|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
53-468 |
5.41e-180 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 509.65 E-value: 5.41e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 53 FKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDS 132
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 133 EEDVVETPAVSHDEHTHQEIKGRK-----TLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLeKQTGAILPPSP 207
Cdd:PLN02528 81 RSDSLLLPTDSSNIVSLAESDERGsnlsgVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYA-AQKGVVKDSSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 208 KAEIMPPPPKPKDMTIPIPVSKppvfTGKDKTEPIKGFQKAMVKTMSAALKIPHFGYCDEVDLTELVKLREELKPIAFAR 287
Cdd:PLN02528 160 AEEATIAEQEEFSTSVSTPTEQ----SYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 288 GIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLG 367
Cdd:PLN02528 236 TVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 368 SVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGSIKAIPRFNQKGEVYKAQIVNVSWSADHRVIDGATMS 447
Cdd:PLN02528 316 AENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVA 395
|
410 420
....*....|....*....|.
gi 1777244800 448 RFSNLWKSYLENPAFMLLDLK 468
Cdd:PLN02528 396 RFCNEWKSYVEKPELLMLHMR 416
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
253-464 |
5.17e-97 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 290.60 E-value: 5.17e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 253 MSAAL-KIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIG 331
Cdd:pfam00198 1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 332 IAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGS 411
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1777244800 412 IKAIPRFNQkGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFML 464
Cdd:pfam00198 161 IRKRPVVVD-GEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
44-465 |
9.38e-75 |
|
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: 9.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 44 AALRGQVVQFKLSDIGeGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVD 123
Cdd:TIGR01348 110 AGQSSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILT 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 124 IETEALKDSEEDVVE-------------------------TPAVSHDEHThqEIKGRKTLATPAVRRLAMENNIKLSEVV 178
Cdd:TIGR01348 189 LSVAGSTPATAPAPAsaqpaaqspaatqpepaaapaaakaQAPAPQQAGT--QNPAKVDHAAPAVRRLAREFGVDLSAVK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 179 GSGKDGRILKEDILNYLEKQTGAIlPPSPKAeimppPPKPKDMTIPIPVSKPPVFtGKDKTEPIKGFQKAMVKTMSAA-L 257
Cdd:TIGR01348 267 GTGIKGRILREDVQRFVKEPSVRA-QAAAAS-----AAGGAPGALPWPNVDFSKF-GEVEEVDMSRIRKISGANLTRNwT 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 258 KIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTE 337
Cdd:TIGR01348 340 MIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTP 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 338 QGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIgaLGSIKAI-- 415
Cdd:TIGR01348 420 NGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAI--LGVSKSGme 497
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1777244800 416 PRFNQKgEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 465
Cdd:TIGR01348 498 PVWNGK-EFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
51-124 |
1.46e-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: 96.32 E-value: 1.46e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1777244800 51 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 124
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
51-124 |
6.23e-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: 86.27 E-value: 6.23e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1777244800 51 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 124
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
53-468 |
5.41e-180 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 509.65 E-value: 5.41e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 53 FKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDS 132
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 133 EEDVVETPAVSHDEHTHQEIKGRK-----TLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLeKQTGAILPPSP 207
Cdd:PLN02528 81 RSDSLLLPTDSSNIVSLAESDERGsnlsgVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYA-AQKGVVKDSSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 208 KAEIMPPPPKPKDMTIPIPVSKppvfTGKDKTEPIKGFQKAMVKTMSAALKIPHFGYCDEVDLTELVKLREELKPIAFAR 287
Cdd:PLN02528 160 AEEATIAEQEEFSTSVSTPTEQ----SYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 288 GIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLG 367
Cdd:PLN02528 236 TVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 368 SVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGSIKAIPRFNQKGEVYKAQIVNVSWSADHRVIDGATMS 447
Cdd:PLN02528 316 AENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVA 395
|
410 420
....*....|....*....|.
gi 1777244800 448 RFSNLWKSYLENPAFMLLDLK 468
Cdd:PLN02528 396 RFCNEWKSYVEKPELLMLHMR 416
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
41-465 |
3.10e-157 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 456.59 E-value: 3.10e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 41 KTTAALRGQVVQFKLSDIGEgIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKP 120
Cdd:PRK11855 110 AAAAAAGGGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 121 LVDIETEALKDSEEDVVETPAVSHDEHTHQE------------------IKGRKTLATPAVRRLAMENNIKLSEVVGSGK 182
Cdd:PRK11855 189 LVVIEVAAAAPAAAAAPAAAAPAAAAAAAPApapaaaaapaaaapaaaaAPGKAPHASPAVRRLARELGVDLSQVKGTGK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 183 DGRILKEDILNYLEkqtGAILPPSPKAEIMPPPPKPKDMTIPIPVskpPVFT--GKDKTEPIKGFQKAMVKTMSAAL-KI 259
Cdd:PRK11855 269 KGRITKEDVQAFVK---GAMSAAAAAAAAAAAAGGGGLGLLPWPK---VDFSkfGEIETKPLSRIKKISAANLHRSWvTI 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 260 PHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQG 339
Cdd:PRK11855 343 PHVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNG 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 340 LIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGSIKAIPrFN 419
Cdd:PRK11855 423 LVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKP-VW 501
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1777244800 420 QKGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 465
Cdd:PRK11855 502 DGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
50-466 |
3.25e-132 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 387.99 E-value: 3.25e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 50 VVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETE-- 127
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEge 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 128 --------------ALKDSEEDVVETPAVSHDEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILN 193
Cdd:PRK11856 82 aeaaaaaeaapeapAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 194 YLEKQTGAILPPSPKaeimppppkpkdmtipiPVSKPPVFTGKDKTEPIKGFQKAMVKTMSAA-LKIPHFGYCDEVDLTE 272
Cdd:PRK11856 162 AAAAAAPAAAAAAAA-----------------AAAPPAAAAEGEERVPLSGMRKAIAKRMVESkREIPHFTLTDEVDVTA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 273 LVKLREELKPIAfargIKLSFMPFFLKAVSLGLLQFPILNASVDEncQNITYKASHNIGIAMDTEQGLIVPNVKNVQICS 352
Cdd:PRK11856 225 LLALRKQLKAIG----VKLTVTDFLIKAVALALKKFPELNASWDD--DAIVLKKYVNIGIAVATDGGLIVPVIRDADKKS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 353 IFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGSIKAIPRFnQKGEVYKAQIVNV 432
Cdd:PRK11856 299 LFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVV-VDGEIVVRKVMPL 377
|
410 420 430
....*....|....*....|....*....|....
gi 1777244800 433 SWSADHRVIDGATMSRFSNLWKSYLENPAFMLLD 466
Cdd:PRK11856 378 SLSFDHRVIDGADAARFLKALKELLENPALLLLE 411
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
253-464 |
5.17e-97 |
|
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Pssm-ID: 425518 [Multi-domain] Cd Length: 212 Bit Score: 290.60 E-value: 5.17e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 253 MSAAL-KIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIG 331
Cdd:pfam00198 1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 332 IAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGS 411
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1777244800 412 IKAIPRFNQkGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFML 464
Cdd:pfam00198 161 IRKRPVVVD-GEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
48-459 |
5.52e-83 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 268.41 E-value: 5.52e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 48 GQVVQFKLSDIGEGirEVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETE 127
Cdd:PRK11854 204 AGVKDVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 128 --------ALKDSEEDV---------VETPAVSHDEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKED 190
Cdd:PRK11854 282 gaapaaapAKQEAAAPApaaakaeapAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGRILKED 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 191 ILNYLEK-----QTGAILPPSPKAEIMPpppkpkdmtIPIPVSKPPVFtGKDKTEPIKGFQKAMVKTMSAAL-KIPHFGY 264
Cdd:PRK11854 362 VQAYVKDavkraEAAPAAAAAGGGGPGL---------LPWPKVDFSKF-GEIEEVELGRIQKISGANLHRNWvMIPHVTQ 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 265 CDEVDLTELVKLREELKPIAFAR--GIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIV 342
Cdd:PRK11854 432 FDKADITELEAFRKQQNAEAEKRklGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTPNGLVV 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 343 PNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGSIKAIPRFNQKg 422
Cdd:PRK11854 512 PVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGK- 590
|
410 420 430
....*....|....*....|....*....|....*..
gi 1777244800 423 EVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLEN 459
Cdd:PRK11854 591 EFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSD 627
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
44-465 |
9.38e-75 |
|
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: 9.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 44 AALRGQVVQFKLSDIGeGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVD 123
Cdd:TIGR01348 110 AGQSSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILT 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 124 IETEALKDSEEDVVE-------------------------TPAVSHDEHThqEIKGRKTLATPAVRRLAMENNIKLSEVV 178
Cdd:TIGR01348 189 LSVAGSTPATAPAPAsaqpaaqspaatqpepaaapaaakaQAPAPQQAGT--QNPAKVDHAAPAVRRLAREFGVDLSAVK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 179 GSGKDGRILKEDILNYLEKQTGAIlPPSPKAeimppPPKPKDMTIPIPVSKPPVFtGKDKTEPIKGFQKAMVKTMSAA-L 257
Cdd:TIGR01348 267 GTGIKGRILREDVQRFVKEPSVRA-QAAAAS-----AAGGAPGALPWPNVDFSKF-GEVEEVDMSRIRKISGANLTRNwT 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 258 KIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHNIGIAMDTE 337
Cdd:TIGR01348 340 MIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVDTP 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 338 QGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIgaLGSIKAI-- 415
Cdd:TIGR01348 420 NGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAI--LGVSKSGme 497
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1777244800 416 PRFNQKgEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 465
Cdd:TIGR01348 498 PVWNGK-EFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
51-467 |
3.17e-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: 236.17 E-value: 3.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 51 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALK 130
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 131 D------SEEDVVETPAVShdEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLEKQTGAILP 204
Cdd:TIGR01347 81 TaappakSGEEKEETPAAS--AAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 205 PSPKAEimppppkpkdmtipipvSKPPVFTGKDKTEPIKGFQKAMVKTM-----SAALkIPHFgycDEVDLTELVKLREE 279
Cdd:TIGR01347 159 AAAAAA-----------------AAPAAATRPEERVKMTRLRQRIAERLkeaqnSTAM-LTTF---NEVDMSAVMELRKR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 280 LKPIAFAR-GIKLSFMPFFLKAVSLGLLQFPILNASVDENcqNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIAT 358
Cdd:TIGR01347 218 YKEEFEKKhGVKLGFMSFFVKAVVAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 359 ELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGSIKAIPRfnqkgeVYKAQIVN-----VS 433
Cdd:TIGR01347 296 EIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERPV------AVNGQIEIrpmmyLA 369
|
410 420 430
....*....|....*....|....*....|....
gi 1777244800 434 WSADHRVIDGATMSRFSNLWKSYLENPAFMLLDL 467
Cdd:TIGR01347 370 LSYDHRLIDGKEAVTFLVTIKELLEDPRRLLLDL 403
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
156-460 |
5.20e-69 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 222.36 E-value: 5.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 156 KTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLEKQTGAilpPSPKAEIMPPPPKPKDMTiPIPVSKPPVFTG 235
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSA---PTPAEAASVSSAQQAAKT-AAPAAAPPKLEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 236 KdkTEPIKGFQKAMVKTMSAALK-IPHFGYCDEVDLTELVKLREELK-PIAFARGIKLSFMPFFLKAVSLGLLQFPILNA 313
Cdd:PRK11857 77 K--REKVAPIRKAIARAMTNSWSnVAYVNLVNEIDMTKLWDLRKSVKdPVLKTEGVKLTFLPFIAKAILIALKEFPIFAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 314 SVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGT 393
Cdd:PRK11857 155 KYDEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1777244800 394 YTKPVIMPPEVAIGALGSIKAIPRFnQKGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENP 460
Cdd:PRK11857 235 YGVPVINYPELAIAGVGAIIDKAIV-KNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
54-467 |
3.58e-68 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 223.17 E-value: 3.58e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 54 KLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEA----L 129
Cdd:PRK05704 6 KVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAaagaA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 130 KDSEEDVVETPAVSHDEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLEKQTGAILPPSPKA 209
Cdd:PRK05704 86 AAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAAAAAAPAAPAAAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 210 eimppppkpkdmtipiPVSKPPVFTGK-DKTEPIKGFQK-------------AMVKTmsaalkiphFgycDEVDLTELVK 275
Cdd:PRK05704 166 ----------------PAAAPAPLGARpEERVPMTRLRKtiaerlleaqnttAMLTT---------F---NEVDMTPVMD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 276 LREELKPIAFAR-GIKLSFMPFFLKAVSLGLLQFPILNASVDENcqNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIF 354
Cdd:PRK05704 218 LRKQYKDAFEKKhGVKLGFMSFFVKAVVEALKRYPEVNASIDGD--DIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 355 DIATELNRLQKLGSVGQLSTTDLTGGTFTLSNigsiGGTY----TKPVIMPPEVAIgaLG--SIKAIPRfnqkgeVYKAQ 428
Cdd:PRK05704 296 EIEKKIAELAKKARDGKLSIEELTGGTFTITN----GGVFgslmSTPIINPPQSAI--LGmhKIKERPV------AVNGQ 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1777244800 429 IVN-----VSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLDL 467
Cdd:PRK05704 364 IVIrpmmyLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLLDL 407
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
48-462 |
2.16e-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: 2.16e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 48 GQVVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI--- 124
Cdd:TIGR02927 124 GEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIgda 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 125 --------ETEALKDSEEDVVETPAVSHDEHTHQEIKGRKTLA----------------------TPAVRRLAMENNIKL 174
Cdd:TIGR02927 204 naapaepaEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPApaktaapaaaapvssgdsgpyvTPLVRKLAKDKGVDL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 175 SEVVGSGKDGRILKEDILNYLEKQTGAILPPSPKAeimppppKPKDMTIPIPVSKPP-VFTGK--DKTEPIKGFQKAMVK 251
Cdd:TIGR02927 284 STVKGTGVGGRIRKQDVLAAAKAAEEARAAAAAPA-------AAAAPAAPAAAAKPAePDTAKlrGTTQKMNRIRQITAD 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 252 TMSAALKI-PHFGYCDEVDLTELVKLREELKPIAFAR-GIKLSFMPFFLKAVSLGLLQFPILNASVDENCQNITYKASHN 329
Cdd:TIGR02927 357 KTIESLQTsAQLTQVHEVDMTRVAALRARAKNDFLEKnGVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEH 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 330 IGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGAL 409
Cdd:TIGR02927 437 VGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGT 516
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1777244800 410 GSIKAIPRF---NQKGEVYKA-QIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAF 462
Cdd:TIGR02927 517 GAIVKRPRVikdEDGGESIAIrSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEEGDF 573
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
62-465 |
2.39e-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: 2.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 62 IREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYY--NLDDIAyVGKPLV-------DIET------ 126
Cdd:TIGR01349 11 MTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVpeGTKDVP-VNKPIAvlveekeDVADafknyk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 127 ------EALKDSEE--------------DVVETPAVSHDEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRI 186
Cdd:TIGR01349 90 lessasPAPKPSEIaptappsapkpspaPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVAGSGPNGRI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 187 LKEDILNYLEKQTgAILPPSPKAEIMPPPPKPkdmtipipvskPPVFTGKDKTEPIKGFQKAMVKTMSAALK-IPHFGYC 265
Cdd:TIGR01349 170 VKKDIESFVPQSP-ASANQQAAATTPATYPAA-----------APVSTGSYEDVPLSNIRKIIAKRLLESKQtIPHYYVS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 266 DEVDLTELVKLREELKPIAFARgIKLSFMPFFLKAVSLGLLQFPILNASVDENcqNITYKASHNIGIAMDTEQGLIVPNV 345
Cdd:TIGR01349 238 IECNVDKLLALRKELNAMASEV-YKLSVNDFIIKASALALREVPEANSSWTDN--FIRRYKNVDISVAVATPDGLITPIV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 346 KNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGSI--KAIPRFNQKGE 423
Cdd:TIGR01349 315 RNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVedVAVVDNDEEKG 394
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1777244800 424 VYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 465
Cdd:TIGR01349 395 FAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
54-467 |
5.47e-60 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 202.22 E-value: 5.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 54 KLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDSE 133
Cdd:PTZ00144 48 KVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 134 EdvVETPAVSHDEHTHQEIKGRKTLATPAvrrlamennIKLSEVVGSGKDgrilkedilnylEKQTGAILPPSPKAEImp 213
Cdd:PTZ00144 128 A--PAAAAAAKAEKTTPEKPKAAAPTPEP---------PAASKPTPPAAA------------KPPEPAPAAKPPPTPV-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 214 pppkpkDMTIPIPVSKPPVFTGKDKTEPIKGFQK--AMVKTMsaalkiphfgycDEVDLTELVKLREELKPIAFAR-GIK 290
Cdd:PTZ00144 183 ------ARADPRETRVPMSRMRQRIAERLKASQNtcAMLTTF------------NECDMSALMELRKEYKDDFQKKhGVK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 291 LSFMPFFLKAVSLGLLQFPILNASVDENCqnITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVG 370
Cdd:PTZ00144 245 LGFMSAFVKASTIALKKMPIVNAYIDGDE--IVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 371 QLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGSIK--AIPRFNQkgeVYKAQIVNVSWSADHRVIDGATMSR 448
Cdd:PTZ00144 323 KLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKkrPVVVGNE---IVIRPIMYLALTYDHRLIDGRDAVT 399
|
410
....*....|....*....
gi 1777244800 449 FSNLWKSYLENPAFMLLDL 467
Cdd:PTZ00144 400 FLKKIKDLIEDPARMLLDL 418
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
64-465 |
4.40e-46 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 167.72 E-value: 4.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 64 EVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYY------------------NLDDIAYVG--KPLVD 123
Cdd:PLN02744 126 EGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKgdgakeikvgeviaitveEEEDIGKFKdyKPSSS 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 124 IETEALKDSE------EDVVETPAVSHDEHTHQE----IKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILN 193
Cdd:PLN02744 206 AAPAAPKAKPsppppkEEEVEKPASSPEPKASKPsappSSGDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIED 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 194 YLEKQ-TGAILPPSPKAEIMPPPPkpkdmtIPIPVSKPPVFTGKdktepikgfqkamvKTMSAALKIPHFGYCDEVDLTE 272
Cdd:PLN02744 286 YLASGgKGATAPPSTDSKAPALDY------TDIPNTQIRKVTAS--------------RLLQSKQTIPHYYLTVDTRVDK 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 273 LVKLREELKPIAFARGIK-LSFMPFFLKAVSLGLLQFPILNAS-VDE---NCQNItykashNIGIAMDTEQGLIVPNVKN 347
Cdd:PLN02744 346 LMALRSQLNSLQEASGGKkISVNDLVIKAAALALRKVPQCNSSwTDDyirQYHNV------NINVAVQTENGLYVPVVKD 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 348 VQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGS-IGGTYTKPVIMPPEVAIGALGSI--KAIPRfNQKGEV 424
Cdd:PLN02744 420 ADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGpFGIKQFCAIINPPQSAILAVGSAekRVIPG-SGPDQY 498
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1777244800 425 YKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 465
Cdd:PLN02744 499 NFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
160-465 |
7.35e-37 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 138.50 E-value: 7.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 160 TPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYL--EKQTGAILPPSPKAEIMPpppkpkdmtipIPVSKPPvfTGKD 237
Cdd:PRK14843 52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALLpeNIENDSIKSPAQIEKVEE-----------VPDNVTP--YGEI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 238 KTEPIKGFQKAMVKTMSAA-LKIPHFGYCDEVDLTELVKLREE-LKPIAFARGIKLSFMPFFLKAVSLGLLQFPILNASV 315
Cdd:PRK14843 119 ERIPMTPMRKVIAQRMVESyLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 316 DENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYT 395
Cdd:PRK14843 199 TEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSF 278
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 396 KPVIMPPEVAIGALGSIKAIPRFnQKGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 465
Cdd:PRK14843 279 GPIINQPNSAILGVSSTIEKPVV-VNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
30-467 |
1.76e-36 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 139.89 E-value: 1.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 30 SFKYSHPHHFLKTTAALRGQVVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYY 109
Cdd:PLN02226 71 SLVSSTLQRWVRPFSSESGDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 110 NLDDIAYVGKPLVDIETEALKDSE----EDVVETPAVSHDEHTHQEIKGRKTLATPAvrrlamenniklsevvgsgkdgr 185
Cdd:PLN02226 151 KEGDTVEPGTKVAIISKSEDAASQvtpsQKIPETTDPKPSPPAEDKQKPKVESAPVA----------------------- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 186 ilkedilnylEKQTGAILPPSPKAEimppppkpkdmtipipvSKPPVFTGKDKTEPIKgfQKAMVKTMSAALKIPHFGYC 265
Cdd:PLN02226 208 ----------EKPKAPSSPPPPKQS-----------------AKEPQLPPKERERRVP--MTRLRKRVATRLKDSQNTFA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 266 -----DEVDLTELVKLREELKPIAFAR-GIKLSFMPFFLKAVSLGLLQFPILNASVDENcqNITYKASHNIGIAMDTEQG 339
Cdd:PLN02226 259 llttfNEVDMTNLMKLRSQYKDAFYEKhGVKLGLMSGFIKAAVSALQHQPVVNAVIDGD--DIIYRDYVDISIAVGTSKG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 340 LIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGSIKAIPRFn 419
Cdd:PLN02226 337 LVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMV- 415
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1777244800 420 QKGEVYKAQIVNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLDL 467
Cdd:PLN02226 416 VGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLLDI 463
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
51-124 |
1.46e-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: 96.32 E-value: 1.46e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1777244800 51 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 124
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
51-124 |
6.23e-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: 86.27 E-value: 6.23e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1777244800 51 VQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 124
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
51-124 |
4.83e-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: 83.80 E-value: 4.83e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1777244800 51 VQFKLSDIGEGIREVtVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 124
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 ... |
158-192 |
1.94e-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: 1.94e-14
10 20 30
....*....|....*....|....*....|....*
gi 1777244800 158 LATPAVRRLAMENNIKLSEVVGSGKDGRILKEDIL 192
Cdd:pfam02817 2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
224-449 |
5.56e-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: 5.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 224 PIPVSKPPVFTGKDKTEPIKGFQKAMVKTMSAALKIPhfgycdevdlTEL------VKLREELKPI-----AFARGIKLS 292
Cdd:PRK12270 102 AAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASLEVP----------TATsvravpAKLLIDNRIVinnhlKRTRGGKVS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 293 FMPFFLKAVSLGLLQFPILNASVDE--NCQNITYKASHNIGIAMDTEQ-----GLIVPNVKNVQICSIFDIATELNRLQK 365
Cdd:PRK12270 172 FTHLIGYALVQALKAFPNMNRHYAEvdGKPTLVTPAHVNLGLAIDLPKkdgsrQLVVPAIKGAETMDFAQFWAAYEDIVR 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 366 LGSVGQLSTTDLTGGTFTLSNIGSIGGTYTKPVIMPPEVAIGALGSIKAIPRFNQKGEVYKAQ-----IVNVSWSADHRV 440
Cdd:PRK12270 252 RARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEYPAEFQGASEERLAElgiskVMTLTSTYDHRI 331
|
....*....
gi 1777244800 441 IDGATMSRF 449
Cdd:PRK12270 332 IQGAESGEF 340
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
59-204 |
2.99e-10 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 61.50 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 59 GEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDSEEDVVe 138
Cdd:PRK14875 11 GLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVSDAEIDAF- 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1777244800 139 tpavshdehthqeikgrktlATPAVRRLAMEnNIKLSEVVGSGKDGRILKEDIlNYLEKQTGAILP 204
Cdd:PRK14875 90 --------------------IAPFARRFAPE-GIDEEDAGPAPRKARIGGRTV-RYLRLGEGDGTP 133
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
55-124 |
8.12e-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: 8.12e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777244800 55 LSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 124
Cdd:cd06663 4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
66-124 |
1.68e-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: 1.68e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1777244800 66 TVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDI 124
Cdd:cd06850 9 TVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
64-107 |
2.34e-03 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 40.29 E-value: 2.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1777244800 64 EVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKL 107
Cdd:PRK11892 16 EGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKI 59
|
|
| |
