|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
1-398 |
0e+00 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 673.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 1 MATEIKAPVFPESVADGTIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEGDTVLSDEVIAQFEAGA 80
Cdd:PRK05704 1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 81 GAAAAAPAAVEQAVAQTQAGAAPVVERNETVSD-QAPAVRKALTESGIAASDVQGTGRGGRITKEDVANHQAKPAANVTP 159
Cdd:PRK05704 81 AAGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDaLSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 160 LSVAV--------GERIEKRVPMTRLRKRVAERLLAATQETAMLTTFNEVNMKPIMELRKQYKDAFEKRHGARLGFMSFF 231
Cdd:PRK05704 161 PAAAApaaapaplGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 232 VKAATEALKRYPAVNASIDGDDIVYHGYYDIGVAVSSDRGLVVPVLRDTDRMSYAEVEAGIAAYAAKARDGKLSIEEMTG 311
Cdd:PRK05704 241 VKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 312 GTFTITNGGTFGSLLSTPILNQPQTGILGMHKIQERPMAVNGQVEILPMMYLALSYDHRMIDGKEAVGFLVAIKELLEEP 391
Cdd:PRK05704 321 GTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDP 400
|
....*..
gi 446102024 392 AKLILDL 398
Cdd:PRK05704 401 ERLLLDL 407
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
3-398 |
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: 586.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 3 TEIKAPVFPESVADGTIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEGDTVLSDEVIAQFEAGAGA 82
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 83 AAAAPAAVEQAVAQT---QAGAAPVVERNETVSdqAPAVRKALTESGIAASDVQGTGRGGRITKEDVANHQAKPAANVTP 159
Cdd:TIGR01347 81 TAAPPAKSGEEKEETpaaSAAAAPTAAANRPSL--SPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 160 LSVAVG------ERIEKRVPMTRLRKRVAERLLAATQETAMLTTFNEVNMKPIMELRKQYKDAFEKRHGARLGFMSFFVK 233
Cdd:TIGR01347 159 AAAAAAaapaaaTRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 234 AATEALKRYPAVNASIDGDDIVYHGYYDIGVAVSSDRGLVVPVLRDTDRMSYAEVEAGIAAYAAKARDGKLSIEEMTGGT 313
Cdd:TIGR01347 239 AVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 314 FTITNGGTFGSLLSTPILNQPQTGILGMHKIQERPMAVNGQVEILPMMYLALSYDHRMIDGKEAVGFLVAIKELLEEPAK 393
Cdd:TIGR01347 319 FTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRR 398
|
....*
gi 446102024 394 LILDL 398
Cdd:TIGR01347 399 LLLDL 403
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
185-395 |
2.26e-90 |
|
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: 271.34 E-value: 2.26e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 185 LLAATQETAMLTTFNEVNMKPIMELRKQYKDAFEKRHGaRLGFMSFFVKAATEALKRYPAVNASIDGDD--IVYHGYYDI 262
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 263 GVAVSSDRGLVVPVLRDTDRMSYAEVEAGIAAYAAKARDGKLSIEEMTGGTFTITNGGTFGSLLSTPILNQPQTGILGMH 342
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446102024 343 KIQERPMAVNGQVEILPMMYLALSYDHRMIDGKEAVGFLVAIKELLEEPAKLI 395
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-73 |
3.16e-25 |
|
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: 97.44 E-value: 3.16e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446102024 1 MATEIKAPVFPESVADGTIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEGDTVLSDEVI 73
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVI 73
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
3-73 |
3.88e-23 |
|
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: 91.70 E-value: 3.88e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446102024 3 TEIKAPVFPESVADGTIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEGDTVLSDEVI 73
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVI 71
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
1-398 |
0e+00 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 673.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 1 MATEIKAPVFPESVADGTIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEGDTVLSDEVIAQFEAGA 80
Cdd:PRK05704 1 MMVEIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 81 GAAAAAPAAVEQAVAQTQAGAAPVVERNETVSD-QAPAVRKALTESGIAASDVQGTGRGGRITKEDVANHQAKPAANVTP 159
Cdd:PRK05704 81 AAGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDaLSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 160 LSVAV--------GERIEKRVPMTRLRKRVAERLLAATQETAMLTTFNEVNMKPIMELRKQYKDAFEKRHGARLGFMSFF 231
Cdd:PRK05704 161 PAAAApaaapaplGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKHGVKLGFMSFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 232 VKAATEALKRYPAVNASIDGDDIVYHGYYDIGVAVSSDRGLVVPVLRDTDRMSYAEVEAGIAAYAAKARDGKLSIEEMTG 311
Cdd:PRK05704 241 VKAVVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 312 GTFTITNGGTFGSLLSTPILNQPQTGILGMHKIQERPMAVNGQVEILPMMYLALSYDHRMIDGKEAVGFLVAIKELLEEP 391
Cdd:PRK05704 321 GTFTITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDP 400
|
....*..
gi 446102024 392 AKLILDL 398
Cdd:PRK05704 401 ERLLLDL 407
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
3-398 |
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: 586.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 3 TEIKAPVFPESVADGTIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEGDTVLSDEVIAQFEAGAGA 82
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 83 AAAAPAAVEQAVAQT---QAGAAPVVERNETVSdqAPAVRKALTESGIAASDVQGTGRGGRITKEDVANHQAKPAANVTP 159
Cdd:TIGR01347 81 TAAPPAKSGEEKEETpaaSAAAAPTAAANRPSL--SPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 160 LSVAVG------ERIEKRVPMTRLRKRVAERLLAATQETAMLTTFNEVNMKPIMELRKQYKDAFEKRHGARLGFMSFFVK 233
Cdd:TIGR01347 159 AAAAAAaapaaaTRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKHGVKLGFMSFFVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 234 AATEALKRYPAVNASIDGDDIVYHGYYDIGVAVSSDRGLVVPVLRDTDRMSYAEVEAGIAAYAAKARDGKLSIEEMTGGT 313
Cdd:TIGR01347 239 AVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 314 FTITNGGTFGSLLSTPILNQPQTGILGMHKIQERPMAVNGQVEILPMMYLALSYDHRMIDGKEAVGFLVAIKELLEEPAK 393
Cdd:TIGR01347 319 FTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRR 398
|
....*
gi 446102024 394 LILDL 398
Cdd:TIGR01347 399 LLLDL 403
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
5-398 |
5.52e-154 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 441.04 E-value: 5.52e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 5 IKAPVFPESVADGTIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEGDTVLSDEVIAQFEAgagaaa 84
Cdd:PTZ00144 47 IKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDT------ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 85 aapaaveqavaqTQAGAAPVVERNETVSDQAPAVRKAL----TESGIAASDVQgtgrggriTKEDVANHQAKPAANVTPL 160
Cdd:PTZ00144 121 ------------GGAPPAAAPAAAAAAKAEKTTPEKPKaaapTPEPPAASKPT--------PPAAAKPPEPAPAAKPPPT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 161 SVAVGERIEKRVPMTRLRKRVAERLLAATQETAMLTTFNEVNMKPIMELRKQYKDAFEKRHGARLGFMSFFVKAATEALK 240
Cdd:PTZ00144 181 PVARADPRETRVPMSRMRQRIAERLKASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKHGVKLGFMSAFVKASTIALK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 241 RYPAVNASIDGDDIVYHGYYDIGVAVSSDRGLVVPVLRDTDRMSYAEVEAGIAAYAAKARDGKLSIEEMTGGTFTITNGG 320
Cdd:PTZ00144 261 KMPIVNAYIDGDEIVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGG 340
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446102024 321 TFGSLLSTPILNQPQTGILGMHKIQERPMAVNGQVEILPMMYLALSYDHRMIDGKEAVGFLVAIKELLEEPAKLILDL 398
Cdd:PTZ00144 341 VFGSLMGTPIINPPQSAILGMHAIKKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLDL 418
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1-397 |
1.39e-121 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 358.33 E-value: 1.39e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 1 MATEIKAPVFPESVADGTIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEGDTVLSDEVI------- 73
Cdd:PRK11856 1 MMFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIavieeeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 74 -----AQFEAGAGAAAAAPAAVEQAVAQTQAGAAPVVERNETVSDQA-PAVRKALTESGIAASDVQGTGRGGRITKEDVA 147
Cdd:PRK11856 81 eaeaaAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKAsPAVRKLARELGVDLSTVKGSGPGGRITKEDVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 148 NH------QAKPAANVTPLSVAVGERIEKRVPMTRLRKRVAERLLAATQETAMLTTFNEVNMKPIMELRKQYKDAFEKrh 221
Cdd:PRK11856 161 AAaaaaapAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRKQLKAIGVK-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 222 garLGFMSFFVKAATEALKRYPAVNASIDGDDIVYHGYYDIGVAVSSDRGLVVPVLRDTDRMSYAEVEAGIAAYAAKARD 301
Cdd:PRK11856 239 ---LTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKARE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 302 GKLSIEEMTGGTFTITNGGTFGSLLSTPILNQPQTGILGMHKIQERPMAVNGQVEILPMMYLALSYDHRMIDGKEAVGFL 381
Cdd:PRK11856 316 GKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFL 395
|
410
....*....|....*.
gi 446102024 382 VAIKELLEEPAKLILD 397
Cdd:PRK11856 396 KALKELLENPALLLLE 411
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
4-398 |
2.86e-112 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 336.34 E-value: 2.86e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 4 EIKAPVFPESVADGTIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEGDTVlsdeviaqfeagagaa 83
Cdd:PLN02226 93 EAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTV---------------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 84 aaapaaveqavaQTQAGAAPVVERNETVSDQAPAvRKALTESGIAASDVQGTGRGGRITKEDVANHQAKPAANVTPLSVA 163
Cdd:PLN02226 157 ------------EPGTKVAIISKSEDAASQVTPS-QKIPETTDPKPSPPAEDKQKPKVESAPVAEKPKAPSSPPPPKQSA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 164 VGERI-----EKRVPMTRLRKRVAERLLAATQETAMLTTFNEVNMKPIMELRKQYKDAFEKRHGARLGFMSFFVKAATEA 238
Cdd:PLN02226 224 KEPQLppkerERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYEKHGVKLGLMSGFIKAAVSA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 239 LKRYPAVNASIDGDDIVYHGYYDIGVAVSSDRGLVVPVLRDTDRMSYAEVEAGIAAYAAKARDGKLSIEEMTGGTFTITN 318
Cdd:PLN02226 304 LQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSN 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 319 GGTFGSLLSTPILNQPQTGILGMHKIQERPMAVNGQVEILPMMYLALSYDHRMIDGKEAVGFLVAIKELLEEPAKLILDL 398
Cdd:PLN02226 384 GGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLLDI 463
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
2-396 |
5.55e-93 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 289.42 E-value: 5.55e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 2 ATEIKAPVFPEsVADGTIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEGDTVLSDEVIAQFEAGAG 81
Cdd:PRK11855 119 VVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 82 AAAAAPAAVEQAVAQTQAGAAPVVERNETVSDQA---------------PAVRKALTESGIAASDVQGTGRGGRITKEDV 146
Cdd:PRK11855 198 APAAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAapaaaaapgkaphasPAVRRLARELGVDLSQVKGTGKKGRITKEDV 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 147 ANHQ------------AKPAANVTPLSVAVGERIE-------KRVPMTRLRKRVAERLLAATQETAMLTTFNEVNMKPIM 207
Cdd:PRK11855 278 QAFVkgamsaaaaaaaAAAAAGGGGLGLLPWPKVDfskfgeiETKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 208 ELRKQYKDAFEKrHGARLGFMSFFVKAATEALKRYPAVNASID--GDDIVYHGYYDIGVAVSSDRGLVVPVLRDTDRMSY 285
Cdd:PRK11855 358 ALRKQLKKEAEK-AGVKLTMLPFFIKAVVAALKEFPVFNASLDedGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSL 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 286 AEVEAGIAAYAAKARDGKLSIEEMTGGTFTITNGGTFGSLLSTPILNQPQTGILGMHKIQERPMAVNGQVEILPMMYLAL 365
Cdd:PRK11855 437 LEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSL 516
|
410 420 430
....*....|....*....|....*....|.
gi 446102024 366 SYDHRMIDGKEAVGFLVAIKELLEEPAKLIL 396
Cdd:PRK11855 517 SYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
185-395 |
2.26e-90 |
|
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: 271.34 E-value: 2.26e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 185 LLAATQETAMLTTFNEVNMKPIMELRKQYKDAFEKRHGaRLGFMSFFVKAATEALKRYPAVNASIDGDD--IVYHGYYDI 262
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET-KLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 263 GVAVSSDRGLVVPVLRDTDRMSYAEVEAGIAAYAAKARDGKLSIEEMTGGTFTITNGGTFGSLLSTPILNQPQTGILGMH 342
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446102024 343 KIQERPMAVNGQVEILPMMYLALSYDHRMIDGKEAVGFLVAIKELLEEPAKLI 395
Cdd:pfam00198 160 RIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
2-390 |
1.27e-82 |
|
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: 263.41 E-value: 1.27e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 2 ATEIKAPVFPESVADGTIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEGDTVLSDEVIAQFEAGAG 81
Cdd:TIGR02927 126 ATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 82 AAAAAPAAVEQAVAQ------------------------------TQAGAAPVVERNETVSDQAPAVRKALTESGIAASD 131
Cdd:TIGR02927 206 APAEPAEEEAPAPSEagsepapdpaaraphaapdppapapapaktAAPAAAAPVSSGDSGPYVTPLVRKLAKDKGVDLST 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 132 VQGTGRGGRITKEDV-------------------ANHQAKPAANVTPLSVAVGERIEKRVPMTRLRKRVAERLLAATQET 192
Cdd:TIGR02927 286 VKGTGVGGRIRKQDVlaaakaaeearaaaaapaaAAAPAAPAAAAKPAEPDTAKLRGTTQKMNRIRQITADKTIESLQTS 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 193 AMLTTFNEVNMKPIMELRKQYKDAFEKRHGARLGFMSFFVKAATEALKRYPAVNASI--DGDDIVYHGYYDIGVAVSSDR 270
Cdd:TIGR02927 366 AQLTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYnaETKEVTYHDVEHVGIAVDTPR 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 271 GLVVPVLRDTDRMSYAEVEAGIAAYAAKARDGKLSIEEMTGGTFTITNGGTFGSLLSTPILNQPQTGILGMHKIQERPMA 350
Cdd:TIGR02927 446 GLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRV 525
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 446102024 351 V-----NGQVEILPMMYLALSYDHRMIDGKEAVGFLVAIKELLEE 390
Cdd:TIGR02927 526 IkdedgGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEE 570
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
2-396 |
1.67e-77 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 251.46 E-value: 1.67e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 2 ATEIKAPVFPE-SVADGTIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEGDTVLSDEVIA------ 74
Cdd:PRK11854 203 AAGVKDVNVPDiGGDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMrfeveg 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 75 ---QFEAGAGAAAAAPAAVEQAVAQTQAGAAPVVERNETVSDQA-----PAVRKALTESGIAASDVQGTGRGGRITKEDV 146
Cdd:PRK11854 283 aapAAAPAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAyvhatPLVRRLAREFGVNLAKVKGTGRKGRILKEDV 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 147 ANH--QAKPAANVTPLSVAVG-----------------ERIEKrVPMTRLRKRVAERLLAATQETAMLTTFNEVNMKPIM 207
Cdd:PRK11854 363 QAYvkDAVKRAEAAPAAAAAGgggpgllpwpkvdfskfGEIEE-VELGRIQKISGANLHRNWVMIPHVTQFDKADITELE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 208 ELRK-QYKDAFEKRHGARLGFMSFFVKAATEALKRYPAVNASI--DGDDIVYHGYYDIGVAVSSDRGLVVPVLRDTDRMS 284
Cdd:PRK11854 442 AFRKqQNAEAEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLseDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 285 YAEVEAGIAAYAAKARDGKLSIEEMTGGTFTITNGGTFGSLLSTPILNQPQTGILGMHKIQERPmaVNGQVEILP--MMY 362
Cdd:PRK11854 522 IIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEP--VWNGKEFAPrlMLP 599
|
410 420 430
....*....|....*....|....*....|....
gi 446102024 363 LALSYDHRMIDGKEAVGFLVAIKELLEEPAKLIL 396
Cdd:PRK11854 600 LSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
4-396 |
4.97e-65 |
|
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: 213.89 E-value: 4.97e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 4 EIKAPVFPESVADGTIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEGD---------TVLSDEVIA 74
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTkdvpvnkpiAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 75 QFEAGAGAAAAAPAAVEQAVAQTQAGA---------APVVERNETVSDQ-------------APAVRKALTESGIAASDV 132
Cdd:TIGR01349 81 VADAFKNYKLESSASPAPKPSEIAPTAppsapkpspAPQKQSPEPSSPAplsdkesgdrifaSPLAKKLAKEKGIDLSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 133 QGTGRGGRITKEDV----------ANHQAK---PAANVTPLSVAVGERIEkrVPMTRLRKRVAERLLAATQETAMLTTFN 199
Cdd:TIGR01349 161 AGSGPNGRIVKKDIesfvpqspasANQQAAattPATYPAAAPVSTGSYED--VPLSNIRKIIAKRLLESKQTIPHYYVSI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 200 EVNMKPIMELRKQYKDAFEKRHgaRLGFMSFFVKAATEALKRYPAVNASIDGDDIVYHGYYDIGVAVSSDRGLVVPVLRD 279
Cdd:TIGR01349 239 ECNVDKLLALRKELNAMASEVY--KLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 280 TDRMSYAEVEAGIAAYAAKARDGKLSIEEMTGGTFTITNGGTFGSLLSTPILNQPQTGILGMHKIQERPMAVNGQ---VE 356
Cdd:TIGR01349 317 ADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEekgFA 396
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 446102024 357 ILPMMYLALSYDHRMIDGKEAVGFLVAIKELLEEPAKLIL 396
Cdd:TIGR01349 397 VASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
13-396 |
1.49e-60 |
|
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: 204.72 E-value: 1.49e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 13 SVADGTIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADG----------------SLVAIIKGEGDTVLSDEVIAQF 76
Cdd:TIGR01348 126 DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGvvksvkvkvgdsvptgDLILTLSVAGSTPATAPAPASA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 77 EAGAGAAAAAPAAVEQAVAQTQA-GAAPVVERNE---TVSDQAPAVRKALTESGIAASDVQGTGRGGRITKEDV------ 146
Cdd:TIGR01348 206 QPAAQSPAATQPEPAAAPAAAKAqAPAPQQAGTQnpaKVDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVqrfvke 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 147 ANHQAK--------PAANVTPLSVAVGER---IEkRVPMTRLRKRVAERLLAATQETAMLTTFNEVNMKPIMELRKQYKD 215
Cdd:TIGR01348 286 PSVRAQaaaasaagGAPGALPWPNVDFSKfgeVE-EVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEAFRKQQNA 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 216 AFEKRhGARLGFMSFFVKAATEALKRYPAVNASID--GDDIVYHGYYDIGVAVSSDRGLVVPVLRDTDRMSYAEVEAGIA 293
Cdd:TIGR01348 365 AVEKE-GVKLTVLHILMKAVAAALKKFPKFNASLDlgGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELS 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 294 AYAAKARDGKLSIEEMTGGTFTITNGGTFGSLLSTPILNQPQTGILGMHKIQERPMAVNGQVEILPMMYLALSYDHRMID 373
Cdd:TIGR01348 444 DLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSLSYDHRVID 523
|
410 420
....*....|....*....|...
gi 446102024 374 GKEAVGFLVAIKELLEEPAKLIL 396
Cdd:TIGR01348 524 GADAARFTTYICESLADIRRLLL 546
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
116-394 |
1.43e-52 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 177.29 E-value: 1.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 116 PAVRKALTESGIAASDVQGTGRGGRITKEDV--------------------ANHQAKPAANVTPLSVAVGERIEKRVPmt 175
Cdd:PRK11857 6 PIARALAKKLGIDISLLKGSGRDGKILAEDVenfikslksaptpaeaasvsSAQQAAKTAAPAAAPPKLEGKREKVAP-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 176 rLRKRVAERLLAATQETAMLTTFNEVNMKPIMELRKQYKDAFEKRHGARLGFMSFFVKAATEALKRYPAVNASID--GDD 253
Cdd:PRK11857 84 -IRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVLKTEGVKLTFLPFIAKAILIALKEFPIFAAKYDeaTSE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 254 IVYHGYYDIGVAVSSDRGLVVPVLRDTDRMSYAEVEAGIAAYAAKARDGKLSIEEMTGGTFTITNGGTFGSLLSTPILNQ 333
Cdd:PRK11857 163 LVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINY 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446102024 334 PQTGILGMHKIQERPMAVNGQVEILPMMYLALSYDHRMIDGKEAVGFLVAIKELLEEPAKL 394
Cdd:PRK11857 243 PELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKPEIL 303
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
12-398 |
1.72e-52 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 180.30 E-value: 1.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 12 ESVADGTIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEGDTVLSDEVIAQFEAGAGAAAAAPAAVE 91
Cdd:PLN02528 8 EGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHLRSDSLLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 92 QAVAQTQAGAAPVVERNETVSD--QAPAVRKALTESGIAASDVQGTGRGGRITKEDVANH--------------QAKPAA 155
Cdd:PLN02528 88 PTDSSNIVSLAESDERGSNLSGvlSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYaaqkgvvkdsssaeEATIAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 156 NV---TPLSVAVGER-IEKRVPMTRLRKRVAERLLAATQETAMLTTfNEVNMKPIMELRKQYKDAfEKRHGARLGFMSFF 231
Cdd:PLN02528 168 QEefsTSVSTPTEQSyEDKTIPLRGFQRAMVKTMTAAAKVPHFHYV-EEINVDALVELKASFQEN-NTDPTVKHTFLPFL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 232 VKAATEALKRYPAVNASIDGD--DIVYHGYYDIGVAVSSDRGLVVPVLRDTDRMSYAEVEAGIAAYAAKARDGKLSIEEM 309
Cdd:PLN02528 246 IKSLSMALSKYPLLNSCFNEEtsEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 310 TGGTFTITN----GGTFGSllstPILNQPQTGILGMHKIQERPMAVN-GQVEILPMMYLALSYDHRMIDGKEAVGFLVAI 384
Cdd:PLN02528 326 TGGTITLSNigaiGGKFGS----PVLNLPEVAIIALGRIQKVPRFVDdGNVYPASIMTVTIGADHRVLDGATVARFCNEW 401
|
410
....*....|....
gi 446102024 385 KELLEEPAKLILDL 398
Cdd:PLN02528 402 KSYVEKPELLMLHM 415
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
4-396 |
4.71e-52 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 181.98 E-value: 4.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 4 EIKAPVFPESVADGTIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEGD-----------TVLSDEV 72
Cdd:PLN02744 114 EIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGDGAkeikvgeviaiTVEEEED 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 73 IA--------QFEAGAGAAAAAPAAVEQAVAQTQAGAAPVVERNETVSDQA--------PAVRKALTESGIAASDVQGTG 136
Cdd:PLN02744 194 IGkfkdykpsSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSsgdrifasPLARKLAEDNNVPLSSIKGTG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 137 RGGRITKEDVANHQAKPAANVTPLSVAVGERIE---KRVPMTRLRKRVAERLLAATQETAMLTTFNEVNMKPIMELRKQY 213
Cdd:PLN02744 274 PDGRIVKADIEDYLASGGKGATAPPSTDSKAPAldyTDIPNTQIRKVTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 214 KDAFEKRHGARLGFMSFFVKAATEALKRYPAVNASIDGDDIVYHGYYDIGVAVSSDRGLVVPVLRDTDRMSYAEVEAGIA 293
Cdd:PLN02744 354 NSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYIRQYHNVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVK 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 294 AYAAKARDGKLSIEEMTGGTFTITN-GGTFGSLLSTPILNQPQTGILGMHKIQER--PMAVNGQVEILPMMYLALSYDHR 370
Cdd:PLN02744 434 QLAQKARENSLKPEDYEGGTFTVSNlGGPFGIKQFCAIINPPQSAILAVGSAEKRviPGSGPDQYNFASFMSVTLSCDHR 513
|
410 420
....*....|....*....|....*.
gi 446102024 371 MIDGKEAVGFLVAIKELLEEPAKLIL 396
Cdd:PLN02744 514 VIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
107-396 |
1.49e-51 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 175.86 E-value: 1.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 107 RNETVSDQAPAVRKALTESGIAASDVQGTGRGGRITKEDVANHQAKPAANVTPLSVAVGERIE------------KRVPM 174
Cdd:PRK14843 44 KDTNVVRISPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLPENIENDSIKSPAQIEKVEevpdnvtpygeiERIPM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 175 TRLRKRVAERLLAATQETAMLTTFNEVNMKPIMELRKQYKDAFEKRHGARLGFMSFFVKAATEALKRYPAVNASI--DGD 252
Cdd:PRK14843 124 TPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLteDGK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 253 DIVYHGYYDIGVAVSSDRGLVVPVLRDTDRMSYAEVEAGIAAYAAKARDGKLSIEEMTGGTFTITNGGTFGSLLSTPILN 332
Cdd:PRK14843 204 TIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGPIIN 283
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446102024 333 QPQTGILGMHKIQERPMAVNGQVEILPMMYLALSYDHRMIDGKEAVGFLVAIKELLEEPAKLIL 396
Cdd:PRK14843 284 QPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1-73 |
3.16e-25 |
|
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: 97.44 E-value: 3.16e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446102024 1 MATEIKAPVFPESVADGTIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEGDTVLSDEVI 73
Cdd:COG0508 1 MAIEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVI 73
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
3-73 |
3.88e-23 |
|
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: 91.70 E-value: 3.88e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446102024 3 TEIKAPVFPESVADGTIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEGDTVLSDEVI 73
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVI 71
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
4-71 |
6.04e-15 |
|
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: 69.39 E-value: 6.04e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446102024 4 EIKAPVFPESVADGTIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEGDTVLSDE 71
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDT 68
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
96-388 |
1.06e-14 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 76.08 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 96 QTQAGAAPVVERNETVSDQAPAVRKALTESGIAASDVQGTGRGGRITKEDVANhQAKPAANVTPLSVAVGERIEKRVPMT 175
Cdd:PRK12270 40 STAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAA-AAAPAAPPAAAAAAAPAAAAVEDEVT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 176 RLR---KRVAERLLAA-TQETAmlTTFNEVNMKPIMELRKQYKDAFEKRHGARLGFMSFFVKAATEALKRYPAVNASIDG 251
Cdd:PRK12270 119 PLRgaaAAVAKNMDASlEVPTA--TSVRAVPAKLLIDNRIVINNHLKRTRGGKVSFTHLIGYALVQALKAFPNMNRHYAE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 252 DD----IVYHGYYDIGVAV-----SSDRGLVVPVLRDTDRMSYAEVEAGIAAYAAKARDGKLSIEEMTGGTFTITNGGTF 322
Cdd:PRK12270 197 VDgkptLVTPAHVNLGLAIdlpkkDGSRQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGI 276
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446102024 323 GSLLSTPILNQPQTGILGMHKIqERPMAVNGQVE-------ILPMMYLALSYDHRMIDGKEAVGFLVAIKELL 388
Cdd:PRK12270 277 GTVHSVPRLMKGQGAIIGVGAM-EYPAEFQGASEerlaelgISKVMTLTSTYDHRIIQGAESGEFLRTIHQLL 348
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
1-147 |
1.05e-13 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 71.90 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 1 MATEIKAPVFPESVADGTIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEGDTVlsdEViaqfeaga 80
Cdd:PRK14875 1 SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETL---PV-------- 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446102024 81 gaaaaapaaveqavaqtqaGAAPVVERNETVSDQ------APAVRKaLTESGIAASDVQGTGRGGRITKEDVA 147
Cdd:PRK14875 70 -------------------GALLAVVADAEVSDAeidafiAPFARR-FAPEGIDEEDAGPAPRKARIGGRTVR 122
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
3-73 |
1.81e-12 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 62.23 E-value: 1.81e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446102024 3 TEIKAPVFPESVADGtIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEGDTVLSDEVI 73
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPL 70
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
116-146 |
4.14e-09 |
|
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: 51.53 E-value: 4.14e-09
10 20 30
....*....|....*....|....*....|.
gi 446102024 116 PAVRKALTESGIAASDVQGTGRGGRITKEDV 146
Cdd:pfam02817 5 PAARKLARELGIDLSDVKGTGPGGRITKEDV 35
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-64 |
1.09e-08 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 56.85 E-value: 1.09e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446102024 1 MATEIKAPVFPESVADGTIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEG 64
Cdd:PRK11892 1 MAIEILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEG 64
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
4-73 |
1.43e-05 |
|
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: 42.40 E-value: 1.43e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446102024 4 EIKAPVfpesvaDGTIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEGDTVLSDEVI 73
Cdd:cd06850 1 EVTAPM------PGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLL 64
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
17-73 |
1.06e-03 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 40.98 E-value: 1.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446102024 17 GTIATWHKKVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEGDTVLSDEVI 73
Cdd:PRK09282 531 GTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVL 587
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
25-73 |
5.39e-03 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 36.80 E-value: 5.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 446102024 25 KVGEPVSRDEVICDIETDKVVLEVVAPADGSLVAIIKGEGDTVLSDEVI 73
Cdd:COG0511 84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPL 132
|
|
| |
