|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
52-506 |
5.02e-157 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 453.02 E-value: 5.02e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 52 VLLADIGEGIVECEVIQWFVQPGARVEEFSPLCEVQSDKASVEITSRFAGVVKKLYYEAGDMAKVGKPFVDIDIEGGAVD 131
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 132 QVDSAAKPDaetpaapvekadedviqqDSKSDVPLTAEEQRRLRIREnnrAIATPAVRHLSKELNVDILQIQGTGKDGRV 211
Cdd:PLN02528 81 RSDSLLLPT------------------DSSNIVSLAESDERGSNLSG---VLSTPAVRHLAKQYGIDLNDILGTGKDGRV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 212 LKEDIYKFVQQR-------NAGAQTPAAPQISPSASTAQPSQQQEETVVQLTNTQVQMFKAMTRSLTIPHFLYTDEIDFT 284
Cdd:PLN02528 140 LKEDVLKYAAQKgvvkdssSAEEATIAEQEEFSTSVSTPTEQSYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 285 NISDLRTRLNkvlattakvstggngtvipsgQSQQDLVAKLSYLPFIIKAVSMALYKYPILNARVDVDPTTekpVVVHRS 364
Cdd:PLN02528 220 ALVELKASFQ---------------------ENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSE---IRLKGS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 365 qHNIGVAMDTPQGLLVPVIKDVGSLNILSIAAELTRLQALAYAGKLTPRDITGGTITVSNIGNIGGTYLSPVIVEKEVAI 444
Cdd:PLN02528 276 -HNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAI 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027062764 445 LGVGRMRAVPAFDEAGNVVKKQVCNFSWSADHRVVDGATMARAAEVVRAVVEEPDVMVMHLR 506
Cdd:PLN02528 355 IALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLMLHMR 416
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
266-501 |
1.57e-82 |
|
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: 254.78 E-value: 1.57e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 266 MTRSL-TIPHFLYTDEIDFTNISDLRTRLNKVLATTAKvstggngtvipsgqsqqdlvaKLSYLPFIIKAVSMALYKYPI 344
Cdd:pfam00198 1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEET---------------------KLTFLPFLVKAVALALKKFPE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 345 LNARVDvdptTEKPVVVHRSQHNIGVAMDTPQGLLVPVIKDVGSLNILSIAAELTRLQALAYAGKLTPRDITGGTITVSN 424
Cdd:pfam00198 60 LNASWD----GEEGEIVYKKYVNIGIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISN 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027062764 425 IGNIGGTYLSPVIVEKEVAILGVGRMRAVPAFdEAGNVVKKQVCNFSWSADHRVVDGATMARAAEVVRAVVEEPDVM 501
Cdd:pfam00198 136 LGMFGVTFFTPIINPPQVAILGVGRIRKRPVV-VDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
27-503 |
2.32e-70 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 234.00 E-value: 2.32e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 27 AALAASAGGPSRWFH-----ETRRQQTVKPVLLADIGeGIVECEVIQWFVQPGARVEEFSPLCEVQSDKASVEITSRFAG 101
Cdd:TIGR01348 89 AAPAPTAGAPAPAAQaqaapAAGQSSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 102 VVKKLYYEAGDMAKVGKPFVDIDIEGgavdqvdsAAKPDAETPAAPVEKADEDVIQQDSKSDVPLTAEEQRRLRIRENNR 181
Cdd:TIGR01348 168 VVKSVKVKVGDSVPTGDLILTLSVAG--------STPATAPAPASAQPAAQSPAATQPEPAAAPAAAKAQAPAPQQAGTQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 182 -----AIATPAVRHLSKELNVDILQIQGTGKDGRVLKEDIYKFVQQRNAGAQTPAAPQISPSASTAQ-P----SQQQEET 251
Cdd:TIGR01348 240 npakvDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQAAAASAAGGAPGALPwPnvdfSKFGEVE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 252 VVQLTNTQVQMFKAMTRS-LTIPHFLYTDEIDFTNISDLRTRLNkvlatTAKVSTGGngtvipsgqsqqdlvaKLSYLPF 330
Cdd:TIGR01348 320 EVDMSRIRKISGANLTRNwTMIPHVTHFDKADITEMEAFRKQQN-----AAVEKEGV----------------KLTVLHI 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 331 IIKAVSMALYKYPILNARVDVDPTTekpvVVHRSQHNIGVAMDTPQGLLVPVIKDVGSLNILSIAAELTRLQALAYAGKL 410
Cdd:TIGR01348 379 LMKAVAAALKKFPKFNASLDLGGEQ----LILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 411 TPRDITGGTITVSNIGNIGGTYLSPVIVEKEVAILGVGRMRAVPAFDEAgNVVKKQVCNFSWSADHRVVDGATMARAAEV 490
Cdd:TIGR01348 455 TPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGK-EFEPRLMLPLSLSYDHRVIDGADAARFTTY 533
|
490
....*....|...
gi 1027062764 491 VRAVVEEPDVMVM 503
Cdd:TIGR01348 534 ICESLADIRRLLL 546
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
50-123 |
5.43e-24 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 95.16 E-value: 5.43e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027062764 50 KPVLLADIGEGIVECEVIQWFVQPGARVEEFSPLCEVQSDKASVEITSRFAGVVKKLYYEAGDMAKVGKPFVDI 123
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
50-123 |
6.84e-21 |
|
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: 86.66 E-value: 6.84e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027062764 50 KPVLLADIGEGIVECEVIQWFVQPGARVEEFSPLCEVQSDKASVEITSRFAGVVKKLYYEAGDMAKVGKPFVDI 123
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
52-506 |
5.02e-157 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 453.02 E-value: 5.02e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 52 VLLADIGEGIVECEVIQWFVQPGARVEEFSPLCEVQSDKASVEITSRFAGVVKKLYYEAGDMAKVGKPFVDIDIEGGAVD 131
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 132 QVDSAAKPDaetpaapvekadedviqqDSKSDVPLTAEEQRRLRIREnnrAIATPAVRHLSKELNVDILQIQGTGKDGRV 211
Cdd:PLN02528 81 RSDSLLLPT------------------DSSNIVSLAESDERGSNLSG---VLSTPAVRHLAKQYGIDLNDILGTGKDGRV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 212 LKEDIYKFVQQR-------NAGAQTPAAPQISPSASTAQPSQQQEETVVQLTNTQVQMFKAMTRSLTIPHFLYTDEIDFT 284
Cdd:PLN02528 140 LKEDVLKYAAQKgvvkdssSAEEATIAEQEEFSTSVSTPTEQSYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 285 NISDLRTRLNkvlattakvstggngtvipsgQSQQDLVAKLSYLPFIIKAVSMALYKYPILNARVDVDPTTekpVVVHRS 364
Cdd:PLN02528 220 ALVELKASFQ---------------------ENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSE---IRLKGS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 365 qHNIGVAMDTPQGLLVPVIKDVGSLNILSIAAELTRLQALAYAGKLTPRDITGGTITVSNIGNIGGTYLSPVIVEKEVAI 444
Cdd:PLN02528 276 -HNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAI 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027062764 445 LGVGRMRAVPAFDEAGNVVKKQVCNFSWSADHRVVDGATMARAAEVVRAVVEEPDVMVMHLR 506
Cdd:PLN02528 355 IALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLMLHMR 416
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
25-503 |
4.89e-136 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 404.20 E-value: 4.89e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 25 TKAALAASAGGpsrwfhetrrqqtVKPVLLADIGEgIVECEVIQWFVQPGARVEEFSPLCEVQSDKASVEITSRFAGVVK 104
Cdd:PRK11855 108 PAAAAAAAGGG-------------VVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 105 KLYYEAGDMAKVGKPFVDIDIEGGAVDqvdSAAKPDAETPAAPVEKADEDVIQQDSKSDVPLTAEEqrrlrIRENNRAIA 184
Cdd:PRK11855 174 EIKVKVGDKVSVGSLLVVIEVAAAAPA---AAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAA-----AAPGKAPHA 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 185 TPAVRHLSKELNVDILQIQGTGKDGRVLKEDIYKFVQQRNAGAQTPAAPQISPSASTAQP--------SQQQEETVVQLT 256
Cdd:PRK11855 246 SPAVRRLARELGVDLSQVKGTGKKGRITKEDVQAFVKGAMSAAAAAAAAAAAAGGGGLGLlpwpkvdfSKFGEIETKPLS 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 257 NTQVQMFKAMTRSL-TIPHFLYTDEIDFTNISDLRTRLNKVlATTAKVstggngtvipsgqsqqdlvaKLSYLPFIIKAV 335
Cdd:PRK11855 326 RIKKISAANLHRSWvTIPHVTQFDEADITDLEALRKQLKKE-AEKAGV--------------------KLTMLPFFIKAV 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 336 SMALYKYPILNARVDVDpTTEkpvVVHRSQHNIGVAMDTPQGLLVPVIKDVGSLNILSIAAELTRLQALAYAGKLTPRDI 415
Cdd:PRK11855 385 VAALKEFPVFNASLDED-GDE---LTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDM 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 416 TGGTITVSNIGNIGGTYLSPVIVEKEVAILGVGRMRAVPaFDEAGNVVKKQVCNFSWSADHRVVDGATMARAAEVVRAVV 495
Cdd:PRK11855 461 QGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKP-VWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLL 539
|
....*...
gi 1027062764 496 EEPDVMVM 503
Cdd:PRK11855 540 ADPRRMLL 547
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
52-504 |
4.43e-119 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 356.02 E-value: 4.43e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 52 VLLADIGEGIVECEVIQWFVQPGARVEEFSPLCEVQSDKASVEITSRFAGVVKKLYYEAGDMAKVGKPFVDIDiEGGAVD 131
Cdd:PRK11856 5 FKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIE-EEGEAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 132 QVDSAAKPDAETPAAPVEKADEDVIQQDSKSDVPLTAEEQrrlrirennRAIATPAVRHLSKELNVDILQIQGTGKDGRV 211
Cdd:PRK11856 84 AAAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAAPAAA---------AAKASPAVRKLARELGVDLSTVKGSGPGGRI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 212 LKEDIYKFvqqrnAGAQTPAAPQISPSASTAQPSQQQEETVVQLTNTQVQMFKAMTRS-LTIPHFLYTDEIDFTNISDLR 290
Cdd:PRK11856 155 TKEDVEAA-----AAAAAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESkREIPHFTLTDEVDVTALLALR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 291 TRLNKVlattakvstggngtvipsgqsqqdlVAKLSYLPFIIKAVSMALYKYPILNARVDVDPttekpvVVHRSQHNIGV 370
Cdd:PRK11856 230 KQLKAI-------------------------GVKLTVTDFLIKAVALALKKFPELNASWDDDA------IVLKKYVNIGI 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 371 AMDTPQGLLVPVIKDVGSLNILSIAAELTRLQALAYAGKLTPRDITGGTITVSNIGNIGGTYLSPVIVEKEVAILGVGRM 450
Cdd:PRK11856 279 AVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAI 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1027062764 451 RAVPAFDEaGNVVKKQVCNFSWSADHRVVDGATMARAAEVVRAVVEEPDVMVMH 504
Cdd:PRK11856 359 VERPVVVD-GEIVVRKVMPLSLSFDHRVIDGADAARFLKALKELLENPALLLLE 411
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
266-501 |
1.57e-82 |
|
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: 254.78 E-value: 1.57e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 266 MTRSL-TIPHFLYTDEIDFTNISDLRTRLNKVLATTAKvstggngtvipsgqsqqdlvaKLSYLPFIIKAVSMALYKYPI 344
Cdd:pfam00198 1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEET---------------------KLTFLPFLVKAVALALKKFPE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 345 LNARVDvdptTEKPVVVHRSQHNIGVAMDTPQGLLVPVIKDVGSLNILSIAAELTRLQALAYAGKLTPRDITGGTITVSN 424
Cdd:pfam00198 60 LNASWD----GEEGEIVYKKYVNIGIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISN 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027062764 425 IGNIGGTYLSPVIVEKEVAILGVGRMRAVPAFdEAGNVVKKQVCNFSWSADHRVVDGATMARAAEVVRAVVEEPDVM 501
Cdd:pfam00198 136 LGMFGVTFFTPIINPPQVAILGVGRIRKRPVV-VDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELL 211
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
27-503 |
2.59e-79 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 259.93 E-value: 2.59e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 27 AALAASAGGPSrwfhetrrqqtVKPVLLADIGEGivECEVIQWFVQPGARVEEFSPLCEVQSDKASVEITSRFAGVVKKL 106
Cdd:PRK11854 195 APAAAPAAAAG-----------VKDVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 107 YYEAGDMAKVGKPFVDIDIEGGAvdQVDSAAKPDAETPAAPVEKADEdviqqdsKSDVPLTAEEQRRLRIRENNRAIATP 186
Cdd:PRK11854 262 KVNVGDKVKTGSLIMRFEVEGAA--PAAAPAKQEAAAPAPAAAKAEA-------PAAAPAAKAEGKSEFAENDAYVHATP 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 187 AVRHLSKELNVDILQIQGTGKDGRVLKEDIYKFVQQRNAGAQTPAAPQISPSA-------STAQPSQQQEETVVQLTNTQ 259
Cdd:PRK11854 333 LVRRLAREFGVNLAKVKGTGRKGRILKEDVQAYVKDAVKRAEAAPAAAAAGGGgpgllpwPKVDFSKFGEIEEVELGRIQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 260 VQMFKAMTRSL-TIPHFLYTDEIDFTNISDLRTRLNKVLAttakvstggngtvipsgqsQQDLVAKLSYLPFIIKAVSMA 338
Cdd:PRK11854 413 KISGANLHRNWvMIPHVTQFDKADITELEAFRKQQNAEAE-------------------KRKLGVKITPLVFIMKAVAAA 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 339 LYKYPILNARVDVDptTEKpvVVHRSQHNIGVAMDTPQGLLVPVIKDVGSLNILSIAAELTRLQALAYAGKLTPRDITGG 418
Cdd:PRK11854 474 LEQMPRFNSSLSED--GQR--LTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGG 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 419 TITVSNIGNIGGTYLSPVIVEKEVAILGVGR--MRAVpafDEAGNVVKKQVCNFSWSADHRVVDGATMARAAEVVRAVVE 496
Cdd:PRK11854 550 CFTISSIGGLGTTHFTPIVNAPEVAILGVSKsaMEPV---WNGKEFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLS 626
|
....*..
gi 1027062764 497 EPDVMVM 503
Cdd:PRK11854 627 DIRRLVL 633
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
27-503 |
2.32e-70 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 234.00 E-value: 2.32e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 27 AALAASAGGPSRWFH-----ETRRQQTVKPVLLADIGeGIVECEVIQWFVQPGARVEEFSPLCEVQSDKASVEITSRFAG 101
Cdd:TIGR01348 89 AAPAPTAGAPAPAAQaqaapAAGQSSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 102 VVKKLYYEAGDMAKVGKPFVDIDIEGgavdqvdsAAKPDAETPAAPVEKADEDVIQQDSKSDVPLTAEEQRRLRIRENNR 181
Cdd:TIGR01348 168 VVKSVKVKVGDSVPTGDLILTLSVAG--------STPATAPAPASAQPAAQSPAATQPEPAAAPAAAKAQAPAPQQAGTQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 182 -----AIATPAVRHLSKELNVDILQIQGTGKDGRVLKEDIYKFVQQRNAGAQTPAAPQISPSASTAQ-P----SQQQEET 251
Cdd:TIGR01348 240 npakvDHAAPAVRRLAREFGVDLSAVKGTGIKGRILREDVQRFVKEPSVRAQAAAASAAGGAPGALPwPnvdfSKFGEVE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 252 VVQLTNTQVQMFKAMTRS-LTIPHFLYTDEIDFTNISDLRTRLNkvlatTAKVSTGGngtvipsgqsqqdlvaKLSYLPF 330
Cdd:TIGR01348 320 EVDMSRIRKISGANLTRNwTMIPHVTHFDKADITEMEAFRKQQN-----AAVEKEGV----------------KLTVLHI 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 331 IIKAVSMALYKYPILNARVDVDPTTekpvVVHRSQHNIGVAMDTPQGLLVPVIKDVGSLNILSIAAELTRLQALAYAGKL 410
Cdd:TIGR01348 379 LMKAVAAALKKFPKFNASLDLGGEQ----LILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 411 TPRDITGGTITVSNIGNIGGTYLSPVIVEKEVAILGVGRMRAVPAFDEAgNVVKKQVCNFSWSADHRVVDGATMARAAEV 490
Cdd:TIGR01348 455 TPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGK-EFEPRLMLPLSLSYDHRVIDGADAARFTTY 533
|
490
....*....|...
gi 1027062764 491 VRAVVEEPDVMVM 503
Cdd:TIGR01348 534 ICESLADIRRLLL 546
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
181-501 |
3.42e-60 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 200.41 E-value: 3.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 181 RAIATPAVRHLSKELNVDILQIQGTGKDGRVLKEDIYKFV------QQRNAGAQTPAAPQISPSASTAQPSQQQEETVVQ 254
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIkslksaPTPAEAASVSSAQQAAKTAAPAAAPPKLEGKREK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 255 LTNTQVQMFKAMTRSLTipHFLYTD---EIDFTNISDLRTR-LNKVLATTAkvstggngtvipsgqsqqdlvAKLSYLPF 330
Cdd:PRK11857 81 VAPIRKAIARAMTNSWS--NVAYVNlvnEIDMTKLWDLRKSvKDPVLKTEG---------------------VKLTFLPF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 331 IIKAVSMALYKYPILNARVDvDPTTEkpvVVHRSQHNIGVAMDTPQGLLVPVIKDVGSLNILSIAAELTRLQALAYAGKL 410
Cdd:PRK11857 138 IAKAILIALKEFPIFAAKYD-EATSE---LVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 411 TPRDITGGTITVSNIGNIGGTYLSPVIVEKEVAILGVGRMRAvPAFDEAGNVVKKQVCNFSWSADHRVVDGATMARAAEV 490
Cdd:PRK11857 214 KPDEMKGGSFTITNYGSVGSLYGVPVINYPELAIAGVGAIID-KAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFASR 292
|
330
....*....|.
gi 1027062764 491 VRAVVEEPDVM 501
Cdd:PRK11857 293 VKELLEKPEIL 303
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
66-503 |
8.12e-57 |
|
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: 195.40 E-value: 8.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 66 VIQWFVQPGARVEEFSPLCEVQSDKASVEITSRFAGVVKKLYYEAGDMA-KVGKPFVDIDIEGGAVDQVDSAAKPDAETP 144
Cdd:TIGR01349 16 LAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVPEGTKDvPVNKPIAVLVEEKEDVADAFKNYKLESSAS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 145 AAPVEKADEDVIQQ--DSKSDVPL-----TAEEQRRLRIRENNRAIATPAVRHLSKELNVDILQIQGTGKDGRVLKEDIY 217
Cdd:TIGR01349 96 PAPKPSEIAPTAPPsaPKPSPAPQkqspePSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVAGSGPNGRIVKKDIE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 218 KFVQQRNAGAQTPAAPQISPSASTAQPSQQQEETVVQLTNTQVQMFKAMTRS-LTIPHFLYTDEIDFTNISDLRTRLNKv 296
Cdd:TIGR01349 176 SFVPQSPASANQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESkQTIPHYYVSIECNVDKLLALRKELNA- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 297 lattakvstggngtvipsgqsQQDLVAKLSYLPFIIKAVSMALYKYPILNArvdvdptTEKPVVVHRSQH-NIGVAMDTP 375
Cdd:TIGR01349 255 ---------------------MASEVYKLSVNDFIIKASALALREVPEANS-------SWTDNFIRRYKNvDISVAVATP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 376 QGLLVPVIKDVGSLNILSIAAELTRLQALAYAGKLTPRDITGGTITVSNIGNIGGTYLSPVIVEKEVAILGVG--RMRAV 453
Cdd:TIGR01349 307 DGLITPIVRNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGavEDVAV 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1027062764 454 PAFDEAGNVVKKQVCNFSWSADHRVVDGATMARAAEVVRAVVEEPDVMVM 503
Cdd:TIGR01349 387 VDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
52-505 |
5.34e-56 |
|
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: 192.26 E-value: 5.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 52 VLLADIGEGIVECEVIQWFVQPGARVEEFSPLCEVQSDKASVEITSRFAGVVKKLYYEAGDMAKVGKPFVDIDIEGGAVD 131
Cdd:TIGR01347 3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDATA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 132 QVDSAAKP-DAETPAAPVEKADEDviqqdsksdvpltaeeqrrlrirENNRAIATPAVRHLSKELNVDILQIQGTGKDGR 210
Cdd:TIGR01347 83 APPAKSGEeKEETPAASAAAAPTA-----------------------AANRPSLSPAARRLAKEHGIDLSAVPGTGVTGR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 211 VLKEDIYKFVQQRnagaqTPAAPQISPSASTAQPSQQQEETVVQLTNTQVQMFKAMTRSLTIPHFLYT-DEIDFTNISDL 289
Cdd:TIGR01347 140 VTKEDIIKKTEAP-----ASAQPPAAAAAAAAPAAATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTfNEVDMSAVMEL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 290 RTRLNKVLATTAKVstggngtvipsgqsqqdlvaKLSYLPFIIKAVSMALYKYPILNARVDVDPttekpvVVHRSQHNIG 369
Cdd:TIGR01347 215 RKRYKEEFEKKHGV--------------------KLGFMSFFVKAVVAALKRFPEVNAEIDGDD------IVYKDYYDIS 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 370 VAMDTPQGLLVPVIKDVGSLNILSIAAELTRLQALAYAGKLTPRDITGGTITVSNIGNIGGTYLSPVIVEKEVAILGVGR 449
Cdd:TIGR01347 269 VAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHG 348
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1027062764 450 MRAVP-AFDeaGNVVKKQVCNFSWSADHRVVDGATMARAAEVVRAVVEEPDVMVMHL 505
Cdd:TIGR01347 349 IKERPvAVN--GQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLLDL 403
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
52-481 |
3.63e-52 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 181.96 E-value: 3.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 52 VLLADIGEGIVECEVIQWFVQPGARVEEFSPLCEVQSDKASVEITSRFAGVVKKLYYEAGDMAKVGKPFVDIDiEGGAVD 131
Cdd:PRK05704 5 IKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRID-EGAAAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 132 QVDSAAKPDAETPAAPVEKAdedviqqdsksdvPLTAEEQRrlrirennRAIATPAVRHLSKELNVDILQIQGTGKDGRV 211
Cdd:PRK05704 84 AAAAAAAAAAAAAAAPAQAQ-------------AAAAAEQS--------NDALSPAARKLAAENGLDASAVKGTGKGGRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 212 LKEDIYKFVQQRNAGAQTPAAPqisPSASTAQPSQQQEETVVQLTN---------TQVQMFKAMtrsLTiphflyT-DEI 281
Cdd:PRK05704 143 TKEDVLAALAAAAAAPAAPAAA---APAAAPAPLGARPEERVPMTRlrktiaerlLEAQNTTAM---LT------TfNEV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 282 DFTNISDLRTRLnkvlattakvstggngtvipsgqsqQDLV-----AKLSYLPFIIKAVSMALYKYPILNARVDVDptte 356
Cdd:PRK05704 211 DMTPVMDLRKQY-------------------------KDAFekkhgVKLGFMSFFVKAVVEALKRYPEVNASIDGD---- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 357 kPVVVHRSQHnIGVAMDTPQGLLVPVIKDVGSLNILSIAAELTRLQALAYAGKLTPRDITGGTITVSNigniGGTYLS-- 434
Cdd:PRK05704 262 -DIVYHNYYD-IGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITN----GGVFGSlm 335
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1027062764 435 --PVIVEKEVAILGVGRM--RAVpafdeagnVVKKQVCN-----FSWSADHRVVDG 481
Cdd:PRK05704 336 stPIINPPQSAILGMHKIkeRPV--------AVNGQIVIrpmmyLALSYDHRIIDG 383
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
36-505 |
3.16e-47 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 169.09 E-value: 3.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 36 PSRWFHETRRQQTVKPVLLADIGEGIVECEVIQWFVQPGARVEEFSPLCEVQSDKASVEITSRFAGVVKKLYYEAGDMAK 115
Cdd:PTZ00144 31 PACSAHFSKSYFSIKVIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 116 VGKPFVDIDIEGGAVDQVDSAAKPDAETPAAPVEKADEDVIQQDSKSDVPLTAEEQRRLRIRENNRAIATPAVRHLSKEL 195
Cdd:PTZ00144 111 VGAPLSEIDTGGAPPAAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPPEPAPAAKPPPTPVARADPRET 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 196 NVDILQIQgtgkdgrvlkediyKFVQQRNAGAQTpaapqispsastaqpsqqqeeTVVQLTNTQvqmfkamtrsltiphf 275
Cdd:PTZ00144 191 RVPMSRMR--------------QRIAERLKASQN---------------------TCAMLTTFN---------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 276 lytdEIDFTNISDLRTRLNKvlattakvstggngtvipsgQSQQDLVAKLSYLPFIIKAVSMALYKYPILNARVDVDPtt 355
Cdd:PTZ00144 220 ----ECDMSALMELRKEYKD--------------------DFQKKHGVKLGFMSAFVKASTIALKKMPIVNAYIDGDE-- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 356 ekpvVVHRSQHNIGVAMDTPQGLLVPVIKDVGSLNILSIAAELTRLQALAYAGKLTPRDITGGTITVSNIGNIGGTYLSP 435
Cdd:PTZ00144 274 ----IVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTP 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1027062764 436 VIVEKEVAILGvgrM-----RAVPAFDEagnVVKKQVCNFSWSADHRVVDGATMARAAEVVRAVVEEPDVMVMHL 505
Cdd:PTZ00144 350 IINPPQSAILG---MhaikkRPVVVGNE---IVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLDL 418
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
63-503 |
2.99e-40 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 152.70 E-value: 2.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 63 ECEVIQWFVQPGARVEEFSPLCEVQSDKASVEITSRFAGVVKKLYYeaGDMAK---VGKpFVDIDIEggavDQVDSAA-- 137
Cdd:PLN02744 126 EGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVK--GDGAKeikVGE-VIAITVE----EEEDIGKfk 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 138 --KPDAETPAAPVEKADEDVIQQDSKSDVPLTAEEQRRLRIRE----NNRAIATPAVRHLSKELNVDILQIQGTGKDGRV 211
Cdd:PLN02744 199 dyKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAppssGDRIFASPLARKLAEDNNVPLSSIKGTGPDGRI 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 212 LKEDIYKFVQQRNAGAQTPaapqisPSASTAQPSQqqeeTVVQLTNTQVQMFKAmTRSL----TIPHFLYTDEIDFTNIS 287
Cdd:PLN02744 279 VKADIEDYLASGGKGATAP------PSTDSKAPAL----DYTDIPNTQIRKVTA-SRLLqskqTIPHYYLTVDTRVDKLM 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 288 DLRTRLNKVLAttakvSTGGNgtvipsgqsqqdlvaKLSYLPFIIKAVSMALYKYPILNARVDVDPTtekpvvvhRSQHN 367
Cdd:PLN02744 348 ALRSQLNSLQE-----ASGGK---------------KISVNDLVIKAAALALRKVPQCNSSWTDDYI--------RQYHN 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 368 --IGVAMDTPQGLLVPVIKDVGSLNILSIAAELTRLQALAYAGKLTPRDITGGTITVSNIGN-IGGTYLSPVIVEKEVAI 444
Cdd:PLN02744 400 vnINVAVQTENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGpFGIKQFCAIINPPQSAI 479
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027062764 445 LGVG--RMRAVPAFDEAgnvvKKQVCNF---SWSADHRVVDGATMARAAEVVRAVVEEPDVMVM 503
Cdd:PLN02744 480 LAVGsaEKRVIPGSGPD----QYNFASFmsvTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
185-503 |
5.58e-27 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 111.54 E-value: 5.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 185 TPAVRHLSKELNVDILQIQGTGKDGRVLKEDIYKFV--QQRNAGAQTPAAPQISPSASTAQPSQQQEEtVVQLTNTQVQM 262
Cdd:PRK14843 52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLpeNIENDSIKSPAQIEKVEEVPDNVTPYGEIE-RIPMTPMRKVI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 263 FKAMTRS-LTIPHFLYTDEIDFTNISDLRTR-LNKVLATTAKvstggngtvipsgqsqqdlvaKLSYLPFIIKAVSMALY 340
Cdd:PRK14843 131 AQRMVESyLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATGK---------------------KTTVTDLLSLAVVKTLM 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 341 KYPILNARVDVDPTTekpVVVHrSQHNIGVAMDTPQGLLVPVIKDVGSLNILSIAAELTRLQALAYAGKLTPRDITGGTI 420
Cdd:PRK14843 190 KHPYINASLTEDGKT---IITH-NYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 421 TVSNIGNIGGTYLSPVIVEKEVAILGVGRMRAVPAFDEaGNVVKKQVCNFSWSADHRVVDGATMARAAEVVRAVVEEPDV 500
Cdd:PRK14843 266 TISNLGMFGVQSFGPIINQPNSAILGVSSTIEKPVVVN-GEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPIS 344
|
...
gi 1027062764 501 MVM 503
Cdd:PRK14843 345 MLI 347
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
2-505 |
8.37e-27 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 112.93 E-value: 8.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 2 FLQRGSRAIRAVHRQWVVSGGNVTKAALAASAggPSRWFH--ETRRQQTVKPVLlADIGEGIVECEVIQWFVQPGARVEE 79
Cdd:PLN02226 45 LLHRGNHAHSFHNLALPGNSGISRSASLVSST--LQRWVRpfSSESGDTVEAVV-PHMGESITDGTLATFLKKPGERVQA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 80 FSPLCEVQSDKASVEITSRFAGVVKKLYYEAGDMAKVGKPFVDIDIEGGAVDQVdsaakpdaetpaAPVEKADEdviQQD 159
Cdd:PLN02226 122 DEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSEDAASQV------------TPSQKIPE---TTD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 160 SKSDVPltAEEQRRLRIRennraiATPAvrhlskelnvdilqiqgtgkdgrvlkediykfvqqrnagAQTPAAPQISP-- 237
Cdd:PLN02226 187 PKPSPP--AEDKQKPKVE------SAPV---------------------------------------AEKPKAPSSPPpp 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 238 --SASTAQPSQQQEETVVQLTNTQVQMFKAMTRSLTIPHFLYT-DEIDFTNISDLRTRLNKVLATTAKVstggngtvips 314
Cdd:PLN02226 220 kqSAKEPQLPPKERERRVPMTRLRKRVATRLKDSQNTFALLTTfNEVDMTNLMKLRSQYKDAFYEKHGV----------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 315 gqsqqdlvaKLSYLPFIIKAVSMALYKYPILNARVDVDPttekpvVVHRSQHNIGVAMDTPQGLLVPVIKDVGSLNILSI 394
Cdd:PLN02226 289 ---------KLGLMSGFIKAAVSALQHQPVVNAVIDGDD------IIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEI 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 395 AAELTRLQALAYAGKLTPRDITGGTITVSNIGNIGGTYLSPVIVEKEVAILGVGRMRAVPAFdEAGNVVKKQVCNFSWSA 474
Cdd:PLN02226 354 EKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMV-VGGSVVPRPMMYVALTY 432
|
490 500 510
....*....|....*....|....*....|.
gi 1027062764 475 DHRVVDGATMARAAEVVRAVVEEPDVMVMHL 505
Cdd:PLN02226 433 DHRLIDGREAVYFLRRVKDVVEDPQRLLLDI 463
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
50-123 |
5.43e-24 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 95.16 E-value: 5.43e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027062764 50 KPVLLADIGEGIVECEVIQWFVQPGARVEEFSPLCEVQSDKASVEITSRFAGVVKKLYYEAGDMAKVGKPFVDI 123
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
50-123 |
6.84e-21 |
|
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: 86.66 E-value: 6.84e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027062764 50 KPVLLADIGEGIVECEVIQWFVQPGARVEEFSPLCEVQSDKASVEITSRFAGVVKKLYYEAGDMAKVGKPFVDI 123
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
50-123 |
4.02e-16 |
|
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: 73.02 E-value: 4.02e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027062764 50 KPVLLADIGEGIVEcEVIQWFVQPGARVEEFSPLCEVQSDKASVEITSRFAGVVKKLYYEAGDMAKVGKPFVDI 123
Cdd:pfam00364 1 TEIKSPMIGESVRE-GVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
225-482 |
4.34e-16 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 81.48 E-value: 4.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 225 AGAQTPAAPQISPSASTAQPSQQQEETVVQLTNTQVQMFKAMTRSLTIPhflytdeidfTNIS----------DLRTRLN 294
Cdd:PRK12270 90 AAAAAAPAAPPAAAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASLEVP----------TATSvravpaklliDNRIVIN 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 295 KVLATTAkvstGGngtvipsgqsqqdlvaKLSYLPFIIKAVSMALYKYPILN---ARVDvdpttEKPVVVHRSQHNIGVA 371
Cdd:PRK12270 160 NHLKRTR----GG----------------KVSFTHLIGYALVQALKAFPNMNrhyAEVD-----GKPTLVTPAHVNLGLA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 372 MDTPQ-----GLLVPVIKDVGSLNILSIAAELTRLQALAYAGKLTPRDITGGTITVSNIGNIGGTYLSPVIVEKEVAILG 446
Cdd:PRK12270 215 IDLPKkdgsrQLVVPAIKGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIG 294
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1027062764 447 VGRMRAVPAF----DE--AGNVVKKqVCNFSWSADHRVVDGA 482
Cdd:PRK12270 295 VGAMEYPAEFqgasEErlAELGISK-VMTLTSTYDHRIIQGA 335
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
183-216 |
1.40e-11 |
|
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: 58.85 E-value: 1.40e-11
10 20 30
....*....|....*....|....*....|....
gi 1027062764 183 IATPAVRHLSKELNVDILQIQGTGKDGRVLKEDI 216
Cdd:pfam02817 2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDV 35
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
48-188 |
5.97e-10 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 61.11 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027062764 48 TVKPVLLADIGEGIVECEVIQWFVQPGARVEEFSPLCEVQSDKASVEITSRFAGVVKKLYYEAGDMAKVGKPFVDIDIEG 127
Cdd:PRK14875 1 SITPITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1027062764 128 GAVDQVDSAAKPdAETPAAPVEKADEDVIQQDSKSDVPltaeeQRRLRIRENNRAIATPAV 188
Cdd:PRK14875 81 VSDAEIDAFIAP-FARRFAPEGIDEEDAGPAPRKARIG-----GRTVRYLRLGEGDGTPVV 135
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
66-123 |
7.56e-06 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 43.56 E-value: 7.56e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1027062764 66 VIQWFVQPGARVEEFSPLCEVQSDKASVEITSRFAGVVKKLYYEAGDMAKVGKPFVDI 123
Cdd:cd06850 10 VVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
52-123 |
2.26e-04 |
|
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: 39.73 E-value: 2.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027062764 52 VLLADIGEGIVECEVIQWFVQPGARVEEFSPLCEVQSDKASVEITSRFAGVVKKLYYEAGDMAKVGKPFVDI 123
Cdd:cd06663 2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| |
