|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
67-482 |
9.46e-180 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 509.65 E-value: 9.46e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 67 FKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDS 146
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 147 EEDVVETPAVSHDEHTHQEIKGQK-----TLATPAVRRLAMENNIKLSEVVGSGKDGRVLKEDILNYLeKQTGAILPPSP 221
Cdd:PLN02528 81 RSDSLLLPTDSSNIVSLAESDERGsnlsgVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYA-AQKGVVKDSSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 222 KAEIIPPPAQPKDRTVPIPISKppvfIGKDKTEPITGFQKAMVKTMSAALKIPHFGYCDEVDLTELLKLREELKPIALAR 301
Cdd:PLN02528 160 AEEATIAEQEEFSTSVSTPTEQ----SYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 302 GIKLSYMPFFIKAASLGLLQFPILNSSVDENCQTITYKASHNIGIAMDTKQGLVVPNVKNVQICSIFEIAAELNRLQNLG 381
Cdd:PLN02528 236 TVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 382 AVGQLSTTDLAGGTFTLSNIGSIGGTYAKAVILPPEVAIGALGSIRALPRFNLNGEVYKAQIMNVSWSADHRIIDGATMS 461
Cdd:PLN02528 316 AENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVA 395
|
410 420
....*....|....*....|.
gi 514479320 462 RFSNLWKSYLENPAFMLLDLK 482
Cdd:PLN02528 396 RFCNEWKSYVEKPELLMLHMR 416
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
267-478 |
4.14e-97 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 291.37 E-value: 4.14e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 267 MSAAL-KIPHFGYCDEVDLTELLKLREELKPIALARGIKLSYMPFFIKAASLGLLQFPILNSSVDENCQTITYKASHNIG 345
Cdd:pfam00198 1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 346 IAMDTKQGLVVPNVKNVQICSIFEIAAELNRLQNLGAVGQLSTTDLAGGTFTLSNIGSIGGTYAKAVILPPEVAIGALGS 425
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 514479320 426 IRALPRFNlNGEVYKAQIMNVSWSADHRIIDGATMSRFSNLWKSYLENPAFML 478
Cdd:pfam00198 161 IRKRPVVV-DGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
58-479 |
2.94e-74 |
|
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: 243.63 E-value: 2.94e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 58 AALCGQVVQFKLSDIGeGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVD 137
Cdd:TIGR01348 110 AGQSSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILT 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 138 IETEALKDSEEDVVE-------------------------TPAVSHDEHTHQeikGQKTL-ATPAVRRLAMENNIKLSEV 191
Cdd:TIGR01348 189 LSVAGSTPATAPAPAsaqpaaqspaatqpepaaapaaakaQAPAPQQAGTQN---PAKVDhAAPAVRRLAREFGVDLSAV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 192 VGSGKDGRVLKEDILNYLEKQTGAIlPPSPKAEIIPPPAQPkdrtvPIPISKPPVFiGKDKTEPITGFQKAMVKTMSAA- 270
Cdd:TIGR01348 266 KGTGIKGRILREDVQRFVKEPSVRA-QAAAASAAGGAPGAL-----PWPNVDFSKF-GEVEEVDMSRIRKISGANLTRNw 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 271 LKIPHFGYCDEVDLTELLKLREELKPIALARGIKLSYMPFFIKAASLGLLQFPILNSSVDENCQTITYKASHNIGIAMDT 350
Cdd:TIGR01348 339 TMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDT 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 351 KQGLVVPNVKNVQICSIFEIAAELNRLQNLGAVGQLSTTDLAGGTFTLSNIGSIGGTYAKAVILPPEVAIgaLGSIRALP 430
Cdd:TIGR01348 419 PNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAI--LGVSKSGM 496
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 514479320 431 RFNLNGEVYKAQIM-NVSWSADHRIIDGATMSRFSNLWKSYLENPAFMLL 479
Cdd:TIGR01348 497 EPVWNGKEFEPRLMlPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
65-138 |
6.06e-25 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 97.48 E-value: 6.06e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514479320 65 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 138
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
65-138 |
3.46e-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: 87.43 E-value: 3.46e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514479320 65 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 138
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
67-482 |
9.46e-180 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 509.65 E-value: 9.46e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 67 FKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDS 146
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 147 EEDVVETPAVSHDEHTHQEIKGQK-----TLATPAVRRLAMENNIKLSEVVGSGKDGRVLKEDILNYLeKQTGAILPPSP 221
Cdd:PLN02528 81 RSDSLLLPTDSSNIVSLAESDERGsnlsgVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYA-AQKGVVKDSSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 222 KAEIIPPPAQPKDRTVPIPISKppvfIGKDKTEPITGFQKAMVKTMSAALKIPHFGYCDEVDLTELLKLREELKPIALAR 301
Cdd:PLN02528 160 AEEATIAEQEEFSTSVSTPTEQ----SYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 302 GIKLSYMPFFIKAASLGLLQFPILNSSVDENCQTITYKASHNIGIAMDTKQGLVVPNVKNVQICSIFEIAAELNRLQNLG 381
Cdd:PLN02528 236 TVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 382 AVGQLSTTDLAGGTFTLSNIGSIGGTYAKAVILPPEVAIGALGSIRALPRFNLNGEVYKAQIMNVSWSADHRIIDGATMS 461
Cdd:PLN02528 316 AENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVA 395
|
410 420
....*....|....*....|.
gi 514479320 462 RFSNLWKSYLENPAFMLLDLK 482
Cdd:PLN02528 396 RFCNEWKSYVEKPELLMLHMR 416
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
55-479 |
5.29e-156 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 454.28 E-value: 5.29e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 55 KTTAALCGQVVQFKLSDIGEgIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKP 134
Cdd:PRK11855 110 AAAAAAGGGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 135 LVDIETEALKDSEEDVVETPAVSHDEHTHQE------------------IKGQKTLATPAVRRLAMENNIKLSEVVGSGK 196
Cdd:PRK11855 189 LVVIEVAAAAPAAAAAPAAAAPAAAAAAAPApapaaaaapaaaapaaaaAPGKAPHASPAVRRLARELGVDLSQVKGTGK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 197 DGRVLKEDILNYLEkqtGAILPPSPKAEIIPPPAQPKDRTVPIPISKPPVFiGKDKTEPITGFQKAMVKTMSAAL-KIPH 275
Cdd:PRK11855 269 KGRITKEDVQAFVK---GAMSAAAAAAAAAAAAGGGGLGLLPWPKVDFSKF-GEIETKPLSRIKKISAANLHRSWvTIPH 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 276 FGYCDEVDLTELLKLREELKPIALARGIKLSYMPFFIKAASLGLLQFPILNSSVDENCQTITYKASHNIGIAMDTKQGLV 355
Cdd:PRK11855 345 VTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGLV 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 356 VPNVKNVQICSIFEIAAELNRLQNLGAVGQLSTTDLAGGTFTLSNIGSIGGTYAKAVILPPEVAIGALGSIRALPrFNLN 435
Cdd:PRK11855 425 VPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKP-VWDG 503
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 514479320 436 GEVYKAQIMNVSWSADHRIIDGATMSRFSNLWKSYLENPAFMLL 479
Cdd:PRK11855 504 KEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
64-480 |
1.26e-129 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 381.83 E-value: 1.26e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 64 VVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETE-- 141
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEge 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 142 --------------ALKDSEEDVVETPAVSHDEHTHQEIKGQKTLATPAVRRLAMENNIKLSEVVGSGKDGRVLKEDILN 207
Cdd:PRK11856 82 aeaaaaaeaapeapAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 208 YLEKQTGAILPPSPKAEIIPPPAQPKDRTVpipiskppvfigkdktePITGFQKAMVKTMSAA-LKIPHFGYCDEVDLTE 286
Cdd:PRK11856 162 AAAAAAPAAAAAAAAAAAPPAAAAEGEERV-----------------PLSGMRKAIAKRMVESkREIPHFTLTDEVDVTA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 287 LLKLREELKPIAlargIKLSYMPFFIKAASLGLLQFPILNSSVDEncQTITYKASHNIGIAMDTKQGLVVPNVKNVQICS 366
Cdd:PRK11856 225 LLALRKQLKAIG----VKLTVTDFLIKAVALALKKFPELNASWDD--DAIVLKKYVNIGIAVATDGGLIVPVIRDADKKS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 367 IFEIAAELNRLQNLGAVGQLSTTDLAGGTFTLSNIGSIGGTYAKAVILPPEVAIGALGSIRALPRFNlNGEVYKAQIMNV 446
Cdd:PRK11856 299 LFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVV-DGEIVVRKVMPL 377
|
410 420 430
....*....|....*....|....*....|....
gi 514479320 447 SWSADHRIIDGATMSRFSNLWKSYLENPAFMLLD 480
Cdd:PRK11856 378 SLSFDHRVIDGADAARFLKALKELLENPALLLLE 411
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
267-478 |
4.14e-97 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 291.37 E-value: 4.14e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 267 MSAAL-KIPHFGYCDEVDLTELLKLREELKPIALARGIKLSYMPFFIKAASLGLLQFPILNSSVDENCQTITYKASHNIG 345
Cdd:pfam00198 1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 346 IAMDTKQGLVVPNVKNVQICSIFEIAAELNRLQNLGAVGQLSTTDLAGGTFTLSNIGSIGGTYAKAVILPPEVAIGALGS 425
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 514479320 426 IRALPRFNlNGEVYKAQIMNVSWSADHRIIDGATMSRFSNLWKSYLENPAFML 478
Cdd:pfam00198 161 IRKRPVVV-DGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
62-473 |
8.82e-78 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 254.93 E-value: 8.82e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 62 GQVVQFKLSDIGEGirEVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETE 141
Cdd:PRK11854 204 AGVKDVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 142 --------ALKDSEEDV---------VETPAVSHDEHTHQEIKGQKTLATPAVRRLAMENNIKLSEVVGSGKDGRVLKED 204
Cdd:PRK11854 282 gaapaaapAKQEAAAPApaaakaeapAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKED 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 205 ILNYLEkqtgAILPPSPKAEIIPPPAQPKDRTVPIPISKPPVFiGKDKTEPITGFQKAMVKTMSAAL-KIPHFGYCDEVD 283
Cdd:PRK11854 362 VQAYVK----DAVKRAEAAPAAAAAGGGGPGLLPWPKVDFSKF-GEIEEVELGRIQKISGANLHRNWvMIPHVTQFDKAD 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 284 LTELLKLREELKPIALAR--GIKLSYMPFFIKAASLGLLQFPILNSSVDENCQTITYKASHNIGIAMDTKQGLVVPNVKN 361
Cdd:PRK11854 437 ITELEAFRKQQNAEAEKRklGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVVPVFKD 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 362 VQICSIFEIAAELNRLQNLGAVGQLSTTDLAGGTFTLSNIGSIGGTYAKAVILPPEVAIGALGSIRALPRFNlNGEVYKA 441
Cdd:PRK11854 517 VNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWN-GKEFAPR 595
|
410 420 430
....*....|....*....|....*....|..
gi 514479320 442 QIMNVSWSADHRIIDGATMSRFSNLWKSYLEN 473
Cdd:PRK11854 596 LMLPLSLSYDHRVIDGADGARFITIINDRLSD 627
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
58-479 |
2.94e-74 |
|
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: 243.63 E-value: 2.94e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 58 AALCGQVVQFKLSDIGeGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVD 137
Cdd:TIGR01348 110 AGQSSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILT 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 138 IETEALKDSEEDVVE-------------------------TPAVSHDEHTHQeikGQKTL-ATPAVRRLAMENNIKLSEV 191
Cdd:TIGR01348 189 LSVAGSTPATAPAPAsaqpaaqspaatqpepaaapaaakaQAPAPQQAGTQN---PAKVDhAAPAVRRLAREFGVDLSAV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 192 VGSGKDGRVLKEDILNYLEKQTGAIlPPSPKAEIIPPPAQPkdrtvPIPISKPPVFiGKDKTEPITGFQKAMVKTMSAA- 270
Cdd:TIGR01348 266 KGTGIKGRILREDVQRFVKEPSVRA-QAAAASAAGGAPGAL-----PWPNVDFSKF-GEVEEVDMSRIRKISGANLTRNw 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 271 LKIPHFGYCDEVDLTELLKLREELKPIALARGIKLSYMPFFIKAASLGLLQFPILNSSVDENCQTITYKASHNIGIAMDT 350
Cdd:TIGR01348 339 TMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDT 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 351 KQGLVVPNVKNVQICSIFEIAAELNRLQNLGAVGQLSTTDLAGGTFTLSNIGSIGGTYAKAVILPPEVAIgaLGSIRALP 430
Cdd:TIGR01348 419 PNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAI--LGVSKSGM 496
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 514479320 431 RFNLNGEVYKAQIM-NVSWSADHRIIDGATMSRFSNLWKSYLENPAFMLL 479
Cdd:TIGR01348 497 EPVWNGKEFEPRLMlPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
65-481 |
3.68e-72 |
|
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: 233.86 E-value: 3.68e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 65 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALK 144
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 145 D------SEEDVVETPAVShdEHTHQEIKGQKTLATPAVRRLAMENNIKLSEVVGSGKDGRVLKEDILNYLEKQTGAILP 218
Cdd:TIGR01347 81 TaappakSGEEKEETPAAS--AAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 219 PSPKAEiiPPPAQPKDRTVPIPISKPPVFIGKDKTEPITgfQKAMVKTMsaalkiphfgycDEVDLTELLKLREELKPIA 298
Cdd:TIGR01347 159 AAAAAA--AAPAAATRPEERVKMTRLRQRIAERLKEAQN--STAMLTTF------------NEVDMSAVMELRKRYKEEF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 299 LAR-GIKLSYMPFFIKAASLGLLQFPILNSSVDENcqTITYKASHNIGIAMDTKQGLVVPNVKNVQICSIFEIAAELNRL 377
Cdd:TIGR01347 223 EKKhGVKLGFMSFFVKAVVAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 378 QNLGAVGQLSTTDLAGGTFTLSNIGSIGGTYAKAVILPPEVAIGALGSIRALPrFNLNGEVYKAQIMNVSWSADHRIIDG 457
Cdd:TIGR01347 301 GKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERP-VAVNGQIEIRPMMYLALSYDHRLIDG 379
|
410 420
....*....|....*....|....
gi 514479320 458 ATMSRFSNLWKSYLENPAFMLLDL 481
Cdd:TIGR01347 380 KEAVTFLVTIKELLEDPRRLLLDL 403
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
170-474 |
5.13e-68 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 220.05 E-value: 5.13e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 170 KTLATPAVRRLAMENNIKLSEVVGSGKDGRVLKEDILNYLEKQTGAilpPSPKAEIIPPPAQPKDRTvPIPISKPPVFIG 249
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSA---PTPAEAASVSSAQQAAKT-AAPAAAPPKLEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 250 KdkTEPITGFQKAMVKTMSAALK-IPHFGYCDEVDLTELLKLREELKPIAL-ARGIKLSYMPFFIKAASLGLLQFPILNS 327
Cdd:PRK11857 77 K--REKVAPIRKAIARAMTNSWSnVAYVNLVNEIDMTKLWDLRKSVKDPVLkTEGVKLTFLPFIAKAILIALKEFPIFAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 328 SVDENCQTITYKASHNIGIAMDTKQGLVVPNVKNVQICSIFEIAAELNRLQNLGAVGQLSTTDLAGGTFTLSNIGSIGGT 407
Cdd:PRK11857 155 KYDEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514479320 408 YAKAVILPPEVAIGALGSIRALPRFNlNGEVYKAQIMNVSWSADHRIIDGATMSRFSNLWKSYLENP 474
Cdd:PRK11857 235 YGVPVINYPELAIAGVGAIIDKAIVK-NGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
68-481 |
3.85e-65 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 215.85 E-value: 3.85e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 68 KLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEA----L 143
Cdd:PRK05704 6 KVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAaagaA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 144 KDSEEDVVETPAVSHDEHTHQEIKGQKTLATPAVRRLAMENNIKLSEVVGSGKDGRVLKEDILNYLEKqtgailPPSPKA 223
Cdd:PRK05704 86 AAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAA------AAAAPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 224 eiiPPPAQPKDRTVPIPISKPpvfigkDKTEPITGFQK-------------AMVKTmsaalkiphFgycDEVDLTELLKL 290
Cdd:PRK05704 160 ---APAAAAPAAAPAPLGARP------EERVPMTRLRKtiaerlleaqnttAMLTT---------F---NEVDMTPVMDL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 291 REELKPIALAR-GIKLSYMPFFIKAASLGLLQFPILNSSVDENcqTITYKASHNIGIAMDTKQGLVVPNVKNVQICSIFE 369
Cdd:PRK05704 219 RKQYKDAFEKKhGVKLGFMSFFVKAVVEALKRYPEVNASIDGD--DIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 370 IAAELNRLQNLGAVGQLSTTDLAGGTFTLSNigsiGGTY----AKAVILPPEVAIgaLG--SIRALPrFNLNGEVYKAQI 443
Cdd:PRK05704 297 IEKKIAELAKKARDGKLSIEELTGGTFTITN----GGVFgslmSTPIINPPQSAI--LGmhKIKERP-VAVNGQIVIRPM 369
|
410 420 430
....*....|....*....|....*....|....*...
gi 514479320 444 MNVSWSADHRIIDGATMSRFSNLWKSYLENPAFMLLDL 481
Cdd:PRK05704 370 MYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLLDL 407
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
31-481 |
1.47e-64 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 214.55 E-value: 1.47e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 31 ILKPKCLCLLGFPALKYNHPHHLLKTTAALCGQVVQFKLS----------DIGEGIREVTVKEWYVKEGDTVSQFDSICE 100
Cdd:PTZ00144 1 STVNLVKRLNKPLLSSVKGMFRRFSLRKLQPACSAHFSKSyfsikvikvpTMGDSISEGTVVEWKKKVGDYVKEDEVICI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 101 VQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDSEEdvVETPAVSHDEHTHQEikgqktlatpavrrl 180
Cdd:PTZ00144 81 IETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPAAA--PAAAAAAKAEKTTPE--------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 181 amenniklsevvgsgkdgrvlkedilnylEKQTGAILPPSPKAEIIPPPAQPKDRTVPIPISKPPVFI-GKDKTE---PI 256
Cdd:PTZ00144 144 -----------------------------KPKAAAPTPEPPAASKPTPPAAAKPPEPAPAAKPPPTPVaRADPREtrvPM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 257 TGFQK-------------AMVKTMsaalkiphfgycDEVDLTELLKLREELKPIALAR-GIKLSYMPFFIKAASLGLLQF 322
Cdd:PTZ00144 195 SRMRQriaerlkasqntcAMLTTF------------NECDMSALMELRKEYKDDFQKKhGVKLGFMSAFVKASTIALKKM 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 323 PILNSSVDENCqtITYKASHNIGIAMDTKQGLVVPNVKNVQICSIFEIAAELNRLQNLGAVGQLSTTDLAGGTFTLSNIG 402
Cdd:PTZ00144 263 PIVNAYIDGDE--IVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 403 SIGGTYAKAVILPPEVAIGALGSI--RALPRfnlNGEVYKAQIMNVSWSADHRIIDGATMSRFSNLWKSYLENPAFMLLD 480
Cdd:PTZ00144 341 VFGSLMGTPIINPPQSAILGMHAIkkRPVVV---GNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLD 417
|
.
gi 514479320 481 L 481
Cdd:PTZ00144 418 L 418
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
62-476 |
1.08e-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: 211.02 E-value: 1.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 62 GQVVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI--- 138
Cdd:TIGR02927 124 GEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIgda 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 139 --------ETEALKDSEEDVVETPAVSHDEHTHQEIKGQKTLA----------------------TPAVRRLAMENNIKL 188
Cdd:TIGR02927 204 naapaepaEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPApaktaapaaaapvssgdsgpyvTPLVRKLAKDKGVDL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 189 SEVVGSGKDGRVLKEDILNYLEKQT---GAILPPSPKAEiippPAQPKDRTVPIPISKPPVfigKDKTEPITGFQKAMVK 265
Cdd:TIGR02927 284 STVKGTGVGGRIRKQDVLAAAKAAEearAAAAAPAAAAA----PAAPAAAAKPAEPDTAKL---RGTTQKMNRIRQITAD 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 266 TMSAALKI-PHFGYCDEVDLTELLKLREELKPIALAR-GIKLSYMPFFIKAASLGLLQFPILNSSVDENCQTITYKASHN 343
Cdd:TIGR02927 357 KTIESLQTsAQLTQVHEVDMTRVAALRARAKNDFLEKnGVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEH 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 344 IGIAMDTKQGLVVPNVKNVQICSIFEIAAELNRLQNLGAVGQLSTTDLAGGTFTLSNIGSIGGTYAKAVILPPEVAIGAL 423
Cdd:TIGR02927 437 VGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGT 516
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 514479320 424 GSIRALPRFNLN---GEVYKA-QIMNVSWSADHRIIDGATMSRFSNLWKSYLENPAF 476
Cdd:TIGR02927 517 GAIVKRPRVIKDedgGESIAIrSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEEGDF 573
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
76-479 |
5.16e-61 |
|
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: 205.80 E-value: 5.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 76 IREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYY--NLDDIAyVGKPLV-------DIET------ 140
Cdd:TIGR01349 11 MTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVpeGTKDVP-VNKPIAvlveekeDVADafknyk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 141 ------EALKDSEED--------------VVETPAVSHDEHTHQEIKGQKTLATPAVRRLAMENNIKLSEVVGSGKDGRV 200
Cdd:TIGR01349 90 lessasPAPKPSEIAptappsapkpspapQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVAGSGPNGRI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 201 LKEDILNYLekqtgailPPSPKaeiiPPPAQPKDRTVPIPISKPPVFIGKDKTEPITGFQKAMVKTMSAALK-IPHFGYC 279
Cdd:TIGR01349 170 VKKDIESFV--------PQSPA----SANQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQtIPHYYVS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 280 DEVDLTELLKLREELKPIALARgIKLSYMPFFIKAASLGLLQFPILNSSVDENcqTITYKASHNIGIAMDTKQGLVVPNV 359
Cdd:TIGR01349 238 IECNVDKLLALRKELNAMASEV-YKLSVNDFIIKASALALREVPEANSSWTDN--FIRRYKNVDISVAVATPDGLITPIV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 360 KNVQICSIFEIAAELNRLQNLGAVGQLSTTDLAGGTFTLSNIGSIGGTYAKAVILPPEVAIGALGSI--RALPRfNLNGE 437
Cdd:TIGR01349 315 RNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVedVAVVD-NDEEK 393
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 514479320 438 VYK-AQIMNVSWSADHRIIDGATMSRFSNLWKSYLENPAFMLL 479
Cdd:TIGR01349 394 GFAvASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
78-479 |
1.19e-48 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 175.04 E-value: 1.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 78 EVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYY------------------NLDDIAYVG--KPLVD 137
Cdd:PLN02744 126 EGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKgdgakeikvgeviaitveEEEDIGKFKdyKPSSS 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 138 IETEALKDSEE------DVVETPAVSHDEHTHQE----IKGQKTLATPAVRRLAMENNIKLSEVVGSGKDGRVLKEDILN 207
Cdd:PLN02744 206 AAPAAPKAKPSppppkeEEVEKPASSPEPKASKPsappSSGDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIED 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 208 YLEKQ-TGAILPPSPKAEIipppaqPKDRTVPIPISKppvfIGKdktepITGFQKAMVKTMsaalkIPHFGYCDEVDLTE 286
Cdd:PLN02744 286 YLASGgKGATAPPSTDSKA------PALDYTDIPNTQ----IRK-----VTASRLLQSKQT-----IPHYYLTVDTRVDK 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 287 LLKLREELKPIALARGIK-LSYMPFFIKAASLGLLQFPILNSS-VDEncqTITYKASHNIGIAMDTKQGLVVPNVKNVQI 364
Cdd:PLN02744 346 LMALRSQLNSLQEASGGKkISVNDLVIKAAALALRKVPQCNSSwTDD---YIRQYHNVNINVAVQTENGLYVPVVKDADK 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 365 CSIFEIAAELNRLQNLGAVGQLSTTDLAGGTFTLSNIGS-IGGTYAKAVILPPEVAIGALGSI--RALPRFNlNGEVYKA 441
Cdd:PLN02744 423 KGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGpFGIKQFCAIINPPQSAILAVGSAekRVIPGSG-PDQYNFA 501
|
410 420 430
....*....|....*....|....*....|....*...
gi 514479320 442 QIMNVSWSADHRIIDGATMSRFSNLWKSYLENPAFMLL 479
Cdd:PLN02744 502 SFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
174-479 |
2.93e-42 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 153.52 E-value: 2.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 174 TPAVRRLAMENNIKLSEVVGSGKDGRVLKEDILnylekqtgAILPPSPKAEIIPPPAQpKDRTVPIPISKPPVfiGKDKT 253
Cdd:PRK14843 52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVL--------ALLPENIENDSIKSPAQ-IEKVEEVPDNVTPY--GEIER 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 254 EPITGFQKAMVKTMSAA-LKIPHFGYCDEVDLTELLKLREE-LKPIALARGIKLSYMPFFIKAASLGLLQFPILNSSVDE 331
Cdd:PRK14843 121 IPMTPMRKVIAQRMVESyLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 332 NCQTITYKASHNIGIAMDTKQGLVVPNVKNVQICSIFEIAAELNRLQNLGAVGQLSTTDLAGGTFTLSNIGSIGGTYAKA 411
Cdd:PRK14843 201 DGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGP 280
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514479320 412 VILPPEVAIGALGSIRALPRFnLNGEVYKAQIMNVSWSADHRIIDGATMSRFSNLWKSYLENPAFMLL 479
Cdd:PRK14843 281 IINQPNSAILGVSSTIEKPVV-VNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
62-481 |
1.38e-40 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 151.45 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 62 GQVVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETE 141
Cdd:PLN02226 89 GDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 142 AlkDSEEDVveTPAvshdehthqeikgQKTLATPAVrrlamenniKLSEVVGSGKDGRVLKEDILnylEKQTGAILPPSP 221
Cdd:PLN02226 169 E--DAASQV--TPS-------------QKIPETTDP---------KPSPPAEDKQKPKVESAPVA---EKPKAPSSPPPP 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 222 KAEIIPPPAQPKDRTVPIPISKPPVFIGKDKTEPITGFqkAMVKTMsaalkiphfgycDEVDLTELLKLREELKPIALAR 301
Cdd:PLN02226 220 KQSAKEPQLPPKERERRVPMTRLRKRVATRLKDSQNTF--ALLTTF------------NEVDMTNLMKLRSQYKDAFYEK 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 302 -GIKLSYMPFFIKAASLGLLQFPILNSSVDENcqTITYKASHNIGIAMDTKQGLVVPNVKNVQICSIFEIAAELNRLQNL 380
Cdd:PLN02226 286 hGVKLGLMSGFIKAAVSALQHQPVVNAVIDGD--DIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINGLAKK 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 381 GAVGQLSTTDLAGGTFTLSNIGSIGGTYAKAVILPPEVAIGALGSIRALPRFnLNGEVYKAQIMNVSWSADHRIIDGATM 460
Cdd:PLN02226 364 ANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMV-VGGSVVPRPMMYVALTYDHRLIDGREA 442
|
410 420
....*....|....*....|.
gi 514479320 461 SRFSNLWKSYLENPAFMLLDL 481
Cdd:PLN02226 443 VYFLRRVKDVVEDPQRLLLDI 463
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
65-138 |
6.06e-25 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 97.48 E-value: 6.06e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514479320 65 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 138
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
65-138 |
3.46e-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: 87.43 E-value: 3.46e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514479320 65 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 138
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
65-138 |
1.10e-20 |
|
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: 85.73 E-value: 1.10e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514479320 65 VQFKLSDIGEGIREVtVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 138
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
172-206 |
1.37e-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: 64.63 E-value: 1.37e-13
10 20 30
....*....|....*....|....*....|....*
gi 514479320 172 LATPAVRRLAMENNIKLSEVVGSGKDGRVLKEDIL 206
Cdd:pfam02817 2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
218-463 |
2.24e-12 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 69.53 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 218 PPSPKAEIIPPPAQPKDRTVPIPiskPPVFIGKDKTEPITGFQKAMVKTMSAALKIPHFGYCDEVDLTELLKLR----EE 293
Cdd:PRK12270 85 KPAAAAAAAAAPAAPPAAAAAAA---PAAAAVEDEVTPLRGAAAAVAKNMDASLEVPTATSVRAVPAKLLIDNRivinNH 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 294 LKpiaLARGIKLSY-------MpffIKAaslgLLQFPILNSSVDE--NCQTITYKASHNIGIAMDT--KQG---LVVPNV 359
Cdd:PRK12270 162 LK---RTRGGKVSFthligyaL---VQA----LKAFPNMNRHYAEvdGKPTLVTPAHVNLGLAIDLpkKDGsrqLVVPAI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 360 KNVQICSIFEIAAELNRLQNLGAVGQLSTTDLAGGTFTLSNIGSIGGTYAKAVILPPEVAIGALGSIRALPRFNLNGEVY 439
Cdd:PRK12270 232 KGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEYPAEFQGASEER 311
|
250 260
....*....|....*....|....*....
gi 514479320 440 KAQ-----IMNVSWSADHRIIDGATMSRF 463
Cdd:PRK12270 312 LAElgiskVMTLTSTYDHRIIQGAESGEF 340
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
73-218 |
5.59e-10 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 60.73 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 73 GEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDSEEDVVe 152
Cdd:PRK14875 11 GLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVSDAEIDAF- 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514479320 153 tpavshdehthqeikgqktlATPAVRRLAMEnNIKLSEVVGSGKDGRVLKEDIlNYLEKQTGAILP 218
Cdd:PRK14875 90 --------------------IAPFARRFAPE-GIDEEDAGPAPRKARIGGRTV-RYLRLGEGDGTP 133
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
69-138 |
5.67e-09 |
|
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: 52.44 E-value: 5.67e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514479320 69 LSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 138
Cdd:cd06663 4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
80-138 |
1.45e-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: 39.71 E-value: 1.45e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 514479320 80 TVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 138
Cdd:cd06850 9 TVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
78-121 |
2.98e-03 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 39.90 E-value: 2.98e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 514479320 78 EVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKL 121
Cdd:PRK11892 16 EGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKI 59
|
|
| |
