|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
67-482 |
1.01e-179 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 509.65 E-value: 1.01e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 67 FKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDS 146
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 147 EEDVVETPAVSHDEHTHQEIKGRK-----TLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLeKQTGAILPPSP 221
Cdd:PLN02528 81 RSDSLLLPTDSSNIVSLAESDERGsnlsgVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYA-AQKGVVKDSSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 222 KAEIMPPPPKPKDMTIPIPVSKppvfTGKDKTEPIKGFQKAMVKTMSAALKIPHFGYCDEVDLTELVKLREELKPIAFAR 301
Cdd:PLN02528 160 AEEATIAEQEEFSTSVSTPTEQ----SYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 302 GIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLG 381
Cdd:PLN02528 236 TVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 382 SVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGSIKAIPRFNQKGEVYKAQIVNVSWSADHRVIDGATMS 461
Cdd:PLN02528 316 AENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVA 395
|
410 420
....*....|....*....|.
gi 402855399 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 |
1.37e-96 |
|
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: 290.21 E-value: 1.37e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 267 MSAAL-KIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIG 345
Cdd:pfam00198 1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 346 IAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGS 425
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 402855399 426 IKAIPRFNQkGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFML 478
Cdd:pfam00198 161 IRKRPVVVD-GEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
58-479 |
1.75e-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: 244.40 E-value: 1.75e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 58 AALRGQVVQFKLSDIGeGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVD 137
Cdd:TIGR01348 110 AGQSSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILT 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 138 IETEALKDSEEDVVE-------------------------TPAVSHDEHThqEIKGRKTLATPAVRRLAMENNIKLSEVV 192
Cdd:TIGR01348 189 LSVAGSTPATAPAPAsaqpaaqspaatqpepaaapaaakaQAPAPQQAGT--QNPAKVDHAAPAVRRLAREFGVDLSAVK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 193 GSGKDGRILKEDILNYLEKQTGAIlPPSPKAeimppPPKPKDMTIPIPVSKPPVFtGKDKTEPIKGFQKAMVKTMSAA-L 271
Cdd:TIGR01348 267 GTGIKGRILREDVQRFVKEPSVRA-QAAAAS-----AAGGAPGALPWPNVDFSKF-GEVEEVDMSRIRKISGANLTRNwT 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 272 KIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTE 351
Cdd:TIGR01348 340 MIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTP 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 352 QGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIgaLGSIKAI-- 429
Cdd:TIGR01348 420 NGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAI--LGVSKSGme 497
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 402855399 430 PRFNQKgEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 479
Cdd:TIGR01348 498 PVWNGK-EFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
65-138 |
1.13e-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: 96.70 E-value: 1.13e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 402855399 65 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 138
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
65-138 |
5.66e-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: 5.66e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 402855399 65 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 138
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
67-482 |
1.01e-179 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 509.65 E-value: 1.01e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 67 FKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDS 146
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 147 EEDVVETPAVSHDEHTHQEIKGRK-----TLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLeKQTGAILPPSP 221
Cdd:PLN02528 81 RSDSLLLPTDSSNIVSLAESDERGsnlsgVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYA-AQKGVVKDSSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 222 KAEIMPPPPKPKDMTIPIPVSKppvfTGKDKTEPIKGFQKAMVKTMSAALKIPHFGYCDEVDLTELVKLREELKPIAFAR 301
Cdd:PLN02528 160 AEEATIAEQEEFSTSVSTPTEQ----SYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 302 GIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLG 381
Cdd:PLN02528 236 TVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 382 SVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGSIKAIPRFNQKGEVYKAQIVNVSWSADHRVIDGATMS 461
Cdd:PLN02528 316 AENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVA 395
|
410 420
....*....|....*....|.
gi 402855399 462 RFSNLWKSYLENPAFMLLDLK 482
Cdd:PLN02528 396 RFCNEWKSYVEKPELLMLHMR 416
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
55-479 |
7.98e-157 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 456.21 E-value: 7.98e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 55 KTTAALRGQVVQFKLSDIGEgIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKP 134
Cdd:PRK11855 110 AAAAAAGGGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 135 LVDIETEALKDSEEDVVETPAVSHDEHTHQE------------------IKGRKTLATPAVRRLAMENNIKLSEVVGSGK 196
Cdd:PRK11855 189 LVVIEVAAAAPAAAAAPAAAAPAAAAAAAPApapaaaaapaaaapaaaaAPGKAPHASPAVRRLARELGVDLSQVKGTGK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 197 DGRILKEDILNYLEkqtGAILPPSPKAEIMPPPPKPKDMTIPIPVskpPVFT--GKDKTEPIKGFQKAMVKTMSAAL-KI 273
Cdd:PRK11855 269 KGRITKEDVQAFVK---GAMSAAAAAAAAAAAAGGGGLGLLPWPK---VDFSkfGEIETKPLSRIKKISAANLHRSWvTI 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 274 PHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQG 353
Cdd:PRK11855 343 PHVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNG 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 354 LIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGSIKAIPrFN 433
Cdd:PRK11855 423 LVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKP-VW 501
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 402855399 434 QKGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 479
Cdd:PRK11855 502 DGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
64-480 |
1.62e-131 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 386.84 E-value: 1.62e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 64 VVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETE-- 141
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEge 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 142 --------------ALKDSEEDVVETPAVSHDEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILN 207
Cdd:PRK11856 82 aeaaaaaeaapeapAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 208 YLEKQTGAILPPSPKAEimppppkpkdmtipipvSKPPVFTGKDKTEPIKGFQKAMVKTMSAA-LKIPHFGYCDEVDLTE 286
Cdd:PRK11856 162 AAAAAAPAAAAAAAAAA-----------------APPAAAAEGEERVPLSGMRKAIAKRMVESkREIPHFTLTDEVDVTA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 287 LVKLREELKPIAfargIKLSFMPFFLKAVSLGLLQFPILNASVDEncQNITYKASHNIGIAMDTEQGLIVPNVKNVQICS 366
Cdd:PRK11856 225 LLALRKQLKAIG----VKLTVTDFLIKAVALALKKFPELNASWDD--DAIVLKKYVNIGIAVATDGGLIVPVIRDADKKS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 367 IFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGSIKAIPRFnQKGEVYKAQIVNV 446
Cdd:PRK11856 299 LFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVV-VDGEIVVRKVMPL 377
|
410 420 430
....*....|....*....|....*....|....
gi 402855399 447 SWSADHRVIDGATMSRFSNLWKSYLENPAFMLLD 480
Cdd:PRK11856 378 SLSFDHRVIDGADAARFLKALKELLENPALLLLE 411
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
267-478 |
1.37e-96 |
|
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: 290.21 E-value: 1.37e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 267 MSAAL-KIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIG 345
Cdd:pfam00198 1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 346 IAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGS 425
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 402855399 426 IKAIPRFNQkGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFML 478
Cdd:pfam00198 161 IRKRPVVVD-GEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
62-473 |
1.05e-82 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 268.02 E-value: 1.05e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 62 GQVVQFKLSDIGEGirEVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETE 141
Cdd:PRK11854 204 AGVKDVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 142 --------ALKDSEEDV---------VETPAVSHDEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKED 204
Cdd:PRK11854 282 gaapaaapAKQEAAAPApaaakaeapAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKED 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 205 ILNYLEK-----QTGAILPPSPKAEIMPpppkpkdmtIPIPVSKPPVFtGKDKTEPIKGFQKAMVKTMSAAL-KIPHFGY 278
Cdd:PRK11854 362 VQAYVKDavkraEAAPAAAAAGGGGPGL---------LPWPKVDFSKF-GEIEEVELGRIQKISGANLHRNWvMIPHVTQ 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 279 CDEVDLTELVKLREELKPIAFAR--GIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIV 356
Cdd:PRK11854 432 FDKADITELEAFRKQQNAEAEKRklGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVV 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 357 PNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGSIKAIPRFNQKg 436
Cdd:PRK11854 512 PVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGK- 590
|
410 420 430
....*....|....*....|....*....|....*..
gi 402855399 437 EVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLEN 473
Cdd:PRK11854 591 EFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSD 627
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
58-479 |
1.75e-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: 244.40 E-value: 1.75e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 58 AALRGQVVQFKLSDIGeGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVD 137
Cdd:TIGR01348 110 AGQSSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILT 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 138 IETEALKDSEEDVVE-------------------------TPAVSHDEHThqEIKGRKTLATPAVRRLAMENNIKLSEVV 192
Cdd:TIGR01348 189 LSVAGSTPATAPAPAsaqpaaqspaatqpepaaapaaakaQAPAPQQAGT--QNPAKVDHAAPAVRRLAREFGVDLSAVK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 193 GSGKDGRILKEDILNYLEKQTGAIlPPSPKAeimppPPKPKDMTIPIPVSKPPVFtGKDKTEPIKGFQKAMVKTMSAA-L 271
Cdd:TIGR01348 267 GTGIKGRILREDVQRFVKEPSVRA-QAAAAS-----AAGGAPGALPWPNVDFSKF-GEVEEVDMSRIRKISGANLTRNwT 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 272 KIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTE 351
Cdd:TIGR01348 340 MIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTP 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 352 QGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIgaLGSIKAI-- 429
Cdd:TIGR01348 420 NGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAI--LGVSKSGme 497
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 402855399 430 PRFNQKgEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 479
Cdd:TIGR01348 498 PVWNGK-EFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
65-481 |
6.77e-73 |
|
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: 235.78 E-value: 6.77e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 65 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALK 144
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 145 D------SEEDVVETPAVShdEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLEKQTGAILP 218
Cdd:TIGR01347 81 TaappakSGEEKEETPAAS--AAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 219 PSPKAEimppppkpkdmtipipvSKPPVFTGKDKTEPIKGFQKAMVKTM-----SAALkIPHFgycDEVDLTELVKLREE 293
Cdd:TIGR01347 159 AAAAAA-----------------AAPAAATRPEERVKMTRLRQRIAERLkeaqnSTAM-LTTF---NEVDMSAVMELRKR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 294 LKPIAFAR-GIKLSFMPFFLKAVSLGLLQFPILNASVDENcqNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIAT 372
Cdd:TIGR01347 218 YKEEFEKKhGVKLGFMSFFVKAVVAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 373 ELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGSIKAIPRfnqkgeVYKAQIVN-----VS 447
Cdd:TIGR01347 296 EIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPV------AVNGQIEIrpmmyLA 369
|
410 420 430
....*....|....*....|....*....|....
gi 402855399 448 WSADHRVIDGATMSRFSNLWKSYLENPAFMLLDL 481
Cdd:TIGR01347 370 LSYDHRLIDGKEAVTFLVTIKELLEDPRRLLLDL 403
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
170-474 |
1.10e-68 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 221.98 E-value: 1.10e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 170 KTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLEKQTGAilpPSPKAEIMPPPPKPKDMTiPIPVSKPPVFTG 249
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSA---PTPAEAASVSSAQQAAKT-AAPAAAPPKLEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 250 KdkTEPIKGFQKAMVKTMSAALK-IPHFGYCDEVDLTELVKLREELK-PIAFARGIKLSFMPFFLKAVSLGLLQFPILNA 327
Cdd:PRK11857 77 K--REKVAPIRKAIARAMTNSWSnVAYVNLVNEIDMTKLWDLRKSVKdPVLKTEGVKLTFLPFIAKAILIALKEFPIFAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 328 SVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGT 407
Cdd:PRK11857 155 KYDEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 402855399 408 YTKPVIMPPEVAIGALGSIKAIPRFnQKGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENP 474
Cdd:PRK11857 235 YGVPVINYPELAIAGVGAIIDKAIV-KNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
68-481 |
9.79e-68 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 222.40 E-value: 9.79e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 68 KLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEA----L 143
Cdd:PRK05704 6 KVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAaagaA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 144 KDSEEDVVETPAVSHDEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLEKQTGAILPPSPKA 223
Cdd:PRK05704 86 AAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAAPAAAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 224 eimppppkpkdmtipiPVSKPPVFTGK-DKTEPIKGFQK-------------AMVKTmsaalkiphFgycDEVDLTELVK 289
Cdd:PRK05704 166 ----------------PAAAPAPLGARpEERVPMTRLRKtiaerlleaqnttAMLTT---------F---NEVDMTPVMD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 290 LREELKPIAFAR-GIKLSFMPFFLKAVSLGLLQFPILNASVDENcqNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIF 368
Cdd:PRK05704 218 LRKQYKDAFEKKhGVKLGFMSFFVKAVVEALKRYPEVNASIDGD--DIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 369 DIATELNRLQKLGSVGQLSTTDLTGGTFTLSNigsiGGTY----TKPVIMPPEVAIgaLG--SIKAIPRfnqkgeVYKAQ 442
Cdd:PRK05704 296 EIEKKIAELAKKARDGKLSIEELTGGTFTITN----GGVFgslmSTPIINPPQSAI--LGmhKIKERPV------AVNGQ 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 402855399 443 IVN-----VSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLDL 481
Cdd:PRK05704 364 IVIrpmmyLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLLDL 407
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
62-476 |
3.49e-65 |
|
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: 220.65 E-value: 3.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 62 GQVVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI--- 138
Cdd:TIGR02927 124 GEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIgda 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 139 --------ETEALKDSEEDVVETPAVSHDEHTHQEIKGRKTLA----------------------TPAVRRLAMENNIKL 188
Cdd:TIGR02927 204 naapaepaEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPApaktaapaaaapvssgdsgpyvTPLVRKLAKDKGVDL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 189 SEVVGSGKDGRILKEDILNYLEKQTGAILPPSPKAeimppppKPKDMTIPIPVSKPP-VFTGK--DKTEPIKGFQKAMVK 265
Cdd:TIGR02927 284 STVKGTGVGGRIRKQDVLAAAKAAEEARAAAAAPA-------AAAAPAAPAAAAKPAePDTAKlrGTTQKMNRIRQITAD 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 266 TMSAALKI-PHFGYCDEVDLTELVKLREELKPIAFAR-GIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHN 343
Cdd:TIGR02927 357 KTIESLQTsAQLTQVHEVDMTRVAALRARAKNDFLEKnGVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEH 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 344 IGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGAL 423
Cdd:TIGR02927 437 VGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGT 516
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 402855399 424 GSIKAIPRF---NQKGEVYKA-QIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAF 476
Cdd:TIGR02927 517 GAIVKRPRVikdEDGGESIAIrSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEEGDF 573
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
76-479 |
3.15e-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: 206.18 E-value: 3.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 76 IREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYY--NLDDIAyVGKPLV-------DIET------ 140
Cdd:TIGR01349 11 MTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVpeGTKDVP-VNKPIAvlveekeDVADafknyk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 141 ------EALKDSEE--------------DVVETPAVSHDEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRI 200
Cdd:TIGR01349 90 lessasPAPKPSEIaptappsapkpspaPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVAGSGPNGRI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 201 LKEDILNYLEKQTgAILPPSPKAEIMPPPPKPkdmtipipvskPPVFTGKDKTEPIKGFQKAMVKTMSAALK-IPHFGYC 279
Cdd:TIGR01349 170 VKKDIESFVPQSP-ASANQQAAATTPATYPAA-----------APVSTGSYEDVPLSNIRKIIAKRLLESKQtIPHYYVS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 280 DEVDLTELVKLREELKPIAFARgIKLSFMPFFLKAVSLGLLQFPILNASVDENcqNITYKASHNIGIAMDTEQGLIVPNV 359
Cdd:TIGR01349 238 IECNVDKLLALRKELNAMASEV-YKLSVNDFIIKASALALREVPEANSSWTDN--FIRRYKNVDISVAVATPDGLITPIV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 360 KNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGSI--KAIPRFNQKGE 437
Cdd:TIGR01349 315 RNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVedVAVVDNDEEKG 394
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 402855399 438 VYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 479
Cdd:TIGR01349 395 FAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
68-481 |
8.40e-60 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 202.22 E-value: 8.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 68 KLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDSE 147
Cdd:PTZ00144 48 KVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 148 EdvVETPAVSHDEHTHQEIKGRKTLATPAvrrlamennIKLSEVVGSGKDgrilkedilnylEKQTGAILPPSPKAEImp 227
Cdd:PTZ00144 128 A--PAAAAAAKAEKTTPEKPKAAAPTPEP---------PAASKPTPPAAA------------KPPEPAPAAKPPPTPV-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 228 pppkpkDMTIPIPVSKPPVFTGKDKTEPIKGFQK--AMVKTMsaalkiphfgycDEVDLTELVKLREELKPIAFAR-GIK 304
Cdd:PTZ00144 183 ------ARADPRETRVPMSRMRQRIAERLKASQNtcAMLTTF------------NECDMSALMELRKEYKDDFQKKhGVK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 305 LSFMPFFLKAVSLGLLQFPILNASVDENCqnITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVG 384
Cdd:PTZ00144 245 LGFMSAFVKASTIALKKMPIVNAYIDGDE--IVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 385 QLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGSIK--AIPRFNQkgeVYKAQIVNVSWSADHRVIDGATMSR 462
Cdd:PTZ00144 323 KLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKkrPVVVGNE---IVIRPIMYLALTYDHRLIDGRDAVT 399
|
410
....*....|....*....
gi 402855399 463 FSNLWKSYLENPAFMLLDL 481
Cdd:PTZ00144 400 FLKKIKDLIEDPARMLLDL 418
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
78-479 |
5.30e-46 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 168.11 E-value: 5.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 78 EVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYY------------------NLDDIAYVG--KPLVD 137
Cdd:PLN02744 126 EGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKgdgakeikvgeviaitveEEEDIGKFKdyKPSSS 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 138 IETEALKDSE------EDVVETPAVSHDEHTHQE----IKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILN 207
Cdd:PLN02744 206 AAPAAPKAKPsppppkEEEVEKPASSPEPKASKPsappSSGDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIED 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 208 YLEKQ-TGAILPPSPKAEIMPPPPkpkdmtIPIPVSKPPVFTGKdktepikgfqkamvKTMSAALKIPHFGYCDEVDLTE 286
Cdd:PLN02744 286 YLASGgKGATAPPSTDSKAPALDY------TDIPNTQIRKVTAS--------------RLLQSKQTIPHYYLTVDTRVDK 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 287 LVKLREELKPIAFARGIK-LSFMPFFLKAVSLGLLQFPILNAS-VDE---NCQNItykashNIGIAMDTEQGLIVPNVKN 361
Cdd:PLN02744 346 LMALRSQLNSLQEASGGKkISVNDLVIKAAALALRKVPQCNSSwTDDyirQYHNV------NINVAVQTENGLYVPVVKD 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 362 VQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGS-IGGTYTKPVIMPPEVAIGALGSI--KAIPRfNQKGEV 438
Cdd:PLN02744 420 ADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGpFGIKQFCAIINPPQSAILAVGSAekRVIPG-SGPDQY 498
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 402855399 439 YKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 479
Cdd:PLN02744 499 NFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
174-479 |
9.26e-37 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 138.50 E-value: 9.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 174 TPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYL--EKQTGAILPPSPKAEIMPpppkpkdmtipIPVSKPPvfTGKD 251
Cdd:PRK14843 52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLpeNIENDSIKSPAQIEKVEE-----------VPDNVTP--YGEI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 252 KTEPIKGFQKAMVKTMSAA-LKIPHFGYCDEVDLTELVKLREE-LKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASV 329
Cdd:PRK14843 119 ERIPMTPMRKVIAQRMVESyLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 330 DENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYT 409
Cdd:PRK14843 199 TEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSF 278
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 410 KPVIMPPEVAIGALGSIKAIPRFnQKGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 479
Cdd:PRK14843 279 GPIINQPNSAILGVSSTIEKPVV-VNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
44-481 |
2.21e-36 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 139.89 E-value: 2.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 44 SFKYSHPHHFLKTTAALRGQVVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYY 123
Cdd:PLN02226 71 SLVSSTLQRWVRPFSSESGDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 124 NLDDIAYVGKPLVDIETEALKDSE----EDVVETPAVSHDEHTHQEIKGRKTLATPAvrrlamenniklsevvgsgkdgr 199
Cdd:PLN02226 151 KEGDTVEPGTKVAIISKSEDAASQvtpsQKIPETTDPKPSPPAEDKQKPKVESAPVA----------------------- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 200 ilkedilnylEKQTGAILPPSPKAEimppppkpkdmtipipvSKPPVFTGKDKTEPIKgfQKAMVKTMSAALKIPHFGYC 279
Cdd:PLN02226 208 ----------EKPKAPSSPPPPKQS-----------------AKEPQLPPKERERRVP--MTRLRKRVATRLKDSQNTFA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 280 -----DEVDLTELVKLREELKPIAFAR-GIKLSFMPFFLKAVSLGLLQFPILNASVDENcqNITYKASHNIGIAMDTEQG 353
Cdd:PLN02226 259 llttfNEVDMTNLMKLRSQYKDAFYEKhGVKLGLMSGFIKAAVSALQHQPVVNAVIDGD--DIIYRDYVDISIAVGTSKG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 354 LIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGSIKAIPRFn 433
Cdd:PLN02226 337 LVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMV- 415
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 402855399 434 QKGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLDL 481
Cdd:PLN02226 416 VGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLLDI 463
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
65-138 |
1.13e-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: 96.70 E-value: 1.13e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 402855399 65 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 138
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
65-138 |
5.66e-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: 5.66e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 402855399 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 |
3.51e-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: 84.19 E-value: 3.51e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 402855399 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 |
2.51e-14 |
|
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: 66.56 E-value: 2.51e-14
10 20 30
....*....|....*....|....*....|....*
gi 402855399 172 LATPAVRRLAMENNIKLSEVVGSGKDGRILKEDIL 206
Cdd:pfam02817 2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
238-463 |
6.02e-13 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 71.46 E-value: 6.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 238 PIPVSKPPVFTGKDKTEPIKGFQKAMVKTMSAALKIPhfgycdevdlTEL------VKLREELKPI-----AFARGIKLS 306
Cdd:PRK12270 102 AAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASLEVP----------TATsvravpAKLLIDNRIVinnhlKRTRGGKVS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 307 FMPFFLKAVSLGLLQFPILNASVDE--NCQNITYKASHNIGIAMDTEQ-----GLIVPNVKNVQICSIFDIATELNRLQK 379
Cdd:PRK12270 172 FTHLIGYALVQALKAFPNMNRHYAEvdGKPTLVTPAHVNLGLAIDLPKkdgsrQLVVPAIKGAETMDFAQFWAAYEDIVR 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 380 LGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGSIKAIPRFNQKGEVYKAQ-----IVNVSWSADHRV 454
Cdd:PRK12270 252 RARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEYPAEFQGASEERLAElgiskVMTLTSTYDHRI 331
|
....*....
gi 402855399 455 IDGATMSRF 463
Cdd:PRK12270 332 IQGAESGEF 340
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
73-218 |
3.15e-10 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 61.50 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 73 GEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDSEEDVVe 152
Cdd:PRK14875 11 GLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVSDAEIDAF- 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 402855399 153 tpavshdehthqeikgrktlATPAVRRLAMEnNIKLSEVVGSGKDGRILKEDIlNYLEKQTGAILP 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 |
7.52e-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: 52.06 E-value: 7.52e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855399 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 |
1.76e-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: 1.76e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 402855399 80 TVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 138
Cdd:cd06850 9 TVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
78-121 |
2.60e-03 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 40.29 E-value: 2.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 402855399 78 EVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKL 121
Cdd:PRK11892 16 EGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKI 59
|
|
| |
