316 EDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVDGKVEILPMMYLALSYDHRLIDGRESVGFLVTIKE 395
Cdd:PLN02226 372 DEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKD 451
|
410
....*....|..
gi 2330900463 396 LLEDPTRLLLDV 407
Cdd:PLN02226 452 VVEDPQRLLLDI 463
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-405 |
3.73e-107 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 326.39 E-value: 3.73e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 2 SSVDILVPDLPEsVADATVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGN 81
Cdd:PRK11855 118 GVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 82 STGKETSAKSEEKD---------------STPAQRQQASLAEQNNDAL-SPSIRRLLGEHNLEASAINGTGVGGRITRED 145
Cdd:PRK11855 197 AAPAAAAAPAAAAPaaaaaaapapapaaaAAPAAAAPAAAAAPGKAPHaSPAVRRLARELGVDLSQVKGTGKKGRITKED 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 146 VEKHLAKAPAAKAEAKAPAAAPAPQAQ---------LGARGEKR-VPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPI 215
Cdd:PRK11855 277 VQAFVKGAMSAAAAAAAAAAAAGGGGLgllpwpkvdFSKFGEIEtKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 216 MDLRKQYGDAFEKrHGIRLGFMSFYVKAVVEALKRYPEVNASID--GDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDLLG 293
Cdd:PRK11855 357 EALRKQLKKEAEK-AGVKLTMLPFFIKAVVAALKEFPVFNASLDedGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKS 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 294 MADIEKNIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPmaVDGKVEILP--MMY 371
Cdd:PRK11855 436 LLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKP--VWDGKEFVPrlMLP 513
|
410 420 430
....*....|....*....|....*....|....
gi 2330900463 372 LALSYDHRLIDGRESVGFLVTIKELLEDPTRLLL 405
Cdd:PRK11855 514 LSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
194-404 |
3.89e-98 |
|
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: 291.37 E-value: 3.89e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 194 LLEAKNSTAMLTTFNEVNMKPIMDLRKQYGDAFEKRHGiRLGFMSFYVKAVVEALKRYPEVNASIDGDD--VVYHNYFDV 271
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 272 SMAVSTPRGLVTPVLRDVDLLGMADIEKNIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMH 351
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2330900463 352 AIKDRPMAVDGKVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRLL 404
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-405 |
1.60e-91 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 288.44 E-value: 1.60e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 2 SSVDILVPDLpeSVADATVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGN 81
Cdd:PRK11854 205 GVKDVNVPDI--GGDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEG 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 82 S------------TGKETSAKSEEKDSTPAQRQQASLAEQNNDAL---SPSIRRLLGEHNLEASAINGTGVGGRITREDV 146
Cdd:PRK11854 283 AapaaapakqeaaAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAYvhaTPLVRRLAREFGVNLAKVKGTGRKGRILKEDV 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 147 EKHLAKAPAAKAEAKAPAAAPAPQAQL-----------GARGEkrVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPI 215
Cdd:PRK11854 363 QAYVKDAVKRAEAAPAAAAAGGGGPGLlpwpkvdfskfGEIEE--VELGRIQKISGANLHRNWVMIPHVTQFDKADITEL 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 216 MDLRK-QYGDAFEKRHGIRLGFMSFYVKAVVEALKRYPEVNASI--DGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDLL 292
Cdd:PRK11854 441 EAFRKqQNAEAEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLseDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKK 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 293 GMADIEKNIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPmaVDGKVEILP--MM 370
Cdd:PRK11854 521 GIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEP--VWNGKEFAPrlML 598
|
410 420 430
....*....|....*....|....*....|....*
gi 2330900463 371 YLALSYDHRLIDGRESVGFLVTIKELLEDPTRLLL 405
Cdd:PRK11854 599 PLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
2-399 |
1.30e-89 |
|
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: 281.90 E-value: 1.30e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 2 SSVDILVPDLPESVADATVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGN 81
Cdd:TIGR02927 125 EATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDAN 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 82 STGKETS--------------------------------AKSEEKDSTPAQRQQASlAEQNNDALSPSIRRLLGEHNLEA 129
Cdd:TIGR02927 205 AAPAEPAeeeapapseagsepapdpaaraphaapdppapAPAPAKTAAPAAAAPVS-SGDSGPYVTPLVRKLAKDKGVDL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 130 SAINGTGVGGRITREDVEKHLAKAPAAKAEAKAPAAAPAPQAQLGA-----------RGEKRvPMTRLRKRVAERLLEAK 198
Cdd:TIGR02927 284 STVKGTGVGGRIRKQDVLAAAKAAEEARAAAAAPAAAAAPAAPAAAakpaepdtaklRGTTQ-KMNRIRQITADKTIESL 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 199 NSTAMLTTFNEVNMKPIMDLRKQYGDAFEKRHGIRLGFMSFYVKAVVEALKRYPEVNASI--DGDDVVYHNYFDVSMAVS 276
Cdd:TIGR02927 363 QTSAQLTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYnaETKEVTYHDVEHVGIAVD 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 277 TPRGLVTPVLRDVDLLGMADIEKNIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDR 356
Cdd:TIGR02927 443 TPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKR 522
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2330900463 357 PMAV---DG--KVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLED 399
Cdd:TIGR02927 523 PRVIkdeDGgeSIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEE 570
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
6-405 |
7.51e-84 |
|
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: 262.81 E-value: 7.51e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 6 ILVPDLPESVADATVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGT---------TVTSRQ---- 72
Cdd:TIGR01349 2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTkdvpvnkpiAVLVEEkedv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 73 ----ILGRLREGNSTGKETSAK--------------SEEKDSTPAQRQQASLAEQNND-ALSPSIRRLLGEHNLEASAIN 133
Cdd:TIGR01349 82 adafKNYKLESSASPAPKPSEIaptappsapkpspaPQKQSPEPSSPAPLSDKESGDRiFASPLAKKLAKEKGIDLSAVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 134 GTGVGGRITREDVEKHL-AKAPAAKAEAKAPAAAPAPQAQLGARGEKR-VPMTRLRKRVAERLLEAKNSTAMLTTFNEVN 211
Cdd:TIGR01349 162 GSGPNGRIVKKDIESFVpQSPASANQQAAATTPATYPAAAPVSTGSYEdVPLSNIRKIIAKRLLESKQTIPHYYVSIECN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 212 MKPIMDLRKQYGDAFEKRhgIRLGFMSFYVKAVVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDL 291
Cdd:TIGR01349 242 VDKLLALRKELNAMASEV--YKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNADA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 292 LGMADIEKNIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPM---AVDGKVEILP 368
Cdd:TIGR01349 320 KGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVvdnDEEKGFAVAS 399
|
410 420 430
....*....|....*....|....*....|....*..
gi 2330900463 369 MMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRLLL 405
Cdd:TIGR01349 400 IMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
5-405 |
4.93e-71 |
|
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: 232.84 E-value: 4.93e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 5 DILVPDLpESVADATVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNST- 83
Cdd:TIGR01348 118 EVTVPDI-GDIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTp 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 84 -GKETSAKSEEKDSTPAQRQQASLA-------------------EQNNDALSPSIRRLLGEHNLEASAINGTGVGGRITR 143
Cdd:TIGR01348 197 aTAPAPASAQPAAQSPAATQPEPAAapaaakaqapapqqagtqnPAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILR 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 144 EDVEKHLAKAPAAKAEAKAPAAAPAP------QAQLGARGE-KRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIM 216
Cdd:TIGR01348 277 EDVQRFVKEPSVRAQAAAASAAGGAPgalpwpNVDFSKFGEvEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEME 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 217 DLRKQYGDAFEKRhGIRLGFMSFYVKAVVEALKRYPEVNASID--GDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDLLGM 294
Cdd:TIGR01348 357 AFRKQQNAAVEKE-GVKLTVLHILMKAVAAALKKFPKFNASLDlgGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGI 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 295 ADIEKNIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAvDGKvEILP--MMYL 372
Cdd:TIGR01348 436 TELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVW-NGK-EFEPrlMLPL 513
|
410 420 430
....*....|....*....|....*....|...
gi 2330900463 373 ALSYDHRLIDGRESVGFLVTIKELLEDPTRLLL 405
Cdd:TIGR01348 514 SLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
5-405 |
3.66e-62 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 209.32 E-value: 3.66e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 5 DILVPDLPESVADATVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGT-----------TVTSRQI 73
Cdd:PLN02744 114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAkeikvgeviaiTVEEEED 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 74 LGRLREGNSTGKETSAKSEEKDSTPA-----QRQQASLAEQNNDAL------------SPSIRRLLGEHNLEASAINGTG 136
Cdd:PLN02744 194 IGKFKDYKPSSSAAPAAPKAKPSPPPpkeeeVEKPASSPEPKASKPsappssgdrifaSPLARKLAEDNNVPLSSIKGTG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 137 VGGRITREDVEKHLAKAPAAKAEAKAPAAAPApqaqlgARGEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIM 216
Cdd:PLN02744 274 PDGRIVKADIEDYLASGGKGATAPPSTDSKAP------ALDYTDIPNTQIRKVTASRLLQSKQTIPHYYLTVDTRVDKLM 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 217 DLRKQYGDAFEKRHGIRLGFMSFYVKAVVEALKRYPEVNASIDGDDV-VYHNyFDVSMAVSTPRGLVTPVLRDVDLLGMA 295
Cdd:PLN02744 348 ALRSQLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIrQYHN-VNINVAVQTENGLYVPVVKDADKKGLS 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 296 DIEKNIKELAVKGRDGKLTVEDLTGGNFTITN-GGVFGSLMSTPIINPPQSAILGMHAIKDR--PMAVDGKVEILPMMYL 372
Cdd:PLN02744 427 TIAEEVKQLAQKARENSLKPEDYEGGTFTVSNlGGPFGIKQFCAIINPPQSAILAVGSAEKRviPGSGPDQYNFASFMSV 506
|
410 420 430
....*....|....*....|....*....|...
gi 2330900463 373 ALSYDHRLIDGRESVGFLVTIKELLEDPTRLLL 405
Cdd:PLN02744 507 TLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
115-403 |
6.97e-54 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 181.15 E-value: 6.97e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 115 SPSIRRLLGEHNLEASAINGTGVGGRITREDVEKHLAKAPAAKAEAKAPAAAPA-----------PQAQLGARGEKRVPm 183
Cdd:PRK11857 5 TPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSAPTPAEAASVSSAqqaaktaapaaAPPKLEGKREKVAP- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 184 trLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGDAFEKRHGIRLGFMSFYVKAVVEALKRYPEVNASID--GD 261
Cdd:PRK11857 84 --IRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDeaTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 262 DVVYHNYFDVSMAVSTPRGLVTPVLRDVDLLGMADIEKNIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIIN 341
Cdd:PRK11857 162 ELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVIN 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2330900463 342 PPQSAILGMHAIKDRPMAVDGKVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRL 403
Cdd:PRK11857 242 YPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
104-405 |
2.07e-52 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 178.56 E-value: 2.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 104 ASLAEQNNDALSPSIRRLLGEHNLEASAINGTGVGGRITREDVEKHLAKAPAAKAEAKAPAAAPAPQA--QLGARGE-KR 180
Cdd:PRK14843 41 ETYKDTNVVRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEEVpdNVTPYGEiER 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 181 VPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGDAFEKRHGIRLGFMSFYVKAVVEALKRYPEVNASI-- 258
Cdd:PRK14843 121 IPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLte 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 259 DGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDLLGMADIEKNIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTP 338
Cdd:PRK14843 201 DGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGP 280
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2330900463 339 IINPPQSAILGMHAIKDRPMAVDGKVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRLLL 405
Cdd:PRK14843 281 IINQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
6-405 |
1.98e-47 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 167.20 E-value: 1.98e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 6 ILVPDLPESVADATVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNSTGK 85
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 86 ETSAKSEEKDSTPAQRQQASLAEQNNDA---LSPSIRRLLGEHNLEASAINGTGVGGRITREDVEKHLAKAPAAKAEAKA 162
Cdd:PLN02528 81 RSDSLLLPTDSSNIVSLAESDERGSNLSgvlSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKGVVKDSSSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 163 PAAAPAPQAQLGARGEKRVPMTRLRKRVAER---LLEAKNSTAMLTT-----FNEVNMKPIMDLRKQYGDAfEKRHGIRL 234
Cdd:PLN02528 161 EEATIAEQEEFSTSVSTPTEQSYEDKTIPLRgfqRAMVKTMTAAAKVphfhyVEEINVDALVELKASFQEN-NTDPTVKH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 235 GFMSFYVKAVVEALKRYPEVNASIDGD--DVVYHNYFDVSMAVSTPRGLVTPVLRDVDLLGMADIEKNIKELAVKGRDGK 312
Cdd:PLN02528 240 TFLPFLIKSLSMALSKYPLLNSCFNEEtsEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 313 LTVEDLTGGNFTITN----GGVFGSlmstPIINPPQSAILGMHAIKDRPMAVD-GKVEILPMMYLALSYDHRLIDGRESV 387
Cdd:PLN02528 320 LNPEDITGGTITLSNigaiGGKFGS----PVLNLPEVAIIALGRIQKVPRFVDdGNVYPASIMTVTIGADHRVLDGATVA 395
|
410
....*....|....*...
gi 2330900463 388 GFLVTIKELLEDPTRLLL 405
Cdd:PLN02528 396 RFCNEWKSYVEKPELLML 413
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
2-77 |
2.18e-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: 100.91 E-value: 2.18e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2330900463 2 SSVDILVPDLPESVADATVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRL 77
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
4-77 |
4.03e-25 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 97.48 E-value: 4.03e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2330900463 4 VDILVPDLPESVADATVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRL 77
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
5-77 |
3.68e-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: 94.82 E-value: 3.68e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2330900463 5 DILVPDLPESVADATVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRL 77
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
197-397 |
2.54e-20 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 93.42 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 197 AKNSTAML-----TTFNEVNMKPIMDLRKQYGDAFEKRHGIRLGFMSFYVKAVVEALKRYPEVNASIDGDD----VVYHN 267
Cdd:PRK12270 128 AKNMDASLevptaTSVRAVPAKLLIDNRIVINNHLKRTRGGKVSFTHLIGYALVQALKAFPNMNRHYAEVDgkptLVTPA 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 268 YFDVSMAVSTP-----RGLVTPVLRDVDLLGMADIEKNIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINP 342
Cdd:PRK12270 208 HVNLGLAIDLPkkdgsRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMK 287
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2330900463 343 PQSAILGMHAIkDRPMAVDGKVE-------ILPMMYLALSYDHRLIDGRESVGFLVTIKELL 397
Cdd:PRK12270 288 GQGAIIGVGAM-EYPAEFQGASEerlaelgISKVMTLTSTYDHRIIQGAESGEFLRTIHQLL 348
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
6-113 |
2.24e-14 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 73.82 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 6 ILVPDLPESVADATVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNSTGK 85
Cdd:PRK14875 5 ITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVSDA 84
|
90 100
....*....|....*....|....*...
gi 2330900463 86 ETSAKseekdSTPAQRQQASLAEQNNDA 113
Cdd:PRK14875 85 EIDAF-----IAPFARRFAPEGIDEEDA 107
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
4-77 |
8.12e-13 |
|
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: 63.39 E-value: 8.12e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2330900463 4 VDILVPDLPESVADAtVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRL 77
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
3-118 |
5.80e-12 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 66.86 E-value: 5.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 3 SVDILVPDLPESVADATVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGT------TVTSRqILGr 76
Cdd:PRK11892 2 AIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTegvkvnTPIAV-LLE- 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2330900463 77 lrEGNSTGKETSAKSEEKDSTPAQRQQASLAEQNNDALSPSI 118
Cdd:PRK11892 80 --EGESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAA 119
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
3-109 |
1.31e-09 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 60.02 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900463 3 SVDILVPDLpeSVADATVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNS 82
Cdd:PRK11854 2 AIEIKVPDI--GADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADG 79
|
90 100
....*....|....*....|....*...
gi 2330900463 83 TGKETSAKSEEK-DSTPAQRQQASLAEQ 109
Cdd:PRK11854 80 AADAAPAQAEEKkEAAPAAAPAAAAAKD 107
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
115-147 |
1.25e-08 |
|
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: 50.38 E-value: 1.25e-08
10 20 30
....*....|....*....|....*....|...
gi 2330900463 115 SPSIRRLLGEHNLEASAINGTGVGGRITREDVE 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 |
5.55e-07 |
|
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: 46.64 E-value: 5.55e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2330900463 19 TVATWHKKPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRL 77
Cdd:cd06850 9 TVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
26-74 |
2.21e-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: 37.95 E-value: 2.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2330900463 26 KPGDAVRRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQIL 74
Cdd:COG0511 84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPL 132
|
|
| |
