|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
1-543 |
0e+00 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 920.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 1 MALLLRHSRKLRRVHGVLDCERGSIARHFSASACSTtLKKEDGVSNSSLEYGKkagslsisqDRKSGKDTHKFKVSPQEA 80
Cdd:PLN02744 3 ASRIINHSKKLRNVSNLLRREHAALVRYFSNSTRSS-LGKGDDIAKRRGYPPL---------ERRSQPKVSSLGLFGSNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 81 RGLYSSNRVLISATGVNSLFSCGQVVLARHFSSAADLPAHEEIGMPSLSPTMTEGNIARWVKKEGDKVSPGEVLCEVETD 160
Cdd:PLN02744 73 SRTARKNGSPMTGSGLFKSLSSSQMQSARGFSSSSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 161 KATVEMECMEEGYLAKIVCGDGAKEIKVGEIIAITVEEEGDIEKFKDYKAPASSAAPaESKPQSESTEPKGEEKELP-KA 239
Cdd:PLN02744 153 KATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAITVEEEEDIGKFKDYKPSSSAAPA-APKAKPSPPPPKEEEVEKPaSS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 240 AEPKATKTEESSHSGDRVFSSPIARKLAEDNNVPLSSLKGTGPDGRILKADIEEYLSSEAKGTKKEA---AAAPGLGHVD 316
Cdd:PLN02744 232 PEPKASKPSAPPSSGDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPstdSKAPALDYTD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 317 LPNSQIRKVTANRLLKSKQTIPHYYLTVDSRVDELIKLRSELNPLQDASGGKKISINDLVIKAAALALRKVPECNSSWMN 396
Cdd:PLN02744 312 IPNTQIRKVTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 397 DFIRQYHNVNINVAVQTEHGLFVPVVRDADKKGLATIADEVKQLALRARDNSLKPEDYEGGTFTVSNLGGPFGIKQFCAI 476
Cdd:PLN02744 392 DYIRQYHNVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGPFGIKQFCAI 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 357110950 477 VNPPQAAILAIGSAEKRVIPGT-DGQFEVGSFMSATLSCDHRVIDGAIGAEWLKAFKGYLENPTTMLL 543
Cdd:PLN02744 472 INPPQSAILAVGSAEKRVIPGSgPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
122-543 |
0e+00 |
|
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: 548.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 122 EIGMPSLSPTMTEGNIARWVKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVCGDGAKEIKVGEIIAITVEEEGD 201
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 202 IEK-FKDYKAPASSAAPAESK---PQSESTEPKGEEKELPKAAEPKATKTEESSHSGDRVFSSPIARKLAEDNNVPLSSL 277
Cdd:TIGR01349 81 VADaFKNYKLESSASPAPKPSeiaPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 278 KGTGPDGRILKADIEEYLSSE---------AKGTKKEAAAAPGLG--HVDLPNSQIRKVTANRLLKSKQTIPHYYLTVDS 346
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQSpasanqqaaATTPATYPAAAPVSTgsYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIEC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 347 RVDELIKLRSELNPLqdASGGKKISINDLVIKAAALALRKVPECNSSWMNDFIRQYHNVNINVAVQTEHGLFVPVVRDAD 426
Cdd:TIGR01349 241 NVDKLLALRKELNAM--ASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNAD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 427 KKGLATIADEVKQLALRARDNSLKPEDYEGGTFTVSNLgGPFGIKQFCAIVNPPQAAILAIGSAEKRVIP--GTDGQFEV 504
Cdd:TIGR01349 319 AKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNL-GMFGIKDFTAIINPPQACILAVGAVEDVAVVdnDEEKGFAV 397
|
410 420 430
....*....|....*....|....*....|....*....
gi 357110950 505 GSFMSATLSCDHRVIDGAIGAEWLKAFKGYLENPTTMLL 543
Cdd:TIGR01349 398 ASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
330-542 |
9.23e-99 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 297.53 E-value: 9.23e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 330 LLKSKQTIPHYYLTVDSRVDELIKLRSELNPlQDASGGKKISINDLVIKAAALALRKVPECNSSWMNDF--IRQYHNVNI 407
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKE-DAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 408 NVAVQTEHGLFVPVVRDADKKGLATIADEVKQLALRARDNSLKPEDYEGGTFTVSNLGGpFGIKQFCAIVNPPQAAILAI 487
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGM-FGVTFFTPIINPPQVAILGV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 357110950 488 GSAEKRVIPgTDGQFEVGSFMSATLSCDHRVIDGAIGAEWLKAFKGYLENPTTML 542
Cdd:pfam00198 159 GRIRKRPVV-VDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
122-194 |
3.29e-28 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 107.11 E-value: 3.29e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357110950 122 EIGMPSLSPTMTEGNIARWVKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVCGDGAKeIKVGEIIAI 194
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
121-194 |
5.75e-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: 98.22 E-value: 5.75e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357110950 121 EEIGMPSLSPTMTEGNIARWVKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVCGDGAKeIKVGEIIAI 194
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAV 75
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
1-543 |
0e+00 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 920.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 1 MALLLRHSRKLRRVHGVLDCERGSIARHFSASACSTtLKKEDGVSNSSLEYGKkagslsisqDRKSGKDTHKFKVSPQEA 80
Cdd:PLN02744 3 ASRIINHSKKLRNVSNLLRREHAALVRYFSNSTRSS-LGKGDDIAKRRGYPPL---------ERRSQPKVSSLGLFGSNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 81 RGLYSSNRVLISATGVNSLFSCGQVVLARHFSSAADLPAHEEIGMPSLSPTMTEGNIARWVKKEGDKVSPGEVLCEVETD 160
Cdd:PLN02744 73 SRTARKNGSPMTGSGLFKSLSSSQMQSARGFSSSSDLPPHQEIGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 161 KATVEMECMEEGYLAKIVCGDGAKEIKVGEIIAITVEEEGDIEKFKDYKAPASSAAPaESKPQSESTEPKGEEKELP-KA 239
Cdd:PLN02744 153 KATVEMECMEEGYLAKIVKGDGAKEIKVGEVIAITVEEEEDIGKFKDYKPSSSAAPA-APKAKPSPPPPKEEEVEKPaSS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 240 AEPKATKTEESSHSGDRVFSSPIARKLAEDNNVPLSSLKGTGPDGRILKADIEEYLSSEAKGTKKEA---AAAPGLGHVD 316
Cdd:PLN02744 232 PEPKASKPSAPPSSGDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIEDYLASGGKGATAPPstdSKAPALDYTD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 317 LPNSQIRKVTANRLLKSKQTIPHYYLTVDSRVDELIKLRSELNPLQDASGGKKISINDLVIKAAALALRKVPECNSSWMN 396
Cdd:PLN02744 312 IPNTQIRKVTASRLLQSKQTIPHYYLTVDTRVDKLMALRSQLNSLQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 397 DFIRQYHNVNINVAVQTEHGLFVPVVRDADKKGLATIADEVKQLALRARDNSLKPEDYEGGTFTVSNLGGPFGIKQFCAI 476
Cdd:PLN02744 392 DYIRQYHNVNINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGPFGIKQFCAI 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 357110950 477 VNPPQAAILAIGSAEKRVIPGT-DGQFEVGSFMSATLSCDHRVIDGAIGAEWLKAFKGYLENPTTMLL 543
Cdd:PLN02744 472 INPPQSAILAVGSAEKRVIPGSgPDQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
122-543 |
0e+00 |
|
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: 548.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 122 EIGMPSLSPTMTEGNIARWVKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVCGDGAKEIKVGEIIAITVEEEGD 201
Cdd:TIGR01349 1 KITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDVPVNKPIAVLVEEKED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 202 IEK-FKDYKAPASSAAPAESK---PQSESTEPKGEEKELPKAAEPKATKTEESSHSGDRVFSSPIARKLAEDNNVPLSSL 277
Cdd:TIGR01349 81 VADaFKNYKLESSASPAPKPSeiaPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 278 KGTGPDGRILKADIEEYLSSE---------AKGTKKEAAAAPGLG--HVDLPNSQIRKVTANRLLKSKQTIPHYYLTVDS 346
Cdd:TIGR01349 161 AGSGPNGRIVKKDIESFVPQSpasanqqaaATTPATYPAAAPVSTgsYEDVPLSNIRKIIAKRLLESKQTIPHYYVSIEC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 347 RVDELIKLRSELNPLqdASGGKKISINDLVIKAAALALRKVPECNSSWMNDFIRQYHNVNINVAVQTEHGLFVPVVRDAD 426
Cdd:TIGR01349 241 NVDKLLALRKELNAM--ASEVYKLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNAD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 427 KKGLATIADEVKQLALRARDNSLKPEDYEGGTFTVSNLgGPFGIKQFCAIVNPPQAAILAIGSAEKRVIP--GTDGQFEV 504
Cdd:TIGR01349 319 AKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNL-GMFGIKDFTAIINPPQACILAVGAVEDVAVVdnDEEKGFAV 397
|
410 420 430
....*....|....*....|....*....|....*....
gi 357110950 505 GSFMSATLSCDHRVIDGAIGAEWLKAFKGYLENPTTMLL 543
Cdd:TIGR01349 398 ASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
122-543 |
3.64e-162 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 467.35 E-value: 3.64e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 122 EIGMPSLSPTMTEGNIARWVKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVCGDGAKeIKVGEIIAiTVEEEGD 201
Cdd:PRK11856 4 EFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDV-VPVGSVIA-VIEEEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 202 IEkfkdykapassaAPAESKPQSESTEPKGEEKELPKAAEPKATKTEESSHSGDRVFSSPIARKLAEDNNVPLSSLKGTG 281
Cdd:PRK11856 82 AE------------AAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 282 PDGRILKADIEEYLSSEAK----GTKKEAAAAPGLGHVD--LPNSQIRKVTANRLLKSKQTIPHYYLTVDSRVDELIKLR 355
Cdd:PRK11856 150 PGGRITKEDVEAAAAAAAPaaaaAAAAAAAPPAAAAEGEerVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 356 SELNPlqdasGGKKISINDLVIKAAALALRKVPECNSSWMNDFIRQYHNVNINVAVQTEHGLFVPVVRDADKKGLATIAD 435
Cdd:PRK11856 230 KQLKA-----IGVKLTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 436 EVKQLALRARDNSLKPEDYEGGTFTVSNLGGpFGIKQFCAIVNPPQAAILAIGSAEKRVIPgTDGQFEVGSFMSATLSCD 515
Cdd:PRK11856 305 EIKDLAEKAREGKLKPEELQGGTFTISNLGM-FGGDYFTPIINPPEVAILGVGAIVERPVV-VDGEIVVRKVMPLSLSFD 382
|
410 420
....*....|....*....|....*...
gi 357110950 516 HRVIDGAIGAEWLKAFKGYLENPTTMLL 543
Cdd:PRK11856 383 HRVIDGADAARFLKALKELLENPALLLL 410
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
330-542 |
9.23e-99 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 297.53 E-value: 9.23e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 330 LLKSKQTIPHYYLTVDSRVDELIKLRSELNPlQDASGGKKISINDLVIKAAALALRKVPECNSSWMNDF--IRQYHNVNI 407
Cdd:pfam00198 1 MTESKQTIPHFTLTDEVDVTELLALREELKE-DAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEgeIVYKKYVNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 408 NVAVQTEHGLFVPVVRDADKKGLATIADEVKQLALRARDNSLKPEDYEGGTFTVSNLGGpFGIKQFCAIVNPPQAAILAI 487
Cdd:pfam00198 80 GIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGM-FGVTFFTPIINPPQVAILGV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 357110950 488 GSAEKRVIPgTDGQFEVGSFMSATLSCDHRVIDGAIGAEWLKAFKGYLENPTTML 542
Cdd:pfam00198 159 GRIRKRPVV-VDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
133-543 |
2.08e-91 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 290.19 E-value: 2.08e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 133 TEGNIARWVKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIvcgdgakEIKVGEiiaiTVEEEGDIEKFKDYKAPA 212
Cdd:PRK11855 131 TEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEI-------KVKVGD----KVSVGSLLVVIEVAAAAP 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 213 SSAAPAESKPQSESTEPKGEEKELPKAAEPKATKTEESShSGDRVFSSPIARKLAEDNNVPLSSLKGTGPDGRILKADIE 292
Cdd:PRK11855 200 AAAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAAAA-PGKAPHASPAVRRLARELGVDLSQVKGTGKKGRITKEDVQ 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 293 EYLSSEAKGTKKEAAAAPGLGH----------VDL---------PNSQIRKVTANRLLKSKQTIPHYYLTVDSRVDELIK 353
Cdd:PRK11855 279 AFVKGAMSAAAAAAAAAAAAGGgglgllpwpkVDFskfgeietkPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEA 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 354 LRSELNPlQDASGGKKISINDLVIKAAALALRKVPECNSSWMND----FIRQYHNvnINVAVQTEHGLFVPVVRDADKKG 429
Cdd:PRK11855 359 LRKQLKK-EAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDgdelTYKKYFN--IGFAVDTPNGLVVPVIKDVDKKS 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 430 LATIADEVKQLALRARDNSLKPEDYEGGTFTVSNLGGpFGIKQFCAIVNPPQAAILAIGSAEKRVIPGtDGQFEVGSFMS 509
Cdd:PRK11855 436 LLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGG-IGGTAFTPIINAPEVAILGVGKSQMKPVWD-GKEFVPRLMLP 513
|
410 420 430
....*....|....*....|....*....|....
gi 357110950 510 ATLSCDHRVIDGAIGAEWLKAFKGYLENPTTMLL 543
Cdd:PRK11855 514 LSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
122-543 |
4.83e-83 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 264.00 E-value: 4.83e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 122 EIGMPSLSPTMTEGNIARWVKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVCGDGAKeIKVGEIIAItVEEEGd 201
Cdd:PRK05704 4 EIKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDT-VTVGQVLGR-IDEGA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 202 iekfkdykapassaapaeSKPQSESTEPKGEEKELPKAAEPKATKTEESSHSgdrvfSSPIARKLAEDNNVPLSSLKGTG 281
Cdd:PRK05704 81 ------------------AAGAAAAAAAAAAAAAAAPAQAQAAAAAEQSNDA-----LSPAARKLAAENGLDASAVKGTG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 282 PDGRILKADIEEYLSSEAKGTKKEAAAAP-----GLGH---VDLPNSQIRKVTANRLLKSKQTIPhyYLTVDSRVD--EL 351
Cdd:PRK05704 138 KGGRVTKEDVLAALAAAAAAPAAPAAAAPaaapaPLGArpeERVPMTRLRKTIAERLLEAQNTTA--MLTTFNEVDmtPV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 352 IKLRSELNPLQDASGGKKISINDLVIKAAALALRKVPECNSSWM-NDFIrqYHN-VNINVAVQTEHGLFVPVVRDADKKG 429
Cdd:PRK05704 216 MDLRKQYKDAFEKKHGVKLGFMSFFVKAVVEALKRYPEVNASIDgDDIV--YHNyYDIGIAVGTPRGLVVPVLRDADQLS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 430 LATIADEVKQLALRARDNSLKPEDYEGGTFTVSNlGGPFGIKQFCAIVNPPQAAILAIGSAEKR--VIpgtDGQFEVGSF 507
Cdd:PRK05704 294 FAEIEKKIAELAKKARDGKLSIEELTGGTFTITN-GGVFGSLMSTPIINPPQSAILGMHKIKERpvAV---NGQIVIRPM 369
|
410 420 430
....*....|....*....|....*....|....*.
gi 357110950 508 MSATLSCDHRVIDGAIGAEWLKAFKGYLENPTTMLL 543
Cdd:PRK05704 370 MYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLL 405
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
122-543 |
5.61e-81 |
|
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: 258.90 E-value: 5.61e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 122 EIGMPSLSPTMTEGNIARWVKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVCGDGAKeIKVGEIIAItVEEEGD 201
Cdd:TIGR01347 2 EIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDT-VESGQVLAI-LEEGND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 202 iekfkdykapassaapaeskPQSESTEPKGEEKELPKAAEPKATKTEEsshsGDRVFSSPIARKLAEDNNVPLSSLKGTG 281
Cdd:TIGR01347 80 --------------------ATAAPPAKSGEEKEETPAASAAAAPTAA----ANRPSLSPAARRLAKEHGIDLSAVPGTG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 282 PDGRILKADIEEYLSSEAKGTKKEAAAAPGLGHVDL------PNSQIRKVTANRLLKSKQTIPhyYLTVDSRVD--ELIK 353
Cdd:TIGR01347 136 VTGRVTKEDIIKKTEAPASAQPPAAAAAAAAPAAATrpeervKMTRLRQRIAERLKEAQNSTA--MLTTFNEVDmsAVME 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 354 LRSELNPLQDASGGKKISINDLVIKAAALALRKVPECNSSWMNDFIRQYHNVNINVAVQTEHGLFVPVVRDADKKGLATI 433
Cdd:TIGR01347 214 LRKRYKEEFEKKHGVKLGFMSFFVKAVVAALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 434 ADEVKQLALRARDNSLKPEDYEGGTFTVSNlGGPFGIKQFCAIVNPPQAAILAIGSAEKRVIpGTDGQFEVGSFMSATLS 513
Cdd:TIGR01347 294 EKEIADLGKKARDGKLTLEDMTGGTFTITN-GGVFGSLMSTPIINPPQSAILGMHGIKERPV-AVNGQIEIRPMMYLALS 371
|
410 420 430
....*....|....*....|....*....|
gi 357110950 514 CDHRVIDGAIGAEWLKAFKGYLENPTTMLL 543
Cdd:TIGR01347 372 YDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
112-543 |
3.61e-73 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 244.91 E-value: 3.61e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 112 SSAADLPAHEEIGMPSLSptMTEGNIARWVKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVCGDGAKeIKVGEI 191
Cdd:PRK11854 198 AAPAAAAGVKDVNVPDIG--GDEVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK-VKTGSL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 192 IAitveeegdieKFKDYKAPASSAAPAESKPQSESTEPKGEEKELPKAAEPKATktEESSHSGDRVFSSPIARKLAEDNN 271
Cdd:PRK11854 275 IM----------RFEVEGAAPAAAPAKQEAAAPAPAAAKAEAPAAAPAAKAEGK--SEFAENDAYVHATPLVRRLAREFG 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 272 VPLSSLKGTGPDGRILKADIEEYLSSEAKGTKKEAAAAP----GLGHVDLPN--------------SQIRKVTANRLLKS 333
Cdd:PRK11854 343 VNLAKVKGTGRKGRILKEDVQAYVKDAVKRAEAAPAAAAagggGPGLLPWPKvdfskfgeieevelGRIQKISGANLHRN 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 334 KQTIPHyyLTVDSRVD--ELIKLRSELN-PLQDASGGKKISINDLVIKAAALALRKVPECNSSWMNDFIR-QYHN-VNIN 408
Cdd:PRK11854 423 WVMIPH--VTQFDKADitELEAFRKQQNaEAEKRKLGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRlTLKKyVNIG 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 409 VAVQTEHGLFVPVVRDADKKGLATIADEVKQLALRARDNSLKPEDYEGGTFTVSNLGGpFGIKQFCAIVNPPQAAILAIG 488
Cdd:PRK11854 501 IAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGG-LGTTHFTPIVNAPEVAILGVS 579
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 357110950 489 SAEKRviPGTDGQ-FEVGSFMSATLSCDHRVIDGAIGAEWLKAFKGYLENPTTMLL 543
Cdd:PRK11854 580 KSAME--PVWNGKeFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSDIRRLVL 633
|
|
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
139-543 |
6.22e-68 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 224.98 E-value: 6.22e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 139 RWVKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVCGDGAKeIKVGE-IIAITVEEEGDIEkfkdykapassaap 217
Cdd:PLN02528 17 RWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDI-VKVGEtLLKIMVEDSQHLR-------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 218 aeskpqSESTEPKGEEKELPKAAEPKAtktEESSHSGdrVFSSPIARKLAEDNNVPLSSLKGTGPDGRILKADIEEYLSS 297
Cdd:PLN02528 82 ------SDSLLLPTDSSNIVSLAESDE---RGSNLSG--VLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYAAQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 298 eaKGTKKEAaaaPGLGHVDLP--------------NSQIRKVTA----NRLLKSKQT----IPHYYLTVDSRVDELIKLR 355
Cdd:PLN02528 151 --KGVVKDS---SSAEEATIAeqeefstsvstpteQSYEDKTIPlrgfQRAMVKTMTaaakVPHFHYVEEINVDALVELK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 356 SELNPLQdASGGKKISINDLVIKAAALALRKVPECNSSWMNDF--IRQYHNVNINVAVQTEHGLFVPVVRDADKKGLATI 433
Cdd:PLN02528 226 ASFQENN-TDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETseIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 434 ADEVKQLALRARDNSLKPEDYEGGTFTVSNLG---GPFGikqfCAIVNPPQAAILAIGSAEKRVIPGTDGQFEVGSFMSA 510
Cdd:PLN02528 305 TKELSRLQHLAAENKLNPEDITGGTITLSNIGaigGKFG----SPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTV 380
|
410 420 430
....*....|....*....|....*....|...
gi 357110950 511 TLSCDHRVIDGAIGAEWLKAFKGYLENPTTMLL 543
Cdd:PLN02528 381 TIGADHRVLDGATVARFCNEWKSYVEKPELLML 413
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
89-543 |
2.10e-67 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 223.79 E-value: 2.10e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 89 VLISATGVNSLFS--CGQVVLARHFSSAADlpAHEEIGMPSLSPTMTEGNIARWVKKEGDKVSPGEVLCEVETDKATVEM 166
Cdd:PTZ00144 13 LLSSVKGMFRRFSlrKLQPACSAHFSKSYF--SIKVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 167 ECMEEGYLAKIVCGDGAKeIKVG-EIIAITVEEEGDIEKFKDYKAPASSAAPAESKPQSESTEPKGEEKELPKAAEPKAT 245
Cdd:PTZ00144 91 RAPASGVITKIFAEEGDT-VEVGaPLSEIDTGGAPPAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 246 KTEESShsgdRVFSSPIARKLAEDNNVPLSSlkgtgpdgrilkadieeylsseakgtkkeaaaapglghvdlpnsqIRKV 325
Cdd:PTZ00144 170 EPAPAA----KPPPTPVARADPRETRVPMSR---------------------------------------------MRQR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 326 TANRLLKSKQTIPhyYLTVDSRVD--ELIKLRSELNPLQDASGGKKISINDLVIKAAALALRKVPECNSSWMNDFIRQYH 403
Cdd:PTZ00144 201 IAERLKASQNTCA--MLTTFNECDmsALMELRKEYKDDFQKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRN 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 404 NVNINVAVQTEHGLFVPVVRDADKKGLATIADEVKQLALRARDNSLKPEDYEGGTFTVSNlGGPFGIKQFCAIVNPPQAA 483
Cdd:PTZ00144 279 YVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISN-GGVFGSLMGTPIINPPQSA 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 484 ILAIGSAEKRVIPGTDgQFEVGSFMSATLSCDHRVIDGAIGAEWLKAFKGYLENPTTMLL 543
Cdd:PTZ00144 358 ILGMHAIKKRPVVVGN-EIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLL 416
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
113-543 |
1.28e-62 |
|
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: 214.74 E-value: 1.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 113 SAADLPAHEEIGMPSLSpTMTEGNIARWVKKEGDKVSPGEVLCEVETDKATVEMECMEEGYL--AKIVCGDgakEIKVGE 190
Cdd:TIGR01348 109 AAGQSSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVksVKVKVGD---SVPTGD 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 191 IIaITVEEEGdiekfkdykaPASSAAPAESKPQSESTEPKGEEKELPKA-----AEPKATKTEESSHSGDRVFSSPIARK 265
Cdd:TIGR01348 185 LI-LTLSVAG----------STPATAPAPASAQPAAQSPAATQPEPAAApaaakAQAPAPQQAGTQNPAKVDHAAPAVRR 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 266 LAEDNNVPLSSLKGTGPDGRILKADIEEYLSSEAKGTKKEAAAA--PGLGHVDLPN--------------SQIRKVTANR 329
Cdd:TIGR01348 254 LAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQAAAASAagGAPGALPWPNvdfskfgeveevdmSRIRKISGAN 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 330 LLKSKQTIPHYYLTVDSRVDELIKLRSELNPLQDASGGKkISINDLVIKAAALALRKVPECNSSWMND----FIRQYhnV 405
Cdd:TIGR01348 334 LTRNWTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVK-LTVLHILMKAVAAALKKFPKFNASLDLGgeqlILKKY--V 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 406 NINVAVQTEHGLFVPVVRDADKKGLATIADEVKQLALRARDNSLKPEDYEGGTFTVSNLGGpFGIKQFCAIVNPPQAAIL 485
Cdd:TIGR01348 411 NIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGG-IGGTAFTPIVNAPEVAIL 489
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 357110950 486 aiGSAEKRVIPGTDG-QFEVGSFMSATLSCDHRVIDGAIGAEWLKAFKGYLENPTTMLL 543
Cdd:TIGR01348 490 --GVSKSGMEPVWNGkEFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
122-536 |
2.70e-61 |
|
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: 211.79 E-value: 2.70e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 122 EIGMPSLSPTMTEGNIARWVKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVCGDGaKEIKVGEIIAITveeeGD 201
Cdd:TIGR02927 128 EVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPED-DTVEVGTVLAII----GD 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 202 IEKFKDYKAPASSAAPAESKPQsESTEPKGEEKELPKAAEPKATKTEESSH--------SGDRV-FSSPIARKLAEDNNV 272
Cdd:TIGR02927 203 ANAAPAEPAEEEAPAPSEAGSE-PAPDPAARAPHAAPDPPAPAPAPAKTAApaaaapvsSGDSGpYVTPLVRKLAKDKGV 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 273 PLSSLKGTGPDGRILKADIEEYLSSE---AKGTKKEAAAA-------------PGLGHV---DLPNSQIRKVTANRLLKS 333
Cdd:TIGR02927 282 DLSTVKGTGVGGRIRKQDVLAAAKAAeeaRAAAAAPAAAAapaapaaaakpaePDTAKLrgtTQKMNRIRQITADKTIES 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 334 KQTIPHYYLTVDSRVDELIKLRSELNPLQDASGGKKISINDLVIKAAALALRKVPECNSSWMNDF--IRQYHNVNINVAV 411
Cdd:TIGR02927 362 LQTSAQLTQVHEVDMTRVAALRARAKNDFLEKNGVNLTFLPFFVQAVTEALKAHPNVNASYNAETkeVTYHDVEHVGIAV 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 412 QTEHGLFVPVVRDADKKGLATIADEVKQLALRARDNSLKPEDYEGGTFTVSNLGGPfGIKQFCAIVNPPQAAILAIGSAE 491
Cdd:TIGR02927 442 DTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSG-GALFDTPILNPPQAAILGTGAIV 520
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 357110950 492 KR--VIPGTDGQFEVG--SFMSATLSCDHRVIDGAIGAEWLKAFKGYLE 536
Cdd:TIGR02927 521 KRprVIKDEDGGESIAirSVCYLPLTYDHRLVDGADAGRFLTTIKKRLE 569
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
260-543 |
8.47e-54 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 185.49 E-value: 8.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 260 SPIARKLAEDNNVPLSSLKGTGPDGRILKADI---------EEYLSSEAKGTKKEAAA--APGLGHVD-LPNSQIRKVTA 327
Cdd:PRK14843 52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVlallpenieNDSIKSPAQIEKVEEVPdnVTPYGEIErIPMTPMRKVIA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 328 NRLLKSKQTIPHYYLTVDSRVDELIKLRSE-LNPLQDASGgKKISINDLVIKAAALALRKVPECNSSWMND--FIRQYHN 404
Cdd:PRK14843 132 QRMVESYLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATG-KKTTVTDLLSLAVVKTLMKHPYINASLTEDgkTIITHNY 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 405 VNINVAVQTEHGLFVPVVRDADKKGLATIADEVKQLALRARDNSLKPEDYEGGTFTVSNLgGPFGIKQFCAIVNPPQAAI 484
Cdd:PRK14843 211 VNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNL-GMFGVQSFGPIINQPNSAI 289
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 485 LAIGSA-EKRVIpgTDGQFEVGSFMSATLSCDHRVIDGAIGAEWLKAFKGYLENPTTMLL 543
Cdd:PRK14843 290 LGVSSTiEKPVV--VNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
256-538 |
1.75e-41 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 151.48 E-value: 1.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 256 RVFSSPIARKLAEDNNVPLSSLKGTGPDGRILKADIEEYLSS-----------------EAKGTKKEAAAAPGLGHVDLP 318
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSlksaptpaeaasvssaqQAAKTAAPAAAPPKLEGKREK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 319 NSQIRKVTANRLLKSKQTIPHYYLTVDSRVDELIKLRSE-LNPLQDASGgKKISINDLVIKAAALALRKVP-------EC 390
Cdd:PRK11857 81 VAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSvKDPVLKTEG-VKLTFLPFIAKAILIALKEFPifaakydEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 391 NSSwmndfIRQYHNVNINVAVQTEHGLFVPVVRDADKKGLATIADEVKQLALRARDNSLKPEDYEGGTFTVSN---LGGP 467
Cdd:PRK11857 160 TSE-----LVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNygsVGSL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357110950 468 FGIkqfcAIVNPPQAAILAIGSAEKRVIPgTDGQFEVGSFMSATLSCDHRVIDGAIGAEWLKAFKGYLENP 538
Cdd:PRK11857 235 YGV----PVINYPELAIAGVGAIIDKAIV-KNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
122-543 |
2.53e-39 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 149.14 E-value: 2.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 122 EIGMPSLSPTMTEGNIARWVKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVCGDGAkeikvgeiiaiTVEEEGD 201
Cdd:PLN02226 93 EAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGD-----------TVEPGTK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 202 IEKFKDYKAPASSAAPAESKPQSESTEPKgeekelPKAAEPKATKTEesshsgdrvfSSPIARKLAEDNNVPlsslkgtg 281
Cdd:PLN02226 162 VAIISKSEDAASQVTPSQKIPETTDPKPS------PPAEDKQKPKVE----------SAPVAEKPKAPSSPP-------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 282 pdgrilkadieeylssEAKGTKKEAAAAPGLGHVDLPNSQIRKVTANRLLKSKQTIPhyYLTVDSRVD--ELIKLRSELN 359
Cdd:PLN02226 218 ----------------PPKQSAKEPQLPPKERERRVPMTRLRKRVATRLKDSQNTFA--LLTTFNEVDmtNLMKLRSQYK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 360 PLQDASGGKKISINDLVIKAAALALRKVPECNSSWMNDFIRQYHNVNINVAVQTEHGLFVPVVRDADKKGLATIADEVKQ 439
Cdd:PLN02226 280 DAFYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTING 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 440 LALRARDNSLKPEDYEGGTFTVSNlGGPFGIKQFCAIVNPPQAAILAIGSAEKRVIPgTDGQFEVGSFMSATLSCDHRVI 519
Cdd:PLN02226 360 LAKKANEGTISIDEMAGGSFTVSN-GGVYGSLISTPIINPPQSAILGMHSIVSRPMV-VGGSVVPRPMMYVALTYDHRLI 437
|
410 420
....*....|....*....|....
gi 357110950 520 DGAIGAEWLKAFKGYLENPTTMLL 543
Cdd:PLN02226 438 DGREAVYFLRRVKDVVEDPQRLLL 461
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
122-248 |
5.74e-30 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 122.72 E-value: 5.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 122 EIGMPSLSPTMTEGNIARWVKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVCGDGAKEIKVGEIIAITVEEEGD 201
Cdd:PRK11892 4 EILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILVPEGTEGVKVNTPIAVLLEEGES 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 357110950 202 IEKFKDYKAPASSAAPAESKPQSESTEPKGEEKELPKAAEPKATKTE 248
Cdd:PRK11892 84 ASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAAD 130
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
122-194 |
3.29e-28 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 107.11 E-value: 3.29e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357110950 122 EIGMPSLSPTMTEGNIARWVKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVCGDGAKeIKVGEIIAI 194
Cdd:cd06849 2 EIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDT-VPVGQVIAV 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
121-194 |
5.75e-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: 98.22 E-value: 5.75e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357110950 121 EEIGMPSLSPTMTEGNIARWVKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVCGDGAKeIKVGEIIAI 194
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDT-VPVGAVIAV 75
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
122-199 |
3.71e-16 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 80.37 E-value: 3.71e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 357110950 122 EIGMPSLSPTMTEGNIARWVKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVCGDGaKEIKVGEIIAITVEEE 199
Cdd:PRK14875 4 PITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEG-ETLPVGALLAVVADAE 80
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
121-194 |
1.14e-15 |
|
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: 71.86 E-value: 1.14e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357110950 121 EEIGMPSLSPTMTEGnIARWVKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVCGDGAKeIKVGEIIAI 194
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDT-VEVGDPLAK 72
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
122-184 |
3.43e-14 |
|
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: 67.47 E-value: 3.43e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357110950 122 EIGMPSLSPTMTEGNIARWVKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVCGDGAK 184
Cdd:cd06663 1 TILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTK 63
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
257-292 |
1.72e-13 |
|
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: 64.24 E-value: 1.72e-13
10 20 30
....*....|....*....|....*....|....*.
gi 357110950 257 VFSSPIARKLAEDNNVPLSSLKGTGPDGRILKADIE 292
Cdd:pfam02817 1 VLASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
359-529 |
1.16e-09 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 61.44 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 359 NPLQDASGGKkISINDLVIKAAALALRKVPECNSSWMND----FIRQYHNVNINVA--VQTEHG---LFVPVVRDADKKG 429
Cdd:PRK12270 160 NHLKRTRGGK-VSFTHLIGYALVQALKAFPNMNRHYAEVdgkpTLVTPAHVNLGLAidLPKKDGsrqLVVPAIKGAETMD 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357110950 430 LATIADEVKQLALRARDNSLKPEDYEGGTFTVSNLGGpFGIKQFCAIVNPPQAAILAIGS----AEKRVI-PGTDGQFEV 504
Cdd:PRK12270 239 FAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGG-IGTVHSVPRLMKGQGAIIGVGAmeypAEFQGAsEERLAELGI 317
|
170 180
....*....|....*....|....*
gi 357110950 505 GSFMSATLSCDHRVIDGAIGAEWLK 529
Cdd:PRK12270 318 SKVMTLTSTYDHRIIQGAESGEFLR 342
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
135-194 |
9.62e-04 |
|
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: 37.78 E-value: 9.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357110950 135 GNIARWVKKEGDKVSPGEVLCEVETDKatveMEcME-----EGYLAKIVCGDGAKeIKVGEIIAI 194
Cdd:cd06850 8 GTVVKVLVKEGDKVEAGQPLAVLEAMK----ME-NEvtapvAGVVKEILVKEGDQ-VEAGQLLVV 66
|
|
| |
