|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
1-405 |
0e+00 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 731.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 1 MTIEILVPDLPESVADATVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATVVSKQVLGILVTQQ 80
Cdd:PRK05704 1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 81 AGDVSLATIKPVNEATPSDRQTASLEPDNSSADALGPSVRRLLAEHGLEASEVKGSGVGGRITREDIEAVVAKRNAKVAE 160
Cdd:PRK05704 81 AAGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 161 K--VENTISTVAYSARSEKRVPMTRLRKRIAERLLEAKNTTAMLTTFNEVDMKPIMDLRKQYGEKFEKQHGVRLGFMSFY 238
Cdd:PRK05704 161 PaaAAPAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 239 IKAVVEALKRYPEVNASIDGDDVVYHNYFDVSIAVSTPRGLVTPVLRDCDKLSMADIEKAIKALAEKGRDGKLTVEDLTG 318
Cdd:PRK05704 241 VKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 319 GNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPVAVDGQVVIRPMMYLALSYDHRLIDGRESVGFLVAIKDLLEDP 398
Cdd:PRK05704 321 GTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDP 400
|
....*..
gi 498484951 399 TRLLLEI 405
Cdd:PRK05704 401 ERLLLDL 407
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
3-405 |
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: 642.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 3 IEILVPDLPESVADATVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATVVSKQVLGIL-VTQQA 81
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILeEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 82 GDVSLATIKPVNEATPSDRQTASLePDNSSADALGPSVRRLLAEHGLEASEVKGSGVGGRITREDIEAVVAKRNAKVAEK 161
Cdd:TIGR01347 81 TAAPPAKSGEEKEETPAASAAAAP-TAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 162 VENTISTVAYSARSEKRVPMTRLRKRIAERLLEAKNTTAMLTTFNEVDMKPIMDLRKQYGEKFEKQHGVRLGFMSFYIKA 241
Cdd:TIGR01347 160 AAAAAAAPAAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 242 VVEALKRYPEVNASIDGDDVVYHNYFDVSIAVSTPRGLVTPVLRDCDKLSMADIEKAIKALAEKGRDGKLTVEDLTGGNF 321
Cdd:TIGR01347 240 VVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 322 TITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPVAVDGQVVIRPMMYLALSYDHRLIDGRESVGFLVAIKDLLEDPTRL 401
Cdd:TIGR01347 320 TITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRL 399
|
....
gi 498484951 402 LLEI 405
Cdd:TIGR01347 400 LLDL 403
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
192-402 |
8.82e-104 |
|
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: 305.62 E-value: 8.82e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 192 LLEAKNTTAMLTTFNEVDMKPIMDLRKQYGEKFEKQhGVRLGFMSFYIKAVVEALKRYPEVNASIDGDD--VVYHNYFDV 269
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADE-ETKLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 270 SIAVSTPRGLVTPVLRDCDKLSMADIEKAIKALAEKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMH 349
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498484951 350 AIKDRPVAVDGQVVIRPMMYLALSYDHRLIDGRESVGFLVAIKDLLEDPTRLL 402
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-77 |
2.44e-28 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 105.92 E-value: 2.44e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498484951 1 MTIEILVPDLPESVADATVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATVVSKQVLGILV 77
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
3-76 |
1.81e-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: 98.25 E-value: 1.81e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498484951 3 IEILVPDLPESVADATVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATVVSKQVLGIL 76
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
1-405 |
0e+00 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 731.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 1 MTIEILVPDLPESVADATVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATVVSKQVLGILVTQQ 80
Cdd:PRK05704 1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 81 AGDVSLATIKPVNEATPSDRQTASLEPDNSSADALGPSVRRLLAEHGLEASEVKGSGVGGRITREDIEAVVAKRNAKVAE 160
Cdd:PRK05704 81 AAGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 161 K--VENTISTVAYSARSEKRVPMTRLRKRIAERLLEAKNTTAMLTTFNEVDMKPIMDLRKQYGEKFEKQHGVRLGFMSFY 238
Cdd:PRK05704 161 PaaAAPAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 239 IKAVVEALKRYPEVNASIDGDDVVYHNYFDVSIAVSTPRGLVTPVLRDCDKLSMADIEKAIKALAEKGRDGKLTVEDLTG 318
Cdd:PRK05704 241 VKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 319 GNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPVAVDGQVVIRPMMYLALSYDHRLIDGRESVGFLVAIKDLLEDP 398
Cdd:PRK05704 321 GTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDP 400
|
....*..
gi 498484951 399 TRLLLEI 405
Cdd:PRK05704 401 ERLLLDL 407
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
3-405 |
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: 642.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 3 IEILVPDLPESVADATVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATVVSKQVLGIL-VTQQA 81
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILeEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 82 GDVSLATIKPVNEATPSDRQTASLePDNSSADALGPSVRRLLAEHGLEASEVKGSGVGGRITREDIEAVVAKRNAKVAEK 161
Cdd:TIGR01347 81 TAAPPAKSGEEKEETPAASAAAAP-TAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 162 VENTISTVAYSARSEKRVPMTRLRKRIAERLLEAKNTTAMLTTFNEVDMKPIMDLRKQYGEKFEKQHGVRLGFMSFYIKA 241
Cdd:TIGR01347 160 AAAAAAAPAAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVKA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 242 VVEALKRYPEVNASIDGDDVVYHNYFDVSIAVSTPRGLVTPVLRDCDKLSMADIEKAIKALAEKGRDGKLTVEDLTGGNF 321
Cdd:TIGR01347 240 VVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 322 TITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPVAVDGQVVIRPMMYLALSYDHRLIDGRESVGFLVAIKDLLEDPTRL 401
Cdd:TIGR01347 320 TITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRL 399
|
....
gi 498484951 402 LLEI 405
Cdd:TIGR01347 400 LLDL 403
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
5-405 |
1.85e-172 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 488.04 E-value: 1.85e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 5 ILVPDLPESVADATVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATV-VSKQvlgiLVTQQAGD 83
Cdd:PTZ00144 47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVeVGAP----LSEIDTGG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 84 VSLATiKPVNEATPSDRQTASLEPDNSSADALGPsvrrllaehglEASEVkgsgvggritrediEAVVAKRNAKVAEKVE 163
Cdd:PTZ00144 123 APPAA-APAAAAAAKAEKTTPEKPKAAAPTPEPP-----------AASKP--------------TPPAAAKPPEPAPAAK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 164 NTISTVAYSARSEKRVPMTRLRKRIAERLLEAKNTTAMLTTFNEVDMKPIMDLRKQYGEKFEKQHGVRLGFMSFYIKAVV 243
Cdd:PTZ00144 177 PPPTPVARADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGVKLGFMSAFVKAST 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 244 EALKRYPEVNASIDGDDVVYHNYFDVSIAVSTPRGLVTPVLRDCDKLSMADIEKAIKALAEKGRDGKLTVEDLTGGNFTI 323
Cdd:PTZ00144 257 IALKKMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 324 TNGGVFGSLMSTPIINPPQSAILGMHAIKDRPVAVDGQVVIRPMMYLALSYDHRLIDGRESVGFLVAIKDLLEDPTRLLL 403
Cdd:PTZ00144 337 SNGGVFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLL 416
|
..
gi 498484951 404 EI 405
Cdd:PTZ00144 417 DL 418
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-404 |
1.46e-148 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 427.28 E-value: 1.46e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 1 MTIEILVPDLPESVADATVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATVVSKQVLGILVTqq 80
Cdd:PRK11856 1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 81 AGDVSLATIKPVNEATPSDRQTASLEPDNSSADALG--------------PSVRRLLAEHGLEASEVKGSGVGGRITRED 146
Cdd:PRK11856 79 EGEAEAAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAaapaapaaaaakasPAVRKLARELGVDLSTVKGSGPGGRITKED 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 147 IEAVVAKRNAKVAEKVENTISTVAYSARSEKRVPMTRLRKRIAERLLEAKNTTAMLTTFNEVDMKPIMDLRKQYgekfeK 226
Cdd:PRK11856 159 VEAAAAAAAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQL-----K 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 227 QHGVRLGFMSFYIKAVVEALKRYPEVNASIDGDDVVYHNYFDVSIAVSTPRGLVTPVLRDCDKLSMADIEKAIKALAEKG 306
Cdd:PRK11856 234 AIGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 307 RDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPVAVDGQVVIRPMMYLALSYDHRLIDGRESVG 386
Cdd:PRK11856 314 REGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAAR 393
|
410
....*....|....*...
gi 498484951 387 FLVAIKDLLEDPTRLLLE 404
Cdd:PRK11856 394 FLKALKELLENPALLLLE 411
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
2-405 |
4.87e-124 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 366.77 E-value: 4.87e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 2 TIEILVPDLPESVADATVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATVVSKQVLGILVTQQa 81
Cdd:PLN02226 91 TVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSE- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 82 gdvslatiKPVNEATPSDR--QTASLEPDNSSADALGPSVRrllaehgleasevkgsgvggritredieavvakrNAKVA 159
Cdd:PLN02226 170 --------DAASQVTPSQKipETTDPKPSPPAEDKQKPKVE----------------------------------SAPVA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 160 EKVENTISTV--AYSARS--------EKRVPMTRLRKRIAERLLEAKNTTAMLTTFNEVDMKPIMDLRKQYGEKFEKQHG 229
Cdd:PLN02226 208 EKPKAPSSPPppKQSAKEpqlppkerERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYEKHG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 230 VRLGFMSFYIKAVVEALKRYPEVNASIDGDDVVYHNYFDVSIAVSTPRGLVTPVLRDCDKLSMADIEKAIKALAEKGRDG 309
Cdd:PLN02226 288 VKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEG 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 310 KLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPVAVDGQVVIRPMMYLALSYDHRLIDGRESVGFLV 389
Cdd:PLN02226 368 TISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLR 447
|
410
....*....|....*.
gi 498484951 390 AIKDLLEDPTRLLLEI 405
Cdd:PLN02226 448 RVKDVVEDPQRLLLDI 463
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-403 |
1.15e-118 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 355.67 E-value: 1.15e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 2 TIEILVPDLPEsVADATVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATVVSKQVLGILVTQQA 81
Cdd:PRK11855 119 VVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 82 GDV-------------SLATIKPVNEATPSDRQTASLEPDNSSADAL-GPSVRRLLAEHGLEASEVKGSGVGGRITREDI 147
Cdd:PRK11855 198 APAaaaapaaaapaaaAAAAPAPAPAAAAAPAAAAPAAAAAPGKAPHaSPAVRRLARELGVDLSQVKGTGKKGRITKEDV 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 148 EAVV--AKRNAKVAEKVENTIST----------VAYSARSEKR-VPMTRLRKRIAERLLEAKNTTAMLTTFNEVDMKPIM 214
Cdd:PRK11855 278 QAFVkgAMSAAAAAAAAAAAAGGgglgllpwpkVDFSKFGEIEtKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 215 DLRKQYGEKFEKQhGVRLGFMSFYIKAVVEALKRYPEVNASID--GDDVVYHNYFDVSIAVSTPRGLVTPVLRDCDKLSM 292
Cdd:PRK11855 358 ALRKQLKKEAEKA-GVKLTMLPFFIKAVVAALKEFPVFNASLDedGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSL 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 293 ADIEKAIKALAEKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPVAVDGQVVIRPMMYLAL 372
Cdd:PRK11855 437 LEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSL 516
|
410 420 430
....*....|....*....|....*....|.
gi 498484951 373 SYDHRLIDGRESVGFLVAIKDLLEDPTRLLL 403
Cdd:PRK11855 517 SYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
192-402 |
8.82e-104 |
|
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: 305.62 E-value: 8.82e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 192 LLEAKNTTAMLTTFNEVDMKPIMDLRKQYGEKFEKQhGVRLGFMSFYIKAVVEALKRYPEVNASIDGDD--VVYHNYFDV 269
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADE-ETKLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 270 SIAVSTPRGLVTPVLRDCDKLSMADIEKAIKALAEKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMH 349
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498484951 350 AIKDRPVAVDGQVVIRPMMYLALSYDHRLIDGRESVGFLVAIKDLLEDPTRLL 402
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
4-397 |
1.36e-97 |
|
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: 302.70 E-value: 1.36e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 4 EILVPDLPESVADATVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATVVSKQVLGILVTQQAGD 83
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANAAP 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 84 VSLATIKPVNEA--------TPSDRQTASLEPDNSSADA---------------------LGPSVRRLLAEHGLEASEVK 134
Cdd:TIGR02927 208 AEPAEEEAPAPSeagsepapDPAARAPHAAPDPPAPAPApaktaapaaaapvssgdsgpyVTPLVRKLAKDKGVDLSTVK 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 135 GSGVGGRITREDIEAVVAKRNAKVAEKVENTISTVAYSARSEKRVP-------------MTRLRKRIAERLLEAKNTTAM 201
Cdd:TIGR02927 288 GTGVGGRIRKQDVLAAAKAAEEARAAAAAPAAAAAPAAPAAAAKPAepdtaklrgttqkMNRIRQITADKTIESLQTSAQ 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 202 LTTFNEVDMKPIMDLRKQYGEKFEKQHGVRLGFMSFYIKAVVEALKRYPEVNASI--DGDDVVYHNYFDVSIAVSTPRGL 279
Cdd:TIGR02927 368 LTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYnaETKEVTYHDVEHVGIAVDTPRGL 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 280 VTPVLRDCDKLSMADIEKAIKALAEKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPVAV- 358
Cdd:TIGR02927 448 LVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIk 527
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 498484951 359 --DG--QVVIRPMMYLALSYDHRLIDGRESVGFLVAIKDLLED 397
Cdd:TIGR02927 528 deDGgeSIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEE 570
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
4-403 |
7.42e-93 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 291.91 E-value: 7.42e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 4 EILVPDLpeSVADATVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATVVSKQVlgILVTQQAGD 83
Cdd:PRK11854 208 DVNVPDI--GGDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSL--IMRFEVEGA 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 84 VSLATIKPVNEATPSDRQTASLEPDNSSADA---------------LGPSVRRLLAEHGLEASEVKGSGVGGRITREDIE 148
Cdd:PRK11854 284 APAAAPAKQEAAAPAPAAAKAEAPAAAPAAKaegksefaendayvhATPLVRRLAREFGVNLAKVKGTGRKGRILKEDVQ 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 149 AVV--AKRNAKVAEKVENT---------ISTVAYSARSE-KRVPMTRLRKRIAERLLEAKNTTAMLTTFNEVDMKPIMDL 216
Cdd:PRK11854 364 AYVkdAVKRAEAAPAAAAAggggpgllpWPKVDFSKFGEiEEVELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAF 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 217 RK-QYGEKFEKQHGVRLGFMSFYIKAVVEALKRYPEVNASI--DGDDVVYHNYFDVSIAVSTPRGLVTPVLRDCDKLSMA 293
Cdd:PRK11854 444 RKqQNAEAEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLseDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGII 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 294 DIEKAIKALAEKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPVAVDGQVVIRPMMYLALS 373
Cdd:PRK11854 524 ELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGKEFAPRLMLPLSLS 603
|
410 420 430
....*....|....*....|....*....|
gi 498484951 374 YDHRLIDGRESVGFLVAIKDLLEDPTRLLL 403
Cdd:PRK11854 604 YDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
4-403 |
1.38e-86 |
|
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: 269.74 E-value: 1.38e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 4 EILVPDLPESVADATVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEG----------ATVVSKQ-- 71
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGtkdvpvnkpiAVLVEEKed 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 72 -----VLGILVTQQAGDVSLATIKPVNEATPSDRQTASLEPDNSSAD-------------ALGPSVRRLLAEHGLEASEV 133
Cdd:TIGR01349 81 vadafKNYKLESSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPEPSSpaplsdkesgdriFASPLAKKLAKEKGIDLSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 134 KGSGVGGRITREDIEAVVAKR----NAKVAEKVENTISTVAYSARSEKR-VPMTRLRKRIAERLLEAKNTTAMLTTFNEV 208
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQSpasaNQQAAATTPATYPAAAPVSTGSYEdVPLSNIRKIIAKRLLESKQTIPHYYVSIEC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 209 DMKPIMDLRKQYGEKFEKQhgVRLGFMSFYIKAVVEALKRYPEVNASIDGDDVVYHNYFDVSIAVSTPRGLVTPVLRDCD 288
Cdd:TIGR01349 241 NVDKLLALRKELNAMASEV--YKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNAD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 289 KLSMADIEKAIKALAEKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPVAVDGQ---VVIR 365
Cdd:TIGR01349 319 AKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEekgFAVA 398
|
410 420 430
....*....|....*....|....*....|....*...
gi 498484951 366 PMMYLALSYDHRLIDGRESVGFLVAIKDLLEDPTRLLL 403
Cdd:TIGR01349 399 SIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
3-403 |
2.63e-75 |
|
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: 244.01 E-value: 2.63e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 3 IEILVPDLPeSVADATVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATVVSKQVlgILVTQQAG 82
Cdd:TIGR01348 117 QEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDL--ILTLSVAG 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 83 DVSLATIKPVNEATPSDRQTASLEP---------------------DNSSADALGPSVRRLLAEHGLEASEVKGSGVGGR 141
Cdd:TIGR01348 194 STPATAPAPASAQPAAQSPAATQPEpaaapaaakaqapapqqagtqNPAKVDHAAPAVRRLAREFGVDLSAVKGTGIKGR 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 142 ITREDIEAVV--AKRNAKVAEKVENT-------ISTVAYSARSE-KRVPMTRLRKRIAERLLEAKNTTAMLTTFNEVDMK 211
Cdd:TIGR01348 274 ILREDVQRFVkePSVRAQAAAASAAGgapgalpWPNVDFSKFGEvEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADIT 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 212 PIMDLRKQYGEKFEKQhGVRLGFMSFYIKAVVEALKRYPEVNASID--GDDVVYHNYFDVSIAVSTPRGLVTPVLRDCDK 289
Cdd:TIGR01348 354 EMEAFRKQQNAAVEKE-GVKLTVLHILMKAVAAALKKFPKFNASLDlgGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDR 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 290 LSMADIEKAIKALAEKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPVAVDGQVVIRPMMY 369
Cdd:TIGR01348 433 KGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLP 512
|
410 420 430
....*....|....*....|....*....|....
gi 498484951 370 LALSYDHRLIDGRESVGFLVAIKDLLEDPTRLLL 403
Cdd:TIGR01348 513 LSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
4-403 |
5.72e-70 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 229.74 E-value: 5.72e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 4 EILVPDLPESVADATVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATVVS-KQVLGILVTQQaG 82
Cdd:PLN02744 114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAKEIKvGEVIAITVEEE-E 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 83 DV----------SLATIKPVNEATPS-------DRQTASLEPDNSSADA---------LGPSVRRLLAEHGLEASEVKGS 136
Cdd:PLN02744 193 DIgkfkdykpssSAAPAAPKAKPSPPppkeeevEKPASSPEPKASKPSAppssgdrifASPLARKLAEDNNVPLSSIKGT 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 137 GVGGRITREDIEAVVAKRNAKVAEKvenTISTVAYSARSEKRVPMTRLRKRIAERLLEAKNTTA--MLTTFNEVDmkPIM 214
Cdd:PLN02744 273 GPDGRIVKADIEDYLASGGKGATAP---PSTDSKAPALDYTDIPNTQIRKVTASRLLQSKQTIPhyYLTVDTRVD--KLM 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 215 DLRKQYGEKFEKQHGVRLGFMSFYIKAVVEALKRYPEVNASIDGDDV-VYHNyFDVSIAVSTPRGLVTPVLRDCDKLSMA 293
Cdd:PLN02744 348 ALRSQLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIrQYHN-VNINVAVQTENGLYVPVVKDADKKGLS 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 294 DIEKAIKALAEKGRDGKLTVEDLTGGNFTITN-GGVFGSLMSTPIINPPQSAILGMHAIKDR--PVAVDGQVVIRPMMYL 370
Cdd:PLN02744 427 TIAEEVKQLAQKARENSLKPEDYEGGTFTVSNlGGPFGIKQFCAIINPPQSAILAVGSAEKRviPGSGPDQYNFASFMSV 506
|
410 420 430
....*....|....*....|....*....|...
gi 498484951 371 ALSYDHRLIDGRESVGFLVAIKDLLEDPTRLLL 403
Cdd:PLN02744 507 TLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
115-403 |
3.51e-60 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 198.59 E-value: 3.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 115 LGPSVRRLLAEHGLEASEVKGSGVGGRITREDIEAVVAkrnakvaEKVENtiSTVAYSARSEK---------------RV 179
Cdd:PRK14843 51 ISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLP-------ENIEN--DSIKSPAQIEKveevpdnvtpygeieRI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 180 PMTRLRKRIAERLLEAKNTTAMLTTFNEVDMKPIMDLRKQYGEKFEKQHGVRLGFMSFYIKAVVEALKRYPEVNASI--D 257
Cdd:PRK14843 122 PMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLteD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 258 GDDVVYHNYFDVSIAVSTPRGLVTPVLRDCDKLSMADIEKAIKALAEKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPI 337
Cdd:PRK14843 202 GKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPI 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498484951 338 INPPQSAILGMHAIKDRPVAVDGQVVIRPMMYLALSYDHRLIDGRESVGFLVAIKDLLEDPTRLLL 403
Cdd:PRK14843 282 INQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
117-401 |
5.56e-60 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 196.94 E-value: 5.56e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 117 PSVRRLLAEHGLEASEVKGSGVGGRITREDIEAVVA--KRNAKVAEKVEN--------TISTVAYSARSE-KRVPMTRLR 185
Cdd:PRK11857 6 PIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKslKSAPTPAEAASVssaqqaakTAAPAAAPPKLEgKREKVAPIR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 186 KRIAERLLEAKNTTAMLTTFNEVDMKPIMDLRKQYGEKFEKQHGVRLGFMSFYIKAVVEALKRYPEVNASID--GDDVVY 263
Cdd:PRK11857 86 KAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDeaTSELVY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 264 HNYFDVSIAVSTPRGLVTPVLRDCDKLSMADIEKAIKALAEKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQS 343
Cdd:PRK11857 166 PDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINYPEL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 498484951 344 AILGMHAIKDRPVAVDGQVVIRPMMYLALSYDHRLIDGRESVGFLVAIKDLLEDPTRL 401
Cdd:PRK11857 246 AIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
5-403 |
7.05e-54 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 184.15 E-value: 7.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 5 ILVPDLPESVADATVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATV-VSKQVLGILVTQQAGD 83
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVkVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 84 VSLATIKPVNEATPSDRQTASLEPDNSSADALGPSVRRLLAEHGLEASEVKGSGVGGRITREDIEAVVAKR--------- 154
Cdd:PLN02528 81 RSDSLLLPTDSSNIVSLAESDERGSNLSGVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQKgvvkdsssa 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 155 ---NAKVAEKVENTISTVAYSARSEKRVPMtrlrkRIAERLLeAKNTTAMLTT-----FNEVDMKPIMDLRKQYGEKfEK 226
Cdd:PLN02528 161 eeaTIAEQEEFSTSVSTPTEQSYEDKTIPL-----RGFQRAM-VKTMTAAAKVphfhyVEEINVDALVELKASFQEN-NT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 227 QHGVRLGFMSFYIKAVVEALKRYPEVNASIDGD--DVVYHNYFDVSIAVSTPRGLVTPVLRDCDKLSMADIEKAIKALAE 304
Cdd:PLN02528 234 DPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEEtsEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 305 KGRDGKLTVEDLTGGNFTITN----GGVFGSlmstPIINPPQSAILGMHAIKDRPVAVD-GQVVIRPMMYLALSYDHRLI 379
Cdd:PLN02528 314 LAAENKLNPEDITGGTITLSNigaiGGKFGS----PVLNLPEVAIIALGRIQKVPRFVDdGNVYPASIMTVTIGADHRVL 389
|
410 420
....*....|....*....|....
gi 498484951 380 DGRESVGFLVAIKDLLEDPTRLLL 403
Cdd:PLN02528 390 DGATVARFCNEWKSYVEKPELLML 413
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-77 |
2.44e-28 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 105.92 E-value: 2.44e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498484951 1 MTIEILVPDLPESVADATVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATVVSKQVLGILV 77
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
3-76 |
1.81e-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: 98.25 E-value: 1.81e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498484951 3 IEILVPDLPESVADATVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATVVSKQVLGIL 76
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
241-395 |
4.49e-23 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 101.89 E-value: 4.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 241 AVVEALKRYPEVNASIDGDD----VVYHNYFDVSIAVSTP-----RGLVTPVLRDCDKLSMADIEKAIKALAEKGRDGKL 311
Cdd:PRK12270 179 ALVQALKAFPNMNRHYAEVDgkptLVTPAHVNLGLAIDLPkkdgsRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 312 TVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIkDRPVAVDG-------QVVIRPMMYLALSYDHRLIDGRES 384
Cdd:PRK12270 259 TADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAM-EYPAEFQGaseerlaELGISKVMTLTSTYDHRIIQGAES 337
|
170
....*....|.
gi 498484951 385 VGFLVAIKDLL 395
Cdd:PRK12270 338 GEFLRTIHQLL 348
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
4-76 |
1.68e-17 |
|
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: 76.33 E-value: 1.68e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498484951 4 EILVPDLPESVADATVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATVVSKQVLGIL 76
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
4-76 |
3.31e-14 |
|
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: 67.24 E-value: 3.31e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498484951 4 EILVPDLPESVADAtVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATVVSKQVLGIL 76
Cdd:pfam00364 2 EIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-119 |
1.51e-13 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 71.87 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 1 MTIEILVPDLPESVADATVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATVVsKQVLGILVTQQ 80
Cdd:PRK11892 1 MAIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGV-KVNTPIAVLLE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 498484951 81 AG-DVSLATIKPVNEATPSDRQTASLEPDNSSADALGPSV 119
Cdd:PRK11892 80 EGeSASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAA 119
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
1-121 |
3.31e-13 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 70.36 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 1 MTIEILVPDLPESVADATVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATVVSKQVLGILVtqq 80
Cdd:PRK14875 1 SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVA--- 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 498484951 81 AGDVSLATIKPVneATPSDRQtasLEPDNSSADALGPSVRR 121
Cdd:PRK14875 78 DAEVSDAEIDAF--IAPFARR---FAPEGIDEEDAGPAPRK 113
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1-104 |
5.89e-12 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 67.33 E-value: 5.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484951 1 MTIEILVPDLpeSVADATVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATVVSKQVLGIL-VTQ 79
Cdd:PRK11854 1 MAIEIKVPDI--GADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFeSAD 78
|
90 100
....*....|....*....|....*
gi 498484951 80 QAGDVSLATIKPVNEATPSDRQTAS 104
Cdd:PRK11854 79 GAADAAPAQAEEKKEAAPAAAPAAA 103
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
117-148 |
9.25e-10 |
|
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid dehydrogenases responsible for the binding of the E3 subunit.
Pssm-ID: 460710 [Multi-domain] Cd Length: 36 Bit Score: 53.46 E-value: 9.25e-10
10 20 30
....*....|....*....|....*....|..
gi 498484951 117 PSVRRLLAEHGLEASEVKGSGVGGRITREDIE 148
Cdd:pfam02817 5 PAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
18-76 |
1.64e-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: 47.80 E-value: 1.64e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 498484951 18 TVATWHKKVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATVVSKQVLGIL 76
Cdd:cd06850 9 TVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
25-73 |
2.11e-04 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 41.03 E-value: 2.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 498484951 25 KVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATVVSKQVL 73
Cdd:COG0511 84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPL 132
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
25-73 |
2.34e-04 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 43.29 E-value: 2.34e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 498484951 25 KVGDSVKRDEVIVEIETDKVVLEVPATSDGVITEIQQGEGATVVSKQVL 73
Cdd:PRK09282 539 KEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVL 587
|
|
| |
