|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
94-509 |
1.03e-179 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 510.80 E-value: 1.03e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 94 FKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDS 173
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 174 EEDVVETPAVSHDEHTHQEIKGRK-----TLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLeKQTGAILPPSP 248
Cdd:PLN02528 81 RSDSLLLPTDSSNIVSLAESDERGsnlsgVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYA-AQKGVVKDSSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 249 KAEIMPPPPKPKDMTIPIPVSKppvfTGKDKTEPIKGFQKAMVKTMSAALKIPHFGYCDEVDLTELVKLREELKPIAFAR 328
Cdd:PLN02528 160 AEEATIAEQEEFSTSVSTPTEQ----SYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 329 GIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLG 408
Cdd:PLN02528 236 TVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 409 SVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGSIKAIPRFNQKGEVYKAQIVNVSWSADHRVIDGATMS 488
Cdd:PLN02528 316 AENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVA 395
|
410 420
....*....|....*....|.
gi 1622825551 489 RFSNLWKSYLENPAFMLLDLK 509
Cdd:PLN02528 396 RFCNEWKSYVEKPELLMLHMR 416
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
294-505 |
5.27e-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: 289.44 E-value: 5.27e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 294 MSAAL-KIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIG 372
Cdd:pfam00198 1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 373 IAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGS 452
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622825551 453 IKAIPRFNQkGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFML 505
Cdd:pfam00198 161 IRKRPVVVD-GEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
85-506 |
3.58e-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: 3.58e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 85 AALRGQVVQFKLSDIGeGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVD 164
Cdd:TIGR01348 110 AGQSSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILT 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 165 IETEALKDSEEDVVE-------------------------TPAVSHDEHThqEIKGRKTLATPAVRRLAMENNIKLSEVV 219
Cdd:TIGR01348 189 LSVAGSTPATAPAPAsaqpaaqspaatqpepaaapaaakaQAPAPQQAGT--QNPAKVDHAAPAVRRLAREFGVDLSAVK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 220 GSGKDGRILKEDILNYLEKQTGAIlPPSPKAeimppPPKPKDMTIPIPVSKPPVFtGKDKTEPIKGFQKAMVKTMSAA-L 298
Cdd:TIGR01348 267 GTGIKGRILREDVQRFVKEPSVRA-QAAAAS-----AAGGAPGALPWPNVDFSKF-GEVEEVDMSRIRKISGANLTRNwT 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 299 KIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTE 378
Cdd:TIGR01348 340 MIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTP 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 379 QGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIgaLGSIKAI-- 456
Cdd:TIGR01348 420 NGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAI--LGVSKSGme 497
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1622825551 457 PRFNQKgEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 506
Cdd:TIGR01348 498 PVWNGK-EFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
92-165 |
8.89e-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: 8.89e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622825551 92 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 165
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
92-165 |
4.07e-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: 87.04 E-value: 4.07e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622825551 92 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 165
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
94-509 |
1.03e-179 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 510.80 E-value: 1.03e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 94 FKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDS 173
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 174 EEDVVETPAVSHDEHTHQEIKGRK-----TLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLeKQTGAILPPSP 248
Cdd:PLN02528 81 RSDSLLLPTDSSNIVSLAESDERGsnlsgVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYA-AQKGVVKDSSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 249 KAEIMPPPPKPKDMTIPIPVSKppvfTGKDKTEPIKGFQKAMVKTMSAALKIPHFGYCDEVDLTELVKLREELKPIAFAR 328
Cdd:PLN02528 160 AEEATIAEQEEFSTSVSTPTEQ----SYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 329 GIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLG 408
Cdd:PLN02528 236 TVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 409 SVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGSIKAIPRFNQKGEVYKAQIVNVSWSADHRVIDGATMS 488
Cdd:PLN02528 316 AENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVA 395
|
410 420
....*....|....*....|.
gi 1622825551 489 RFSNLWKSYLENPAFMLLDLK 509
Cdd:PLN02528 396 RFCNEWKSYVEKPELLMLHMR 416
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
82-506 |
8.51e-157 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 457.36 E-value: 8.51e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 82 KTTAALRGQVVQFKLSDIGEgIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKP 161
Cdd:PRK11855 110 AAAAAAGGGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 162 LVDIETEALKDSEEDVVETPAVSHDEHTHQE------------------IKGRKTLATPAVRRLAMENNIKLSEVVGSGK 223
Cdd:PRK11855 189 LVVIEVAAAAPAAAAAPAAAAPAAAAAAAPApapaaaaapaaaapaaaaAPGKAPHASPAVRRLARELGVDLSQVKGTGK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 224 DGRILKEDILNYLEkqtGAILPPSPKAEIMPPPPKPKDMTIPIPVskpPVFT--GKDKTEPIKGFQKAMVKTMSAAL-KI 300
Cdd:PRK11855 269 KGRITKEDVQAFVK---GAMSAAAAAAAAAAAAGGGGLGLLPWPK---VDFSkfGEIETKPLSRIKKISAANLHRSWvTI 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 301 PHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQG 380
Cdd:PRK11855 343 PHVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNG 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 381 LIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGSIKAIPrFN 460
Cdd:PRK11855 423 LVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKP-VW 501
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1622825551 461 QKGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 506
Cdd:PRK11855 502 DGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
91-507 |
2.97e-131 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 387.22 E-value: 2.97e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 91 VVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETE-- 168
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEge 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 169 --------------ALKDSEEDVVETPAVSHDEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILN 234
Cdd:PRK11856 82 aeaaaaaeaapeapAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 235 YLEKQTGAILPPSPKaeimppppkpkdmtipiPVSKPPVFTGKDKTEPIKGFQKAMVKTMSAA-LKIPHFGYCDEVDLTE 313
Cdd:PRK11856 162 AAAAAAPAAAAAAAA-----------------AAAPPAAAAEGEERVPLSGMRKAIAKRMVESkREIPHFTLTDEVDVTA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 314 LVKLREELKPIAfargIKLSFMPFFLKAVSLGLLQFPILNASVDEncQNITYKASHNIGIAMDTEQGLIVPNVKNVQICS 393
Cdd:PRK11856 225 LLALRKQLKAIG----VKLTVTDFLIKAVALALKKFPELNASWDD--DAIVLKKYVNIGIAVATDGGLIVPVIRDADKKS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 394 IFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGSIKAIPRFnQKGEVYKAQIVNV 473
Cdd:PRK11856 299 LFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVV-VDGEIVVRKVMPL 377
|
410 420 430
....*....|....*....|....*....|....
gi 1622825551 474 SWSADHRVIDGATMSRFSNLWKSYLENPAFMLLD 507
Cdd:PRK11856 378 SLSFDHRVIDGADAARFLKALKELLENPALLLLE 411
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
294-505 |
5.27e-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: 289.44 E-value: 5.27e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 294 MSAAL-KIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIG 372
Cdd:pfam00198 1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 373 IAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGS 452
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622825551 453 IKAIPRFNQkGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFML 505
Cdd:pfam00198 161 IRKRPVVVD-GEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
89-500 |
6.46e-83 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 269.56 E-value: 6.46e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 89 GQVVQFKLSDIGEGirEVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETE 168
Cdd:PRK11854 204 AGVKDVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 169 --------ALKDSEEDV---------VETPAVSHDEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKED 231
Cdd:PRK11854 282 gaapaaapAKQEAAAPApaaakaeapAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKED 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 232 ILNYLEK-----QTGAILPPSPKAEIMPpppkpkdmtIPIPVSKPPVFtGKDKTEPIKGFQKAMVKTMSAAL-KIPHFGY 305
Cdd:PRK11854 362 VQAYVKDavkraEAAPAAAAAGGGGPGL---------LPWPKVDFSKF-GEIEEVELGRIQKISGANLHRNWvMIPHVTQ 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 306 CDEVDLTELVKLREELKPIAFAR--GIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIV 383
Cdd:PRK11854 432 FDKADITELEAFRKQQNAEAEKRklGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVV 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 384 PNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGSIKAIPRFNQKg 463
Cdd:PRK11854 512 PVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGK- 590
|
410 420 430
....*....|....*....|....*....|....*..
gi 1622825551 464 EVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLEN 500
Cdd:PRK11854 591 EFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSD 627
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
85-506 |
3.58e-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: 3.58e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 85 AALRGQVVQFKLSDIGeGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVD 164
Cdd:TIGR01348 110 AGQSSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILT 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 165 IETEALKDSEEDVVE-------------------------TPAVSHDEHThqEIKGRKTLATPAVRRLAMENNIKLSEVV 219
Cdd:TIGR01348 189 LSVAGSTPATAPAPAsaqpaaqspaatqpepaaapaaakaQAPAPQQAGT--QNPAKVDHAAPAVRRLAREFGVDLSAVK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 220 GSGKDGRILKEDILNYLEKQTGAIlPPSPKAeimppPPKPKDMTIPIPVSKPPVFtGKDKTEPIKGFQKAMVKTMSAA-L 298
Cdd:TIGR01348 267 GTGIKGRILREDVQRFVKEPSVRA-QAAAAS-----AAGGAPGALPWPNVDFSKF-GEVEEVDMSRIRKISGANLTRNwT 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 299 KIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTE 378
Cdd:TIGR01348 340 MIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTP 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 379 QGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIgaLGSIKAI-- 456
Cdd:TIGR01348 420 NGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAI--LGVSKSGme 497
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1622825551 457 PRFNQKgEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 506
Cdd:TIGR01348 498 PVWNGK-EFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
92-508 |
8.00e-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: 236.55 E-value: 8.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 92 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALK 171
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 172 D------SEEDVVETPAVShdEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLEKQTGAILP 245
Cdd:TIGR01347 81 TaappakSGEEKEETPAAS--AAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 246 PSPKAEimppppkpkdmtipipvSKPPVFTGKDKTEPIKGFQKAMVKTM-----SAALkIPHFgycDEVDLTELVKLREE 320
Cdd:TIGR01347 159 AAAAAA-----------------AAPAAATRPEERVKMTRLRQRIAERLkeaqnSTAM-LTTF---NEVDMSAVMELRKR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 321 LKPIAFAR-GIKLSFMPFFLKAVSLGLLQFPILNASVDENcqNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIAT 399
Cdd:TIGR01347 218 YKEEFEKKhGVKLGFMSFFVKAVVAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 400 ELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGSIKAIPRfnqkgeVYKAQIVN-----VS 474
Cdd:TIGR01347 296 EIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPV------AVNGQIEIrpmmyLA 369
|
410 420 430
....*....|....*....|....*....|....
gi 1622825551 475 WSADHRVIDGATMSRFSNLWKSYLENPAFMLLDL 508
Cdd:TIGR01347 370 LSYDHRLIDGKEAVTFLVTIKELLEDPRRLLLDL 403
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
197-501 |
2.00e-68 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 221.98 E-value: 2.00e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 197 KTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLEKQTGAilpPSPKAEIMPPPPKPKDMTiPIPVSKPPVFTG 276
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSA---PTPAEAASVSSAQQAAKT-AAPAAAPPKLEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 277 KdkTEPIKGFQKAMVKTMSAALK-IPHFGYCDEVDLTELVKLREELK-PIAFARGIKLSFMPFFLKAVSLGLLQFPILNA 354
Cdd:PRK11857 77 K--REKVAPIRKAIARAMTNSWSnVAYVNLVNEIDMTKLWDLRKSVKdPVLKTEGVKLTFLPFIAKAILIALKEFPIFAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 355 SVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGT 434
Cdd:PRK11857 155 KYDEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622825551 435 YTKPVILPPEVAIGALGSIKAIPRFnQKGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENP 501
Cdd:PRK11857 235 YGVPVINYPELAIAGVGAIIDKAIV-KNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
95-508 |
7.22e-68 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 223.56 E-value: 7.22e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 95 KLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEA----L 170
Cdd:PRK05704 6 KVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAaagaA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 171 KDSEEDVVETPAVSHDEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLEKQTGAILPPSPKA 250
Cdd:PRK05704 86 AAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAAPAAAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 251 eimppppkpkdmtipiPVSKPPVFTGK-DKTEPIKGFQK-------------AMVKTmsaalkiphFgycDEVDLTELVK 316
Cdd:PRK05704 166 ----------------PAAAPAPLGARpEERVPMTRLRKtiaerlleaqnttAMLTT---------F---NEVDMTPVMD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 317 LREELKPIAFAR-GIKLSFMPFFLKAVSLGLLQFPILNASVDENcqNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIF 395
Cdd:PRK05704 218 LRKQYKDAFEKKhGVKLGFMSFFVKAVVEALKRYPEVNASIDGD--DIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 396 DIATELNRLQKLGSVGQLSTTDLTGGTFTLSNigsiGGTY----TKPVILPPEVAIgaLG--SIKAIPRfnqkgeVYKAQ 469
Cdd:PRK05704 296 EIEKKIAELAKKARDGKLSIEELTGGTFTITN----GGVFgslmSTPIINPPQSAI--LGmhKIKERPV------AVNGQ 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1622825551 470 IVN-----VSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLDL 508
Cdd:PRK05704 364 IVIrpmmyLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLLDL 407
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
89-503 |
2.96e-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: 221.42 E-value: 2.96e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 89 GQVVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI--- 165
Cdd:TIGR02927 124 GEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIgda 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 166 --------ETEALKDSEEDVVETPAVSHDEHTHQEIKGRKTLA----------------------TPAVRRLAMENNIKL 215
Cdd:TIGR02927 204 naapaepaEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPApaktaapaaaapvssgdsgpyvTPLVRKLAKDKGVDL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 216 SEVVGSGKDGRILKEDILNYLEKQTGAILPPSPKAeimppppKPKDMTIPIPVSKPP-VFTGK--DKTEPIKGFQKAMVK 292
Cdd:TIGR02927 284 STVKGTGVGGRIRKQDVLAAAKAAEEARAAAAAPA-------AAAAPAAPAAAAKPAePDTAKlrGTTQKMNRIRQITAD 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 293 TMSAALKI-PHFGYCDEVDLTELVKLREELKPIAFAR-GIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHN 370
Cdd:TIGR02927 357 KTIESLQTsAQLTQVHEVDMTRVAALRARAKNDFLEKnGVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEH 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 371 IGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGAL 450
Cdd:TIGR02927 437 VGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGT 516
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622825551 451 GSIKAIPRF---NQKGEVYKA-QIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAF 503
Cdd:TIGR02927 517 GAIVKRPRVikdEDGGESIAIrSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEEGDF 573
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
103-506 |
5.49e-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: 206.57 E-value: 5.49e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 103 IREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYY--NLDDIAyVGKPLV-------DIET------ 167
Cdd:TIGR01349 11 MTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVpeGTKDVP-VNKPIAvlveekeDVADafknyk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 168 ------EALKDSEE--------------DVVETPAVSHDEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRI 227
Cdd:TIGR01349 90 lessasPAPKPSEIaptappsapkpspaPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVAGSGPNGRI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 228 LKEDILNYLEKQTgAILPPSPKAEIMPPPPKPkdmtipipvskPPVFTGKDKTEPIKGFQKAMVKTMSAALK-IPHFGYC 306
Cdd:TIGR01349 170 VKKDIESFVPQSP-ASANQQAAATTPATYPAA-----------APVSTGSYEDVPLSNIRKIIAKRLLESKQtIPHYYVS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 307 DEVDLTELVKLREELKPIAFARgIKLSFMPFFLKAVSLGLLQFPILNASVDENcqNITYKASHNIGIAMDTEQGLIVPNV 386
Cdd:TIGR01349 238 IECNVDKLLALRKELNAMASEV-YKLSVNDFIIKASALALREVPEANSSWTDN--FIRRYKNVDISVAVATPDGLITPIV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 387 KNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGSI--KAIPRFNQKGE 464
Cdd:TIGR01349 315 RNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVedVAVVDNDEEKG 394
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1622825551 465 VYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 506
Cdd:TIGR01349 395 FAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
95-508 |
1.53e-59 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 202.22 E-value: 1.53e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 95 KLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDSE 174
Cdd:PTZ00144 48 KVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 175 EdvVETPAVSHDEHTHQEIKGRKTLATPAvrrlamennIKLSEVVGSGKDgrilkedilnylEKQTGAILPPSPKAEImp 254
Cdd:PTZ00144 128 A--PAAAAAAKAEKTTPEKPKAAAPTPEP---------PAASKPTPPAAA------------KPPEPAPAAKPPPTPV-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 255 pppkpkDMTIPIPVSKPPVFTGKDKTEPIKGFQK--AMVKTMsaalkiphfgycDEVDLTELVKLREELKPIAFAR-GIK 331
Cdd:PTZ00144 183 ------ARADPRETRVPMSRMRQRIAERLKASQNtcAMLTTF------------NECDMSALMELRKEYKDDFQKKhGVK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 332 LSFMPFFLKAVSLGLLQFPILNASVDENCqnITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVG 411
Cdd:PTZ00144 245 LGFMSAFVKASTIALKKMPIVNAYIDGDE--IVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 412 QLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGSIK--AIPRFNQkgeVYKAQIVNVSWSADHRVIDGATMSR 489
Cdd:PTZ00144 323 KLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKkrPVVVGNE---IVIRPIMYLALTYDHRLIDGRDAVT 399
|
410
....*....|....*....
gi 1622825551 490 FSNLWKSYLENPAFMLLDL 508
Cdd:PTZ00144 400 FLKKIKDLIEDPARMLLDL 418
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
105-506 |
5.84e-46 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 168.49 E-value: 5.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 105 EVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYY------------------NLDDIAYVG--KPLVD 164
Cdd:PLN02744 126 EGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKgdgakeikvgeviaitveEEEDIGKFKdyKPSSS 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 165 IETEALKDSE------EDVVETPAVSHDEHTHQE----IKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILN 234
Cdd:PLN02744 206 AAPAAPKAKPsppppkEEEVEKPASSPEPKASKPsappSSGDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIED 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 235 YLEKQ-TGAILPPSPKAEIMPPPPkpkdmtIPIPVSKPPVFTGKdktepikgfqkamvKTMSAALKIPHFGYCDEVDLTE 313
Cdd:PLN02744 286 YLASGgKGATAPPSTDSKAPALDY------TDIPNTQIRKVTAS--------------RLLQSKQTIPHYYLTVDTRVDK 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 314 LVKLREELKPIAFARGIK-LSFMPFFLKAVSLGLLQFPILNAS-VDE---NCQNItykashNIGIAMDTEQGLIVPNVKN 388
Cdd:PLN02744 346 LMALRSQLNSLQEASGGKkISVNDLVIKAAALALRKVPQCNSSwTDDyirQYHNV------NINVAVQTENGLYVPVVKD 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 389 VQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGS-IGGTYTKPVILPPEVAIGALGSI--KAIPRfNQKGEV 465
Cdd:PLN02744 420 ADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGpFGIKQFCAIINPPQSAILAVGSAekRVIPG-SGPDQY 498
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1622825551 466 YKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 506
Cdd:PLN02744 499 NFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
201-506 |
1.23e-36 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 138.50 E-value: 1.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 201 TPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYL--EKQTGAILPPSPKAEIMPpppkpkdmtipIPVSKPPvfTGKD 278
Cdd:PRK14843 52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLpeNIENDSIKSPAQIEKVEE-----------VPDNVTP--YGEI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 279 KTEPIKGFQKAMVKTMSAA-LKIPHFGYCDEVDLTELVKLREE-LKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASV 356
Cdd:PRK14843 119 ERIPMTPMRKVIAQRMVESyLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 357 DENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYT 436
Cdd:PRK14843 199 TEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSF 278
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 437 KPVILPPEVAIGALGSIKAIPRFnQKGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 506
Cdd:PRK14843 279 GPIINQPNSAILGVSSTIEKPVV-VNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
71-508 |
6.16e-36 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 139.12 E-value: 6.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 71 SFKYSHPHHFLKTTAALRGQVVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYY 150
Cdd:PLN02226 71 SLVSSTLQRWVRPFSSESGDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 151 NLDDIAYVGKPLVDIETEALKDSE----EDVVETPAVSHDEHTHQEIKGRKTLATPAvrrlamenniklsevvgsgkdgr 226
Cdd:PLN02226 151 KEGDTVEPGTKVAIISKSEDAASQvtpsQKIPETTDPKPSPPAEDKQKPKVESAPVA----------------------- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 227 ilkedilnylEKQTGAILPPSPKAEimppppkpkdmtipipvSKPPVFTGKDKTEPIKgfQKAMVKTMSAALKIPHFGYC 306
Cdd:PLN02226 208 ----------EKPKAPSSPPPPKQS-----------------AKEPQLPPKERERRVP--MTRLRKRVATRLKDSQNTFA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 307 -----DEVDLTELVKLREELKPIAFAR-GIKLSFMPFFLKAVSLGLLQFPILNASVDENcqNITYKASHNIGIAMDTEQG 380
Cdd:PLN02226 259 llttfNEVDMTNLMKLRSQYKDAFYEKhGVKLGLMSGFIKAAVSALQHQPVVNAVIDGD--DIIYRDYVDISIAVGTSKG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 381 LIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGSIKAIPRFn 460
Cdd:PLN02226 337 LVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMV- 415
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1622825551 461 QKGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLDL 508
Cdd:PLN02226 416 VGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLLDI 463
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
92-165 |
8.89e-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: 8.89e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622825551 92 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 165
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
92-165 |
4.07e-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: 87.04 E-value: 4.07e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622825551 92 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 165
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
92-165 |
2.36e-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: 84.96 E-value: 2.36e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622825551 92 VQFKLSDIGEGIREVtVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 165
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 ... |
199-233 |
2.12e-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: 66.94 E-value: 2.12e-14
10 20 30
....*....|....*....|....*....|....*
gi 1622825551 199 LATPAVRRLAMENNIKLSEVVGSGKDGRILKEDIL 233
Cdd:pfam02817 2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
265-490 |
1.10e-11 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 67.61 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 265 PIPVSKPPVFTGKDKTEPIKGFQKAMVKTMSAALKIPhfgycdevdlTEL------VKLREELKPI-----AFARGIKLS 333
Cdd:PRK12270 102 AAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASLEVP----------TATsvravpAKLLIDNRIVinnhlKRTRGGKVS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 334 FMPFFLKAVSLGLLQFPILNASVDE--NCQNITYKASHNIGIAMDTEQ-----GLIVPNVKNVQICSIFDIATELNRLQK 406
Cdd:PRK12270 172 FTHLIGYALVQALKAFPNMNRHYAEvdGKPTLVTPAHVNLGLAIDLPKkdgsrQLVVPAIKGAETMDFAQFWAAYEDIVR 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 407 LGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVILPPEVAIGALGSIKAIPRFNQKGEVYKAQ-----IVNVSWSADHRV 481
Cdd:PRK12270 252 RARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEYPAEFQGASEERLAElgiskVMTLTSTYDHRI 331
|
....*....
gi 1622825551 482 IDGATMSRF 490
Cdd:PRK12270 332 IQGAESGEF 340
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
100-245 |
3.47e-10 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 61.50 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 100 GEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDSEEDVVe 179
Cdd:PRK14875 11 GLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVSDAEIDAF- 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622825551 180 tpavshdehthqeikgrktlATPAVRRLAMEnNIKLSEVVGSGKDGRILKEDIlNYLEKQTGAILP 245
Cdd:PRK14875 90 --------------------IAPFARRFAPE-GIDEEDAGPAPRKARIGGRTV-RYLRLGEGDGTP 133
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
96-165 |
6.55e-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: 6.55e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825551 96 LSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 165
Cdd:cd06663 4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
107-165 |
1.63e-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: 1.63e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622825551 107 TVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 165
Cdd:cd06850 9 TVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
105-148 |
2.44e-03 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 40.29 E-value: 2.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1622825551 105 EVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKL 148
Cdd:PRK11892 16 EGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKI 59
|
|
| |
