|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
67-482 |
0e+00 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 518.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 67 FKLSDIGEGIREVTIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKRLYYNLDDIAYVGKPLIDIETEALKDS 146
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 147 EEDVVETPAVSHDEHTHQEIKGQK-----TLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILSFLeKQTGAILPPSP 221
Cdd:PLN02528 81 RSDSLLLPTDSSNIVSLAESDERGsnlsgVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYA-AQKGVVKDSSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 222 KSEITPPPPQPKDRTFPTPIAKppvfTGKDRTEPVTGFQKAMVKTMSAALKIPHFGYCDEIDLTQLVKLREELKPVALAR 301
Cdd:PLN02528 160 AEEATIAEQEEFSTSVSTPTEQ----SYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 302 GIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGIAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLG 381
Cdd:PLN02528 236 TVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 382 SSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGAIKALPRFDQKGDVYKAQIMNVSWSADHRVIDGATMS 461
Cdd:PLN02528 316 AENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVA 395
|
410 420
....*....|....*....|.
gi 170172520 462 RFSNLWKSYLENPAFMLLDLK 482
Cdd:PLN02528 396 RFCNEWKSYVEKPELLMLHMR 416
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
267-478 |
4.19e-95 |
|
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: 286.36 E-value: 4.19e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 267 MSAAL-KIPHFGYCDEIDLTQLVKLREELKPVALARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIG 345
Cdd:pfam00198 1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 346 IAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGA 425
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 170172520 426 IKALPRFDQkGDVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFML 478
Cdd:pfam00198 161 IRKRPVVVD-GEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
57-479 |
4.06e-73 |
|
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: 240.55 E-value: 4.06e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 57 AAVLQGQVVQFKLSDIGeGIREVTIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKRLYYNLDDIAYVGKPLI 136
Cdd:TIGR01348 109 AAGQSSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLIL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 137 DIETEALKDSEEDVVE-------------------------TPAVSHDEHTHQeikGQKTL-ATPAVRRLAMENNIKLSE 190
Cdd:TIGR01348 188 TLSVAGSTPATAPAPAsaqpaaqspaatqpepaaapaaakaQAPAPQQAGTQN---PAKVDhAAPAVRRLAREFGVDLSA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 191 VVGSGKDGRILKEDILSFLEKQTGAIlPPSPKSEITPPPPQPkdrtfPTPIAKPPVFtGKDRTEPVTGFQKAMVKTMSAA 270
Cdd:TIGR01348 265 VKGTGIKGRILREDVQRFVKEPSVRA-QAAAASAAGGAPGAL-----PWPNVDFSKF-GEVEEVDMSRIRKISGANLTRN 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 271 -LKIPHFGYCDEIDLTQLVKLREELKPVALARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGIAMD 349
Cdd:TIGR01348 338 wTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVD 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 350 TELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIgaLGAIKAL 429
Cdd:TIGR01348 418 TPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAI--LGVSKSG 495
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 170172520 430 --PRFDQKGDVYKaQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 479
Cdd:TIGR01348 496 mePVWNGKEFEPR-LMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
65-138 |
6.63e-25 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 97.48 E-value: 6.63e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170172520 65 VQFKLSDIGEGIREVTIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKRLYYNLDDIAYVGKPLIDI 138
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
65-138 |
6.25e-21 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 86.66 E-value: 6.25e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170172520 65 VQFKLSDIGEGIREVTIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKRLYYNLDDIAYVGKPLIDI 138
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02528 |
PLN02528 |
2-oxoisovalerate dehydrogenase E2 component |
67-482 |
0e+00 |
|
2-oxoisovalerate dehydrogenase E2 component
Pssm-ID: 215289 [Multi-domain] Cd Length: 416 Bit Score: 518.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 67 FKLSDIGEGIREVTIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKRLYYNLDDIAYVGKPLIDIETEALKDS 146
Cdd:PLN02528 1 VPLAQTGEGIAECELLRWFVKEGDQVEEFQPLCEVQSDKATIEITSRYKGKVAQINFSPGDIVKVGETLLKIMVEDSQHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 147 EEDVVETPAVSHDEHTHQEIKGQK-----TLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILSFLeKQTGAILPPSP 221
Cdd:PLN02528 81 RSDSLLLPTDSSNIVSLAESDERGsnlsgVLSTPAVRHLAKQYGIDLNDILGTGKDGRVLKEDVLKYA-AQKGVVKDSSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 222 KSEITPPPPQPKDRTFPTPIAKppvfTGKDRTEPVTGFQKAMVKTMSAALKIPHFGYCDEIDLTQLVKLREELKPVALAR 301
Cdd:PLN02528 160 AEEATIAEQEEFSTSVSTPTEQ----SYEDKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 302 GIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGIAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLG 381
Cdd:PLN02528 236 TVKHTFLPFLIKSLSMALSKYPLLNSCFNEETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 382 SSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGAIKALPRFDQKGDVYKAQIMNVSWSADHRVIDGATMS 461
Cdd:PLN02528 316 AENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVA 395
|
410 420
....*....|....*....|.
gi 170172520 462 RFSNLWKSYLENPAFMLLDLK 482
Cdd:PLN02528 396 RFCNEWKSYVEKPELLMLHMR 416
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
56-479 |
4.68e-157 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 456.98 E-value: 4.68e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 56 TAAVLQGQVVQFKLSDIGEgIREVTIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKRLYYNLDDIAYVGKPL 135
Cdd:PRK11855 111 AAAAAGGGVVEVKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 136 IDIETEALKDSEEDVVETPAVSHDEHTHQE------------------IKGQKTLATPAVRRLAMENNIKLSEVVGSGKD 197
Cdd:PRK11855 190 VVIEVAAAAPAAAAAPAAAAPAAAAAAAPApapaaaaapaaaapaaaaAPGKAPHASPAVRRLARELGVDLSQVKGTGKK 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 198 GRILKEDILSFLE-KQTGAILPPSPKSEITPPPPQPKdrtfPTPIAKPPVFtGKDRTEPVTGFQKAMVKTMSAAL-KIPH 275
Cdd:PRK11855 270 GRITKEDVQAFVKgAMSAAAAAAAAAAAAGGGGLGLL----PWPKVDFSKF-GEIETKPLSRIKKISAANLHRSWvTIPH 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 276 FGYCDEIDLTQLVKLREELKPVALARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGIAMDTELGLI 355
Cdd:PRK11855 345 VTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNASLDEDGDELTYKKYFNIGFAVDTPNGLV 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 356 VPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGAIKALPrFDQK 435
Cdd:PRK11855 425 VPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKP-VWDG 503
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 170172520 436 GDVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 479
Cdd:PRK11855 504 KEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
64-480 |
1.15e-130 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 384.53 E-value: 1.15e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 64 VVQFKLSDIGEGIREVTIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKRLYYNLDDIAYVGKPLIDIETE-- 141
Cdd:PRK11856 2 MFEFKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEge 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 142 --------------ALKDSEEDVVETPAVSHDEHTHQEIKGQKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILS 207
Cdd:PRK11856 82 aeaaaaaeaapeapAPEPAPAAAAAAAAAPAAAAAPAAPAAAAAKASPAVRKLARELGVDLSTVKGSGPGGRITKEDVEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 208 FLEKQtgailppspkseitpppPQPKDRTFPTPIAKPPVFTGKDRTEPVTGFQKAMVKTMSAA-LKIPHFGYCDEIDLTQ 286
Cdd:PRK11856 162 AAAAA-----------------APAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESkREIPHFTLTDEVDVTA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 287 LVKLREELKPVAlargIKLSFMPFFLKAASLGLLQFPILNASVDEncQNITYKASHNIGIAMDTELGLIVPNVKNVQVRS 366
Cdd:PRK11856 225 LLALRKQLKAIG----VKLTVTDFLIKAVALALKKFPELNASWDD--DAIVLKKYVNIGIAVATDGGLIVPVIRDADKKS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 367 VFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGAIKALPRFdQKGDVYKAQIMNV 446
Cdd:PRK11856 299 LFELAREIKDLAEKAREGKLKPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVV-VDGEIVVRKVMPL 377
|
410 420 430
....*....|....*....|....*....|....
gi 170172520 447 SWSADHRVIDGATMSRFSNLWKSYLENPAFMLLD 480
Cdd:PRK11856 378 SLSFDHRVIDGADAARFLKALKELLENPALLLLE 411
|
|
| 2-oxoacid_dh |
pfam00198 |
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ... |
267-478 |
4.19e-95 |
|
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: 286.36 E-value: 4.19e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 267 MSAAL-KIPHFGYCDEIDLTQLVKLREELKPVALARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIG 345
Cdd:pfam00198 1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 346 IAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGA 425
Cdd:pfam00198 81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 170172520 426 IKALPRFDQkGDVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFML 478
Cdd:pfam00198 161 IRKRPVVVD-GEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
57-473 |
6.43e-79 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 258.01 E-value: 6.43e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 57 AAVLQGQVVQFKLSDIGEGirEVTIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKRLYYNLDDIAYVGKPLI 136
Cdd:PRK11854 199 APAAAAGVKDVNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIM 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 137 DIETE--------ALKDSEEDV---------VETPAVSHDEHTHQEIKGQKTLATPAVRRLAMENNIKLSEVVGSGKDGR 199
Cdd:PRK11854 277 RFEVEgaapaaapAKQEAAAPApaaakaeapAAAPAAKAEGKSEFAENDAYVHATPLVRRLAREFGVNLAKVKGTGRKGR 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 200 ILKEDILSFLEK-----QTGAILPPSPKSEITPPPpqpkdrtfpTPIAKPPVFtGKDRTEPVTGFQKAMVKTMSAAL-KI 273
Cdd:PRK11854 357 ILKEDVQAYVKDavkraEAAPAAAAAGGGGPGLLP---------WPKVDFSKF-GEIEEVELGRIQKISGANLHRNWvMI 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 274 PHFGYCDEIDLTQLVKLREELKPVALAR--GIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGIAMDTE 351
Cdd:PRK11854 427 PHVTQFDKADITELEAFRKQQNAEAEKRklGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAVDTP 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 352 LGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGAIKALPR 431
Cdd:PRK11854 507 NGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPV 586
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 170172520 432 FDQKGDVYKaQIMNVSWSADHRVIDGATMSRFSNLWKSYLEN 473
Cdd:PRK11854 587 WNGKEFAPR-LMLPLSLSYDHRVIDGADGARFITIINDRLSD 627
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
57-479 |
4.06e-73 |
|
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: 240.55 E-value: 4.06e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 57 AAVLQGQVVQFKLSDIGeGIREVTIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKRLYYNLDDIAYVGKPLI 136
Cdd:TIGR01348 109 AAGQSSGVQEVTVPDIG-DIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLIL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 137 DIETEALKDSEEDVVE-------------------------TPAVSHDEHTHQeikGQKTL-ATPAVRRLAMENNIKLSE 190
Cdd:TIGR01348 188 TLSVAGSTPATAPAPAsaqpaaqspaatqpepaaapaaakaQAPAPQQAGTQN---PAKVDhAAPAVRRLAREFGVDLSA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 191 VVGSGKDGRILKEDILSFLEKQTGAIlPPSPKSEITPPPPQPkdrtfPTPIAKPPVFtGKDRTEPVTGFQKAMVKTMSAA 270
Cdd:TIGR01348 265 VKGTGIKGRILREDVQRFVKEPSVRA-QAAAASAAGGAPGAL-----PWPNVDFSKF-GEVEEVDMSRIRKISGANLTRN 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 271 -LKIPHFGYCDEIDLTQLVKLREELKPVALARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGIAMD 349
Cdd:TIGR01348 338 wTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDLGGEQLILKKYVNIGVAVD 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 350 TELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIgaLGAIKAL 429
Cdd:TIGR01348 418 TPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAI--LGVSKSG 495
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 170172520 430 --PRFDQKGDVYKaQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 479
Cdd:TIGR01348 496 mePVWNGKEFEPR-LMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
65-481 |
2.88e-72 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 234.24 E-value: 2.88e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 65 VQFKLSDIGEGIREVTIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKRLYYNLDDIAYVGKPLIDIETEALK 144
Cdd:TIGR01347 1 IEIKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 145 D------SEEDVVETPAVShdEHTHQEIKGQKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILSFLEKQTGAILP 218
Cdd:TIGR01347 81 TaappakSGEEKEETPAAS--AAAAPTAAANRPSLSPAARRLAKEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 219 PSPKSEitppppqpkdrtfptpiAKPPVFTGKDRTEPVTGFQKAMVKTM-----SAALkIPHFgycDEIDLTQLVKLREE 293
Cdd:TIGR01347 159 AAAAAA-----------------AAPAAATRPEERVKMTRLRQRIAERLkeaqnSTAM-LTTF---NEVDMSAVMELRKR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 294 LKPVALAR-GIKLSFMPFFLKAASLGLLQFPILNASVDENcqNITYKASHNIGIAMDTELGLIVPNVKNVQVRSVFEIAM 372
Cdd:TIGR01347 218 YKEEFEKKhGVKLGFMSFFVKAVVAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 373 ELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGAIKALPrFDQKGDVYKAQIMNVSWSADH 452
Cdd:TIGR01347 296 EIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERP-VAVNGQIEIRPMMYLALSYDH 374
|
410 420
....*....|....*....|....*....
gi 170172520 453 RVIDGATMSRFSNLWKSYLENPAFMLLDL 481
Cdd:TIGR01347 375 RLIDGKEAVTFLVTIKELLEDPRRLLLDL 403
|
|
| PRK11857 |
PRK11857 |
dihydrolipoamide acetyltransferase; Reviewed |
170-474 |
1.04e-71 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237002 [Multi-domain] Cd Length: 306 Bit Score: 229.68 E-value: 1.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 170 KTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILSFLEKQTGAilpPSPKSEITPPPPQPKDRTfPTPIAKPPVFTG 249
Cdd:PRK11857 1 KILATPIARALAKKLGIDISLLKGSGRDGKILAEDVENFIKSLKSA---PTPAEAASVSSAQQAAKT-AAPAAAPPKLEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 250 KdrTEPVTGFQKAMVKTMSAALK-IPHFGYCDEIDLTQLVKLREELK-PVALARGIKLSFMPFFLKAASLGLLQFPILNA 327
Cdd:PRK11857 77 K--REKVAPIRKAIARAMTNSWSnVAYVNLVNEIDMTKLWDLRKSVKdPVLKTEGVKLTFLPFIAKAILIALKEFPIFAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 328 SVDENCQNITYKASHNIGIAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGT 407
Cdd:PRK11857 155 KYDEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARERKIKPDEMKGGSFTITNYGSVGSL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170172520 408 YAKPVILPPEVAIGALGAIKALPRFdQKGDVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENP 474
Cdd:PRK11857 235 YGVPVINYPELAIAGVGAIIDKAIV-KNGQIVAGKVMHLTVAADHRWIDGATIGRFASRVKELLEKP 300
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
68-481 |
3.14e-67 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 221.25 E-value: 3.14e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 68 KLSDIGEGIREVTIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKRLYYNLDDIAYVGKPLIDIETEA----L 143
Cdd:PRK05704 6 KVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAaagaA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 144 KDSEEDVVETPAVSHDEHTHQEIKGQKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILSFLEKqtgailPPSPKS 223
Cdd:PRK05704 86 AAAAAAAAAAAAAPAQAQAAAAAEQSNDALSPAARKLAAENGLDASAVKGTGKGGRVTKEDVLAALAA------AAAAPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 224 EITPPPPQPkdrtfptpiakPPVFTGkDRTE---PVTGFQK-------------AMVKTmsaalkiphFgycDEIDLTQL 287
Cdd:PRK05704 160 APAAAAPAA-----------APAPLG-ARPEervPMTRLRKtiaerlleaqnttAMLTT---------F---NEVDMTPV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 288 VKLREELKPVALAR-GIKLSFMPFFLKAASLGLLQFPILNASVDENcqNITYKASHNIGIAMDTELGLIVPNVKNVQVRS 366
Cdd:PRK05704 216 MDLRKQYKDAFEKKhGVKLGFMSFFVKAVVEALKRYPEVNASIDGD--DIVYHNYYDIGIAVGTPRGLVVPVLRDADQLS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 367 VFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNigsiGGTY----AKPVILPPEVAIgaLG--AIKALPrFDQKGDVYK 440
Cdd:PRK05704 294 FAEIEKKIAELAKKARDGKLSIEELTGGTFTITN----GGVFgslmSTPIINPPQSAI--LGmhKIKERP-VAVNGQIVI 366
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 170172520 441 AQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLDL 481
Cdd:PRK05704 367 RPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLLDL 407
|
|
| SucB_Actino |
TIGR02927 |
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ... |
62-476 |
2.48e-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: 221.04 E-value: 2.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 62 GQVVQFKLSDIGEGIREVTIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKRLYYNLDDIAYVGKPLIDI--- 138
Cdd:TIGR02927 124 GEATEVKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIgda 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 139 --------ETEALKDSEEDVVETPAVSHDEHTHQEIKGQKTLA----------------------TPAVRRLAMENNIKL 188
Cdd:TIGR02927 204 naapaepaEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPApaktaapaaaapvssgdsgpyvTPLVRKLAKDKGVDL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 189 SEVVGSGKDGRILKEDILSFLEKQTGAILPPSPkseiTPPPPQPKDRTFPTPIAKPPVFTGKDRTEPVTGFQKAMVKTMS 268
Cdd:TIGR02927 284 STVKGTGVGGRIRKQDVLAAAKAAEEARAAAAA----PAAAAAPAAPAAAAKPAEPDTAKLRGTTQKMNRIRQITADKTI 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 269 AALKI-PHFGYCDEIDLTQLVKLREELKPVALAR-GIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGI 346
Cdd:TIGR02927 360 ESLQTsAQLTQVHEVDMTRVAALRARAKNDFLEKnGVNLTFLPFFVQAVTEALKAHPNVNASYNAETKEVTYHDVEHVGI 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 347 AMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGAI 426
Cdd:TIGR02927 440 AVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAI 519
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 170172520 427 KALPRF--DQKGDVYKA--QIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAF 476
Cdd:TIGR02927 520 VKRPRVikDEDGGESIAirSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEEGDF 573
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
68-481 |
5.51e-64 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 213.01 E-value: 5.51e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 68 KLSDIGEGIREVTIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKRLYYNLDDIAYVGKPLIDIETEALKDSE 147
Cdd:PTZ00144 48 KVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPPAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 148 EdvVETPAVSHDEHTHQEikgqktlatpavrrlamenniklsevvgsgkdgrilkedilsflEKQTGAILPPSPKSEiTP 227
Cdd:PTZ00144 128 A--PAAAAAAKAEKTTPE--------------------------------------------KPKAAAPTPEPPAAS-KP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 228 PPPqPKDRTFPTPIAKPPVFTGKDRTEPVTGFQK--AMVKTMSAALK--------IPHFgycDEIDLTQLVKLREELKPV 297
Cdd:PTZ00144 161 TPP-AAAKPPEPAPAAKPPPTPVARADPRETRVPmsRMRQRIAERLKasqntcamLTTF---NECDMSALMELRKEYKDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 298 ALAR-GIKLSFMPFFLKAASLGLLQFPILNASVDENCqnITYKASHNIGIAMDTELGLIVPNVKNVQVRSVFEIAMELNR 376
Cdd:PTZ00144 237 FQKKhGVKLGFMSAFVKASTIALKKMPIVNAYIDGDE--IVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELAD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 377 LQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGAIKALP--RFDQkgdVYKAQIMNVSWSADHRV 454
Cdd:PTZ00144 315 LAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPvvVGNE---IVIRPIMYLALTYDHRL 391
|
410 420
....*....|....*....|....*..
gi 170172520 455 IDGATMSRFSNLWKSYLENPAFMLLDL 481
Cdd:PTZ00144 392 IDGRDAVTFLKKIKDLIEDPARMLLDL 418
|
|
| PDHac_trf_mito |
TIGR01349 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
76-479 |
1.51e-62 |
|
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: 209.65 E-value: 1.51e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 76 IREVTIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKRLYY--NLDDIAyVGKPLI-------DIET------ 140
Cdd:TIGR01349 11 MTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILVpeGTKDVP-VNKPIAvlveekeDVADafknyk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 141 ------EALKDSEE--------------DVVETPAVSHDEHTHQEIKGQKTLATPAVRRLAMENNIKLSEVVGSGKDGRI 200
Cdd:TIGR01349 90 lessasPAPKPSEIaptappsapkpspaPQKQSPEPSSPAPLSDKESGDRIFASPLAKKLAKEKGIDLSAVAGSGPNGRI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 201 LKEDILSFLekqtgailPPSPKseitPPPPQPKDRTFPTPIAKPPVFTGKDRTEPVTGFQKAMVKTMSAALK-IPHFGYC 279
Cdd:TIGR01349 170 VKKDIESFV--------PQSPA----SANQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQtIPHYYVS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 280 DEIDLTQLVKLREELKPVALARgIKLSFMPFFLKAASLGLLQFPILNASVDENcqNITYKASHNIGIAMDTELGLIVPNV 359
Cdd:TIGR01349 238 IECNVDKLLALRKELNAMASEV-YKLSVNDFIIKASALALREVPEANSSWTDN--FIRRYKNVDISVAVATPDGLITPIV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 360 KNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGAI--KALPRFDQKGD 437
Cdd:TIGR01349 315 RNADAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVedVAVVDNDEEKG 394
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 170172520 438 VYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 479
Cdd:TIGR01349 395 FAVASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
|
|
| PLN02744 |
PLN02744 |
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
78-479 |
5.64e-46 |
|
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Pssm-ID: 215397 [Multi-domain] Cd Length: 539 Bit Score: 167.72 E-value: 5.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 78 EVTIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKRLYYN--LDDIAyVGKPL-IDIETE----ALKD----- 145
Cdd:PLN02744 126 EGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLAKIVKGdgAKEIK-VGEVIaITVEEEedigKFKDykpss 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 146 ---------------SEEDVVETPAVSHDEHTHQE----IKGQKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDIL 206
Cdd:PLN02744 205 saapaapkakpspppPKEEEVEKPASSPEPKASKPsappSSGDRIFASPLARKLAEDNNVPLSSIKGTGPDGRIVKADIE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 207 SFLEkqtgailppSPKSEITPPPPQPKDRTfptpiakppvftGKDRTE-PVTGFQKAMVKTM-SAALKIPHFGYCDEIDL 284
Cdd:PLN02744 285 DYLA---------SGGKGATAPPSTDSKAP------------ALDYTDiPNTQIRKVTASRLlQSKQTIPHYYLTVDTRV 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 285 TQLVKLREELKPVALARGIK-LSFMPFFLKAASLGLLQFPILNAS-VDE---NCQNItykashNIGIAMDTELGLIVPNV 359
Cdd:PLN02744 344 DKLMALRSQLNSLQEASGGKkISVNDLVIKAAALALRKVPQCNSSwTDDyirQYHNV------NINVAVQTENGLYVPVV 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 360 KNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGS-IGGTYAKPVILPPEVAIGALG-AIKALPRFDQKGD 437
Cdd:PLN02744 418 KDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGpFGIKQFCAIINPPQSAILAVGsAEKRVIPGSGPDQ 497
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 170172520 438 VYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 479
Cdd:PLN02744 498 YNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
|
|
| PLN02226 |
PLN02226 |
2-oxoglutarate dehydrogenase E2 component |
34-481 |
2.24e-38 |
|
2-oxoglutarate dehydrogenase E2 component
Pssm-ID: 177871 [Multi-domain] Cd Length: 463 Bit Score: 145.67 E-value: 2.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 34 PKCVCSVGYplfKYSQPRHSLRTAAVLQGQVVQFKLSDIGEGIREVTIKEWYVKEGDTVSQFDSICEVQSDKASVTITSR 113
Cdd:PLN02226 64 SGISRSASL---VSSTLQRWVRPFSSESGDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASP 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 114 YDGVIKRLYYNLDDIAYVGKPLIDIETEAlkDSEEDVveTPAvshdehthqeikgQKTLATPAVRRLAmenniklsevvg 193
Cdd:PLN02226 141 ASGVIQEFLVKEGDTVEPGTKVAIISKSE--DAASQV--TPS-------------QKIPETTDPKPSP------------ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 194 SGKDGRILKEDILSFLEKQTGAILPPSPKSEITPPPPQPKDRtfptpiakppvftgkDRTEPVTGFQKAMVKTMSAALK- 272
Cdd:PLN02226 192 PAEDKQKPKVESAPVAEKPKAPSSPPPPKQSAKEPQLPPKER---------------ERRVPMTRLRKRVATRLKDSQNt 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 273 IPHFGYCDEIDLTQLVKLREELKPVALAR-GIKLSFMPFFLKAASLGLLQFPILNASVDENcqNITYKASHNIGIAMDTE 351
Cdd:PLN02226 257 FALLTTFNEVDMTNLMKLRSQYKDAFYEKhGVKLGLMSGFIKAAVSALQHQPVVNAVIDGD--DIIYRDYVDISIAVGTS 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 352 LGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGAIKALPR 431
Cdd:PLN02226 335 KGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPM 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 170172520 432 FdQKGDVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLDL 481
Cdd:PLN02226 415 V-VGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLLDI 463
|
|
| PRK14843 |
PRK14843 |
dihydrolipoamide acetyltransferase; Provisional |
174-479 |
3.05e-38 |
|
dihydrolipoamide acetyltransferase; Provisional
Pssm-ID: 184847 [Multi-domain] Cd Length: 347 Bit Score: 142.74 E-value: 3.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 174 TPAVRRLAMENNIKLSEVVGSGKDGRILKEDILSFLekqtgailpPSPKSEITPPPPQPKDRTFPTPIAKPPvfTGKDRT 253
Cdd:PRK14843 52 SPLAKRIALEHNIAWQEIQGTGHRGKIMKKDVLALL---------PENIENDSIKSPAQIEKVEEVPDNVTP--YGEIER 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 254 EPVTGFQKAMVKTMSAA-LKIPHFGYCDEIDLTQLVKLREE-LKPVALARGIKLSFMPFFLKAASLGLLQFPILNASVDE 331
Cdd:PRK14843 121 IPMTPMRKVIAQRMVESyLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATGKKTTVTDLLSLAVVKTLMKHPYINASLTE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 332 NCQNITYKASHNIGIAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKP 411
Cdd:PRK14843 201 DGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSFGP 280
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170172520 412 VILPPEVAIGALGAIKALPRFdQKGDVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLL 479
Cdd:PRK14843 281 IINQPNSAILGVSSTIEKPVV-VNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
65-138 |
6.63e-25 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 97.48 E-value: 6.63e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170172520 65 VQFKLSDIGEGIREVTIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKRLYYNLDDIAYVGKPLIDI 138
Cdd:cd06849 1 TEIKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
65-138 |
6.25e-21 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 86.66 E-value: 6.25e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170172520 65 VQFKLSDIGEGIREVTIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKRLYYNLDDIAYVGKPLIDI 138
Cdd:COG0508 3 IEIKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
65-138 |
9.87e-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: 83.03 E-value: 9.87e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170172520 65 VQFKLSDIGEGIREVtIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKRLYYNLDDIAYVGKPLIDI 138
Cdd:pfam00364 1 TEIKSPMIGESVREG-VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
218-463 |
1.42e-14 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 76.47 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 218 PPSPKSEITPPPPQPKDRTFPTPIAKPPVftgKDRTEPVTGFQKAMVKTMSAALKIPhfgycdeidlTQL------VKLR 291
Cdd:PRK12270 85 KPAAAAAAAAAPAAPPAAAAAAAPAAAAV---EDEVTPLRGAAAAVAKNMDASLEVP----------TATsvravpAKLL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 292 EELKPV-----ALARGIKLSFMPFFLKAASLGLLQFPILNASVDE--NCQNITYKASHNIGIAMDTE-----LGLIVPNV 359
Cdd:PRK12270 152 IDNRIVinnhlKRTRGGKVSFTHLIGYALVQALKAFPNMNRHYAEvdGKPTLVTPAHVNLGLAIDLPkkdgsRQLVVPAI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 360 KNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGAIKALPRF-----DQ 434
Cdd:PRK12270 232 KGAETMDFAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEYPAEFqgaseER 311
|
250 260
....*....|....*....|....*....
gi 170172520 435 KGDVYKAQIMNVSWSADHRVIDGATMSRF 463
Cdd:PRK12270 312 LAELGISKVMTLTSTYDHRIIQGAESGEF 340
|
|
| E3_binding |
pfam02817 |
e3 binding domain; This family represents a small domain of the E2 subunit of 2-oxo-acid ... |
172-206 |
4.88e-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: 65.79 E-value: 4.88e-14
10 20 30
....*....|....*....|....*....|....*
gi 170172520 172 LATPAVRRLAMENNIKLSEVVGSGKDGRILKEDIL 206
Cdd:pfam02817 2 LASPAARKLARELGIDLSDVKGTGPGGRITKEDVE 36
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
73-218 |
7.64e-10 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 60.34 E-value: 7.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 73 GEGIREVTIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKRLYYNLDDIAYVGKPLIDIETEALKDSEEDVVe 152
Cdd:PRK14875 11 GLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEVSDAEIDAF- 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170172520 153 tpavshdehthqeikgqktlATPAVRRLAMEnNIKLSEVVGSGKDGRILKEDIlSFLEKQTGAILP 218
Cdd:PRK14875 90 --------------------IAPFARRFAPE-GIDEEDAGPAPRKARIGGRTV-RYLRLGEGDGTP 133
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
69-138 |
4.29e-08 |
|
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: 50.13 E-value: 4.29e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170172520 69 LSDIGEGIREVTIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKRLYYNLDDIAYVGKPLIDI 138
Cdd:cd06663 4 IPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
80-138 |
3.15e-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: 38.94 E-value: 3.15e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 170172520 80 TIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKRLYYNLDDIAYVGKPLIDI 138
Cdd:cd06850 9 TVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
78-154 |
4.81e-03 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 39.13 E-value: 4.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170172520 78 EVTIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIkrlyynlddiayvGKPLIDIETEALKdseedvVETP 154
Cdd:PRK11892 16 EGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTL-------------GKILVPEGTEGVK------VNTP 73
|
|
| |
